Unnamed: 0
int64 0
562k
| Entry
stringlengths 6
10
| Sequence
stringlengths 2
35.2k
| Protein names
stringlengths 1
2.59k
| Organism
stringlengths 8
196
| Organism (ID)
int64 14
3.4M
| Length
int64 2
35.2k
| Mass
int64 260
3.91M
| Keywords
stringlengths 3
1.61k
⌀ | Gene Ontology IDs
stringlengths 10
3.48k
⌀ | Protein existence
stringclasses 5
values | Annotation
float64 1
5
| Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Signal peptide
stringlengths 11
302
⌀ | Transmembrane
stringlengths 31
5.51k
⌀ | Pfam
stringlengths 8
232
⌀ | InterPro
stringlengths 10
820
⌀ | PDB
stringlengths 5
11.6k
⌀ | Taxonomic lineage
stringlengths 49
843
| Gene Names
stringlengths 1
583
⌀ | Toxin
bool 2
classes |
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
400 |
A0A2K5QCI5
|
MKAAVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDSVKDSGRDYVSQFESSALGKQLNLKLLDNWDSLTSTVNKLREDLGPVTQEFWDNLEKETGWLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEVKLYSQKLEPLRTEFQEGALQKLQDLQEKLSPLAEQVRDRARAHVDTLRTQLAPYSDELRQRLATRLEVLKESGGASLAEYHAKASEHLSALGEKAKPALEDLRQGLLPVLESFKVSFLSALEEYAKKLSSQ
|
Apolipoprotein A-I (Apo-AI) (ApoA-I) (Apolipoprotein A1) [Cleaved into: Proapolipoprotein A-I (ProapoA-I); Truncated apolipoprotein A-I]
|
Cebus imitator (Panamanian white-faced capuchin) (Cebus capucinus imitator)
| 2,715,852 | 267 | 30,548 |
Cholesterol metabolism;HDL;Lipid metabolism;Lipid transport;Lipoprotein;Oxidation;Palmitate;Phosphoprotein;Reference proteome;Repeat;Secreted;Signal;Steroid metabolism;Sterol metabolism;Transport
|
GO:0001540; GO:0001935; GO:0002719; GO:0005543; GO:0006656; GO:0006695; GO:0007186; GO:0007229; GO:0008035; GO:0008211; GO:0010804; GO:0010875; GO:0010903; GO:0015485; GO:0019899; GO:0019915; GO:0030139; GO:0030300; GO:0030325; GO:0031072; GO:0032489; GO:0032691; GO:0033344; GO:0033700; GO:0034115; GO:0034191; GO:0034205; GO:0034361; GO:0034362; GO:0034366; GO:0034375; GO:0034380; GO:0035025; GO:0042158; GO:0042627; GO:0042632; GO:0042803; GO:0043534; GO:0043691; GO:0045499; GO:0050728; GO:0050766; GO:0050821; GO:0051180; GO:0051496; GO:0055091; GO:0060228; GO:0060354; GO:0070328; GO:0070508; GO:0070653; GO:0071402; GO:0090205; GO:0120020; GO:1900026; GO:1902995; GO:1903561
|
Inferred from homology
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02647}.
|
SIGNAL 1..18; /evidence="ECO:0000255"
| null |
PF01442;
|
IPR000074;IPR050163;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Primates (order), Haplorrhini (suborder), Simiiformes (infraorder), Platyrrhini (parvorder), Cebidae (family), Cebinae (subfamily), Cebus (genus)
|
APOA1
| false |
401 |
A0A2K5TU92
|
MSVNYAAGLSPYADKGKCGLPEIFDPPEELERKVWELARLVWQSSHVVFHTGAGISTASGIPDFRGPHGVWTMEERGLAPKFDTTFESARPTQTHMALVQLERVGLLRFLVSQNVDGLHVRSGFPRDKLAELHGNMFVEECAKCKTQYVRDTVVGTMGLKATGRLCTVAKARGLRACRGELRDTILDWEDSLPDRDLALADEASRNADLSITLGTSLQIRPSGNLPLATKRRGGRLVIVNLQPTKHDRHADLRIHGYVDEVMTRLMKHLGLEIPAWDGPHVLERALPPLPRPPTPKLEPKEESPTRINGSIPAGSCLEPCAQHNGSEPASPKRERPTSPAPNRPPKRVKAEAVPS
|
NAD-dependent protein deacylase sirtuin-6 (EC 2.3.1.-) (NAD-dependent protein deacetylase sirtuin-6) (EC 2.3.1.286) (Protein mono-ADP-ribosyltransferase sirtuin-6) (EC 2.4.2.-)
|
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
| 9,541 | 355 | 39,078 |
Acetylation;Acyltransferase;Chromatin regulator;Chromosome;Developmental protein;DNA damage;DNA repair;DNA-binding;Endoplasmic reticulum;Glycosyltransferase;Isopeptide bond;Metal-binding;NAD;Nucleotidyltransferase;Nucleus;Phosphoprotein;Reference proteome;RNA-binding;Telomere;Transferase;Tumor suppressor;Ubl conjugation;Zinc
|
GO:0000122; GO:0000785; GO:0003684; GO:0003714; GO:0005634; GO:0005654; GO:0005721; GO:0005783; GO:0006302; GO:0006606; GO:0008340; GO:0009411; GO:0010526; GO:0010569; GO:0016779; GO:0019216; GO:0030182; GO:0031490; GO:0031491; GO:0031508; GO:0031509; GO:0031648; GO:0032024; GO:0032206; GO:0032436; GO:0032922; GO:0034244; GO:0034979; GO:0035033; GO:0035861; GO:0042181; GO:0042308; GO:0042752; GO:0042803; GO:0045600; GO:0045721; GO:0045820; GO:0046827; GO:0046872; GO:0046969; GO:0050994; GO:0051697; GO:0055007; GO:0070403; GO:0097372; GO:0099115; GO:0106222; GO:0106274; GO:0120162; GO:0120186; GO:0120187; GO:0140612; GO:0140765; GO:0140773; GO:0140774; GO:1902459; GO:1902732; GO:1903076; GO:1904841; GO:1905555; GO:1905564; GO:1990166; GO:2000738; GO:2000773; GO:2000781
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P59941}. Chromosome {ECO:0000250|UniProtKB:Q8N6T7}. Chromosome, telomere {ECO:0000250|UniProtKB:Q8N6T7}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P59941}. Note=Predominantly nuclear. Associated with pericentric heterochromatin and telomeric heterochromatin regions. Localizes to DNA damage sites: directly recognizes and binds double-strand breaks (DSBs) sites via a tunnel-like structure that has high affinity for DSBs (By similarity). A fraction localizes to the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P59941, ECO:0000250|UniProtKB:Q8N6T7}.
| null | null |
PF02146;
|
IPR029035;IPR050134;IPR003000;IPR026590;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Primates (order), Haplorrhini (suborder), Simiiformes (infraorder), Catarrhini (parvorder), Cercopithecoidea (superfamily), Cercopithecidae (family), Cercopithecinae (subfamily), Macaca (genus)
|
SIRT6
| false |
402 |
A0A2K6TRM6
|
MKAVVLTLAVLFLTGSQARHFWQQDEPPQSPWDRVKDLATVYVDSVKESGKDYVSQFETSALGKQLNLKLLDNWDSLTSTVNKLREQLGPVTQEFWDNLEKETEQLRQEMNKDLEEVKAKVQPYLDDFQKKWQEEMNLYSQKLEPLRTEFQEGAFQKLQDLREKLRPVAEQVRDRARAHVDTLRTQLAPYSDELRQRLATRLEALKESGATLAEYQAKASEHLSALGEKAKPAFEDLRQGLLPVLESFKVSFLSALDEYAKKLSSQ
|
Apolipoprotein A-I (Apo-AI) (ApoA-I) (Apolipoprotein A1) [Cleaved into: Proapolipoprotein A-I (ProapoA-I); Truncated apolipoprotein A-I]
|
Saimiri boliviensis boliviensis (Bolivian squirrel monkey)
| 39,432 | 266 | 30,705 |
Cholesterol metabolism;HDL;Lipid metabolism;Lipid transport;Lipoprotein;Oxidation;Palmitate;Phosphoprotein;Reference proteome;Repeat;Secreted;Signal;Steroid metabolism;Sterol metabolism;Transport
|
GO:0001540; GO:0001935; GO:0002719; GO:0005543; GO:0006656; GO:0006695; GO:0007186; GO:0007229; GO:0008035; GO:0008211; GO:0010804; GO:0010875; GO:0010903; GO:0015485; GO:0019899; GO:0019915; GO:0030139; GO:0030300; GO:0030325; GO:0031072; GO:0032489; GO:0032691; GO:0033344; GO:0033700; GO:0034115; GO:0034191; GO:0034205; GO:0034361; GO:0034362; GO:0034366; GO:0034375; GO:0034380; GO:0035025; GO:0042158; GO:0042627; GO:0042632; GO:0042803; GO:0043534; GO:0043691; GO:0045499; GO:0050728; GO:0050766; GO:0050821; GO:0051180; GO:0051496; GO:0055091; GO:0060228; GO:0060354; GO:0070328; GO:0070508; GO:0070653; GO:0071402; GO:0090205; GO:0120020; GO:1900026; GO:1902995; GO:1903561
|
Inferred from homology
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02647}.
|
SIGNAL 1..18; /evidence="ECO:0000255"
| null |
PF01442;
|
IPR000074;IPR050163;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Primates (order), Haplorrhini (suborder), Simiiformes (infraorder), Platyrrhini (parvorder), Cebidae (family), Saimiriinae (subfamily), Saimiri (genus), Saimiri boliviensis (species)
|
APOA1
| false |
403 |
A0A2K8FQU5
|
MASKMVEIVSKMFIKPSSPTPQSLRRYNLSSIDQTIDSEVTSLAFFYTYNPSHESSKIGDLLKNSLSKTLVSYYQFAGRLIENDYIDCNDEGVEFVEVRIHGRMNDILKRGKSFATDLVLPTRIIALHEDSLLIVQLSHFDCGGIAIGFGASHKVSDGVSNVMFMKDWASSTSLSTFHKPTPLLTADSIFPPEDNKLLSNKSIVSFQQCLGKRFVFSTEAIEKLKSKAIEYGIQKPSRVEVVTAFLCQCAANCDLPRKKPYAIISAVNLRPYLALPQNSIGNIFSFYFCINDEGMDNQFSALISKLRNGKQKLLENIISKEKLTYESQMQELTKCLDQLNISSLDTYFCSSWCRFPVYDIDFGWGKPILVSPFQPHVKDLILLMDSPEGDGIEALITMEEKKMAAFEKNEELRSFAYLDSPEPEALIIPEEDKSFE
|
Tabersonine-19-hydroxy-O-acetyltransferase (EC 2.3.1.-)
|
Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)
| 4,058 | 436 | 49,141 |
Acyltransferase;Alkaloid metabolism;Cytoplasm;Nucleus;Transferase
|
GO:0005634; GO:0005737; GO:0009753; GO:0016407; GO:0035835
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29438577}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:29438577}.
| null | null |
PF02458;
|
IPR023213;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Gentianales (order), Apocynaceae (family), Rauvolfioideae (subfamily), Vinceae (tribe), Catharanthinae (subtribe), Catharanthus (genus)
|
TAT
| false |
404 |
A0A2K9RFZ2
|
MSLRFNLIVTPFSNHRIRNRRETFPAQEFPVATSKSAVKVKCNLITSTDLVGKVREKINGKVDNSLEVPAIHPVDIPSNLCMIDTLERLGVDRYFQSEIDGVLEETYRLWQQKEKDIFADVTCRAMAFRLLRVKGYEVSSDELAPYADQAHVNLQISDVTAVIELYRASQERIYEEESTLEKLHAWTSTYLKQQLVSGTISDKKLHKQVEYYLKNYHGILDLVGIRRSLDLYDIDHYQILKAADRFRTICKDLLAFSRQDFNNCQAQYQRELQLLQRWYEDCRLDKLNYGRDVLRISYFVSSAIIGDPELSDARLAFAKYCVLTTCIDDFFDHAGSREESYRILELVKEWKEKPAEDYGSKEVEFLFTAVYNTVNELAEMAYVEQGRCVKSLLIKLWVELLTSFKKELDSWTDDTALSLDEYLSSSWVSITSRINILTSIQFLGLKLSEEMLSSQECTDLCRHGSLVVRLLNDMQTFEKERRENTKNSVSILLEAPKHEGAITEEEVISKIKEIVEQNRRKLMQMVYQRGTIFPRKCKDVFLKSCRGGYYLYSNGDEFTSPVQIMEDMKLCYEPLTFHPLEANNGGNKN
|
Class I diterpene synthase 2, chloroplastic (VacTPS2) ((13S)-vitexifolin A synthase) (EC 4.2.3.-) (9,13-epoxylabda-14-ene synthase) (EC 4.2.3.189) (Viteagnusin D synthase) (EC 4.2.3.-)
|
Vitex agnus-castus (Chaste tree)
| 54,477 | 589 | 68,332 |
Chloroplast;Lyase;Magnesium;Metal-binding;Plastid;Transit peptide
|
GO:0000287; GO:0009507; GO:0009686; GO:0010333; GO:0062203; GO:0062204; GO:0106239
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
| null | null |
PF01397;PF03936;
|
IPR008949;IPR001906;IPR036965;IPR050148;IPR005630;IPR008930;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Lamiales (order), Lamiaceae (family), Viticoideae (subfamily), Vitex (genus)
|
TPS2
| false |
405 |
A0A2L0VXR5
|
MRIPNVFLSYLRQVAVDGTLSSCSGVKSRKPVIAYGFDDSQDSLVDENDEKILEPFGYYRHLLKGKSARTVLMHCFNAFLGLPEDWVIGVTKAIEDLHNASLLIDDIEDESALRRGSPAAHMKYGIALTMNAGNLVYFTVLQDVYDLGMKTGGTQVANAMARIYTEEMIELHRGQGIEIWWRDQRSPPSVDQYIHMLEQKTGGLLRLGVRLLQCHPGVNNRADLSDIALRIGVYYQLRDDYINLMSTSYHDERGFAEDMTEGKYTFPMLHSLKRSPDSGLREILDLKPADIALKKKAIAIMQDTGSLVATRNLLGAVKNDLSGLVAEQRGDDYAMSAGLERFLEKLYIAE
|
Geranylgeranyl pyrophosphate synthase (GGPP synthase) (GGPPSase) (GGS) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10) (Pleuromutilin biosynthetic cluster protein synthesis protein G)
|
Clitopilus passeckerianus (Pleurotus passeckerianus)
| 648,682 | 350 | 39,229 |
Antibiotic biosynthesis;Isoprene biosynthesis;Magnesium;Metal-binding;Transferase
|
GO:0004161; GO:0004311; GO:0004337; GO:0016114; GO:0017000; GO:0046872
|
Evidence at transcript level
| 5 | null | null | null |
PF00348;
|
IPR008949;IPR000092;IPR033749;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Basidiomycota (phylum), Agaricomycotina (subphylum), Agaricomycetes (class), Agaricomycetidae (subclass), Agaricales (order), Tricholomatineae (suborder), Entolomataceae (family), Clitopilus (genus)
|
GGPS ggs
| false |
406 |
A0A2L2DDD0
|
MAFLKKSLFLVLFLGIVSLSVCEEEKREGEEKEEKREEEEGKEENEDGNEEHKEKRFLGAILKIGHALAKTVLPMVTNAFKPKQ
|
Figainin 2 (Br22)
|
Boana raniceps (Chaco tree frog) (Hyla roeschmanni)
| 192,750 | 84 | 9,632 |
Amphibian defense peptide;Antibiotic;Antimicrobial;Antiviral protein;Cleavage on pair of basic residues;Cytolysis;Direct protein sequencing;Hemolysis;Immunity;Innate immunity;Secreted;Signal
|
GO:0005576; GO:0042832; GO:0044179; GO:0045087; GO:0050688; GO:0050829; GO:0050830; GO:0051607
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32443921}.
|
SIGNAL 1..22; /evidence="ECO:0000255"
| null |
PF03032;
|
IPR004275;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amphibia (class), Batrachia (superorder), Anura (order), Neobatrachia (suborder), Hyloidea (superfamily), Hylidae (family), Hylinae (subfamily), Cophomantini (tribe), Boana (genus)
| null | false |
407 |
A0A2L2DDE6
|
MAFLKKSLFLVLFLGLVSLSIGEEEKREEEEKNEEGANQEENAENKEKRFIGTLIPLALGALTKLFKG
|
Figainin 1 (Br24)
|
Boana raniceps (Chaco tree frog) (Hyla roeschmanni)
| 192,750 | 68 | 7,640 |
Amidation;Amphibian defense peptide;Antibiotic;Antimicrobial;Cleavage on pair of basic residues;Cytolysis;Direct protein sequencing;Hemolysis;Immunity;Innate immunity;Secreted;Signal
|
GO:0005576; GO:0042832; GO:0044179; GO:0045087; GO:0050829; GO:0050830
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:32967114}.
|
SIGNAL 1..22; /evidence="ECO:0000255"
| null |
PF03032;
|
IPR004275;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amphibia (class), Batrachia (superorder), Anura (order), Neobatrachia (suborder), Hyloidea (superfamily), Hylidae (family), Hylinae (subfamily), Cophomantini (tribe), Boana (genus)
| null | false |
408 |
A0A2N6JFX7
|
MIRIDATPYPYQFHPRSTALVVIDMQRDFIEEGGFGSALGNDVRPLAAIVPTVAALLQLAREAGMLVVHTRESHLPDLSDCPRSKRLRGNPTLGIGDVGPMGRILVQGEPGNQILPQLAPVEGELVIDKPGKGAFYATDLHAQLQERRITHLLVAGVTTEVCVQTSMREANDRGYECLVIEDACASYFPDFHRITLEMLTAQGGIVGWRTPLAQLQAGVAAYTGENP
|
Triuret hydrolase TrtA (EC 3.5.1.-) (Cysteine hydrolase)
|
Herbaspirillum sp. (strain BH-1)
| 2,058,884 | 227 | 24,638 |
3D-structure;Hydrolase
|
GO:0016811; GO:0042802; GO:0042803; GO:0043605
|
Evidence at protein level
| 5 | null | null | null |
PF00857;
|
IPR000868;IPR050272;IPR036380;
|
6XIX;6XJ4;6XJE;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Betaproteobacteria (class), Burkholderiales (order), Oxalobacteraceae (family), Herbaspirillum (genus), unclassified Herbaspirillum (no rank)
|
trtA HBH1_00246
| false |
409 |
A0A2P1GIW2
|
MNSSTDPTSDETIWDLSPYIKIFKDGRVERLHNSPYVPPSLNDPETGVSWKDVPISSQVSARVYIPKISDHEKLPIFVYVHGAGFCLESAFRSFFHTFVKHFVAETKVIGVSIEYRLAPEHLLPAAYEDCWEALQWVASHVGLDNSGLKTAIDKDPWIINYGDFDRLYLAGDSPGANIVHNTLIRAGKEKLKGGVKILGAILYYPYFIIPTSTKLSDDFEYNYTCYWKLAYPNAPGGMNNPMINPIAENAPDLAGYGCSRLLVTLVSMISTTPDETKDINAVYIEALEKSGWKGELEVADFDADYFELFTLETEMGKNMFRRLASFIKHE
|
Catharanthine synthase (EC 5.5.1.37) (Hydrolase 1) (CrHL1)
|
Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)
| 4,058 | 330 | 37,132 |
3D-structure;Alkaloid metabolism;Cytoplasm;Isomerase;Nucleus
|
GO:0005634; GO:0005829; GO:0009821; GO:0016787; GO:0016853; GO:0035834
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:29724909}. Nucleus {ECO:0000269|PubMed:29724909}.
| null | null |
PF07859;
|
IPR013094;IPR029058;IPR050466;
|
6RT8;
|
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Gentianales (order), Apocynaceae (family), Rauvolfioideae (subfamily), Vinceae (tribe), Catharanthinae (subtribe), Catharanthus (genus)
|
CS HL1 Caros025416
| false |
410 |
A0A2P1GIW3
|
MGSSDETIFDLPPYIKVFKDGRVERLHSSPYVPPSLNDPETGGVSWKDVPISSVVSARIYLPKINNHDEKLPIIVYFHGAGFCLESAFKSFFHTYVKHFVAEAKAIAVSVEFRLAPENHLPAAYEDCWEALQWVASHVGLDISSLKTCIDKDPWIINYADFDRLYLWGDSTGANIVHNTLIRSGKEKLNGGKVKILGAILYYPYFLIRTSSKQSDYMENEYRSYWKLAYPDAPGGNDNPMINPTAENAPDLAGYGCSRLLISMVADEARDITLLYIDALEKSGWKGELDVADFDKQYFELFEMETEVAKNMLRRLASFIK
|
Tabersonine synthase (EC 5.5.1.38) (2-hydroxyisoflavanone dehydratase-like protein 3) (CrHID3) (HID-like protein 3) (Hydrolase 2) (CrHL2)
|
Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)
| 4,058 | 320 | 36,192 |
3D-structure;Alkaloid metabolism;Cytoplasm;Isomerase;Lyase;Nucleus
|
GO:0005634; GO:0005829; GO:0009821; GO:0016787; GO:0016829; GO:0016853; GO:0035834
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:29724909}. Nucleus {ECO:0000269|PubMed:29724909}.
| null | null |
PF07859;
|
IPR013094;IPR029058;IPR050466;
|
6RS4;
|
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Gentianales (order), Apocynaceae (family), Rauvolfioideae (subfamily), Vinceae (tribe), Catharanthinae (subtribe), Catharanthus (genus)
|
TS HID3 HL2
| false |
411 |
A0A2P2GK84
|
MNASPTPTATTTTEPATAVVRCRTRLARRVVAAVGPDGLLPAPCESRVLESALALALLTEERAEADATARLTAYLRTTLRTAPPDPFQCAVARAVLGGAGERGERVGDEGDMDAGTALDAGLDGFDHFTAGRKRLMFRTVLAALGATGFPAVPWEAYDTRPQQSWLHMEMKALKVLAAHGTGHPDVVRDEDWRALLPALEPGPAWECNNLAQLLALLALRHSPRHRPALGDVLKHVAGRLRPDGGMPFIDGMTVFTTAAAGLALSLLPAPPACVTPMADALALRRNPDGGYGFHSGVAQSDVDDTCYVLEFLRRAAPDRHRTAVAEAEGYLLALRNPDGGFPTFARGTSSEIAMTAAAASALAHDPDRREEVDEAVRYVVRHQRPDGTFERSWSRNATNAVFRAVLALTGVAAHGEERRSRARAAERALAHLAATQNGDGGWGHAEAEPSDPISTAYAVIALARGPRARPGGPLDRALAYLVERQHPDGGYRSRPDQAGPRPLLYDVPALADVFVLLALAHATATPDPEGCSR
|
Drimenyl diphosphate synthase (DMS) (EC 5.4.99.-)
|
Streptomyces showdoensis
| 68,268 | 533 | 56,702 |
3D-structure;Isomerase;Magnesium;Metal-binding;Reference proteome;Repeat
|
GO:0016853; GO:0046872
|
Evidence at protein level
| 5 | null | null | null |
PF13243;
|
IPR032696;IPR008930;
|
7XQ4;7XQZ;7XR7;7XRA;7XRU;
|
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Actinomycetota (phylum), Actinomycetes (class), Kitasatosporales (order), Streptomycetaceae (family), Streptomyces (genus)
|
VO63_21045
| false |
412 |
A0A2R2JFI5
|
METSTQTKAGSLTIVGTGIESIGQMTLQALSYIEAAAKVFYCVIDPATEAFILTKNKNCVDLYQYYDNGKSRLNTYTQMSELMVREVRKGLDVVGVFYGHPGVFVNPSHRALAIAKSEGYRARMLPGVSAEDCLFADLCIDPSNPGCLTYEASDFLIRDRPVSIHSHLVLFQVGCVGIADFNFTGFDNNKFGVLVDRLEQEYGAEHPVVHYIAAMMPHQDPVTDKYTVAQLREPEIAKRVGGVSTFYIPPKARKASNLDIIRRLELLPAGQVPDKKARIYPANQWEPDVPEVEPYRPSDQAAIAQLADHAPPEQYQPLATSKAMSDVMTKLALDPKALADYKADHRAFAQSVPDLTPQERAALELGDSWAIRCAMKNMPSSLLDAARESGEEASQNGFPWVIVVGVIGVIGSVMSTE
|
Methyltransferase/ribosomally synthesized cyclic peptide omphalotin A precursor ophMA (Omphalotin A biosynthesis cluster protein MA) [Cleaved into: N-methyltranferase ophM (EC 2.1.1.-); Ribosomally synthesized omphalotin core peptide; Follower peptide]
|
Omphalotus olearius (Jack o'lantern)
| 72,120 | 417 | 45,790 |
3D-structure;Methylation;Methyltransferase;S-adenosyl-L-methionine;Transferase;Virulence
|
GO:0008168; GO:0032259
|
Evidence at protein level
| 5 | null | null | null |
PF00590;
|
IPR000878;IPR035996;IPR014777;
|
5N0N;5N0O;5N0P;5N0Q;5N0R;5N0S;5N0T;5N0U;5N0V;5N0W;5N0X;5N4I;5OUF;6GEW;6QZY;6QZZ;6R00;6TSC;8QAQ;8QAS;8QBP;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Basidiomycota (phylum), Agaricomycotina (subphylum), Agaricomycetes (class), Agaricomycetidae (subclass), Agaricales (order), Marasmiineae (suborder), Omphalotaceae (family), Omphalotus (genus)
|
ophMA
| false |
413 |
A0A2R4QKX7
|
MGFSFVTNAAIAAHMPPSKQEIIRRDAKFHPTIWGDHFIQYLDTPIDPPQKVVERMEELKKQVRAMLRDTNLDISLIDWIQRTGIAYHFEEQIAETLKHVYEASTLTTDSSKYLEHFDLRHIALRFRLSRQQGYHASTDVFKRFMDEGDKFKQSIANDIEGMLSLYEASFMSVKGEAILDEALAFTGKNLEATLPNLTGSLAQQVECALEIPLRRCTDLVKARRSISCYENKNGRNEVVLELAKLDFNLLQAVHQRELALLTSWWNELGASTNLPFTRNRVVELYFWVLEVLSKPEHARAREIMVKSIIMASILDDVYDVYGTLEELQLFTSALERWDLQALEQLPNTIKTAYSIVLRVFKEYEDLLKPHEVYRVGFARKALIPYMNAYFLEAKWFYSHHHPSFEEYMDNALVSCGYPFLFLVSLVGLDEIATKDVFEWAIKRPNIVVAASMICRNRDDIVGHKEEQERGDVPSGVECYTKDHGCTEEEACMALQAMVDDAWKDINCELLHDTSMPKAILMRAVGLARIISILYQYRDGYSDSTHETKAHVTQVLVQPIPL
|
Terpene synthase 3 (PnTPS3) (Copaene synthase) (PnCop) (EC 4.2.3.133) (Germacrene D synthase) (PnGDS) (EC 4.2.3.-)
|
Piper nigrum (Black pepper)
| 13,216 | 561 | 64,520 |
Lyase;Magnesium;Metal-binding
|
GO:0000287; GO:0010333; GO:0010597; GO:0016102; GO:0051762; GO:0052577; GO:0102877; GO:1901931
|
Evidence at protein level
| 5 | null | null | null |
PF01397;PF03936;
|
IPR008949;IPR034741;IPR044814;IPR001906;IPR036965;IPR050148;IPR005630;IPR008930;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), Magnoliidae (clade), Piperales (order), Piperaceae (family), Piper (genus)
|
TPS3
| false |
414 |
A0A2R6W0K6
|
MAFSAAASASTNLVPAVASGRGGAAASASQHGETARLARFGVSSSACANALSLSSSRSCASMGEVLWANGGAVRLAARRTLRVRAAGAGTIVQPEGFQITSVPTTPIDGQKTGTSGLRKKVKEFQSPNYLANWIQALFDSLPAEDVKGSTLVLGGDGRYFNKEASQIIIKIAAGNGVGKILVGREGIASTPAVSAIIRARKANGGFVMSASHNPGGPKYDWGIKFNYSSGQPAPESITDKIYGNTLSIKEIKQADIPDVNLSELGVHKFGDFSVEVIDPVADYLNLLEEVFDFDLLKGLLTSKDFRFKFDAMHAVTGAYAKPIFVDRLGAPEDSIFNGVPLEDFGGGHPDPNLTYAEELVKIMYGTDAPDFGAASDGDGDRNMILGNHFFITPSDSVAMIAANADAIPYFKTGLKGLARSMPTSGALDRVAKELGLPFFETPTGWKFFGNLMDAGKCSVCGEESFGTGSDHVREKDGIWAVLAWISIVAYKNRDRKVGEKLVTVADIAKEHWAKYGRNFFSRYDYEECESAGANKMVEHLRDIIAKSKKGDKYGNYELELADDFAYTDPIDGSVATKQGIRFIFSDGSRIIFRLSGTGSAGATIRIYVEQYEQDTTKHDLDAQDALKPLIDIALSVSKLQEFTGRTKPTVIT
|
Phosphoglucomutase 1, chloroplastic (MpPGM1) (EC 5.4.2.2) (Glucose phosphomutase)
|
Marchantia polymorpha (Common liverwort) (Marchantia aquatica)
| 3,197 | 652 | 69,918 |
Carbohydrate metabolism;Chloroplast;Glucose metabolism;Isomerase;Magnesium;Metal-binding;Phosphoprotein;Plastid;Reference proteome;Transit peptide
|
GO:0000287; GO:0004614; GO:0005829; GO:0005975; GO:0005986; GO:0006006; GO:0009409; GO:0009570; GO:0009590; GO:0010319; GO:0019252
|
Inferred from homology
| 5 |
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
| null | null |
PF24947;PF02878;PF02879;PF02880;
|
IPR005844;IPR016055;IPR005845;IPR005846;IPR036900;IPR016066;IPR005841;IPR045244;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Marchantiophyta (clade), Marchantiopsida (class), Marchantiidae (subclass), Marchantiales (order), Marchantiaceae (family), Marchantia (genus)
|
PGM1 Mapoly0202s0014 MARPO_0202s0014
| false |
415 |
A0A2R6XIK6
|
MVVREAMIVPQTVQGGGKGVNGCSLVSNYQNSRDLCLQSAAMEQKSKGVIENCNLGPHDVGVGWKRNSSEGSISSMDSLPCGETVFSPSDPHNSVFRKPRRLGVSESDDESVIDQSQEESLLRKSKRSVMGGTVQPHSAMAQSVDEAAPDHSSTPSDDGKDFPSSRVKFMCSFGGKILPRPSDQQLRYVGGQTRIIGINRDVNFSELRNKMRESFGQCYTFKYQLPDEDLDALVTVSSDEDLENMMEEYDKLEADGSSRLRVFLFPADQDATSFDIDSTGDLRNSEQRYVDAVNGIAESSTRRISDGVLGASPVSSDLLGLELSEPSWGLARGPDAVPMAMLATHHDPNLIHQVPVAHPVSALTGNLSNRSNAPSAPSSAPSSPPLLARNLHGKLPLVGELHQFQYLQDSQFKGVGPQYTGMPSEVAHQDSESYGGSGGSSAASQHEMHYRSTDSRRGPESPPKKFHDALHQDHPITVEQRRLSGTKMPRIGSHGKLTRLSEHSELAPSSRVDSQQMPDIHMAPGELQRLFPQQVPLQQTLWPHAMDTQQDSYRRPDMLQSSGAQPAVSGQQQQGYQPQQQLQHLFRSGLSQTGANHEGAYRQGDQQQQSQQFQEDLHVNPNYIPRSVSSHAIAAGIAAGQSTSYHGSAPSSPRPGFRELPSRHLPGGPQLQHQWTFNGAGYVDQGFGRRVMNYPDQATRSFRLSSSPPRYRDHHPHSEERLHRQAQQVSEPLHHEQVPVSGQLKFETNSVSQAQYDLVPRPQVPQYKGHNPFQEKITSFQDHQEVGDIRRHVLQQGKDNQLLAGQQHLHSILQPQRIDYQESLKQQGDQSIPIHPRFQDGQEKVAEWMVQERALEEEEARKRVLGRIRQAELEEEAAAEAVVSQHKDTHQGVYAGLHLPNDEDLLTSSLGDYPSGNRRNERLESSISNAFPFRHLPPSVLGGYTAPKSRVNPTETSHVAQYVSRPVDTDYLAVAGLRGGGNGQDMRSAALFEVNGLQQTSGYQMPSGPHRLMEERLMPSAFNPITQLQKLRINDNLALNNDMRWSGSEDVRNEPSIPARDRMGGIYEDHHQGLPGLTLGRSAGKLSRPSSNTSIPNLLDETIGEGSLLPSGPSYGTQAQGTNLIDITQSISAIDNPLYSTSYASRLSNTSLGLDSPLVTSGGMLNSSLEGTSFSDYYKIKMGDDLPNAKMPSSKIPSAEDNLSRSSSSSLSELSKSGSEDGLGGQLTMDQRTVDMVVAALDLDRSGSVVQSVLESSDAKEASLSESVHDHSLGKLGSVVGSVGTQSVWPLDSAPTLAAGLWEKKLDEAGMTEETFERHITSDGTTFEELTADDHEVLASTVDKENQEEVRTGLDEPADEDKANSTGLGSDPAAKAIARGLQTIKNADLEELRELGSGTFGTVYHGKWRGTDVAIKRIKASCFAGRPSEQERLIEDFWREACNLGHLHHPNVVAFYGVVADGPGGTLATVTEYMVNGSLKQVLQKKDRTIDRRKRLLIAMDAAFGMEYLHGKNIVHFDLKCENLLVNMRDPHRPICKVGDLGLSKVKHQTMVSGGVRGTLPWMAPELLNGNSSLVTEKVDVFSFGIVMWELLTGEEPYDKMHYGAIIGGIVNNTLRPLIPSWCDPAWRSLMERCWANEPAVRPSFSDIAKELRTMAAALQPKTQAQTQGQSHPHPQMQIV
|
RAF-like serine/threonine-protein kinase PRAF (EC 2.7.11.1) (Protein PHOTOSYNTHESIS-RELATED RAF) (MpPRAF)
|
Marchantia polymorpha (Common liverwort) (Marchantia aquatica)
| 3,197 | 1,680 | 184,303 |
ATP-binding;Auxin signaling pathway;Cytoplasm;Kinase;Nucleotide-binding;Phosphoprotein;Reference proteome;Serine/threonine-protein kinase;Transferase
|
GO:0004672; GO:0004674; GO:0005524; GO:0005737; GO:0005985; GO:0007165; GO:0009637; GO:0009646; GO:0009733; GO:0009734; GO:0010109; GO:0010114; GO:0010928; GO:0071365
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:38128538}. Note=Broadly distributed to both membrane-associated and intracellular punctate structures. {ECO:0000269|PubMed:38128538}.
| null | null |
PF00564;PF07714;
|
IPR011009;IPR053793;IPR000270;IPR000719;IPR017441;IPR001245;IPR008271;IPR050167;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Marchantiophyta (clade), Marchantiopsida (class), Marchantiidae (subclass), Marchantiales (order), Marchantiaceae (family), Marchantia (genus)
|
PRAF Mapoly0013s0150 MARPO_0013s0150
| false |
416 |
A0A2R8Q1W5
|
MTECKAEVTPSASNGHRVFSYTLESHTAAAFAIMNELRRERQLCDVTLRVRYCPLDTHVDFVAHKVVLASSSPVFRAMFTNGLKECGMEVVPIEGIHPKVMGRLIEFAYTASISVGEKCVIHVMNGAVMYQIDSVVQACCDFLVEQLDPSNAIGIASFAEQIGCTELHQKAREYIYMNFSQVATQEEFFTLSHCQLVTLISRDELNVRCESEVFHACVAWVQYDREERRPYVQALLQAVRCHSLTPHFLQRQLEHFEWDAQSKDYLSQIFRDLTLHKPTKVIPLRTPKVPQLIYTVGGYFRQSLSFLEAFNPCSGAWLRLADLQVPRSGLAACVISGLLYAVGGRNNGPDGNMDSHTLDCYNPMNNCWRPCAHMSVPRNRIGVGVIDGMIYAVGGSHGCTHHNSVERYDPERDSWQLVSPMLTRRIGVGVAVINRLLYAVGGFDGTHRLSSAECYNPERDEWRSIAAMNTVRSGAGVCALGNYIYVMGGYDGTNQLNTVERYDVEKDSWSFSASMRHRRSALGVTTHHGRIYVLGGYDGNTFLDSVECFDPETDSWTEVTHMKSGRSGVGVAVTMEPCHKELIPCQC
|
Kelch-like ECH-associated protein 1B
|
Danio rerio (Zebrafish) (Brachydanio rerio)
| 7,955 | 587 | 65,690 |
Alternative splicing;Cytoplasm;Kelch repeat;Nucleus;Reference proteome;Repeat;Ubl conjugation pathway
|
GO:0005634; GO:0005737; GO:0006511; GO:0010506; GO:0016234; GO:0016567; GO:0030536; GO:0031463; GO:0034599; GO:0043161; GO:0071379; GO:0071466; GO:1990756
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Z2X8}. Nucleus {ECO:0000250|UniProtKB:Q9Z2X8}. Note=Mainly cytoplasmic. {ECO:0000250|UniProtKB:Q9Z2X8}.
| null | null |
PF07707;PF00651;PF01344;PF24681;
|
IPR011705;IPR017096;IPR000210;IPR047098;IPR030563;IPR015915;IPR006652;IPR011333;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Actinopterygii (superclass), Actinopteri (class), Neopterygii (subclass), Teleostei (infraclass), Osteoglossocephalai (clade), Clupeocephala (no rank), Otomorpha (cohort), Ostariophysi (subcohort), Otophysi (clade), Cypriniphysae (superorder), Cypriniformes (order), Cyprinoidei (suborder), Danionidae (family), Danioninae (subfamily), Danio (genus)
|
keap1b
| false |
417 |
A0A2R8QCI3
|
MDITVSELMSNFMDSPLVVWVKTFGPLGFSSEDKLSMFMDLVDGVFLHKIMTHIDPSPMNQRVNKQVNNDVNLRIQNLNTVIRHIKNYYQEHLQQLIVMNLPNVLAIAKDPLSGKSMEEMKRMLLLILGCAVQCDRKEEIIEKIKLLDIETQAAIVTHIQEVTHNQENVLDLQWMEVAEIPAEQLDPLSRTMAFHLRKLIDERDESAELVIELTQERDYLQSQQPSGLLGFPSPERTSLSPITLLSKEDRQHLAVELADTKAKLRRSRQELEEKTEQLIDAKNEIERLDSDIQKLKQENTQLLAEARSVRAYRDEVDSLRERAGKVDRLETELSRFKEKLNDVHFYKTRIEELREDNLTLLETKSMLEEQLTGARGRCDKLHELEKENLQLRSKLHDIEIDRDSDKKRLEELLEENMLLEISQKQSMNESAHLGWELEQLAKNNEVNEARKSFVFELNESASSRLLKLEKENQCLQSTIQELREASINMEEGQLHSLELEKENQSLSKKLERLQSQLDQEKQTTQDMENLGEELIKEKQRMEKTLETIQAEKDRQISELEQEKEHLTQAVSSLRKRAQANSEARVREVETENRILHQTISETGGKLARLEAEKRQVTKELESLRERGERCEELEREVPRLERVREQLQREAAALKIGSERAEALERENATLEQDNRRLKKLADTAQNATLRLAVLEKDHQQLEEENLEQRRALETLRPAAARLAQLQQEHAELEREHEEMCRTMEELRSQAKRSERLEKSCGSLSLENQRLQQTLENSSTKMQGLESELRQNEAEMKDLQRELEGLRQKVTWAETLEKENRGMEQELSQLEKEKKQLEKEARRFRQQLEVKEAALEENCLRLASMEKEGTALSKELGRVKEAAGRLKELERENKDLQKQATMDKKTLATLREELVNEKLRVQQQCNELEKLSHELEKIGLNREKLLQEEHSCEDNKYKILETKIESALKKTLELREEKIQSLESRLEESSSLNQQLRTELTTVKKNLEALKQRHEEEAAHSEISQQTLGQTRSLPDKEKWEMEQREATAELLKLKDRLIDVEKNVRQRHVSIDIHRVIFSIVICFCDSLQNAALQTEKYLLKDQLKQIDSQNAQLNAQTLALQKQAASLQEHNTSLHKETAKLQVENSTLSSQSSSLMAQYGALQAQLQTLESEAESLQKQREEASAARDRVTQDHERLLGVHERQASEYEQLIAQHAALKASQRALEQENRTLENKYMVLLKQKDAMEALEESLQRDRESLGEEIRKNTLILGENRSLREEVDRVSHMHTQLRQEYDSLQLQTKELKTSLNESQLELNRWQARYDQLKEQHQGLDISMTKLDNHCELLTRLKGNLEEENHHLLSQIQMLSQQNQTLLERTMESKELYHEEQKQYIDKLNSLRRQKEKLEEKIMDQYKFYDPTPKKSRQWVGAKAIAKFIKPKKESSRERPDAPRERIRSAPDIPLPEIPTCIDCPESAPPPPPPPLPPRQSRPSLDSMNSQSVEENHVQSPTLSSPALNGRVLNESGGSRSRDGYRSIGGGSESMNGYEELLRWRSREPGGATCSTPLSRNSHNAPGFTSSSSLRPGRRPKGLVSEEDLRHHSPDAGFGSGVHGNTGHRPSSAEFSRNTSSSNSPVSSKGSLDCLQGRSASLSSDDVVGLAHEGSRLSQSSLLPRSSTLPCDSPSASRPSQRPASRRPSSPGSEMVTLEEFLQESNALSPPTVQTGSREDLMTDYFTRSTRPVPLRDGAKTPTNYVTPTVKTTPPELDARTPKPGHSVKPSVRLTDTSTPPSHSQTLPNRGAGLRPSALQQSSPRGSVGGSASLSRTFSLASADLLRSNGPDSYRTEAASPNQNDVVMRRPGAVARERPMSARVTGSSPLPGDPGHISVDPRRLSLAQPRDEFSLVSPPPLHSSSMSLQAEREYVGSGSSRAGAARSGSAQPRGAPHRGEVAMVTPVRAVPALRLNDLEEEPQEQREAESPLLKKADTTNLSYASKEQPTSKPASPDPNNDPQTVWYEYGCV
|
Protein Daple (Coiled-coil domain-containing protein 88C)
|
Danio rerio (Zebrafish) (Brachydanio rerio)
| 7,955 | 2,023 | 230,337 |
Alternative splicing;Cell junction;Coiled coil;Cytoplasm;Guanine-nucleotide releasing factor;Reference proteome;Wnt signaling pathway
|
GO:0001841; GO:0001965; GO:0003383; GO:0005085; GO:0005737; GO:0005813; GO:0007264; GO:0008017; GO:0016055; GO:0030054; GO:0030705; GO:0031122; GO:0051959; GO:0070161
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9P219}. Cell junction {ECO:0000250|UniProtKB:Q9P219}. Note=Enriched at apical cell junctions. {ECO:0000250|UniProtKB:Q9P219}.
| null | null |
PF19047;
|
IPR001715;IPR036872;IPR043936;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Actinopterygii (superclass), Actinopteri (class), Neopterygii (subclass), Teleostei (infraclass), Osteoglossocephalai (clade), Clupeocephala (no rank), Otomorpha (cohort), Ostariophysi (subcohort), Otophysi (clade), Cypriniphysae (superorder), Cypriniformes (order), Cyprinoidei (suborder), Danionidae (family), Danioninae (subfamily), Danio (genus)
|
ccdc88c
| false |
418 |
A0A2R8QF68
|
MQRIAGITKMVTHRRWLGLLLLLLCVGYSHGMPHVLRFGGIFESIESGPSGAEELAFKFALNTINRNRTLLPNTTLTYDIQRINIHDSFEASRKACDQLSLGVAAIFGPSHSSSANAVQSICNALGVPHIQTKWKHQVSDNRDSFYVNLYPDFSSLSRAILDLVHFFKWKTVTVVYDDSTGLIRLQELIKAPSRYNIRLKIRQLPADTKDAKPLLKEMKRGKEFHVIFDCGHEMAAGILKQALAMGMMTEYYHYIFTTLDLFALDVEPYRYSGVNMTGFRILNTENSQVSSIIEKWSMERLQAPPKPDSGLLDGFMTTDAALMYDAVHVVAVAVQQSPQITVSSLQCNRHKPWRFGNRFMTLIKEAHWDGLTGRINFNRTNGLRTDFDLDVISLKEEGLEKIGTWDPASGLNMTENQKGKTANVTDSLSNRSLVVSTILEEPYVMFKKSDKPLYGNDRFEGYCVDLLRELAAILGFGYELRLVEDGRYGAQDESSGQWNGMVRELMDHKADLAVAPLAITYVREKVIDFSKPFMTLGISILYRKPNGTNPGVFSFLNPLSPDIWMYILLAYLGVSCVLFVIARFSPYEWYNPHPCNPDSDVVENNFTLLNSFWFGVGALMQQGSELMPKALSTRIVGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGVVEDGSTMTFFKKTKISTYDKMWEFMSSRRHSVMVKSIEEGIERVLTSDYAFLMESTTIEFVTQRNCNLTQIGGLIDSKAYGVGTPMGSPYRDKITIAILQLQEEGKLHMMKEKWWRGNGCPEEENKEASALGVQNIGGIFIVLAAGLVLSVFVAVGEFLYKSKQNAQLEKRSFCSAMVDELRVSLKCQRRLKHKPQPPVMVKTDEVINMHTFNDRRLPGKETMA
|
Glutamate receptor ionotropic, kainate 2 (GluK2)
|
Danio rerio (Zebrafish) (Brachydanio rerio)
| 7,955 | 908 | 102,520 |
Cell membrane;Disulfide bond;Glycoprotein;Ion channel;Ion transport;Ligand-gated ion channel;Membrane;Postsynaptic cell membrane;Receptor;Reference proteome;Signal;Synapse;Transmembrane;Transmembrane helix;Transport
|
GO:0005886; GO:0015277; GO:0022849; GO:0032983; GO:0035249; GO:0042734; GO:0050804; GO:0098839; GO:1904315
|
Inferred from homology
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P42260}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P42260}; Multi-pass membrane protein {ECO:0000255}.
|
SIGNAL 1..31; /evidence="ECO:0000255"
|
TRANSMEM 562..582; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 639..659; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 820..840; /note="Helical"; /evidence="ECO:0000255"
|
PF01094;PF00060;PF10613;
|
IPR001828;IPR019594;IPR001508;IPR015683;IPR001320;IPR028082;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Actinopterygii (superclass), Actinopteri (class), Neopterygii (subclass), Teleostei (infraclass), Osteoglossocephalai (clade), Clupeocephala (no rank), Otomorpha (cohort), Ostariophysi (subcohort), Otophysi (clade), Cypriniphysae (superorder), Cypriniformes (order), Cyprinoidei (suborder), Danionidae (family), Danioninae (subfamily), Danio (genus)
|
grik2
| false |
419 |
A0A2R8VHR8
|
MLKMSGWQRQSQNNSRNLRRECSRRKCIFIHHHT
|
DDIT3 upstream open reading frame protein (Alternative DDIT3 proteins) (AltDDIT3)
|
Mus musculus (Mouse)
| 10,090 | 34 | 4,240 |
Alternative initiation;Cytoplasm;Nucleus;Reference proteome
|
GO:0002086; GO:0003677; GO:0003700; GO:0005634; GO:0005770; GO:0006355; GO:0006357; GO:0006983; GO:0007605; GO:0009611; GO:0010467; GO:0030968; GO:0036119; GO:0045454; GO:0045599; GO:0060840; GO:0061771; GO:0070059; GO:0070509; GO:1904738; GO:1990874
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H6Z9}. Cytoplasm {ECO:0000250|UniProtKB:Q9H6Z9}. Note=Colocalizes with WDR83 in the cytoplasm. {ECO:0000250|UniProtKB:Q62630}.
| null | null | null | null | null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Glires (clade), Rodentia (order), Myomorpha (suborder), Muroidea (clade), Muridae (family), Murinae (subfamily), Mus (genus), Mus (subgenus)
|
Ddit3
| false |
420 |
A0A2R9YJI3
|
MESMPSSLTHQRFGLLNKHLTRTGNTREGRMHTPPVLGFQAIMSNVTVLDNIEPLDFEMDLKTPYPVSFQVSLTGFLMLEIVLGLSSNLTVLALYCMKSNLVSSVSNIVTMNLHVLDVLVCVGCIPLTIVVVLLPLEGNNALICCFHEACVSFASVATAANVLAITLDRYDISVRPANRVLTMGRAVALLGSIWALSFFSFLVPFIEEGFFSQAGNERNQTEAEEPSNEYYTELGLYYHLLAQIPIFFFTAVVMLVTYYKILQALNIRIGTRFHSVPKKKPRKKKTISMTSTQPESTDASQSSAGRNAPLGMRTSVSVIIALRRAVKRHRERRERQKRVFRMSLLIISTFLLCWTPITVLNTVILSVGPSNFTVRLRLGFLVMAYGTTIFHPLLYAFTRQKFQKVLKSKMKKRVVSVVEADPMPNNVVIHNSWIDPKRNKKVTFEETEVRQKCLSSEDVE
|
G-protein coupled receptor 22
|
Danio rerio (Zebrafish) (Brachydanio rerio)
| 7,955 | 460 | 51,763 |
Cell membrane;Cilium biogenesis/degradation;G-protein coupled receptor;Membrane;Receptor;Reference proteome;Transducer;Transmembrane;Transmembrane helix
|
GO:0001947; GO:0003140; GO:0004930; GO:0005886; GO:0007186; GO:0007368; GO:0030030; GO:0032870; GO:0061371; GO:0070121; GO:0071907; GO:0071910
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:D4A3U0}; Multi-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 75..95; /note="Helical; Name=1"; /evidence="ECO:0000255"; TRANSMEM 115..135; /note="Helical; Name=2"; /evidence="ECO:0000255"; TRANSMEM 145..165; /note="Helical; Name=3"; /evidence="ECO:0000255"; TRANSMEM 186..206; /note="Helical; Name=4"; /evidence="ECO:0000255"; TRANSMEM 236..256; /note="Helical; Name=5"; /evidence="ECO:0000255"; TRANSMEM 344..364; /note="Helical; Name=6"; /evidence="ECO:0000255"; TRANSMEM 378..398; /note="Helical; Name=7"; /evidence="ECO:0000255"
|
PF00001;
|
IPR000276;IPR017452;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Actinopterygii (superclass), Actinopteri (class), Neopterygii (subclass), Teleostei (infraclass), Osteoglossocephalai (clade), Clupeocephala (no rank), Otomorpha (cohort), Ostariophysi (subcohort), Otophysi (clade), Cypriniphysae (superorder), Cypriniformes (order), Cyprinoidei (suborder), Danionidae (family), Danioninae (subfamily), Danio (genus)
|
gpr22a
| false |
421 |
A0A2S1XB67
|
MIKKVPIVLSIFCFLLLLSSSHGSIPEAFLNCISNKFSLDVSILNILHVPSNSSYDSVLKSTIQNPRFLKSPKPLAIITPVLHSHVQSAVICTKQAGLQIRIRSGGADYEGLSYRSEVPFILLDLQNLRSISVDIEDNSAWVESGATIGEFYHEIAQNSPVHAFPAGVSSSVGIGGHLSSGGFGTLLRKYGLAADNIIDAKIVDARGRILDRESMGEDLFWAIRGGGGASFGVIVSWKVKLVKVPPMVTVFILSKTYEEGGLDLLHKWQYIEHKLPEDLFLAVSIMDDSSSGNKTLMAGFMSLFLGKTEDLLKVMAENFPQLGLKKEDCLEMNWIDAAMYFSGHPIGESRSVLKNRESHLPKTCVSIKSDFIQEPQSMDALEKLWKFCREEENSPIILMLPLGGMMSKISESEIPFPYRKDVIYSMIYEIVWNCEDDESSEEYIDGLGRLEELMTPYVKQPRGSWFSTRNLYTGKNKGPGTTYSKAKEWGFRYFNNNFKKLALIKGQVDPENFFYYEQSIPPLHLQVEL
|
O-acetylstemmadenine oxidase (CrASO) (EC 1.21.3.11) (Precondylocarpine acetate synthase)
|
Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)
| 4,058 | 529 | 59,214 |
Alkaloid metabolism;Disulfide bond;Endoplasmic reticulum;FAD;Flavoprotein;Glycoprotein;Oxidoreductase;Signal;Vacuole
|
GO:0005773; GO:0005783; GO:0009820; GO:0016491; GO:0031982; GO:0071949
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:29724909}. Vacuole {ECO:0000269|PubMed:29724909}. Vesicle {ECO:0000269|PubMed:29724909}. Note=First targeted to endoplasmic reticulum (ER) and progressively secreted to vacuole by ER-derived vesicles. {ECO:0000269|PubMed:29724909}.
|
SIGNAL 1..23; /evidence="ECO:0000255"
| null |
PF08031;PF01565;
|
IPR012951;IPR016166;IPR036318;IPR016167;IPR016169;IPR006094;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Gentianales (order), Apocynaceae (family), Rauvolfioideae (subfamily), Vinceae (tribe), Catharanthinae (subtribe), Catharanthus (genus)
|
ASO PAS
| false |
422 |
A0A2S4N3N0
|
MKKTAIAIAVALAGFATVAQAAPKDNTWYTGAKLGWSQYHDTGFIPNNGPTHENQLGAGAFGGYQVNPYVGFEMGYDWLGRMPYKGDNINGAYKAQGVQLTAKLGYPITDDLDIYTRLGGMVWRADTKANVPGGASFKDHDTGVSPVFAGGVEYAITPEIATRLEYQWTNNIGDANTIGTRPDNGLLSLGVSYRFGQGEAAPVVAPAPAPEVQTKHFTLKSDVLFNFNKATLKPEGQAALDQLYSQLSNLDPKDGSVVVLGYTDRIGSDAYNQGLSERRAQSVVDYLISKGIPADKISARGMGESNPVTGNTCDNVKQRAALIDCLAPDRRVEIEVKGIKDVVTQPQA
|
Outer membrane protein A (Outer membrane porin A)
|
Shigella flexneri
| 623 | 348 | 37,283 |
3D-structure;Cell outer membrane;Conjugation;Direct protein sequencing;Disulfide bond;Host-virus interaction;Ion transport;Membrane;Porin;Reference proteome;Repeat;Signal;Transmembrane;Transmembrane beta strand;Transport
|
GO:0009279; GO:0015288; GO:0034220; GO:0046930
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Extracellular vesicle. Note=(Microbial infection) Upon infection with phage Sf6 is found in extracellular vesicles that associate with the tails of mature phage particles. {ECO:0000269|PubMed:22386055}.; SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250|UniProtKB:P0A910, ECO:0000255|HAMAP-Rule:MF_00842}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00842, ECO:0000305|PubMed:21071053}.
|
SIGNAL 1..21; /evidence="ECO:0000255|HAMAP-Rule:MF_00842, ECO:0000269|PubMed:21071053"
|
TRANSMEM 27..37; /note="Beta stranded"; /evidence="ECO:0000255|HAMAP-Rule:MF_00842"; TRANSMEM 55..66; /note="Beta stranded"; /evidence="ECO:0000255|HAMAP-Rule:MF_00842"; TRANSMEM 70..78; /note="Beta stranded"; /evidence="ECO:0000255|HAMAP-Rule:MF_00842"; TRANSMEM 96..107; /note="Beta stranded"; /evidence="ECO:0000255|HAMAP-Rule:MF_00842"; TRANSMEM 112..120; /note="Beta stranded"; /evidence="ECO:0000250|UniProtKB:P0A910, ECO:0000255|HAMAP-Rule:MF_00842"; TRANSMEM 146..155; /note="Beta stranded"; /evidence="ECO:0000255|HAMAP-Rule:MF_00842"; TRANSMEM 160..167; /note="Beta stranded"; /evidence="ECO:0000255|HAMAP-Rule:MF_00842"; TRANSMEM 186..194; /note="Beta stranded"; /evidence="ECO:0000255|HAMAP-Rule:MF_00842"
|
PF00691;PF01389;
|
IPR050330;IPR011250;IPR006664;IPR002368;IPR006665;IPR006690;IPR036737;IPR000498;
|
3NB3;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Shigella (genus)
|
ompA SF0957
| false |
423 |
A0A2T4VDM4
|
MGLCSDPAITYLKRLGYNVVRLPREGIQPLHLLGQQRGTVEYLGSLEKLITQPPSEPPAITRDQAAAGINGQKTENLSFSIGINILKSVLAQFGAGAGIEAQYNQARKVRFEFSNVLADSVEPLAVGQFLKMAEVDADNPVLKQYVLGNGRLYVITQVIKSNEFTVAAEKSGGGSIQLDVPEIQKVVGGKLKVEASVSSQSTVTYKGEKQLVFGFKCFEIGVKNGEITLFASQPGAIAMALDAAGGVMPSDSALLDEGGLLDLEGF
|
Gasdermin bGSDM (bGSDM) (Bacterial gasdermin) [Cleaved into: Gasdermin bGSDM, N-terminus]
|
Vitiosangium sp. (strain GDMCC 1.1324)
| 2,138,576 | 266 | 28,275 |
3D-structure;Antiviral defense;Cell inner membrane;Cell membrane;Cytoplasm;Lipoprotein;Membrane;Palmitate;Reference proteome;Transmembrane;Transmembrane beta strand
|
GO:0005737; GO:0005886; GO:0051607
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: [Gasdermin bGSDM]: Cytoplasm {ECO:0000305|PubMed:35025633}.; SUBCELLULAR LOCATION: [Gasdermin bGSDM, N-terminus]: Cell inner membrane {ECO:0000305|PubMed:38509367}; Multi-pass membrane protein {ECO:0000305|PubMed:38509367}.
| null |
TRANSMEM 69..85; /note="Beta stranded"; /evidence="ECO:0000305|PubMed:38509367, ECO:0007744|PDB:8SL0"; TRANSMEM 97..114; /note="Beta stranded"; /evidence="ECO:0000305|PubMed:38509367, ECO:0007744|PDB:8SL0"; TRANSMEM 163..180; /note="Beta stranded"; /evidence="ECO:0000305|PubMed:38509367, ECO:0007744|PDB:8SL0"; TRANSMEM 189..205; /note="Beta stranded"; /evidence="ECO:0000305|PubMed:38509367, ECO:0007744|PDB:8SL0"
| null | null |
7N51;8SL0;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Myxococcota (phylum), Myxococcia (class), Myxococcales (order), Cystobacterineae (suborder), Archangiaceae (family), Vitiosangium (genus), unclassified Vitiosangium (no rank)
|
DAT35_31115 Ga0334635_1658
| false |
424 |
A0A2T5Y4G4
|
MKKRIFIGSSSEQLTILNEIVDLLGDDVECIPWTDAFALNKSGLDSLIKQTRLADYSILIATKDDLTKQRGESLTKPRDNVVFEFGLFLGAAGPEKCYLIAEEDTDLPTDLDGITVAKFTRNSGQYNSLDKIVESIRTHLVKIAEMSQLGLLPSTALAIGYYNSFIKRVCEEIHGSECVELEGKKIKVKSFRVDVVIPETLDDNGVGNFTTLYNKRYGLSKATTCTNPALLGTRGFPFHFKVDPPDANQESPVDIHLLDIPSTLSTIVESLKLYLPSNQVGQDFDMDYLEMRELENFAKVLKYLIGRNAATKGYVNVLTNVKL
|
CD-NTase-associated protein 12 (Cap12) (NAD(+) hydrolase) (EC 3.2.2.5) (TIR-STING) (SfSTING)
|
Sphingobacterium faecium (strain DSM 11690 / JCM 21820 / NBRC 15299 / NCIMB 13408 / KS 0470)
| 1,220,575 | 323 | 35,943 |
3D-structure;Antiviral defense;Hydrolase;Nucleotide-binding
|
GO:0000166; GO:0003953; GO:0050135; GO:0051607
|
Evidence at protein level
| 5 | null | null | null |
PF10137;PF20300;
|
IPR019302;IPR046876;
|
7UN8;7UN9;7UNA;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), FCB group (clade), Bacteroidota/Chlorobiota group (clade), Bacteroidota (phylum), Sphingobacteriia (class), Sphingobacteriales (order), Sphingobacteriaceae (family), Sphingobacterium (genus), Sphingobacterium faecium (species)
|
cap12 C8N37_104320 SF1_08920
| false |
425 |
A0A2U1LIM9
|
MQSTTSVKLSPFDLMTALLNGKVSFDTSNTSDTNIPLAVFMENRELLMILTTSVAVLIGCVVVLVWRRSSSAAKKAAESPVIVVPKKVTEDEVDDGRKKVTVFFGTQTGTAEGFAKALVEEAKARYEKAVFKVIDLDDYAAEDDEYEEKLKKESLAFFFLATYGDGEPTDNAARFYKWFTEGEEKGEWLEKLQYAVFGLGNRQYEHFNKIAKVVDEKLVEQGAKRLVPVGMGDDDQCIEDDFTAWKELVWPELDQLLRDEDDTSVATPYTAAVAEYRVVFHDKPETYDQDQLTNGHAVHDAQHPCRSNVAVKKELHSPLSDRSCTHLEFDISNTGLSYETGDHVGVYVENLSEVVDEAEKLIGLPPHTYFSVHTDNEDGTPLGGASLPPPFPPCTLRKALASYADVLSSPKKSALLALAAHATDSTEADRLKFLASPAGKDEYAQWIVASHRSLLEVMEAFPSAKPPLGVFFASVAPRLQPRYYSISSSPKFAPNRIHVTCALVYEQTPSGRVHKGVCSTWMKNAVPMTESQDCSWAPIYVRTSNFRLPSDPKVPVIMIGPGTGLAPFRGFLQERLAQKEAGTELGTAILFFGCRNRKVDFIYEDELNNFVETGALSELVTAFSREGATKEYVQHKMTQKASDIWNLLSEGAYLYVCGDAKGMAKDVHRTLHTIVQEQGSLDSSKAELYVKNLQMAGRYLRDVW
|
NADPH--cytochrome P450 reductase 1 (CPR 1) (P450R 1) (EC 1.6.2.4)
|
Artemisia annua (Sweet wormwood)
| 35,608 | 704 | 78,182 |
Endoplasmic reticulum;FAD;Flavoprotein;FMN;Glycoprotein;Membrane;NADP;Oxidoreductase;Reference proteome;Transmembrane;Transmembrane helix
|
GO:0003958; GO:0005789; GO:0005829; GO:0010181; GO:0016491; GO:0050660; GO:0050661; GO:0051762
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212}.
| null |
TRANSMEM 46..66; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03212"
|
PF00667;PF00258;PF00175;
|
IPR003097;IPR017927;IPR001094;IPR008254;IPR001709;IPR029039;IPR039261;IPR023173;IPR001433;IPR023208;IPR017938;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), campanulids (clade), Asterales (order), Asteraceae (family), Asteroideae (subfamily), Anthemideae (tribe), Artemisiinae (subtribe), Artemisia (genus)
|
CPR1 CPR CTI12_AA484860
| false |
426 |
A0A2U9GGW3
|
MAPLGVSGLVGKLSTELEVDCDAEKYYNMYKHGEDVKKAVPHLCVDVKIISGDPTSSGCIKEWNVNIDGKTIRSVEETTHDDETKTLRHRVFEGDVMKDFKKFDTIMVVNPKPDGNGCVVTRSIEYEKTNENSPTPFDYLQFGHQAIEDMNKYLRDSESN
|
Thebaine synthase 2 (EC 4.2.99.24)
|
Papaver somniferum (Opium poppy)
| 3,469 | 160 | 18,066 |
3D-structure;Alkaloid metabolism;Lyase
|
GO:0006952; GO:0009820; GO:0016835; GO:0042803
|
Evidence at protein level
| 5 | null | null | null |
PF00407;
|
IPR000916;IPR052006;IPR023393;
|
6KA2;6KA3;
|
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), Ranunculales (order), Papaveraceae (family), Papaveroideae (subfamily), Papaver (genus)
|
THS2
| false |
427 |
A0A2Y9GHM3
|
MKVLWAALVVALLAGCWADVEPESPLQGKPEPELEPELEPKRELEQEVEAEAGWQAGQPWELALARFWDYLRWVQTLSDQVQEDMLSNQVTQELTTLMEETMKEIKAYRAELEEQLGPMASETQARVAKELQAAQARLRSDMEDVRTRLTQYRGEVQAMLGQSTEELRARFASHMRKLRKRVLRDAEDLQKRLAVYRAGVREGAERSVSSIRERLWPLLEQARTRHANLATQPLRERVDALGQQLRGRLEEVGSRARSHLDEVREQMEEVQAKMEEQANQMRQQVEAFQARLKSWFEPLVEDMQRQWAGLVEKVQVAVGTSPTTPPLETK
|
Apolipoprotein E (Apo-E)
|
Neomonachus schauinslandi (Hawaiian monk seal) (Monachus schauinslandi)
| 29,088 | 330 | 38,091 |
Chylomicron;Endosome;Extracellular matrix;Glycoprotein;HDL;Heparin-binding;Lipid-binding;Oxidation;Phosphoprotein;Reference proteome;Repeat;Secreted;Signal;VLDL
|
GO:0005543; GO:0008201; GO:0008203; GO:0032438; GO:0033344; GO:0033700; GO:0034361; GO:0034362; GO:0034364; GO:0042157; GO:0042627; GO:0055090; GO:0060228; GO:0070062; GO:0097487; GO:0120020
|
Inferred from homology
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P02649}. Note=In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. Colocalizes with CD63 and PMEL at exosomes and in intraluminal vesicles within multivesicular endosomes. {ECO:0000250|UniProtKB:P02649}.
|
SIGNAL 1..18; /evidence="ECO:0000255"
| null |
PF01442;
|
IPR000074;IPR050163;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Carnivora (order), Caniformia (suborder), Pinnipedia (clade), Phocidae (family), Monachinae (subfamily), Monachini (tribe), Neomonachus (genus)
|
APOE
| false |
428 |
A0A2Z5D854
|
MDPAAIFLILAIPIASVYLLFYHKKRVNGLSSPPGPRGLPFIGHFYQIYKSECAHEYISNLSKQYGSLMTLHLGSVPALVVSSPKMAQEVLKTQDLVFCSRAQMTGSGKLSYNGLEMAFAPYGEHWRNVRKMCTLELFTQKRAQFNFRPVREDEVSRMVGRLSEAAAASEDVNAYECFTNFATSIISRVAFGKRYDEDNLGKEKFQRMVADIEAMFAAFFVSDFFPMFGWIDRLSGVKAVLDRNFNEMDTFYQELIDEHLKPDRPESLNGDLIDVMLKNKGSFLTMDSIKAILLNVFSGGIGTTGSALVFAMTALLRNQRVMKKAQEEVRSVIGKKEIVDEDDIQKLPYLRAVVKETLRLYPPGPLLIPRVAMESCVLGEDEDHMYMIKPNTIVYVNTWGIGRDPKYWKNPLEFMPERFFERPDLNYTGQQFEYLPFGSGRRICAGIIIGQNNVEVGLANLLYSFDWEPPTGKTFEDIDDQPCNGLTLAKKNPLYIRPKIYVHP
|
Xanthotoxol synthase (EC 1.14.14.-) (Cytochrome P450 CYP71AZ4) (Fraxetin synthase) (EC 1.14.14.-)
|
Pastinaca sativa (Wild parsnip) (Anethum pastinaca)
| 4,041 | 504 | 57,254 |
Endoplasmic reticulum;Heme;Iron;Membrane;Metal-binding;Microsome;Monooxygenase;Oxidoreductase;Transmembrane;Transmembrane helix
|
GO:0004497; GO:0005506; GO:0005783; GO:0009611; GO:0009805; GO:0016020; GO:0016705; GO:0020037
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:Q6QNI4}; Single-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 3..23; /note="Helical"; /evidence="ECO:0000255"
|
PF00067;
|
IPR001128;IPR017972;IPR002401;IPR036396;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), campanulids (clade), Apiales (order), Apiineae (suborder), Apiaceae (family), Apioideae (subfamily), apioid superclade (clade), Tordylieae (tribe), Tordyliinae (subtribe), Pastinaca (genus)
|
CYP71AZ4
| false |
429 |
A0A2Z5GDY5
|
MENTLSALRSLMASHSPPLDALVVPSEDYHQSEYVSARDKRREFVSGFSGSAGLALITKDVALLWTDGRYFLQAEQQLSDEWKLMRIGEDPAVDTWMADNLLKEASIGVDPWCISIDTAQRWERSFAEKQQKLVQTTKNLVDEVWADRPPAEINAVVVQPLKFAGRSVADKLKDLRKKLVQEQARGIIFTSLDEVAWLYNIRGNDVAYCPVVHAFAIVTSNSAFLYVDKRKVSAEVKSHLEENGIEIREYTAVSFDVALLATDELDTTSTAKDTLAEITKQAEKFVSETNKSVNGKHQAKENSNNLIWADPGSCCYAVYSKLNPDTVLLQQSPLALAKALKNPVELEGLKQAHIRDGAAVVQYLVWLDKQMQDIFGASGYFSEGNTVKKEELSQSLKLTEVTVSDKLEGFRASKKHFRGLSFPTISSVGPNGAVIHYSPKAETCAELDPDKIYLFDSGAQYLDGTTDITRTVHFGKPSAHEKACYTAVLKGHIALGNAVFPNGTNGHALDILARIPLWKNGLDYRHGTGHGIGSYLNVHEGPHLISFKPRNVPLQSSMTVTDEPGYYEDGAFGIRLENVLIINEADTKFNFGDKGYLSFEHITWAPYQTKLIDLNLLTPDEINWLNSYHSRCRDILQPHLDDAAENEWLKKATEPVGV
|
Aminopeptidase P1 (LjAPP1) (EC 3.4.11.9)
|
Lotus japonicus (Lotus corniculatus var. japonicus)
| 34,305 | 658 | 73,207 |
Aminopeptidase;Cell membrane;Cytoplasm;Endoplasmic reticulum;Hydrolase;Manganese;Membrane;Metal-binding;Metalloprotease;Microsome;Nodulation;Nucleus;Protease;Zinc
|
GO:0005634; GO:0005737; GO:0005783; GO:0006508; GO:0009609; GO:0009877; GO:0019897; GO:0046872; GO:0070006
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|Ref.1}. Cytoplasm {ECO:0000269|Ref.1}. Cell membrane {ECO:0000269|Ref.1}; Peripheral membrane protein {ECO:0000269|Ref.1}. Microsome membrane {ECO:0000250|UniProtKB:F4JQH3}; Peripheral membrane protein {ECO:0000250|UniProtKB:F4JQH3}.
| null | null |
PF01321;PF16189;PF00557;PF16188;
|
IPR029149;IPR036005;IPR000587;IPR000994;IPR033740;IPR032416;IPR001131;IPR050422;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), rosids (clade), fabids (clade), Fabales (order), Fabaceae (family), Papilionoideae (subfamily), 50 kb inversion clade (clade), NPAAA clade (clade), Hologalegina (clade), robinioid clade (clade), Loteae (tribe), Lotus (genus)
|
APP1
| false |
430 |
A0A2Z5QKZ7
|
MALVNHRENVKGRAQILAIGTANPKNCFRQVDYPDYYFRVTKSDHLIDLKAKFKRMCEKSMIEKRYMHVNEEILEQNPSMNHGGEKMVSSLDVRLDMEIMEIPKLAAEAATKAMDEWGQPKSRITHLVFHSTLGTVMPGVDYELIKLLGLNPSVKRFMLYHLGCYGGGTVLRLAKDLAENNPGSRVLVLCCEMMPSGFHGPPSLQHAHLDILTGHAIFGDGAGAVIVGCVDPSGGTNGVVERGVRRYEQPLFEIHSAYQTVLPDSKDAVGGRLREAGLIYYLSKRLSNDVSGKIDECCLAEAFSAAIKDNFEDWNSLFWIVHPAGRPILDKLDAKLGLNKEKLRASRNVLRDYGNMWSSSVLFVLDEMRKGSIAQRKTTTGEGFEWGVLLGFGPGVTVETVVLRSVPTAKLK
|
Orcinol synthase (RdORS) (EC 2.3.1.-)
|
Rhododendron dauricum (Azalea daurica)
| 880,079 | 412 | 45,708 |
Acyltransferase;Transferase
|
GO:0016114; GO:0016747; GO:0030639; GO:0042802; GO:0042803; GO:0046197
|
Evidence at protein level
| 5 | null | null | null |
PF02797;PF00195;
|
IPR012328;IPR001099;IPR018088;IPR011141;IPR016039;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), Ericales (order), Ericaceae (family), Ericoideae (subfamily), Rhodoreae (tribe), Rhododendron (genus)
|
ORS
| false |
431 |
A0A2Z5XAU0
|
MSEPTSSSSLDITSNCIIETPLQPSDFLPKSANLFPKFPERISVDSWELWEFDTFDTNGSVAFGCSLYRDARGVEQGGFHAEVNALWPDGTHWGETLYFAVSEVVENSDGTTGGKWLSKDGGSITFHIASDYTAAALDFNVPGKVSGTMELRNHANVSPTSNLPASDAEAQLCPGVYYTFPMGPVATSVTATFSSVGANGESRELFISSGYGGMVRGWSARPWPTFMNDAYYVVAQVGPYMLQILRTLGSVFVQHKPFAVARLYLDGSLVSAANTVVGDELTAHADDVKGDAVRLTKVQPDEKSQGLSGKFRDGNVGYVLEFAKKDSEHGWTFQISHKRAVWSEPTSAPGPDGTGKSGWIEAISGGAKGENYEGHGFGGQLQIPVP
|
Diels-Alderase phm7 (EC 5.5.1.-) (Phomasetin biosynthesis cluster protein 7)
|
Pyrenochaetopsis sp
| 1,756,125 | 386 | 41,434 |
3D-structure;Isomerase
|
GO:0016853
|
Evidence at protein level
| 5 | null | null | null |
PF22903;PF24137;
|
IPR054499;
|
7DMO;7E5U;7E5V;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), dothideomyceta (clade), Dothideomycetes (class), Pleosporomycetidae (subclass), Pleosporales (order), Pleosporineae (suborder), Pyrenochaetopsidaceae (family), Pyrenochaetopsis (genus), unclassified Pyrenochaetopsis (no rank)
|
phm7
| false |
432 |
A0A336U966
|
MGFYRNLVLVAASCTQALGLCPAPRCDSPDIRHEWGELSREDRLSYISAVQCMKDRPPELSVEEVPAVRSRYDDFTAVHINYTLQIHNSGIFLPWHRHFIWLWEKALREECGFTGTLPYWDWVMWPNLAASPLFDGTETSLSGDGEFNATEQPTELNPEPGLTITIPRGAGGGCVRTGPFKDWVINMGPFAFNESYEPALPDHAFDYNPRCLVRSLNDWVIQTYNNQTVVDTLLDSPDIVEFQNIMGGFPNPPIPIGPHAMGHRSLGPDMLDFFASPQDPAFWQHHGMVDRLWTVWQDADEPWRRFALNGSSTTWYKDDTPEVTLQTTVEFGILDEPRPLYELMSPTAGPYCYTYT
|
Tyrosinase P (EC 1.14.18.-)
|
Aspergillus terreus
| 33,178 | 356 | 40,470 |
Copper;Endoplasmic reticulum;Glycoprotein;Golgi apparatus;Metal-binding;Oxidoreductase;Signal
|
GO:0005788; GO:0005796; GO:0016491; GO:0046872
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:27133313, ECO:0000269|PubMed:29270299}. Golgi apparatus lumen {ECO:0000269|PubMed:27133313, ECO:0000269|PubMed:29270299}. Note=The oxidizing environment of Golgi or endoplasmic reticulum (ER) is required for tyrP to be active. {ECO:0000269|PubMed:29270299}.
|
SIGNAL 1..19; /evidence="ECO:0000255"
| null |
PF00264;
|
IPR008922;IPR050316;IPR002227;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), Eurotiomycetes (class), Eurotiomycetidae (subclass), Eurotiales (order), Aspergillaceae (family), Aspergillus (genus), Aspergillus subgen. Circumdati (subgenus)
|
tyrP
| false |
433 |
A0A343URW6
|
MEFVVSLFAFVVSCFILLKVAKNSKNPKRNTNLELPPGPKQLPIIGNLHQLGGGLAHHVLRNLGKQYGPLMHLKIGELSTIVVSSTEIAKEVFKTHDIHFSNRPSHILVFKIVSYDYKDIVLSQYGKYWRELRKVCNLELLSPNRVQSFRSIREDAVLNMMKSISSNDGKVVNLSEMILSLIYGITARAAFGVWSKKHEEFIRLESEIQRLATTFVLADMFPSIKFLGALSGLRYKVEKVHKKVDDILEGILKEHRRQNNNMTEENGKKDLVDVLLNIQKNGDMETPFTDQHIKAIIFDMFSAGTLTSTIAVDWAMAEMMKNPSVLKRAQDEVRNVYNGIGNVDESKLDELKYLQAVIKETLRIHPGTPIVHRETREECEINGYRIPAKARVMVNAWAISRDPNYWPEPDIFKPERFLGSEVDFKGTHFEYIPFGAGRRICPGISYAIANVQLPLAQLLYHFEWKLPGGMKPEELDMTEILGTAAQRKENLLLIPNSHSCSSLKQV
|
Tabersonine 6,7-epoxidase isoform 1 (EC 1.14.14.-) (Cytochrome P450 71D521)
|
Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)
| 4,058 | 506 | 57,513 |
Alkaloid metabolism;Endoplasmic reticulum;Glycoprotein;Heme;Iron;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Transmembrane;Transmembrane helix
|
GO:0004497; GO:0005506; GO:0005789; GO:0016705; GO:0020037; GO:0035835
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29934299}; Single-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 1..21; /note="Helical"; /evidence="ECO:0000255"
|
PF00067;
|
IPR001128;IPR017972;IPR002401;IPR036396;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Gentianales (order), Apocynaceae (family), Rauvolfioideae (subfamily), Vinceae (tribe), Catharanthinae (subtribe), Catharanthus (genus)
|
TEX1 CYP71D521
| false |
434 |
A0A348FUE1
|
MSPMDLQESAAALVRQLGERVEDRRGFGFMSPAIYDTAWVSMISKTIDDQKTWLFAECFQYILSHQLEDGGWAMYASEIDAILNTSASLLSLKRHLSNPYQITSITQEDLSARINRAQNALQKLLNEWNVDSTLHVGFEILVPALLRYLEDEGIAFAFSGRERLLEIEKQKLSKFKAQYLYLPIKVTALHSLEAFIGAIEFDKVSHHKVSGAFMASPSSTAAYMMHATQWDDECEDYLRHVIAHASGKGSGGVPSAFPSTIFESVWPLSTLLKVGYDLNSAPFIEKIRSYLHDAYIAEKGILGFTPFVGADADDTATTILVLNLLNQPVSVDAMLKEFEEEHHFKTYSQERNPSFSANCNVLLALLYSQEPSLYSAQIEKAIRFLYKQFTDSEMDVRDKWNLSPYYSWMLMTQAITRLTTLQKTSKLSTLRDDSISKGLISLLFRIASTVVKDQKPGGSWGTRASKEETAYAVLILTYAFYLDEVTESLRHDIKIAIENGCSFLSERTMQSDSEWLWVEKVTYKSEVLSEAYILAALKRAADLPDENAEAAPVINGISTNGFEHTDRINGKLKVNGTNGTNGSHETNGINGTHEIEQINGVNGTNGHSDVPHDTNGWVEEPTAINETNGHYVNGTNHETPLTNGISNGDSVSVHTDHSDSYYQRSDWTADEEQILLGPFDYLESLPGKNMRSQLIQSFNTWLKVPTESLDVIIKVISMLHTASLLIDDIQDQSILRRGQPVAHSIFGTAQAMNSGNYVYFLALREVQKLQNPKAISIYVDSLIDLHRGQGMELFWRDSLMCPTEEQYLDMVANKTGGLFCLAIQLMQAEATIQVDFIPLVRLLGIIFQICDDYLNLKSTAYTDNKGLCEDLTEGKFSFPIIHSIRSNPGNRQLINILKQKPREDDIKRYALSYMESTNSFEYTRGVVRKLKTEAIDTIQGLEKHGLEENIGIRKILARMSLEL
|
Copalyl diphosphate synthase (CPS) (Bifunctional diterpene synthase PvCPS) [Includes: Type II terpene cyclase (EC 5.5.1.12); Geranylgeranyl diphosphate synthase (GGDP synthase) (GGS) (EC 2.5.1.29)]
|
Talaromyces verruculosus (Penicillium verruculosum)
| 198,730 | 963 | 108,180 |
3D-structure;Isomerase;Isoprene biosynthesis;Magnesium;Metal-binding;Multifunctional enzyme;Transferase
|
GO:0004659; GO:0008299; GO:0016853; GO:0043386; GO:0046165; GO:0046872
|
Evidence at protein level
| 5 | null | null | null |
PF00348;
|
IPR008949;IPR000092;IPR033749;IPR008930;
|
6V0K;7S09;7S0A;7S0H;7S0L;7S0M;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), Eurotiomycetes (class), Eurotiomycetidae (subclass), Eurotiales (order), Trichocomaceae (family), Talaromyces (genus), Talaromyces sect. Talaromyces (section)
|
PvCPS
| false |
435 |
A0A383ZFX3
|
MLGRSRLTFVLLSVTVTCSVAQHVPPWTEDCRKSTYPPSGPTYRGPVPWYTINLDLPPYKRWHELMVDKAPALKVIVNYLKNMINAFEPSGKIVQLVDQKLPGLLGSFPGPFEEEMKGIAAVTEIPLGEIILFNIFYEFFTICTSIITEDKEGHLLHARNMDFGVFLGWNVNNNTWVVTEELKPLTVNLDFQRNSKTVFKAAGFAGYVGMLTGFKPGLFSLTLNERFSTNGGFMGVIEWILGKKDAKWIGFIIRSVLENSTSYEEAKTILTKSKILAPAYFILGGSKSGEGCVITRDRVQSLDIYELDPKQGIWYVVQTNYDRWKNPFFLDNRRTPAKMCLNRTTQENISFATMYDVLSTKPVLNKLTVYTALIDVTKGQFETYLRDCPDPCIGW
|
Acid ceramidase (AC) (ACDase) (Acid CDase) (EC 3.5.1.23) (Acylsphingosine deacylase) (N-acylethanolamine hydrolase ASAH1) (EC 3.5.1.-) (N-acylsphingosine amidohydrolase) [Cleaved into: Acid ceramidase subunit alpha; Acid ceramidase subunit beta]
|
Balaenoptera acutorostrata scammoni (North Pacific minke whale) (Balaenoptera davidsoni)
| 310,752 | 395 | 44,743 |
3D-structure;Disulfide bond;Glycoprotein;Hydrolase;Lipid metabolism;Lysosome;Reference proteome;Secreted;Signal;Sphingolipid metabolism;Zymogen
|
GO:0005576; GO:0005764; GO:0006631; GO:0006665; GO:0016020; GO:0017040; GO:0017064
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q13510}. Secreted {ECO:0000250|UniProtKB:Q13510}. Note=Secretion is extremely low and localization to lysosomes is mannose-6-phosphate receptor-dependent. {ECO:0000250|UniProtKB:Q13510}.
|
SIGNAL 1..21; /evidence="ECO:0000255"
| null |
PF02275;PF15508;
|
IPR016699;IPR029130;IPR029132;
|
5U84;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Artiodactyla (order), Whippomorpha (suborder), Cetacea (infraorder), Mysticeti (parvorder), Balaenopteridae (family), Balaenoptera (genus), Balaenoptera acutorostrata (species)
|
ASAH1
| false |
436 |
A0A384J6C4
|
MRSSTISASAVVLLSGLASAQTFTDCNPTEKTCPSDPAIGGLQVTDFTAGKSSYWEVEDGTTMSYDGTLGAQFVISTATDAPTIKNIGYIMFGRIETWVRASAGTGIVSSFILESDDLDEIDWEWLGANNAEAENNFFGKGNTTTYDRAQYPAVATPIDTFHNYTIDWTAKSTIWYIDGVAVRTLLYDDKQTVGGKNYPQTPMLVKMGSWIGCASKAAETDSATAGTCSWAGGAVDLTQGPFTMYVKNVTIQDYGCATEYTYGDLTGDYTSIKATGGCSADGSAASPSASSSSAASGSSSSTKSSSGSSTLSTVTGTTSAIAVGTATGTATLSAGEKATAAAISGSTTSSSTIAKVTTTSDANSLKKPKHEYGMIDLGVMVLGLGLGYLVM
|
Crh-like protein 1 [Includes: Chitinase crh1 (EC 3.2.1.14); Chitin transglycosylase crh1 (EC 2.4.-.-)]
|
Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
| 332,648 | 391 | 40,365 |
Cell wall biogenesis/degradation;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Glycosidase;Glycosyltransferase;GPI-anchor;Host cytoplasm;Hydrolase;Lipoprotein;Membrane;Reference proteome;Secreted;Signal;Transferase;Vacuole
|
GO:0004553; GO:0005975; GO:0009277; GO:0016757; GO:0031505; GO:0098552
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}. Vacuole {ECO:0000269|PubMed:33846308}. Endoplasmic reticulum {ECO:0000269|PubMed:33846308}. Secreted {ECO:0000269|PubMed:33846308}. Host cytoplasm {ECO:0000269|PubMed:33846308}. Note=Under saprophytic conditions, is localized inside vacuoles and the endoplasmic reticulum (PubMed:33846308). During pathogenic development, high levels of the protein are observed in developing infection cushions, before being secreted to the plant apoplasm (PubMed:33846308). {ECO:0000269|PubMed:33846308}.
|
SIGNAL 1..20; /evidence="ECO:0000255"
| null |
PF00722;
|
IPR013320;IPR000757;IPR017168;IPR050546;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), sordariomyceta (clade), Leotiomycetes (class), Helotiales (order), Sclerotiniaceae (family), Botrytis (genus), Botryotinia fuckeliana (species)
|
crh1 BCIN_01g06010
| false |
437 |
A0A384K116
|
MVGKSTLLSVLASASVAFAACSLDSHCPEETPCCSQYGECGTGAYCLGGCDPRMSFSLESCVPEPVCESASYTFTSMDGITSNTKYLGDASKSNWVYSGSPVIYNDNVLLTMSANSVGTVMASSTYMWYGNVKAKFKTSRGQGVITAFILFSDVKDEIDYEFVGSELTTAQSNYYFQGITNYDNELNITLSDTYANYHEYEIDWTPDEITWLVDGQVGRTKKRADTWNATANQWNFPQTPARVQLSLWPGGLASNGAGTIAWAGGEIDWNSEDIQNNGYYYAAFESVDISCYNAKSAPGTNSGKSYYYNSVLGTNNTVIDSKNATILSSLLATGTNMTAGESAAASGSTAASTAATVPGLTGSGGGGVGDNHSDDGSSSSDSSSGSATSSSSGSSSTGSSGFSQGDGSTSTSKSSADSLVANQERVLKGSLFAGIVAVVAMMAL
|
Crh-like protein 3 [Includes: Chitinase crh3 (EC 3.2.1.14); Chitin transglycosylase crh3 (EC 2.4.-.-)]
|
Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea)
| 332,648 | 444 | 46,296 |
Cell membrane;Cell wall biogenesis/degradation;Disulfide bond;Glycoprotein;Glycosidase;Glycosyltransferase;GPI-anchor;Hydrolase;Lipoprotein;Membrane;Reference proteome;Signal;Transferase
|
GO:0000144; GO:0004553; GO:0005975; GO:0006030; GO:0009277; GO:0016757; GO:0031505; GO:0098552
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}.
|
SIGNAL 1..19; /evidence="ECO:0000255"
| null |
PF00722;
|
IPR013320;IPR000757;IPR017168;IPR050546;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), sordariomyceta (clade), Leotiomycetes (class), Helotiales (order), Sclerotiniaceae (family), Botrytis (genus), Botryotinia fuckeliana (species)
|
crh3 BCIN_13g03640
| false |
438 |
A0A386CAB9
|
MSSDYTDRNNLASAIKTLGDMLEKDEAFQRLMYNASTKGEINRGRVNKVFLKALLSAGDKVGEFLNELIDHLNLFKVLGDFSWNPPVLKEAELNERTSQLRTQQHKYVERVSGFSHYGFGETGTPARGDITSPRGPQVASIEEDLATSKLAELLLAVGDHLEKIEKKGQFLPENVERFSLDCFITSESVKLSSEAVELAPCYTEPVIIQRSKEQTEKYCQEYVRSPHTSSHLLSNDKTQSIRIGQLFSPDSDGNTPKTVILCGDSGRGKSFVLEKIILDWVHLEHHFENFDAVFLLKYEELKCLSEEMSLTELLSRSCSLTSDQISQILQLTPEKVLFLIDGIDDFSFNAHIQISSPTDPSQKAPVISIIHCLMRDLLLVESSVIVTTRYTAAAELSSLCKRPQRFTEIEGFSERRVQEYFQKFFQDEQLFKKAYESMKTNETLLTFCSVPLLCWMVCFCLKKDADQVMTELKTTTSIYVHFVSTLLEDHHQSQSFLRSLGQLAEEGMKNRQNLFDEKSVTRTGLDPATRVFMNKIYLKRKKKHELLFKFKHLSFQEFFAALYYIMLDEEESWCKVSELFNMMESEALIHRSPPIFRGRLSNPIPSVMMFLCGLFNKKVSSSLFEKMKSTFSHNVKLKKKELKKKLMKMIPAMIRQYGFELFALHCLYELQDERFVTKVLETHKFIDLSNVSLRSTDCLVLCYCLRLCPNIRELNFMNCDLTAAKLKILQPALGLCETLRFSVEHLSEIGDLIQILSESKILRELKVREDEYGVESPRWSFNLSVTRGDVLLTLSSSEKNPSFSSVLNIRLTCAQSQISRTDWTLFLQRLRKTGTLTEDSSADDDHVSLQLSSLHSVGLKSLDLTLVSLNESWASGIISLIQNCTSLQQLKVSVTGLLLEEGLKLLKKSLTDPHCTVIIEGRRNCSEPSEEHLRQSYEKVEIHFKPKLLEELAELSICNPGSSALNIHCQSCVDVADSDQWVQVEPSVCRGEGGTEFRITTPAGRFQCSRTRMRWVCDGDVTLHYRAVDGHFLNAELERLQCERVAPVLDVNVISGKLEEAHLPHYMCLAESDPALTNAVKLLSVEDEGISLESVELTRFHAKILQPMFSPKTVLVKLGIPVKVHCDLLIFMTHTCPIILNVYFFPSDSLVEENIKTEEKSSHQIKCSRPEAPLQMKKQHSLEVPDAVVQPEAIKLRGNMKPNFFQVKQPVVNDITMILSRVDDQKSVWTGTIWKKLIDIKLNKTESDLFQSGQKHKTSQPAHSFDKAQFFDTHWCNLIKSVENVDTVADKLLQKQIIHEQFYSEIIHHKSTSEESMRKICVIVRKGSAAVKEIFISILLQENPNLLNHLPSSDS
|
NACHT, LRR and PYD domains-containing protein 1 homolog (EC 3.4.-.-) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1, C-terminus (NLRP1-CT); NACHT, LRR and PYD domains-containing protein 1, N-terminus (NLRP1-NT)]
|
Danio rerio (Zebrafish) (Brachydanio rerio)
| 7,955 | 1,355 | 154,257 |
ATP-binding;Cytoplasm;Hydrolase;Immunity;Inflammasome;Inflammatory response;Innate immunity;Necrosis;Nucleotide-binding;Protease;Reference proteome;Repeat;Ubl conjugation
|
GO:0002221; GO:0005524; GO:0005737; GO:0006508; GO:0006954; GO:0008233; GO:0012501; GO:0032731; GO:0042981; GO:0045087; GO:0050729; GO:0061702; GO:0072558
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30150286}. Note=Co-localizes with pycard, caspa and caspb in the cytoplasm. {ECO:0000269|PubMed:30150286}.; SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein 1, C-terminus]: Inflammasome {ECO:0000269|PubMed:30150286}.
| null | null |
PF00619;PF13553;PF05729;PF17776;PF17779;PF23679;
|
IPR001315;IPR011029;IPR025307;IPR032675;IPR007111;IPR041267;IPR050637;IPR041075;IPR027417;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Actinopterygii (superclass), Actinopteri (class), Neopterygii (subclass), Teleostei (infraclass), Osteoglossocephalai (clade), Clupeocephala (no rank), Otomorpha (cohort), Ostariophysi (subcohort), Otophysi (clade), Cypriniphysae (superorder), Cypriniformes (order), Cyprinoidei (suborder), Danionidae (family), Danioninae (subfamily), Danio (genus)
|
nlrp1 si:ch211-66k16.28
| false |
439 |
A0A386KZ50
|
MKFATSIVAAIATTGAAFTVIPQKLSHPSQLNALNTMGSISSITAESPKEVLSRVQDAGLTLTNPNDLYWMVDFLKEKYYDNGDYYYPIKTVCDGESIDVKFYCPFEPSLSPHYLELYGSRDERASIYETTMKKYNRINSEKTSAICTPYSSYGDTQIVAYFYSMMYYINDQTAHLKLPESEIESELIDILNDDILIYLNEFMSIFEPEDAQDLERIWDFLDFYQPYFSKVDGKIVLDEKYLVRTPSQMPLIKTICEYVSEQFAPSKNITQVIWEVVRYIKGVKDEIHIRGDKSFTLSLQEYDDFRDKVTASPMAHAVSDLTHERFSYEAYTNPAFMELENRCSEIITYFNDVCTSDRERLDEDPFNSVFILMDLDPSLNFAKSCDVVVEHAYNKMQAFLKLKEEILESASDEEERLALARMIKTREDSLIGYVLHEVCCVEDGYARDHKPLMKAFLEEEITKSLAEKVKFNPVESESVRLN
|
Magnesium-dependent glutamate N-prenyltransferase (EC 2.5.1.-) (Domoic acid biosynthesis cluster protein A) (PmDabA)
|
Pseudo-nitzschia multiseries (Marine planktonic diatom) (Nitzschia pungens f. multiseries)
| 37,319 | 482 | 55,647 |
3D-structure;Magnesium;Metal-binding;Transferase
|
GO:0016036; GO:0016740; GO:0046872; GO:0071244
|
Evidence at protein level
| 5 | null | null | null |
PF19086;
|
IPR008949;
|
6VKZ;6VL0;6VL1;
|
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Stramenopiles (clade), Ochrophyta (clade), Bacillariophyta (phylum), Bacillariophyceae (class), Bacillariophycidae (clade), Bacillariales (order), Bacillariaceae (family), Pseudo-nitzschia (genus)
|
dabA
| false |
440 |
A0A396GMX6
|
MKREHKLEHEDMSSGSGKSGVCWEDDGGGMDELLAVVGYKVKSSDMAEVAQKLEQLEQAMMGNNFHDHDESTIAQHLSNDTVHYNPSDISNWLQTMLSNFDPQPNNPSVNSDDNDLNAIPGKAIYAADEFTSRKRVKRNESVTVTTESTTTRPIMVVETQEKGIRLVHSLMACAEAVEQNNLKMAEALVKQIGYLAVSQEGAMRKVATYFAEGLARRIYGVFPQHSVSDSLQIHFYETCPNLKFAHFTANQAILEAFQGKSSVHVIDFSINQGMQWPALMQALALRPGGPPAFRLTGIGPPASDNSDHLQQVGWRLAQFAQTIHVQFEYRGFVANSLADLDASMLELRSPETESVAVNSVFELHKLNARPGALEKVFSVIRQIRPEIVTVVEQEANHNGPAFLDRFTESLHYYSTLFDSLEGSSVEPQDKAMSEVYLGKQICNVVACEGTDRVERHETLNQWRNRFNSAGFSPVHLGSNAFKQASMLLALFAGGDGYKVEENDGCLMLGWHTRPLIATSAWKLAAANSVVVSH
|
DELLA protein 2 (MtDELLA2)
|
Medicago truncatula (Barrel medic) (Medicago tribuloides)
| 3,880 | 533 | 58,991 |
Gibberellin signaling pathway;Nucleus;Reference proteome;Transcription;Transcription regulation;Ubl conjugation
|
GO:0003700; GO:0005634; GO:0006355; GO:0009610; GO:0009723; GO:0009737; GO:0009740; GO:0009863; GO:0009867; GO:0009938; GO:0010187; GO:0016036; GO:0036377; GO:0042538; GO:0043565; GO:0045944; GO:2000033; GO:2000377
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A0A396IUP1}.
| null | null |
PF12041;PF03514;
|
IPR038088;IPR021914;IPR005202;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), rosids (clade), fabids (clade), Fabales (order), Fabaceae (family), Papilionoideae (subfamily), 50 kb inversion clade (clade), NPAAA clade (clade), Hologalegina (clade), IRL clade (clade), Trifolieae (tribe), Medicago (genus)
|
DELLA2 MtrunA17_Chr8g0376381
| false |
441 |
A0A396IUP1
|
MKREHQESFGGGVISNNNKTNTNHLNSSKNINFGECSSMQNTNTKQNMWREEKETNGGGMDELLAALGYKVRSSDMADVAQKLEQLEMVMGSAQEEGINHLSSDTVHYDPTDLYSWVQTMLTELNPDSSQINDPLASLGSSSEILNNTFNDDSEYDLSAIPGMAAYPPQEENTAAKRMKTWSEPESEPAVVMSPPPAVENTRPVVLVDTQETGVRLVHTLMACAEAIQQKNLKLAEALVKHISLLASLQTGAMRKVASYFAQALARRIYGNPEETIDSSFSEILHMHFYESSPYLKFAHFTANQAILEAFAGAGRVHVIDFGLKQGMQWPALMQALALRPGGPPTFRLTGIGPPQADNTDALQQVGWKLAQLAQTIGVQFEFRGFVCNSIADLDPNMLEIRPGEAVAVNSVFELHTMLARPGSVEKVLNTVKKINPKIVTIVEQEANHNGPVFVDRFTEALHYYSSLFDSLEGSNSSSNNSNSNSTGLGSPSQDLLMSEIYLGKQICNVVAYEGVDRVERHETLTQWRSRMGSAGFEPVHLGSNAFKQASTLLALFAGGDGYRVEENNGCLMLGWHTRSLIATSAWKLPQNESK
|
DELLA protein 1 (MtDELLA1)
|
Medicago truncatula (Barrel medic) (Medicago tribuloides)
| 3,880 | 594 | 65,226 |
Gibberellin signaling pathway;Nucleus;Reference proteome;Transcription;Transcription regulation;Ubl conjugation
|
GO:0003700; GO:0005634; GO:0006355; GO:0006357; GO:0009610; GO:0009723; GO:0009737; GO:0009740; GO:0009863; GO:0009867; GO:0009938; GO:0010187; GO:0016036; GO:0036377; GO:0042538; GO:0043565; GO:0045944; GO:2000033; GO:2000377
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24297892}.
| null | null |
PF12041;PF03514;
|
IPR038088;IPR021914;IPR005202;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), rosids (clade), fabids (clade), Fabales (order), Fabaceae (family), Papilionoideae (subfamily), 50 kb inversion clade (clade), NPAAA clade (clade), Hologalegina (clade), IRL clade (clade), Trifolieae (tribe), Medicago (genus)
|
DELLA1 MTR_3g065980 MtrunA17_Chr3g0110971
| false |
442 |
A0A396JG59
|
MHKKQLMALLMVPQTSDSQDATITKLESAYSDLESLLRSSKQMEQNIETMETRFDLLHGSITTASRRVHPLQSLSMSRKALDTRINRAISPALALLETFKLAESLQNNLLNLSSKLSTEKTHQKRLSKLLDYMDCVDQLNEAINSISEVVEPVIMRLQEVVEFISRTKAADQYRTQRLREALITLKALYETEVDEMRFEGLLDQALLHMQDEFEVLLLKLKHRKLGDMSHMQNGGEDCDDHFEVSFELGSELEIEVLRRISNTLAANDCLDICIDIYVKVRYKRAAKALMKLNPDYLRTYTPEGIDEMEWENLETSITLWTQHFEVATKKVLLSEKKLCESVLGEIIDGLIHPECFVKISDKIMAVFFRFGEGVARSNKEPQKLFKLLDMFESLEKLKPYVLEIFDGESGEDICARFRELEKLIIDASSKVFWEFGLQIEGNVDGFLPPPQDGSVPKIVRYAVNYLKYLSTENYRTTMAKVLRTELTWKTELMLSSKQSETDEDLLKHAICNVMEALQRNIESKRLSCKDKILVNIFMMNTYWYMYMRTKNTELGDLLGEKYIKESYKAVAEESAYLYQKQAWLVLVKILDQDDDDIKEQKQGKEKSIGRLVNEKIETFFKCLSEICDRHRSFYSIPDVDLREQMRDSTVKLLVPVYAEFLESYSGFLQRKVYPSPQRLQGLLGKAFGSTNDWNLNGGRNSGSLETDIRRSR
|
Exocyst complex component EXO70I (MtExo70I) (Exocyst subunit Exo70 family protein I)
|
Medicago truncatula (Barrel medic) (Medicago tribuloides)
| 3,880 | 712 | 82,325 |
Cell membrane;Coiled coil;Exocytosis;Glycoprotein;Membrane;Protein transport;Reference proteome;Signal;Transport
|
GO:0000145; GO:0005546; GO:0005886; GO:0006887; GO:0009609; GO:0009610; GO:0015031; GO:0036377; GO:0085042
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26234213}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=During arbuscule branching, restricted to zones adjacent to the periarbuscular membrane (PAM) around the arbuscule hyphal tips. {ECO:0000269|PubMed:26234213}.
|
SIGNAL 1..18; /evidence="ECO:0000255"
| null |
PF03081;
|
IPR016159;IPR004140;IPR046364;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), rosids (clade), fabids (clade), Fabales (order), Fabaceae (family), Papilionoideae (subfamily), 50 kb inversion clade (clade), NPAAA clade (clade), Hologalegina (clade), IRL clade (clade), Trifolieae (tribe), Medicago (genus)
|
EX70I MTR_1g017910 MtrunA17_Chr1g0152401
| false |
443 |
A0A3F2YLY8
|
MKKPVKSWLIASTVAALLAVPAVSQANSEVEKLTKNPANWATWGGNYHGTRYSELKQINTSNVKNLQPAWTFSTGVLRGHEGGPLVVNDVMYIHTPFPNTVYAIDQKTQAVIWEYTPQQDADVTIPVMCCDTVNRGLAYGDGKIFLQQSDTVLTALDAKTGKRVWSVQNGDPKLGMTNTQAPLVVKDKVITGISGGEFGVRGFLAAYNIRTGELDWKGYSMGPDADTLINPTKTTTWKDGKVQPVGKDSSTSTWEGDQWKIGGGTTWGWYSYDPELNLVYYGSGNPSTWNPAQRPGDNKWSMSLWARNADTGEVKWVYQMTPHDEWDYDGINEVALVDQEIKGQMRKTAVHFDRNGFGYTLDRVTGELLVAEKFDKAVNWASHVDMKSGRPQVVSQYSTEYNGEDVNTEGVCPAALGSKNQQPVSYSPQTGYFYISGNHVCMDYEPFEVEYTAGQPYVGATLSMFPAGKDVITGKEDGSNNLGQFTAWDATTGKIIWSNKEQFSVWSGSLATAGGVVFYGTLEGYLKAVDAKTGKELYRFKTPSGIIGNVNTWEYEGKQYVGVLSGVGGWAGIGIAAGLDSGEESSNSEGLGAVGAYRSLSSYTKLGGTLTVFALPN
|
Lanthanide-dependent methanol dehydrogenase XoxF (Lanthanide-dependent MDH) (Ln(3+)-dependent MDH) (EC 1.1.2.10)
|
Methylotuvimicrobium buryatense (Methylomicrobium buryatense)
| 95,641 | 617 | 67,220 |
3D-structure;Disulfide bond;Metal-binding;Methanol utilization;Oxidoreductase;Periplasm;PQQ;Signal
|
GO:0005509; GO:0015945; GO:0016020; GO:0016614; GO:0030288
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:30132076}.
|
SIGNAL 1..26; /evidence="ECO:0000255"
| null |
PF01011;
|
IPR018391;IPR017512;IPR002372;IPR011047;IPR001479;
|
6DAM;
|
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Methylococcales (order), Methylococcaceae (family), Methylotuvimicrobium (genus)
|
xoxF EQU24_18605
| false |
444 |
A0A3L7I2I8
|
MQFFGRLVNTLSSVTNLFSNPFRVKEISVADYTSHERVREEGQLILFQNASNRTWDCILVSPRNPHSGFRLFQLESEADALVNFQQFSSQLPPFYESSVQVLHVEVLQHLSDLIRSHPSWTVTHLAVELGIRECFHHSRIISCANSTENEEGCTPLHLACRKGDSEILVELVQYCHAQMDVTDNKGETAFHYAVQGDNSQVLQLLGKNASAGLNQVNKQGLTPLHLACQMGKQEMVRVLLLCNARCNVMGPSGFPIHTAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMARMLLKRGCDVDSTSAAGNTALHVAVMRNRFDCVMVLLTYGANAGTPGEHGNTPLHLAISKDNMEMIKALIVFGAEVDTPNDFGETPAFMASKISKLITRKALLSLLRTVGADHRFPLIQGVPTDQSSAATPHPIFSLDKTQPPAISLNNLELQDLMPISRARKPAFILSSMRDEKRIHDHLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRQPAELHLFRNYDAPEVIREPRFNQNINLKPPTQPADQLVWRAARSSGAAPTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDMIRKGQGNKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAKTVFGAKELGKMVVDCCTDPDGRAVDRARAWSEMVGIQYFRLNPQLGSDIMLDEVNDAVLVNALWETEVYIYEHREEFQKLVQMLLSP
|
85/88 kDa calcium-independent phospholipase A2 (CaI-PLA2) (EC 3.1.1.4) (2-lysophosphatidylcholine acylhydrolase) (EC 3.1.1.5) (Group VI phospholipase A2) (GVI PLA2) (Intracellular membrane-associated calcium-independent phospholipase A2 beta) (iPLA2-beta) (PLA2G6) (Palmitoyl-CoA hydrolase) (EC 3.1.2.2) (Patatin-like phospholipase domain-containing protein 9) (PNPLA9)
|
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
| 10,029 | 807 | 89,776 |
3D-structure;Alternative splicing;ANK repeat;Cell membrane;Cell projection;Cytoplasm;Hydrolase;Lipid metabolism;Membrane;Mitochondrion;Phospholipid metabolism;Repeat;Transmembrane;Transmembrane helix
|
GO:0003847; GO:0004622; GO:0005615; GO:0005739; GO:0005886; GO:0015630; GO:0016607; GO:0017171; GO:0019731; GO:0031143; GO:0034638; GO:0035774; GO:0035965; GO:0042802; GO:0046338; GO:0046469; GO:0046473; GO:0047499; GO:0052816; GO:2000304
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60733}. Cell membrane {ECO:0000250|UniProtKB:O60733}. Mitochondrion {ECO:0000250|UniProtKB:P97819}. Cell projection, pseudopodium {ECO:0000250|UniProtKB:O60733}. Note=Recruited to the membrane-enriched pseudopods upon MCP1/CCL2 stimulation in monocytes. {ECO:0000250|UniProtKB:O60733}.
| null |
TRANSMEM 481..501; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 512..532; /note="Helical"; /evidence="ECO:0000255"
|
PF12796;PF01734;
|
IPR016035;IPR002110;IPR036770;IPR047148;IPR002641;
|
6AUN;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Glires (clade), Rodentia (order), Myomorpha (suborder), Muroidea (clade), Cricetidae (family), Cricetinae (subfamily), Cricetulus (genus)
|
PLA2G6 PLPLA9
| false |
445 |
A0A3Q0KDV9
|
MTADVLKALPPDVRTLKLSGHVGFDSLPDQLVNKAISQGFVFNILCVGETGIGKSTLLETLFNQKFDFSPSNHDLTDPKLKAVTYDLKEANVKLKLTVVETCGYGDQINKENNIKPVVDYIDNQFENYLQEELKMKRSMQAFHDTRVHVCLYFIAPTGHSLKSIDLVAMKKLENKVNVIPVIAKSDTITKSELQKFKARILSEIQSNEIGIYQFPTDDEAVSETNSVMNQHIPFAVVGSSEEVKINGKTVRVRQYPWGSVQVENENHCDFVRLREMLLRVNMEDLRERTHGVHYETYRRQRLIEMGFRDDEKMSLQETYEKRRELQRKELQQKEEEMRQMFVQRVKEKEQVLKEAERELQTKFESLKKTHAEEKKKLEEKKRFLEEEIAAFERRKQLAEQARQGNLTMKKRK
|
Septin-10 (SmSEPT10)
|
Schistosoma mansoni (Blood fluke)
| 6,183 | 412 | 48,090 |
3D-structure;Coiled coil;Cytoplasm;Cytoskeleton;Direct protein sequencing;Glycoprotein;GTP-binding;Magnesium;Metal-binding;Nucleotide-binding;Reference proteome
|
GO:0000287; GO:0005525; GO:0019003; GO:0031105; GO:0031982; GO:0042802; GO:0042803; GO:0046982; GO:0051260
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8C1B7}. Note=Colocalizes with actin in the longitudinal and circular muscles of the sporocyst. {ECO:0000269|PubMed:24367716}.
| null | null |
PF00735;
|
IPR030379;IPR027417;IPR016491;
|
4KV9;4KVA;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Spiralia (clade), Lophotrochozoa (clade), Platyhelminthes (phylum), Trematoda (class), Digenea (subclass), Strigeidida (order), Schistosomatoidea (superfamily), Schistosomatidae (family), Schistosoma (genus)
|
SEPT10 Smp_029890
| false |
446 |
A0A3Q0KGQ7
|
MLYDFASWYRRWRFGEGKRIDLVLIGPPGSGKGTQAVKIAERYNICHLSTGDILRAIIASGSELGQKVQKITESGGLVSDDIVCDLIAQKINSPECKNGLLFDGFPRTIEQAKKLDNLLRDRQIHLLAALEFKLDPSILEKRICGRLFHLASGRSYHELFNPPKVPMVDDITGDRLVHRSDDKPEALKKRLYEYDKNVAPILHFYESQNKLLRINANKDVNQVFSDIQELVRTKLAEEK
|
Adenylate kinase 2 (ADK2) (AK 2) (EC 2.7.4.3) (ATP-AMP transphosphorylase 2) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase) (SmADK2)
|
Schistosoma mansoni (Blood fluke)
| 6,183 | 239 | 27,202 |
ATP-binding;Cytoplasm;Kinase;Nucleotide biosynthesis;Nucleotide-binding;Purine salvage;Reference proteome;Transferase
|
GO:0004017; GO:0005524; GO:0005737; GO:0005829; GO:0006166; GO:0006172; GO:0006756; GO:0016208; GO:0046083
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P07170}.
| null | null |
PF00406;PF05191;
|
IPR006259;IPR000850;IPR033690;IPR007862;IPR027417;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Spiralia (clade), Lophotrochozoa (clade), Platyhelminthes (phylum), Trematoda (class), Digenea (subclass), Strigeidida (order), Schistosomatoidea (superfamily), Schistosomatidae (family), Schistosoma (genus)
|
Smp_061940
| false |
447 |
A0A3Q0KJ78
|
MVKPDGVQRGLVGEVIQRFERRGYKLVAIKMMHASEQLLQTHYEALKSLSFFPKLVAYMSSGPVVPMVFEGRKVVENGRTMLGATKPEASCPGSIRGDYCQDVGRNVVHGSDSTESANREINLWFSPQELCQYKQAVDPWIHE
|
Nucleoside diphosphate kinase (NDK) (NDP kinase) (NDPK) (EC 2.7.4.6) (SmNDPK)
|
Schistosoma mansoni (Blood fluke)
| 6,183 | 143 | 16,072 |
3D-structure;ATP-binding;Kinase;Magnesium;Nucleotide biosynthesis;Nucleotide-binding;Purine salvage;Reference proteome;Transferase
|
GO:0004550; GO:0005524; GO:0006166; GO:0006183; GO:0006228; GO:0006241; GO:0009202; GO:0032261; GO:0034214; GO:0042802; GO:0043531
|
Evidence at protein level
| 5 | null | null | null |
PF00334;
|
IPR034907;IPR036850;IPR001564;
|
5IOL;5IOM;5KK8;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Spiralia (clade), Lophotrochozoa (clade), Platyhelminthes (phylum), Trematoda (class), Digenea (subclass), Strigeidida (order), Schistosomatoidea (superfamily), Schistosomatidae (family), Schistosoma (genus)
|
Smp_092750
| false |
448 |
A0A3Q0KQY7
|
MLETDSQRLRVVEDSLGKINVPLERYYGAQTARSLGNFNVCTRSDTMPLQIVYSLAMIKEVAACTNFKLGRISSKLSDAIVKACREVYHGQHDNEFPLVIWQTGSGTQTNMNVNEVLSSRASELIDGSRSSRLTVHPNDHVNLGQSSNDIFPTAMNLSIAMETAWKVLPSLNHLINVLKIKMHEFMNVIKIGRTHMQDAVPMSVGQELSGYVSQLQQAVDSIKSQLPLICHLAVGGTAVGTGLNCSKGFDEELCVSLTQLTDRLYRTMYKESTPVVDLIFKPAENKFAALAGHDALLQLSGCFNTTATALMRLSNDFCLLSSGPNCGLSEFVLPANEPGSSIMPGKVNPTQCESLRMVCLQIMGNHFTTSMAASQGQLELNVCKPLIAANLLHTCELLTDSTRCFADKCVRDLQLNREKIQEYVDKSLMLVTVLTPHIGYDLSAKLVQHASKFKKGLRESAIELNLLCGEKFDEIVKPMEMAFPHNNK
|
Fumarate hydratase (Fumarase) (EC 4.2.1.2) (Class II fumarase) (SmFHII)
|
Schistosoma mansoni (Blood fluke)
| 6,183 | 488 | 53,776 |
3D-structure;Cytoplasm;Lyase;Reference proteome
|
GO:0000050; GO:0004333; GO:0005739; GO:0005829; GO:0006099; GO:0006106; GO:0006108; GO:0006525; GO:0051289
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P07954}.
| null | null |
PF10415;PF00206;
|
IPR005677;IPR024083;IPR018951;IPR020557;IPR000362;IPR022761;IPR008948;
|
6U4O;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Spiralia (clade), Lophotrochozoa (clade), Platyhelminthes (phylum), Trematoda (class), Digenea (subclass), Strigeidida (order), Schistosomatoidea (superfamily), Schistosomatidae (family), Schistosoma (genus)
|
Smp_158240
| false |
449 |
A0A3Q0KR05
|
MPQSTAQLKSPLLHTLLENLTQSSICTSTAIWHVPNPVNFVCNHNENSFDNKNNSVTTITTTDVSTNNHKNTNYDYEQQEQWSNEEINSNQESNEIYTMTFLKLNNAANRVAMNLANYLERKWSSITNKINRTQLNQHSLSIDEPIELRNQSDTVIALFMPPGIDRIVVQIACMKLHLAYMPLDRNVPAGRITQILHKLKPILILIDKDYYDFIYDDDHNDNDKMSDLSSSIDNNNKSLLSRKLSSNDFIIGNLNQLKLTFQLFDVKVYEYIKLMKLSKYYSRSDIYTASIPIRVCLFPFESDPIVLVLFTSGSTSSGPKPVKLRTTQLFNRLEWQWDSTSDMDLPNFENATCNSNTSVKRIGLAKTAWGFVDAFTELFSCLLAGIPVVVPGGSACPSEKSITDVQQLINLTKHFKISHITTVPTQMNLWLKQLRLKPKEIVTSHLSSLRTVIVSGDIVHPKMACEFFQLFKNPEMRLINLYGTTEVAGDVTGLVFRGEIDVKKHTKVVPCGLERENNKSGKPVLSVGTVIQGTAIFIVQDDDDHHLHHEKDNENQPDKWSNPSLSIIGSVDRKPNWDKFPFKILPKGHIGHVCILGQQVSDSASRCQRIESLPEDLNCVDTNKCKSDVESCENNSSKEIRVFMPGDLGFIDPQTNHLYICGRTNELIKINGIRFHANDIDNLFIELKKNWKAKNMTNCTREELLVNKVSETVTLTIQTVHGRDLKLVCFYVLHMNENQNTMNIEPKENYDKLEDLPKQDDFIAVFSHYLPPYLSPTFINIDHIPLMRTSGKVDKEYLRQYYYSKHHCEISEITKVLQPGWVNDPVKHMTENNNSTSDQSFGKNSRDFKLSRGRERARKVLAEVLGIRGPNGDVIPGRPKDDEDFYLLGGDSLLTVLTTEQLRQLGFNVNLDVFTKTGKIGSILTSLQNTESDFLKTQEPFTSDSWTVKEISMNKVLKKSHTCNLINRIPLMEDECYLSPTICPQGSYEIFIEQWNDGNFSVTERHEIVDVLVNAFIEKDRLSHALKLDRTDLTEAIEVFLNAHKSNPGIVLTARYYYENPYEHTFVKNKLVGVIISLPAKHVPSLHLTPKLALVQRFFDECSNKDQFQDISMDNLLATQMVAITSQSPYSKSKYLQYMLSNWKKISLKLLTRLERDLLRIAAKQGYSGVITFNTNEVTEEVCSQLGYKVIQTTMLKSFMNKENLLLLPQYERIRCSYMIKELNPSS
|
Beta-alanyl-bioamine nonribosomal peptide synthetase (EC 6.3.2.-) (Nonribosomal peptide synthetase) (SmNRPS)
|
Schistosoma mansoni (Blood fluke)
| 6,183 | 1,227 | 140,064 |
Ligase;Phosphopantetheine;Phosphoprotein;Reference proteome
|
GO:0003833; GO:0030540; GO:0043042
|
Evidence at protein level
| 5 | null | null | null |
PF00501;PF00550;
|
IPR045851;IPR000873;IPR042099;IPR009081;IPR006162;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Spiralia (clade), Lophotrochozoa (clade), Platyhelminthes (phylum), Trematoda (class), Digenea (subclass), Strigeidida (order), Schistosomatoidea (superfamily), Schistosomatidae (family), Schistosoma (genus)
|
NRPS Smp_158480
| false |
450 |
A0A3Q0NBH7
|
MKIRWIRLSLVAILIIAVVFIGVIGFQKYQFSKSRNKVIMQMDRLMKDQDGGNFRRLDKKENGVEIISYIPKTTEKKDNEIIQKEIGKATDAEVKKLNRDKETQGIIFYTYQKHRMAEQAISYKAVQSEYVKEGRTKFVLKDKKDICKNIVTDAETGALLTLGEVLIKSNQTKLNLKTAVEEELIKTGDFSLKDVGNLGKIKSLVKWNQTDFEITNSEIILPVKIPGAPEPKKVKVKLADIASSVNKRYLPSSVKVPEVPKAKTNKRIALTFDDGPSSSVTPGVLDTLKRHNVKATFFVLGSSVIQNPGLVKRELEEGHQVGSHSWDHPQLTKQSTQEVYNQILKTQKAVFDQTGYFPTTMRPPYGAVNKQVAEEIGLPIIQWSVDTEDWKYRNAGIVTKKVLAGATDGAIVLMHDIHKTTAASLDTTLTKLKSQGYEFVTIDELYGEKLQIGKQYFDKTDSRMVK
|
Peptidoglycan-N-acetylglucosamine deacetylase PgdA (Peptidoglycan GlcNAc deacetylase) (EC 3.5.1.104) (N-acetylglucosamine de-N-acetylase PgdA) (Peptidoglycan N-deacetylase) (PG N-deacetylase) (Petptidoglycan deacetylase) (PG deacetylase)
|
Listeria monocytogenes serotype 1/2a (strain EGD / Mackaness)
| 1,334,565 | 466 | 52,496 |
Cell membrane;Cell wall;Hydrolase;Membrane;Metal-binding;Secreted;Transmembrane;Transmembrane helix;Virulence;Zinc
|
GO:0001896; GO:0005576; GO:0005886; GO:0005975; GO:0008270; GO:0009275; GO:0042545; GO:0042803; GO:0050119; GO:0060241; GO:0141043
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8Y9V5}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q8Y9V5, ECO:0000255}; Extracellular side {ECO:0000250|UniProtKB:Q8Y9V5}. Secreted, cell wall {ECO:0000305|PubMed:19809250}.
| null |
TRANSMEM 6..26; /note="Helical"; /evidence="ECO:0000255"
|
PF01522;
|
IPR011330;IPR002509;IPR017219;IPR050248;
| null |
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Listeriaceae (family), Listeria (genus), Listeria monocytogenes (species)
|
pgdA LMON_0423
| false |
451 |
A0A3Q2TTB3
|
MKRKWEERVKKVEELASYYERNPLPTVYKPRLSKPLQPSRVWKIFCRQADAFRFVKTCKEDVHVFALERNTQNGQRFYLVTTYQELWYYYTKGYKTSLMHCYEVIPEKDACKLYFDLEFYKAANPGADGKDMVAKLIELVSQKLKELYDVNCSARDVLNLDSSTDEKFSRHLIFLPCKTVFKDNIHVGNFVRTILQPAIRLVGSNVAAPIAEGGAGYTSQCSAPTVELDGPLTNLTAVEDASKGWPAIADQRKETETSHHGENSEFSFLIVNNKEGDKQLFVDLGVYTRNRNFRMYKSSKAGKNVILTIAEDNKFVPNCEENVSLEEAYFLSSLVCNVRFEDGTKILSSNFVEEEIKMSAFLRSKTTRSTREPMEGYQESPYPEIDCFVRSLINKDGVQGGIRQWNYFSGEEILVYDISGYRWCENIGRAHRSNNIMILVDLKKEVWYQKCHDPVCREKNFKSQSLPLPSRICLSSLFIEEEDHMVTDERENTEVTSHSNPADLSESSAYLAINTSQDTQWDNASDDAYLVETAEDVELAEAADYSLGYDTEEIPDEVLLEMSWKQDTCSKDDS
|
DNA-directed primase/polymerase protein (EC 2.7.7.102) (EC 2.7.7.7)
|
Gallus gallus (Chicken)
| 9,031 | 574 | 65,865 |
Alternative splicing;Chromosome;Coiled coil;DNA damage;DNA repair;DNA-directed DNA polymerase;DNA-directed RNA polymerase;Manganese;Metal-binding;Mitochondrion;Nucleotidyltransferase;Nucleus;Reference proteome;Transcription;Transferase;Zinc
|
GO:0000428; GO:0003682; GO:0003887; GO:0003899; GO:0005634; GO:0005657; GO:0005759; GO:0006264; GO:0008270; GO:0009411; GO:0019985; GO:0030145; GO:0031297; GO:0042276; GO:0043504; GO:0062176
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96LW4}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q96LW4}. Chromosome {ECO:0000250|UniProtKB:Q96LW4}.
| null | null |
PF03121;
|
IPR044917;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Sauropsida (clade), Sauria (clade), Archelosauria (clade), Archosauria (clade), Dinosauria (clade), Saurischia (clade), Theropoda (clade), Coelurosauria (clade), Aves (class), Neognathae (infraclass), Galloanserae (superorder), Galliformes (order), Phasianidae (family), Phasianinae (subfamily), Gallus (genus)
|
PRIMPOL
| false |
452 |
A0A3Q7FGP1
|
MADELNKAALEEYKSSSVEDRGEEGEIVGESDDTASSLGKQITMKHPLEHSWTFWFDNPSGKSKQAAWGSSIRPIYTFSTAEDFWSVYNNIHHPSKLAVGADFHCFKNKIEPKWEDPVCANGGKWTMNFSRGKSDTCWLYTLLALIGEQFDYGDEICGAVINVRVRQEKIALWTRNAANETAQVSIGKQWKEFLDYNDTIGFIFHDDAKKLDRAAKNRYSV
|
Eukaryotic translation initiation factor 4E-2 (eIF4E-2) (eIF-4F 25 kDa subunit) (eIF-4F p26 subunit) (mRNA cap-binding protein)
|
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
| 4,081 | 221 | 25,104 |
Cytoplasm;Disulfide bond;Host-virus interaction;Initiation factor;Nucleus;Plant defense;Protein biosynthesis;Reference proteome;RNA-binding;Translation regulation
|
GO:0000340; GO:0003723; GO:0003743; GO:0005634; GO:0005737; GO:0006413; GO:0006417; GO:0016281; GO:0051607
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:C6ZJZ3}. Cytoplasm {ECO:0000250|UniProtKB:C6ZJZ3}.
| null | null |
PF01652;
|
IPR023398;IPR001040;IPR019770;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Solanales (order), Solanaceae (family), Solanoideae (subfamily), Solaneae (tribe), Solanum (genus), Solanum subgen. Lycopersicon (subgenus)
|
eIF4E2 Solyc02g021550
| false |
453 |
A0A3Q7GYG2
|
MASNNNICAYELIEAEAQSWDYILSYLRPSCIKCAIQLGIPDILHKNADPIMSLSDLIAALPNLNPSKTTFIPILMRVLVDFGLFNYHQQQGDGYSLTTVGRLLVENHHFGNRSFFLFAQHPVVLNTAASVGDWLKDDLRTAFETADGKSHWDYCGADPEFNGVFNDAMAGDSRLMSNLLISDCCAGVFEGLTSLVDIGGGTGAVAMAIAGAFPSLKCIVLDLPHVIADRKGSGNLEFVAGSMFDKIPHANAILLKWILHNWDDEDCVKLLKKCKESISSRENGGKVIIIDMIMEDNYNNKQLVQSQHLMDLIMRITYASKERTEKEWEKLFLEAGFSGYKIITSLGLRSLIEIYP
|
Myricetin 7/4'-O-methyltransferase 2 (SlMOMT2a) (SlMOMT2b) (EC 2.1.1.-) (3',4',5'-trimethyl myricetin 7-O-methyltransferase) (EC 2.1.1.-) (3',5'-dimethyl myricetin 7-O-methyltransferase) (7-O-methyl syringetin synthase) (Syringetin 7-O-methyltransferase) (EC 2.1.1.-) (3'-methyl quercetin 4'-O-methyltransferase) (4'-O-methyl isorhamnetin synthase) (Isorhamnetin 4'-O-methyltransferase) (EC 2.1.1.-) (3-methyl quercetin 7-O-methyltransferase) (EC 2.1.1.82) (4'-methyl kaempferol 7-O-methyltransferase) (7-O-methyl kaempferide synthase) (Kaempferide 7-O-methyltransferase) (EC 2.1.1.-) (7-methyl quercetin 4'-O-methyltransferase) (Rhamnacene synthase) (Rhamnetin 4'-O-methyltransferase) (EC 2.1.1.-) (Kaempferol 4'-O-methyltransferase) (Kaempferide synthase) (EC 2.1.1.155) (Myricetin 7-O-methyltransferase) (EC 2.1.1.-) (Quercetin 7-O-methyltransferase) (Rhamnetin synthase) (EC 2.1.1.-)
|
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
| 4,081 | 356 | 39,490 |
Methyltransferase;Reference proteome;S-adenosyl-L-methionine;Transferase
|
GO:0008171; GO:0008757; GO:0009058; GO:0009813; GO:0032259; GO:0046983
|
Evidence at protein level
| 5 | null | null | null |
PF08100;PF00891;
|
IPR016461;IPR001077;IPR012967;IPR029063;IPR036388;IPR036390;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Solanales (order), Solanaceae (family), Solanoideae (subfamily), Solaneae (tribe), Solanum (genus), Solanum subgen. Lycopersicon (subgenus)
|
MOMT2 Solyc06g064500
| false |
454 |
A0A3Q7HJG4
|
MGNIKFLLLVFFLIVVVVNGCWEEERNALLELQTNIMSSNGELLVDWAGYNAAHFVDCCFWDRVKCSLETGRVIKLDLEADFGTGDGWLFNASLFLPFKSLQVLLLSSQNIIGWTKNEGFSKLRQLPNLKEVDLQYNPIDPKVLLSSLCWISSLEVLKLGVDVDTSFSIPMTYNTNMMSKKCGGLSNLRELWFEGYEINDINILSALGELRNLEKLILDDNNFNSTIFSSLKIFPSLKHLNLAANEINGNVEMNDIIDLSNLEYLDLSDNNIHSFATTKGNKKMTSLRSLLLGSSYSNSSRVIRSLKSFSSLKSLSYKNSNLTSPSIIYALRNLSTVEYLYFKGSSLNDNFLPNIGQMTSLKVLNMPSGGNNGTLPNQGWCELKYIEELDFLNNNFVGTLPLCLGNLTSLRWLSLAGNNLHGNIASHSIWRRLTSLEYLDIADNQFDVPLSFSQFSDHKKLIYLNVGYNTIITDTEYQNWIPNFQLEFFAIQRCIALQKLPSFLHYQYDLRILAIEGNQLQGKFPTWLLENNTRLAAIYGRDNAFSGPLKLPSSVHLHLEAVDVSNNKLNGHIPQNMSLAFPKLLSLNMSHNHLEGPIPSKISGIYLTILDLSVNFLSGEVPGDLAVVDSPQLFYLRLSNNKLKGKIFSEEFRPHVLSFLYLNDNNFEGALPSNVFLSSLITLDASRNNFSGEIPGCTRDNRRLLQLDLSKNHLQGLIPVEICNLKIINVLAISENKISGSIPSCVSSLPLKHIHLQKNQLGGELGHVIFNFSSLITLDLRYNNFAGNIPYTIGSLSNLNYLLLSNNKLEGDIPTQICMLNNLSIVDLSFNKLYGPLPPCLGYLTQTKKDAEISWTYFAENYRGSWLNFVIWMRSKRHYHDSHGLLSDLFLMDVETQVQFSTKKNSYTYKGNILKYMSGIDLSSNRLTGEIPVELGNMSNIHALNLSHNHLNGRIPNTFSNLQEIESLDLSCNRLNGSIPVGLLELNSLAVFSVAYNNLSGAVPDFKAQFGTFNKSSYEGNPFLCGYPLDNKCGMSPKLSNTSNINGDEESSELEDIQCFYIGFVVSFGAILLGLAAALCLNRHWRRAWFRMIEALMFYCYYFVLDNIVTPIKSRWYKNVG
|
Cuscuta receptor 1 (CuRe1) (Leucine-rich repeat receptor-like protein Solyc08g016270) (LRR-RLP Solyc08g016270)
|
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
| 4,081 | 1,121 | 126,156 |
Cell membrane;Glycoprotein;Immunity;Leucine-rich repeat;Membrane;Plant defense;Reference proteome;Repeat;Signal;Transmembrane;Transmembrane helix
|
GO:0002218; GO:0002242; GO:0002752; GO:0002768; GO:0005886; GO:0009626; GO:0009986; GO:0038187; GO:0140426
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27471302}; Single-pass membrane protein {ECO:0000255, ECO:0000305|PubMed:27471302}. Cell surface {ECO:0000305|PubMed:27471302}.
|
SIGNAL 1..20; /evidence="ECO:0000255"
|
TRANSMEM 1059..1079; /note="Helical"; /evidence="ECO:0000255"
|
PF00560;PF13855;
|
IPR001611;IPR003591;IPR032675;IPR051502;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Solanales (order), Solanaceae (family), Solanoideae (subfamily), Solaneae (tribe), Solanum (genus), Solanum subgen. Lycopersicon (subgenus)
|
Solyc08g016270
| false |
455 |
A0A3Q7HRZ6
|
MTEYSLPTMNLWNNSTSDDNVSMMEAFMSSDLSFWATNNSTSAAVVGVNSNLPHASSNTPSVFAPSSSTSASTLSAAATVDASKSMPFFNQETLQQRLQALIDGARETWTYAIFWQSSVVDFSSPSVLGWGDGYYKGEEDKAKRKLSVSSPAYIAEQEHRKKVLRELNSLISGAPPGTDDAVDEEVTDTEWFFLISMTQSFVNGSGLPGQALYSSSPIWVAGTEKLAASHCERVRQAQGFGLQTIVCIPSANGVVELGSTELIVQSSDLMNKVRVLFNFSNDLGSGSWAVQPESDPSALWLTDPSSSGMEVRESLNTVQTNSVPSSNSNKQIAYGNENNHPSGNGQSCYNQQQQKNPPQQQTQGFFTRELNFSEFGFDGSSNRNGNSSVSCKPESGEILNFGDSTKKSASSANVNLFTGQSQFGAGEENNNKNKKRSATSRGSNEEGMLSFVSGTVLPSSGMKSGGGGGEDSEHSDLEASVVKEADSSRVVEPEKRPRKRGRKPANGREEPLNHVEAERQRREKLNQRFYALRAVVPNVSKMDKASLLGDAISYINELKSKLQNTESDKEDLKSQIEDLKKESRRPGPPPPPNQDLKMSSHTGGKIVDVDIDVKIIGWDAMIRIQCNKKNHPAARLMAALMELDLDVHHASVSVVNDLMIQQATVKMGSRHYTEEQLRVALTSKIAETH
|
Transcription factor MYC2 (LeMYC2) (SlMYC2) (Basic helix-loop-helix protein 147) (Transcription factor bHLH147) (bHLH transcription factor bHLH147)
|
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
| 4,081 | 689 | 75,041 |
Activator;Developmental protein;DNA-binding;Growth regulation;Jasmonic acid signaling pathway;Nucleus;Plant defense;Reference proteome;Stress response;Transcription;Transcription regulation
|
GO:0000976; GO:0003700; GO:0005634; GO:0006355; GO:0006952; GO:0043565; GO:0045893; GO:0046983
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
| null | null |
PF14215;PF22754;PF00010;
|
IPR045084;IPR054502;IPR011598;IPR036638;IPR025610;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Solanales (order), Solanaceae (family), Solanoideae (subfamily), Solaneae (tribe), Solanum (genus), Solanum subgen. Lycopersicon (subgenus)
|
MYC2 BHLH147 JAMYC2 Solyc08g076930
| false |
456 |
A0A3Q7HYF0
|
MALSMDNIVISNEEEIYMMKAMHIPCGLYLNMVLRAAIELDLFEIIAKSTTQKLSSYEIASQIPTKNPNASSLVLERILRFLASQSFLTCNITKNDDGNVHTSYNLTPLSQSLILDKDGTSIAPFLLLATDPVAVNSWFHFKDAILEGEIPFNKAHGVHAFEYHGKDSRFNGVFNKAMQNVTCIDMKRVLECYNGFEGVKEIIDVGGGLGISLASIISKYPNIKGINFDLPHVIKDAPTYEGIEHVGGDMFKSVPQRELILLKAILHDWDDECCVKILKNCWRALPKDGKVVVIEQMQPEYPEINLISKNSFSVDMLMMTMLDGGKERTKQQFEDLAKQAGFTVFKIVARAYYCWVIELYK
|
Myricetin 3-O-methyltransferase 3 (SlMOMT3) (EC 2.1.1.-) (3',4',5'-trimethyl myricetin 3-O-methyltransferase) (EC 2.1.1.-) (3',5'-dimethyl myricetin 3-O-methyltransferase) (Syringetin 3-O-methyltransferase) (EC 2.1.1.-) (3'-methyl myricetin 3-O-methyltransferase) (Laricitrin 3-O-methyltransferase) (EC 2.1.1.-) (3'-methyl quercetin 3-O-methyltransferase) (Isorhamnetin 3-O-methyltransferase) (EC 2.1.1.-) (4'-methyl kaempferol 3-O-methyltransferase) (Kaempferide 3-O-methyltransferase) (EC 2.1.1.-) (7-methyl quercetin 3-O-methyltransferase) (Rhamnetin 3-O-methyltransferase) (EC 2.1.1.-) (Kaempferol 3-O-methyltransferase) (EC 2.1.1.-) (Quercetin 3-O-methyltransferase) (EC 2.1.1.76)
|
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
| 4,081 | 361 | 40,649 |
Methyltransferase;Reference proteome;S-adenosyl-L-methionine;Transferase
|
GO:0008171; GO:0008757; GO:0009058; GO:0009813; GO:0030755; GO:0032259; GO:0046983; GO:0102440; GO:0102449
|
Evidence at protein level
| 5 | null | null | null |
PF08100;PF00891;
|
IPR016461;IPR001077;IPR012967;IPR029063;IPR036388;IPR036390;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Solanales (order), Solanaceae (family), Solanoideae (subfamily), Solaneae (tribe), Solanum (genus), Solanum subgen. Lycopersicon (subgenus)
|
MOMT3 Solyc06g083445
| false |
457 |
A0A3Q7I7R4
|
MATEAPVEATEIPSVAAAETVEKQPHKLERKWTFWFDNQSKPKQGVAWGSSLRKAYTFETVEEFWSLYDQIFKPSKVTVNADFHLFKAGIEPKWEDPECANGGKWTATSSRKANLETMWLETLMALVGEQFDESEDICGVVASVRRSQDKLSLWTKTATNEAAQMGIGRKWKEIIDAEKISYSFHDDSKRERSAKSRYTV
|
Eukaryotic translation initiation factor isoform 4E (SleIF(iso)4E) (eIF(iso)-4E) (eIF-(iso)4F 25 kDa subunit) (eIF-(iso)4F p28 subunit) (mRNA cap-binding protein)
|
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
| 4,081 | 200 | 22,823 |
Cytoplasm;Disulfide bond;Initiation factor;Nucleus;Protein biosynthesis;Reference proteome;RNA-binding;Translation regulation
|
GO:0000340; GO:0003743; GO:0005634; GO:0006413; GO:0006417; GO:0009615; GO:0016281; GO:0050687
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A445AGS0}. Nucleus {ECO:0000250|UniProtKB:A0A445AGS0}.
| null | null |
PF01652;
|
IPR023398;IPR001040;IPR019770;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Solanales (order), Solanaceae (family), Solanoideae (subfamily), Solaneae (tribe), Solanum (genus), Solanum subgen. Lycopersicon (subgenus)
|
eIFiso4E
| false |
458 |
A0A3Q8GL18
|
MASTANPMQVMKKKLEGKVVIVTGGASGIGQTAARVFAQHGARAVVIADIQSEVGKSVAKSIGDPCCYVQCDVSDEEEVKSMIEWTASAYGGLDMMFSNVGIMSKSAQTVMDLDLLEFDKVMRVNARGMAACLKHAARKMVELGTRGTIICTTTPLSSRGGQSMTDYAMSKHAVMGLVRSASIQLGAHGIRVNCVTPSVVLTPLAQRMGLATPDDFHTHFGNFTSLKGVYLTPEQVAEAVVYLASDDAAFITGHDLVLDGGLLCLPFFAPS
|
(+)-cis,trans-nepetalactol synthase NEPS1 (EC 5.5.1.34) (Nepetalactol-related short-chain dehydrogenase) (Nepetalactol dehydrogenase) (EC 1.1.1.419) (Nepetalactol-related short-chain reductase 1) (Nepetalactol-related SDR1) (NmNEPS1)
|
Nepeta racemosa (Catmint) (Raceme catnip)
| 54,731 | 271 | 28,683 |
Isomerase;NAD;Oxidoreductase
|
GO:0016491; GO:0016853
|
Evidence at protein level
| 5 | null | null | null |
PF13561;
|
IPR036291;IPR002347;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), lamiids (clade), Lamiales (order), Lamiaceae (family), Nepetoideae (subfamily), Mentheae (tribe), Nepetinae (subtribe), Nepeta (genus)
|
NEPS1
| false |
459 |
A0A3S5XFG0
|
MHSVRTSTTSTSSMVSSTMHPFDAFNAPQPYQQHHPPRWNIHNPHFSQTNGHSIQKTPSMIKLHSSEGTVPTTNGADTLHQRNMEEKIISAPLHYITGLPGKDIRGKLISAFNEWFRIPDEQLEIIKRVVGLLHVASLLIDDIEDSSKLRRGFPVAHSIFGIPQTINSANYAYFQAQSEVLKLRNCNAAFTIFTEELLRLHRGQGMDLYWRDSLTCPTEEEYLDMVANKTGGLFRLAIKLIQLESDVEDDCVPLVDLLGIIFQIRDDYQNLQNEQYAKNKGFAEDITEGKFSYPIVHSIRSGAANCSSGSSELMNILRQKTDDEAVKRYTICILEKTGSFEYTRRKLTELMAAARAMLAEFGSAEAAGLGGILDFLELKE
|
Geranylgeranyl pyrophosphate synthase cle6 (GGPP synthase) (GGPPSase) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase) (15-deoxyoxalicine B biosynthesis cluster protein C) (Dimethylallyltranstransferase) (EC 2.5.1.1) (Diterpenoid pyrone biosynthesis cluster protein D) (Farnesyl diphosphate synthase) (Farnesyltranstransferase) (EC 2.5.1.29) (Geranylgeranyl diphosphate synthase) (Geranyltranstransferase) (EC 2.5.1.10)
|
Aspergillus versicolor
| 46,472 | 380 | 42,725 |
Magnesium;Metal-binding;Transferase
|
GO:0004659; GO:0008299; GO:0043386; GO:0046165; GO:0046872
|
Evidence at protein level
| 5 | null | null | null |
PF00348;
|
IPR008949;IPR000092;IPR033749;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), Eurotiomycetes (class), Eurotiomycetidae (subclass), Eurotiales (order), Aspergillaceae (family), Aspergillus (genus), Aspergillus subgen. Nidulantes (subgenus)
|
cle6
| false |
460 |
A0A3S5YBC7
|
MRKTVVAFAAAIAACSAVLSSTTTSAAPPATPITTLQADGTHLVDGYGRTVLLHGVNNVDKDAPYLPAGETLTPQDIDILVRHGFNTVRLGTSFDALMPQRGQIDEAYLDRLTGVVDALTARGMHVLLDNHQDGLSKAWGGNGFPEWAIESRPREWEPNPGFPLYYLMPSLNAGWDEVWGNTHGALDHLGTALGALAERVEGKPGVMGIELLNEPWPGSRFLSCFPNGCPDFDRTYQAAMQKLTDAVRAQNPTIPVYWEPNVTWNQMMPSNLFAPPVTPALTTADVVFAPHDYCIPSQLAIYLGLPQALRGLCVPQQDLTWSNIDAITERANVPTVITEFGDGDPTVLKNTLARADERFIGWQYWHFGAGNATDPFLGEVGRQLVRTYPQATAGEPGRMIFDADNGDFAYRFTPRAATRPTEIFVSDLHYPDGYAVQVDGGQVTSAPGARIVTVVADGSGPVTVKINRPGSAGAEVPDGPIETSSSGSSGSS
|
Endoglycoceramidase I (EGCase I) (EC 3.2.1.123)
|
Rhodococcus hoagii (strain 103S) (Rhodococcus equi)
| 685,727 | 492 | 52,830 |
3D-structure;Disulfide bond;Glycosidase;Hydrolase;Lipid metabolism;Lipoprotein;Membrane;Palmitate;Secreted;Signal;Sphingolipid metabolism
|
GO:0000272; GO:0005576; GO:0006683; GO:0016020; GO:0047876
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28179425}. Membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
|
SIGNAL 1..14; /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
| null |
PF00150;PF18564;
|
IPR041036;IPR001547;IPR013780;IPR017853;IPR052066;
|
5CCU;5J14;5J7Z;
|
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Actinomycetota (phylum), Actinomycetes (class), Mycobacteriales (order), Nocardiaceae (family), Prescottella (genus), Rhodococcus hoagii (species)
|
REQ_38260
| false |
461 |
A0A3S7WQS5
|
MDDRSLKLAEDFVSARYIEAGRESLRATARIMRSILAQRCCPDEGLTDAAIELILRQLSLMDTNNLAHHVGGGEREGRVVSALVRMRHFHLTHGIGRSGDLFSEQPKAAGSSLLYKITNVLMLDLIRQAGAPSTAAAVVVPMATGMTLALVLRCVAKTHMKELMKEAEAVQLQRTVTKDSTSATSAAPVQEPPMSEADRDRHDRTSLPVPATPRYVIWPRIDQKTALKCIDAAGLVPVPVQLRPAVPLARSAAPCVSTNRDSLDRGQDSIGSPSTPTSSSSLFLECHVDDVAAAVNAVGGPSQVVCVLSTTSCFAPRLPDNTVAIAQYCKKAGIPYVVNNAYGVQSRRIMTRLDAAQRLGRVDFVVQSGDKNFLVPVGGSIICSGDKERCKAVAALYAGRASMSPIVDLFITALSLGRRGMQTLWSDRYKCRARLIRQLRVFARERREVLLVDDSDDDKADEDTVGGSQRTSNAVVPRNDISVAVTMRAYGLPAAEASSSGAQLGSEQAGRVTNWAAARALGAQLFRSAVTGPRVITPAPSTPTTIAGCTFRNYGMHQDREPPCPLLVIACGIGMSESEVDALMARLRDLWPVPA
|
O-phosphoseryl-tRNA(Sec) selenium transferase (EC 2.9.1.2) (Selenocysteine synthase) (Selenocysteinyl-tRNA(Sec) synthase) (Sep-tRNA:Sec-tRNA synthase)
|
Leishmania donovani
| 5,661 | 595 | 63,923 |
Cytoplasm;Protein biosynthesis;Pyridoxal phosphate;RNA-binding;Selenium;Transferase;tRNA-binding
|
GO:0000049; GO:0001514; GO:0001717; GO:0005737; GO:0016785; GO:0098621
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PIRNR:PIRNR017689, ECO:0000269|PubMed:26586914}.
| null | null |
PF05889;
|
IPR015424;IPR015421;IPR019872;IPR008829;
| null |
cellular organisms (no rank), Eukaryota (domain), Discoba (clade), Euglenozoa (phylum), Kinetoplastea (class), Metakinetoplastina (subclass), Trypanosomatida (order), Trypanosomatidae (family), Leishmaniinae (subfamily), Leishmania (genus), Leishmania (subgenus), Leishmania donovani species complex (no rank)
|
SepSecS LdCL_090015500
| false |
462 |
A0A411MR89
|
MSHVPPHVPFELSGAELRDAIVQYATNPIYHDNLDWLNHDNPYRRQLRPQVLPHLDYDKVPGRENILNYASLAVQRLLTSVYEADLVFFPKSGLKGKEEDFRAFYSPANRALGERIRPALERYAFGFLDDEVETSGTWTAQSLDAYLDSLDTAGGAEQSPVEKAILGSADRERAARMWLVQFAPDFLSEASPMMRNVLGYYGPAQSEWFKVVIDEYGYGVHDTKHSTLFERTLESVGLESDLHRYWQYYLNSSLLLNNYFHYLGKNHELFFRYVGALYYTESSLVDFCRRADHLLREVFGDTVDTTYFTEHIHIDQHHGRMAREKIIKPLVEAHGDGIIPEIVRGIEEYRVLLEIGDFDFSEQIAWMDAQPELKKLHDPVFEGLKQGKVDAPVAHLVEPRGELSNTHCHDGDELCHIVSGTMRFESGLGSSLTLQAGEGVVIKRNRLHGANIESDECVYEIHSVGDYRKCL
|
Nitrosourea synthase (EC 1.14.13.250) (Multi-domain metalloenzyme SznF)
|
Streptomyces achromogenes subsp. streptozoticus
| 285,532 | 471 | 53,802 |
3D-structure;Antibiotic biosynthesis;Iron;Metal-binding;Monooxygenase;Oxidoreductase
|
GO:0004497; GO:0017000; GO:0046872
|
Evidence at protein level
| 5 | null | null | null |
PF07883;PF14518;
|
IPR013096;IPR016084;IPR014710;IPR011051;
|
6VZY;6XCV;8E8W;
|
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Actinomycetota (phylum), Actinomycetes (class), Kitasatosporales (order), Streptomycetaceae (family), Streptomyces (genus), Streptomyces achromogenes (species)
|
sznF stzF
| false |
463 |
A0A445AGS0
|
MATETAGAVVESSSAATVPSPAPEAGSKHKLERKWTFWFDNQSKPKQGAAWGTSLREVYTFDTVEEFWCLYDQVFKPSKLPGNADFHLFKTGIEPKWEDPECAKGGKWTVTSNRKANLDNMWLETMMALIGEQFDDAEDICGVVASVRQRQDKLSLWTKTAANEAAQMGIGRKWKEIIDVTDKIIYNFHDDSRTRSSKSRYSV
|
Eukaryotic translation initiation factor isoform 4E (PeaeIF(iso)4E) (eIF(iso)-4E) (eIF-(iso)4F 25 kDa subunit) (eIF-(iso)4F p28 subunit) (mRNA cap-binding protein)
|
Arachis hypogaea (Peanut)
| 3,818 | 203 | 22,953 |
Cytoplasm;Disulfide bond;Host-virus interaction;Initiation factor;Nucleus;Plant defense;Protein biosynthesis;Reference proteome;RNA-binding;Translation regulation
|
GO:0000340; GO:0003743; GO:0005634; GO:0005737; GO:0006417; GO:0016281; GO:0051607
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28344571}. Nucleus {ECO:0000269|PubMed:28344571}.; SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28344571}. Nucleus {ECO:0000269|PubMed:28344571}. Note=(Microbial infection) Binds to potyvirus viral genome-linked protein (VPg) in the nucleus and with viral helper component proteinase (HC-Pro) in the cytoplasm. {ECO:0000269|PubMed:28344571}.
| null | null |
PF01652;
|
IPR023398;IPR001040;IPR019770;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), rosids (clade), fabids (clade), Fabales (order), Fabaceae (family), Papilionoideae (subfamily), 50 kb inversion clade (clade), dalbergioids sensu lato (clade), Dalbergieae (tribe), Pterocarpus clade (clade), Arachis (genus)
|
eIF(iso)4E Ahy_B02g059482
| false |
464 |
A0A452E9Y6
|
MLVCLHLQVFLASVALFEVAASDTIAQAASTTTISDAVSKVKTQVNKAFLDSRTRLKTALSSEAPTTRQLSEYFKHAKGRTRTAIRNGQVWEESLKRLRRDTTLTNVTDPSLDLTALSWEVGCGAPVPLVKCDENSPYRTITGDCNNRRSPALGAANRALARWLPAEYEDGLAVPFGWTQRKTRNGFRVPLAREVSNKIVGYLDEEGVLDQNRSLLFMQWGQIVDHDLDFAPETELGSSEHSKVQCEEYCIQGDNCFPIMFPKNDPKLKTQGKCMPFFRAGFVCPTPPYQSLARDQINAVTSFLDASLVYGSEPSLASRLRNLSSPLGLMAVNQEAWDHGLAYPPFNNVKPSPCEFINTTAHVPCFQAGDSRASEQILLATVHTLLLREHNRLARELKRLNPHWDGEMLYQEARKILGAFIQIITFRDYLPIVLGSEMQKWIPPYQGYNNSVDPRISNVFTFAFRFGHMEVPSTVSRLDENYQPWGPEAELPLHTLFFNTWRIIKDGGIDPLVRGLLAKKSKLMNQNKMVTSELRNKLFQPTHKIHGFDLAAINLQRCRDHGMPGYNSWRGFCGLSQPKTLKGLQAVLKNKILAKKLLDLYKTPDNIDIWIGGNAEPMVERGRVGPLLACLLGRQFQQIRDGDRFWWENPGVFTEKQRDSLQKVSFSRLICDNTHVTKVPLHAFQANNYPHDFVDCSAVDKLDLSPWASREN
|
Lactoperoxidase (LPO) (EC 1.11.1.7)
|
Capra hircus (Goat)
| 9,925 | 712 | 80,366 |
3D-structure;Antibiotic;Antimicrobial;Calcium;Cytoplasm;Direct protein sequencing;Disulfide bond;Glycoprotein;Heme;Hydrogen peroxide;Iron;Metal-binding;Nitration;Oxidoreductase;Peroxidase;Phosphoprotein;Reference proteome;Secreted;Signal
|
GO:0001580; GO:0004601; GO:0005509; GO:0005615; GO:0005737; GO:0006979; GO:0016323; GO:0019731; GO:0019732; GO:0020037; GO:0036393; GO:0042744; GO:0046265; GO:0140825
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18191143, ECO:0000269|PubMed:27398304, ECO:0000269|PubMed:30296068}. Cytoplasm {ECO:0000250|UniProtKB:Q5SW46}.
|
SIGNAL 1..21; /evidence="ECO:0000255"
| null |
PF03098;
|
IPR019791;IPR010255;IPR037120;
|
2E9E;2EFB;2EHA;2OJV;2R5L;3N8F;3NAK;3NIU;3QF1;3R55;3RKE;3SXV;4MSF;4OEK;4QJQ;5FF1;5HPW;6LF7;8ING;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Artiodactyla (order), Ruminantia (suborder), Pecora (infraorder), Bovidae (family), Caprinae (subfamily), Capra (genus)
|
LPO
| false |
465 |
A0A452G813
|
MTDSPFLELWQSRTVAIRERLGIGDQPNDSYCYNSAKNSTVLQGVTFGGIPTVLFIDVSCFLFLIVVFSIIRRKFWDYGRIALVSEGNSESRFRRLSSSSSGQQDFESELGCCSWLTAIFRLHDDQILEWCGEDAIHYLSFQRHIIFLLVVVSCLSLCIILPVNLSGDLLDKDPYSFGRTTIANLQTDNNLLWLHTIFAILYLILTVVFMRHHTQSIKYKEESLVRRTLFVTGLPKDAKKETVESHFRDAYPTCEVVEVQLCYNVAKLIYLCKERKKTEKSLTYYTNLQVKTGQRTFINPKPCGQFCCCEVRGCEWEDAISYYTRMKDRLMERITEEECRVQDQPLGMAFVTFQEKSMATYILKDFNACKCQGLQCKGEPQPSSHSRELGISRWSVTFAAYPEDICWKNLSIQGFRWWFQWLGINFILFVGLFFLTTPSIILSTMDKFNVTKPIHALNDPIISQFFPTLLLWSFSALLPTIVCYSTLLESHWTKSGENRIMMTKVYIFLIFMVLILPSLGLTSLDFFFRWLFDKTSSEASIRLECVFLPDQGAFFVNYVIASAFIGNGMELLRLPGLILYTFRMVMAKTAADRRNVKQHQAFEYEFGAMYAWMLCVFTVIMAYSITCPIIVPFGLIYILLKHMVDRHNLYFAYLPAKLEKRIHFAAVNQALAAPILCLFWLYFFSFLRLGLKAPLTLFTFLVLLLTILVCLAYTCFGCFRHLSPLNYKTEESANDKGNEAGAHVPPPFTPYVPRILNSSSSEKTALSPQQQTYGAINNISGTVAGQGLAQSPEDSVAAADQED
|
Mechanosensitive cation channel TMEM63A (Transmembrane protein 63A)
|
Capra hircus (Goat)
| 9,925 | 803 | 91,821 |
Calcium;Cell membrane;Endosome;Ion channel;Ion transport;Lysosome;Membrane;Phosphoprotein;Reference proteome;Transmembrane;Transmembrane helix;Transport
|
GO:0001817; GO:0003676; GO:0005227; GO:0005765; GO:0005886; GO:0007040; GO:0031901; GO:0032944; GO:0045428; GO:0050764; GO:0160069; GO:1990760
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:O94886}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:O94886}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O94886}; Multi-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 52..74; /note="Helical; Name=TM0"; /evidence="ECO:0000250|UniProtKB:O94886"; TRANSMEM 134..166; /note="Helical; Name=TM1"; /evidence="ECO:0000250|UniProtKB:O94886"; TRANSMEM 191..216; /note="Helical; Name=TM2"; /evidence="ECO:0000250|UniProtKB:O94886"; TRANSMEM 416..443; /note="Helical; Name=TM3"; /evidence="ECO:0000250|UniProtKB:O94886"; TRANSMEM 462..489; /note="Helical; Name=TM4"; /evidence="ECO:0000250|UniProtKB:O94886"; TRANSMEM 495..531; /note="Helical; Name=TM5"; /evidence="ECO:0000250|UniProtKB:O94886"; TRANSMEM 554..585; /note="Helical; Name=TM6"; /evidence="ECO:0000250|UniProtKB:O94886"; TRANSMEM 606..623; /note="Helical; Name=TM7"; /evidence="ECO:0000250|UniProtKB:O94886"; TRANSMEM 628..650; /note="Helical; Name=TM8"; /evidence="ECO:0000250|UniProtKB:O94886"; TRANSMEM 661..688; /note="Helical; Name=TM9"; /evidence="ECO:0000250|UniProtKB:O94886"; TRANSMEM 694..708; /note="Helical; Name=TM10"; /evidence="ECO:0000250|UniProtKB:O94886"
|
PF14703;PF02714;PF13967;
|
IPR045122;IPR003864;IPR027815;IPR032880;IPR012677;IPR035979;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Artiodactyla (order), Ruminantia (suborder), Pecora (infraorder), Bovidae (family), Caprinae (subfamily), Capra (genus)
|
TMEM63A
| false |
466 |
A0A455R4Z0
|
MPQLAGKLILAGLIPLGAWVLHGFASCNGLIQMFEDFGKQTVLSDGVTDYTGAFTGLEGLDRLLRTLLNFFWPVANGHDWALSLHAFMFAGQGVPLLVLNMLEGARPGNKSLVVSYVTVFGILYMVVGLAIMAPLYLFLHLLTSRTATAPSKAKVAVDPNTAKAVGFGVFVGYVLPTIFMSLPHPSLLSTDTKVLSVVFWQAVPLWASVCAYFASTALGQSATSRSSSNLPSALGAVYAASLIIATATHVATFAISANLSDTWSGIFTFLIPPNPFNTDMRISSFLEGATWFLQWDYTMMSLAYMVWAIGIRHGVEVPRSSHHFETLGKIALRSMAKLLVMGPIGAALSLVWERDQLLWQLDSESGEKGEKNRSRRMSRKWMFS
|
Terpene cyclase ascI (EC 5.4.99.-) (Ascofuranone/ascochlorin biosynthesis clusters protein I)
|
Acremonium egyptiacum (Oospora egyptiaca)
| 749,675 | 384 | 41,823 |
Glycoprotein;Isomerase;Membrane;Signal;Transmembrane;Transmembrane helix
|
GO:0016020; GO:0016114; GO:0016853
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
|
SIGNAL 1..25; /evidence="ECO:0000255"
|
TRANSMEM 82..102; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 119..139; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 164..184; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 194..214; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 235..255; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 291..311; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 330..350; /note="Helical"; /evidence="ECO:0000255"
| null | null | null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), sordariomyceta (clade), Sordariomycetes (class), Hypocreomycetidae (subclass), Hypocreales (order), Hypocreales incertae sedis (no rank), Acremonium (genus)
|
ascI
| false |
467 |
A0A481NV25
|
MKDMDIKAVFIGDKAENGPVYKMLLNKMVDEHLGWRENYIPSDMPAISEGDKLTPDYLATRDHMIEVLDEVSQRLRAGSIPWHSAGRYWGQMNAETLMPALLAYNYAMLWNPNNVALESSMATSQMEAEVGQDFASLFNMADGWGHIAADGSIANLEGLWYARCIKSIPLAVKEVLPEKVKNMSEWALLNLSVEEILEMTESFTDEEMDEVKAASSRSGKNIQKLGKWLVPQTKHYSWMKALDICGVGLDQMVAIPVQEDYRMDINALEKTIRELADQKIPILGVVAVVGTTEEGQVDSVDKIIQLREKLKDEGIYFYLHVDAAYGGYARSLFLNEAGEFVPYASLAEFFEEHHVFHHYVTIDKEVYEGFRAISEADSVTIDPHKMGYVPYAAGGIVIKHKNMRNIISYFAPYVFEKSVKAPDMLGAYILEGSKAGATAAAVWTAHRVLPLNVTGYGQLIGASIEAAQRFREFLEQLHFTVKGKTIEVYPLNHPDFNMVNWVFKVQDCTDLNAINELNEKMFDRSSYMDGDVYGERFITSHTTFTQEDYGDSPIRFIERMGLSKEEWQKEQQITLLRAAIMTPYLNDDRIFNFYTKEIAKAMEKKLNEIIK
|
L-tyrosine decarboxylase (TDC) (EC 4.1.1.25) (Levodopa decarboxylase) (L-dopa decarboxylase) (EC 4.1.1.-)
|
Enterococcus faecium (Streptococcus faecium)
| 1,352 | 611 | 69,341 |
Coiled coil;Decarboxylase;Lyase;Pyridoxal phosphate
|
GO:0004837; GO:0030170; GO:0036468; GO:1903184
|
Evidence at protein level
| 5 | null | null | null |
PF00282;PF21391;
|
IPR050477;IPR002129;IPR015424;IPR015421;IPR021115;IPR049373;IPR022397;
| null |
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Lactobacillales (order), Enterococcaceae (family), Enterococcus (genus)
|
tdc mfnA_1
| false |
468 |
A0A482A9N4
|
MPSTKVAALSAVLALASTVAGHGYVQNIVIDGESYSGYIVTQFPYESNPPAVIGWATTATDLGYVDPTEYTNADIICHKNATPGALSAPVAAGGTVELQWTTWPDSHHGPVISYLANCNGNCSTVDKTKLDFVKIDASGLIDDTTVPGTWASDQLIAANNSWTVTIPETIAPGNYVLRHEIIALHSAENTDGAQNYPQCINLEITGSGTASPTGTPGEELYTPTDPGILVNIYQSLSTYVIPGPTLWSGAANNAVASATAAASATATPTTLVTSVASATDSPSTVAPASSTTATSVLTSVVPSVTSFVPVVTVTDVVTVTTVITTTVF
|
AA9 family lytic polysaccharide monooxygenase A (LPMO9A) (EC 1.14.99.56) (AA9 family lytic polysaccharide monooxygenase 1) (LPMO1) (Cellulase LPMO9A) (Endo-beta-1,4-glucanase LPMO9A) (Endoglucanase LPMO9A) (Glycosyl hydrolase 61 family protein LPMO9A)
|
Talaromyces verruculosus (Penicillium verruculosum)
| 198,730 | 328 | 33,652 |
3D-structure;Carbohydrate metabolism;Cellulose degradation;Direct protein sequencing;Disulfide bond;Glycoprotein;Methylation;Monooxygenase;Oxidoreductase;Polysaccharide degradation;Secreted;Signal
|
GO:0004497; GO:0005576; GO:0030245
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30847851}.
|
SIGNAL 1..21; /evidence="ECO:0000269|PubMed:31672609"
| null |
PF03443;
|
IPR049892;IPR005103;
|
7A8V;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), Eurotiomycetes (class), Eurotiomycetidae (subclass), Eurotiales (order), Trichocomaceae (family), Talaromyces (genus), Talaromyces sect. Talaromyces (section)
|
lpmo1 LPMO9A
| false |
469 |
A0A482D308
|
MAKNTITKTLKLRIVRPYNSAEVEKIVADEKNNREKIALEKNKDKVKEACSKHLKVAAYCTTQVERNACLFCKARKLDDKFYQKLRGQFPDAVFWQEISEIFRQLQKQAAEIYNQSLIELYYEIFIKGKGIANASSVEHYLSDVCYTRAAELFKNAAIASGLRSKIKSNFRLKELKNMKSGLPTTKSDNFPIPLVKQKGGQYTGFEISNHNSDFIIKIPFGRWQVKKEIDKYRPWEKFDFEQVQKSPKPISLLLSTQRRKRNKGWSKDEGTEAEIKKVMNGDYQTSYIEVKRGSKIGEKSAWMLNLSIDVPKIDKGVDPSIIGGIDVGVKSPLVCAINNAFSRYSISDNDLFHFNKKMFARRRILLKKNRHKRAGHGAKNKLKPITILTEKSERFRKKLIERWACEIADFFIKNKVGTVQMENLESMKRKEDSYFNIRLRGFWPYAEMQNKIEFKLKQYGIEIRKVAPNNTSKTCSKCGHLNNYFNFEYRKKNKFPHFKCEKCNFKENADYNAALNISNPKLKSTKEEP
|
CRISPR-associated endodeoxyribonuclease Cas12f1 (Un1Cas12f1) (EC 3.1.-.-) (CRISPR-associated endodeoxyribonuclease Cas14a1)
|
Uncultured archaeon
| 115,547 | 529 | 61,517 |
3D-structure;Antiviral defense;DNA-binding;Endonuclease;Hydrolase;Metal-binding;Nuclease;RNA-binding;Zinc
|
GO:0003677; GO:0003723; GO:0004519; GO:0046872; GO:0051607
|
Evidence at protein level
| 5 | null | null | null |
PF07282;
|
IPR010095;
|
7C7L;
|
cellular organisms (no rank), Archaea (domain), environmental samples (no rank)
|
cas12f cas14a1
| false |
470 |
A0A482N9V7
|
MAANDSNNQTKPQLPEEPVAIVGSSCRFPGSSNSPSKLWDLLRQPRDVLKEFDPDRLNLKRFYHPDGDTHGSTDVTNKSYLLEEDSRLFDASFFTINPAEAAGMDPQQRILLETVYEAFESAGMTLEQLRGSLTAVHVGTMTNDYAGIQLRDLETIAKYNATGTANSIVSNRISYVFDLKGPSETIDTACSSSLVALHHAARGLLNGDCETAVVAGVNLIYDAASYIAESKLHMLSPDSQSRMWDKSANGYARGEGAAALLLKPLSRALRDGDHIEGVIRATGVNSDGQSPGITMPFAPTQAALIRQTYRRAGLDPVKDRPQYFECHGTGTPAGDPVEARAISEAFEPSADNPIYVGSIKTIIGHLEGCAGLAGVMKVILALKNRTIPPNMLFNELNPAIAPFYGPLQIPKKAMPWPELPENTPIRASVNSFGFGGTNAHVIIESFESSTPSSDSEKCEEGALGPLLFSAGSGASLLHTVQAYVQYLDQNPSVDLRDLSWLLQTRRSTHRVRTHFSGTSSDAILESMIKFVNNNEKTPSTEVGHQPKLINPKEVPGILGVFTGQGAQWPQMGKELIGKSPIFRRTLEDCDATLQALPSSDIPKWSLVKELMANASSSRVAEAAISQPLCTAVQLGLVNMLKASGLNFDAVVGHSSGEIAATYASGIINLQAAIQIAYYRGFHAKLAKGEKGQQGGMLAAGLTLDKAKQLCLREEFVGRLQVAASNAPQTVTLSGDLDAIEEVKKYLDEENVFARQLKVDTAYHSHHMKPCAEPYLKSLLACDIEVRKPTPGQCIWNSSVRGDTGLLKGDLSSLKGPYWVANMVQTVLFSQAVESSIWHGGPWDLAIEVGPHPALKGPTEQTLKAVYGVVPLYTGVLKRGASDVEAFSTAIGVTWSQLGPSFVDFAGYRKTFYESEPPTPKVIKDLPGYSWDHDKVYWRESRISKRYRTGRDQTHELLGRRTPDDNEFELRWRNVLKLSEMPWLRGHEVLEEVLLPGAAYVSIAVEASKHIATSKGKSIELLEVEDVDIQRPVVVPDNKEGVETLFTARLLPGSSSDKVLKALFSYYICNDQSTGTMVHTCSGRLSVHLGEAKEDVLPQRDPVPQNLVNINTDRAYGMFKDIGLNYTGVFRSIKESSRTLQYSAATGIWPEGSLSDKYLVHPAMLDVAFQTLFIARAHPASRLITSALLPSHIERIQVSPSVPILHARENSDEIKADFDCWVVHQTASSLTGDLNIYDKVSGKTFLQVEGLTTKMVGEQDASGDRPVFTKTVWGSDGSLGLDEPERDPVGDAEGLSLAEAAERMALFYMKRVVKEISPEERTKFQWYHQRMFEAFEQHLVNVGSGSHPMLKSEWLSDDSSIMDGLDRIHPTSIDLKLLRACGENMPDVVREKTQLLEVMSKDDMLNRFYMDNCAARINNDIAKVVKQISFKFPRANILEIGAGTGGTTWSILKDINDAYDSYTFTDISSGFFPKAAEKFSDFAHKMIFKTLDVEKQPSEQGFAENSYDVIVAANVLHATRSLETTLRNARSLLRPGGYLILMEITNPESLRTTFIFGGFSGWWLSEEPHRKLGPVVTAMDWDTVLNDTGYSGADMVVHDLAEESKHLTSLIVSQAVDDDFLRLREPLSNLADMSAPTESILVIGGKKLLTSKMVNEINKLLPKSWKRHISSAGSIDDIDINELKPGTEVISLQELDDPLFSTPMTAERMSTIQNLMMSAKTLLWVTTAGKSHAPRASMFHGIARIVPSELQHLQIQVLGLEAGSTPAIATRHCVEAFLRLRGTSDTTREMLWAIEPEVEIMADGQVLIPRVVPDETLNQTYNASRRVVTKTVDATDLAVEAVAGPTKMMLQTAELQAGERKTRIQVKYALHLPAMDGKGIYVVYGQRQDDTSSFVLAVSKSNSSIVDVDSKHAVSVSDNCEPATLNVLATYLIARAIATLSKQAGSVLLSEPEESLAAIVATETAKQGTQAYFLSSKKVSPVEWIKVHANASKRAIQKAVPHDVQLLIDCSGIEASGNAVMASMPLHCVERQLDAHLLFDALESTESKPESLLEEAYQYATQLITQEQVQSECEVFPASDLPLTNMLSLVHKKYVTDWQQRDSLVVSVPPLDLEGIFKADKTYLMVGAAGGLGLSICEWMIRNGAKNLIITSRKPQVDQNMIEEASRVGATVKVMAMDVSSKESVAEVVQQAQEIMPPIAGVCNAAMVLSDKMFLDMDVDQLNGTLAAKVYGTEHLDAVFADAPLDFFIVLSSTATTIGNIGQANYHVANLFMTSLVAQRRARGLAGSVIHIGYVADVGYVTRQDRERQLEQHFRNVRLMALSETDVHHAFAEAVRGGRPGNTVGSPDIIMGLEPASVPLEPERQTLWLSNPCFGHLVPSTLQNDSSQTGGTGNGSSVRRQVEEAQTEDEAVDAVLDGFCAKLEAILQLREGSVKENVQRAVIDLGIDSLVAVEIRTWFLKELGAEVPVVKILGGDTVLQICTTAAKKVMANAMKKKEEDAVAEEGGREAASKKEPAPAASAPTPAPVAPSLLDVPARAFEPDSATISEVGDDSAFSNKGSSSSATGASSPKELSDSESVPDTSKDQSHVRPETVRDERMSPAQARIWFLTKHLDDPSAYNMVFHYRVKGPLKTVRLRHALQVATGHHESLRTLFYSRLEDGQPMQGVMPASAYELKHVPGADEADLKKELALLKAREWDLENGRTFSVSVLSRAADEHDVVFGYHHIIMDVVGWYFFVRDLDRAYRMQPFDKKISGSYVDYSVMQLSQKNTAAASDDLAFWQKEFSTVPDPIPLLPIAAVSARPTDSGRKVSHHEYLELDPAQNLAVKETCEKLRISPFHFHVAVLRALIGGYTNIDDMCIGVVDANRGDERFAQTVGCFVNMLPVRVEAPSDATFADIARSASRKALMAFAHSSAPLDMILDAVKAPRSSETTPLFQVAVNYRTGGVWDLPMGDCQMKLSLTDGKDAENPFDISLGIAETGKGCVIEMHCQKTLYSSDATRTLLNTYLRLVDTFCKNTHVKLKDCVIHDQAKVSEALQIGKGPTTDFGWPSTLSHRVLETCLKSPKNAAIQFKGELLSYEQLASRIHLVAAAIVRAGASKGSRVAVLCEPSADAIISMLATLHIGGVYIPMDVSLPTARHAAMMNGGQPTLLLSHAATKHRVEDLVNETGSTISVLQVDTISSVEEKETVSCAAEPHNNAVLLFTSGSTGTPKGIMLSQANFVNHLALKTDRLQLGQENVLQQSSMGFDMSLIQMFCALANGGCLVIAPSEMRRDPVELTNLVHNSQISLTIATPSEYLAWLRYGTASLKDHTIWRHACMGGEPVSRQLKTEFWRLDLANLQLTNCYGPTEITAAATFETIRLDDQDDDNDRAQHAVGKALPNYSVRILDTAGRPQPVDHIGEICIGGASVALGYLGLPEQTKAKFTVDPVSGERLYLTGDKGKLLSDGTLLCLGRLDGDTQIKHRGLRIELQEVESALIQTANGLFSSAVVSARGSILVAHATISQSQAEPSESDLAKILSRLKLPQYFIPATIGILPTMPTTANGKLDRKAIASLPLPQKVTGEEGPQEKMNIREGELRLLWERVLPDTATTTPLGPSSDFFLCGGNSMLLMKLQAAIKESIGIEISTRVLYQASTLREMALCVDEQREEQADALEQHFDWQAETSLPKWLLDQIEDLPKTTKQPPKPNGIDILMTGATSFIGGRLLRSLVRSPSVRKVHCVAVLADEQDQLYQDEKVKCYTGSLLSSTLGLNNGERDQLARNVDVVIHAGSSGHCLNTYGSLRTPNLVSLQFLASLALPRSIPLLLLSSNRVPLLSGNTALPPTSVAAFPPATDGREGYTATKWASEVFLEKLVGAVQKKAPRPWVASVHRPCVVVSEHAPNSDALNAILRYSASMKCVPHLESATGYLDFASVESIVDSMAESAIEMATGNVTDQPSIRFQHHSGGVKVPIGDFKVHMENVYGGNFEEVHLEEWMHRAAAAGLDPLITAYMEGIIEAGAPIVFPYLGETV
|
Hybrid PKS-NRPS synthetase iccA (PKS-NRPS iccA) (EC 2.3.1.-) (EC 6.3.2.-) (Ilicicolin H biosynthesis cluster protein A)
|
Talaromyces variabilis (Penicillium variabile)
| 28,576 | 4,015 | 438,112 |
Ligase;Methyltransferase;Multifunctional enzyme;Oxidoreductase;Phosphopantetheine;Phosphoprotein;Repeat;Transferase
|
GO:0004312; GO:0004315; GO:0006633; GO:0008168; GO:0016218; GO:0016491; GO:0016874; GO:0031177; GO:0032259; GO:0140781; GO:1904091
|
Evidence at protein level
| 5 | null | null | null |
PF00698;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF08242;PF07993;PF21089;PF00550;PF14765;
|
IPR010071;IPR001227;IPR036736;IPR014043;IPR016035;IPR045851;IPR020845;IPR000873;IPR042099;IPR023213;IPR001242;IPR013120;IPR018201;IPR014031;IPR014030;IPR016036;IPR013217;IPR036291;IPR032821;IPR020841;IPR042104;IPR020807;IPR049551;IPR049552;IPR013968;IPR049900;IPR050091;IPR020806;IPR009081;IPR006162;IPR029063;IPR016039;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), Eurotiomycetes (class), Eurotiomycetidae (subclass), Eurotiales (order), Trichocomaceae (family), Talaromyces (genus)
|
iccA
| false |
471 |
A0A494BA31
|
MKLPGQGDFESSDAHENAHSEEPDSGLGPGPGLNGPSGIDIGESQVSKDPLLFIQLNELLGWPQALEWRETGRWLLFEEKLDMGAGRWSAPHVPTLELPSLQKLRSLLAEGIVLLDCQAQSLLELVEQVVSGESLSPELRGQLQALLLQRPQHHIQTMGIRPCRESNAFRKASRDEDAPLKHQNPLRQKLPAGAEAAAVLAGELGFLEQPLGAFVRLRNPIVLEPLTEMILPSRFFCLLLGPPTLGRSYHEMGRAAAVLLSDPQFQWSVRRASHLPDLLAALDAFLQEVTALPPGRWDRTARIPPPKYLPSQHKRFPSKLQEVTSLSRQSAALAEDKHHHGPHTPIPELQRTGRLFGGLIQDVRRKACWYTSDFLDALHPQCFSAVFYIYLATVTNAITFGGLLGDATEGAQGVLESFLGTAVAGAAFCLMAGQPLTILSSTGPVLVFERLLFSFSRDYSLDYLPFRLWVGIWVTAFCLALVATEASLLVRYFTRFTEEGFCALISLIFIYDAMGKMLNLIRAYPIQRPGSSAYGCFCQYPGTGGNTSEWTSAKLKDTEDILSVPGLVNASFLPPPECIRQGGHPLGPSCHTVPDIAFFSLLLFFTSFLCAIALKHIKNSRFFPSVVRKVLGDFSSVLAILLGCGLDTFLGLATPKLLVPTEFKPTLSGRGWLVSPFGANPWWLSVAAALPALLLSILIFMDQQITAVILNRAEYRLQKGAGFHLDLFCVAVLMLFTSALGLPWYVSATVISLAHIDSLRRESKACIPGEAPNFLGIREQRLTGLVVFVLTGVSIFLAPVLKFIPMPVLYGIFLYMGVAALSSIQFVKRVQLLLMPRKHQPDMLLLRHVPLSRVHLFTAIQLACLGLLWVVKSTPAAIVFPLMLLGLVAIRKALEWVFSPQELLWLDELMPEEEETIPENRSEPEHLFSGNDSEDSELMYQPKAPEINISVN
|
Anion exchange protein 4 (AE 4) (Anion exchanger 4) (Solute carrier family 4 member 9)
|
Mus musculus (Mouse)
| 10,090 | 952 | 104,989 |
Cell membrane;Glycoprotein;Ion transport;Membrane;Reference proteome;Sodium;Sodium transport;Transmembrane;Transmembrane helix;Transport
|
GO:0008510; GO:0016020; GO:0016323; GO:0022853; GO:0035725; GO:0045177; GO:0046541; GO:0140892; GO:0140900
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:12225984, ECO:0000269|PubMed:23610411, ECO:0000305|PubMed:34585968}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in the basolateral membrane of the cortical collecting duct (CCD)and submandibular gland (SMG) duct. {ECO:0000269|PubMed:12225984, ECO:0000269|PubMed:23610411}.
| null |
TRANSMEM 385..405; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 413..433; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 470..490; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 501..521; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 593..613; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 634..654; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 681..701; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 727..747; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 784..804; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 807..827; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 870..890; /note="Helical"; /evidence="ECO:0000255"
|
PF07565;PF00955;
|
IPR013769;IPR011531;IPR003020;IPR003024;IPR016152;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Glires (clade), Rodentia (order), Myomorpha (suborder), Muroidea (clade), Muridae (family), Murinae (subfamily), Mus (genus), Mus (subgenus)
|
Slc4a9 AE4
| false |
472 |
A0A498JQK2
|
MTSSEPASPEIEQQANSAPRRPRILLAASGSVAAIKFGNLCHSFSEWAEVKAVATRASLHFIDRASLPKDVILYTEEDEWSTWNKVGDSVLHIELRSWADILVIAPLSANTLGKIAGGLCDNLLTCIVRAWDYSKPFFVAPAMNTLMWKNPFTEQHIMSIDELGVSLIPPVTKRLACGDYGNGAMAEPSVIYSTVRLFFESRVQQSGNIVQQPV
|
Phosphopantothenoylcysteine decarboxylase HAL3 (PPCDC) (EC 4.1.1.36) (Halotolerance protein 3) (MdHAL3)
|
Malus domestica (Apple) (Pyrus malus)
| 3,750 | 214 | 23,535 |
Cell membrane;Coenzyme A biosynthesis;Cytoplasm;Decarboxylase;Flavoprotein;FMN;Growth regulation;Lyase;Membrane;Reference proteome;Stress response
|
GO:0004633; GO:0005737; GO:0005886; GO:0009651; GO:0010181; GO:0015937; GO:0071513; GO:1901002; GO:2000280
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:32761275}. Cytoplasm {ECO:0000269|PubMed:32761275}.
| null | null |
PF02441;
|
IPR036551;IPR003382;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), rosids (clade), fabids (clade), Rosales (order), Rosaceae (family), Amygdaloideae (subfamily), Maleae (tribe), Malus (genus)
|
HAL3 DVH24_008624
| false |
473 |
A0A499UB99
|
MATNNIVVLGAGVSGLTTAWLLSKDPSNKITVAAKHMPGDYDIEYCSPWAGANYLPVGAENSRVGQWERATWPHLRDIAQNHPEAGIHFQDTVVYNRTKDQGSTTGQWFSELVKPNPWYGKVLPNFRELSKDELPPGIDNANRFTSVCINTAVYLPWLVGQCRKNGVVFKRAVFKHVAEAANAHHSGQKADLVVNCTGLSSRKLGGVQDNTLLPARGQIVVVRNDPGLMCSISGTDDGDDEVTYMMTRAAGGGTILGGTYQKHNWDSLPDPNLAVRIMKRCIELCPSLVAPGQGIEGLDIIRHGVGLRPVREDGPRIEKELIDGVWVVHNYGHGGYGYQTSFGCATTAVEVVREALQQQKQRRDKARL
|
D-amino-acid oxidase (DAAO) (DAMOX) (DAO) (EC 1.4.3.3) (ReDAO)
|
Talaromyces emersonii (Thermophilic fungus) (Rasamsonia emersonii)
| 68,825 | 368 | 40,294 |
3D-structure;Disulfide bond;FAD;Flavoprotein;Oxidoreductase;Peroxisome
|
GO:0003884; GO:0005782; GO:0019478; GO:0019740; GO:0046416; GO:0071949
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:Q9HGY3}.
| null | null |
PF01266;
|
IPR006181;IPR023209;IPR006076;
|
7CT4;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), Eurotiomycetes (class), Eurotiomycetidae (subclass), Eurotiales (order), Trichocomaceae (family), Rasamsonia (genus)
|
DAO1
| false |
474 |
A0A4P8DY91
|
MTTTELIPPTIQVDEEEEEACMFAMQLASASVLPMVLKSAIELDLLESIAKAGPGAYVSPSELAAKLPSSQPDTPVMLDRILRLLASYSVLKCKVQDLPQGGVERLYALAPVCKFLTKNSDGVSMAPLLLMNQDKILMESWYHLKDAVLDGGIPFNKAYGMTAFEYHGKDPRFNKVFNLGMSNHSTITMKKILQTYNGFAGLKTVVDVGGGTGATLNMIISKYPNIKGINFDLPHVVEDAPSYPGVEHVGGDMFVSVPEGDAIFMKWICHDWSDAHCLSFLKNCYKALPQNGKVILAECILPEAPDSKLTTKNVIHIDVIMLAHNPGGKERTEKEFEALGKMAGFKSFNKVCCAHNTWIMEFLK
|
Esculetin O-methyltransferase (EC 2.1.1.-) (Bergaptol O-methyltransferase) (EC 2.1.1.69) (Isoscopoletin O-methyltransferase) (EC 2.1.1.-) (Scopoletin O-methyltransferase) (EC 2.1.1.-) (Xanthotoxol O-methyltransferase) (EC 2.1.1.70)
|
Kitagawia praeruptora (Peucedanum praeruptorum)
| 312,531 | 364 | 39,979 |
3D-structure;Methyltransferase;S-adenosyl-L-methionine;Transferase
|
GO:0008171; GO:0008757; GO:0009411; GO:0009805; GO:0016206; GO:0032259; GO:0042542; GO:0046983
|
Evidence at protein level
| 5 | null | null | null |
PF08100;PF00891;
|
IPR016461;IPR001077;IPR012967;IPR029063;IPR036388;IPR036390;
|
6IWT;
|
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), asterids (clade), campanulids (clade), Apiales (order), Apiineae (suborder), Apiaceae (family), Apioideae (subfamily), apioid superclade (clade), Selineae (tribe), Kitagawia (genus)
|
COMT-S
| false |
475 |
A0A4S8L4Q5
|
MESSTQTKPGSLIVVGTGIESIGQMTLQALSYIEAASKVFYCVIDPATEAFILTKNKNCVDLYQYYDNGKSRMDTYTQMAELMLKEVRNGLDVVGVFYGHPGVFVNPSHRALAIARSEGYQARMLPGVSAEDCLFADLCIDPSNPGCLTYEASDFLIRERPVNVHSHLILFQVGCVGIADFNFSGFDNSKFTILVDRLEQEYGPDHTVVHYIAAMMPHQDPVTDKFTIGQLREPEIAKRVGGVSTFYIPPKARKDINTDIIRLLEFLPAGKVPDKHTQIYPPNQWEPDVPTLPPYGQNEQAAITRLEAHAPPEEYQPLATSKAMTDVMTKLALDPKALAEYKADHRAFAQSVPDLTPQERAALELGDSWAIRCAMKNMPSSLLEAASQSVEEASMNGFPWVIVTGIVGVIGSVVSSA
|
Methyltransferase/ribosomally synthesized cyclic peptide dendrothelin A precursor dbihMA (Dendrothelin A biosynthesis cluster protein MA) [Cleaved into: N-methyltranferase dbiM (EC 2.1.1.-); Ribosomally synthesized cyclic peptide dendrothelin core peptide; Follower peptide]
|
Dendrothele bispora (strain CBS 962.96)
| 1,314,807 | 417 | 45,850 |
3D-structure;Methylation;Methyltransferase;Reference proteome;S-adenosyl-L-methionine;Transferase;Virulence
|
GO:0008168; GO:0032259
|
Evidence at protein level
| 5 | null | null | null |
PF00590;
|
IPR000878;IPR035996;IPR014777;
|
6MJF;6MJG;
|
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Basidiomycota (phylum), Agaricomycotina (subphylum), Agaricomycetes (class), Agaricomycetidae (subclass), Agaricales (order), Agaricales incertae sedis (no rank), Dendrothele (genus), Dendrothele bispora (species)
|
dbiMA dbophM K435DRAFT_765759
| false |
476 |
A0A4X1UM84
|
MPPQLSNGLNHSAKVVRGTLDSLPQAVRDFVESSAKLCQPDQIHICDGSEEENQQLLSHMEEEGVIKRLKKYDNCWLALTDPRDVARIESKTVIITQEQRDAVPIPRSGLSQLGRWMSPEDFEKAFNARFPGCMKGRTMYVIPFSMGPLGSPLSKIGIELTDSPYVVASMRIMTRMGSAVLDALGAGEFIKGLHSVGCPLPLKKPLVNNWACNPELTLIAHLPDRREIISFGSGYGGNSLLGKKCFALRMASRLAKEEGWLAEHMLILGVTNPEGQKKYFAAAFPSACGKTNLAMMNPTLPGWKVECVGDDIAWMKFDQQGNLRAINPENGFFGVAPGTSVKTNPNAIKTIQSNTIFTNVAETSDGGVYWEGIDQPLAPGIKLTSWKGTEWDPKDGEPCAHPNSRFCTPASQCPIIDPAWEAPEGVPIEGIIFGGRRPAGVPLVYEALSWQHGVFVGAAMRSEATAAAEHKGKVIMHDPFAMRPFFGYNFGKYLAHWLSMAQHPAAKLPKIFHVNWFRKDKDGRFLWPGFGENCRVLAWMFDRVQGKGGARLTPIGYVPEEAALDLRGLEAIRVSELFQVSKEFWEEEADEIHKYLEEQVNADLPYEIQSEVLALKQRISQM
|
Phosphoenolpyruvate carboxykinase, cytosolic [GTP] (PEPCK-C) (EC 4.1.1.32) (Serine-protein kinase PCK1) (EC 2.7.11.-)
|
Sus scrofa (Pig)
| 9,823 | 622 | 68,884 |
Acetylation;Cytoplasm;Decarboxylase;Endoplasmic reticulum;Gluconeogenesis;GTP-binding;Kinase;Lyase;Manganese;Metal-binding;Nucleotide-binding;Phosphoprotein;Reference proteome;Transferase;Ubl conjugation
|
GO:0000287; GO:0004613; GO:0005525; GO:0005783; GO:0005829; GO:0006094; GO:0006107; GO:0009617; GO:0018105; GO:0030145; GO:0031406; GO:0032869; GO:0043382; GO:0045944; GO:0046166; GO:0046327; GO:0046889; GO:0046890; GO:0051365; GO:0071333; GO:0072350; GO:0106264
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P35558}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P35558}. Note=Phosphorylation at Ser-90 promotes translocation to the endoplasmic reticulum. {ECO:0000250|UniProtKB:P35558}.
| null | null |
PF00821;PF17297;
|
IPR018091;IPR013035;IPR008209;IPR035077;IPR035078;IPR008210;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Laurasiatheria (superorder), Artiodactyla (order), Suina (suborder), Suidae (family), Sus (genus)
|
PCK1 PEPCK1
| false |
477 |
A0A4Y1WBN6
|
MGLHFSVLASGSTGNMLYVGTDEKKLLVDAGLSGKATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYANEKTWNAMEHLIGNIPTDQKFIFSVGDVKTFGDIEVESFGVSHDAAEPMFYAFHNNNRKLALITDTGYVSDRMKGVIKGANAFVFESNHDVEMLRMGRYPWSIKRRILSDVGHVCNEDAALAMADVITDETKHIYLAHLSLDNNMKELARMSVSQVLEEKGFGVGEAFEIHDTDPKMPTKIQYV
|
Exodeoxyribonuclease YycJ (EC 3.1.11.-)
|
Bacillus anthracis
| 1,392 | 264 | 29,293 |
Exonuclease;Hydrolase;Metal-binding;Nuclease;Reference proteome
|
GO:0004527; GO:0046872
|
Evidence at protein level
| 5 | null | null | null |
PF12706;
|
IPR001279;IPR036866;IPR052533;
| null |
cellular organisms (no rank), Bacteria (domain), Bacillati (kingdom), Bacillota (phylum), Bacilli (class), Bacillales (order), Bacillaceae (family), Bacillus (genus), Bacillus cereus group (no rank)
|
yycJ GBAA_5711
| false |
478 |
A0A4Y6HUD7
|
MTILSGTTAAPRVNGTTMNGHSKPHTNGVHLNGHAPKATTESPWPQSEEKTLLDKFVEAYYEFESYKSGQTVKVDGKTLSLAGVVAAARHHAKISLDDSASIKDKVVKSRKVIADKVASGASVYGLSTGFGGSADTRTDQPLSLGHALLQHQHVGVLPSSSQPLDVLPLSDPMSATSMPEAWVRAAMLIRMNSLIRGHSGVRWELIEKIAEIFDANITPVVPLRSSISASGDLSPLSYIAGTVVGNPSIRVFDGPAAFGAREMVPSAKALASHGIDPLPLASKEPLGILNGTAFSAAVGALALNEAVHFAMLAQVCTAMGTEALVGTRLSFEPFIHATCRPHPGQIEAARNIYNLLEGTTFASVHHEEVHIAEDQGTLRQDRYPLRTSPQFLGPQLEDILHAYVSVTQECNSTTDNPLIDGETGEIHHGGNFQAMAVTNAMEKTRLALHHIGKLLFAQCTELVNPAMNNGLPPSLAATDPSLNYHTKGIDIATAAYVSELGYLANPVSTHIQSAEMHNQAVNSLALISARATVNSLDVLSLLISSYLYILCQALDLRALQMEFVKGVEEIIREELSLLFASVVSPAELEALTSKVLSAAQTSLDTSGSMDAPARMKKMASTTTIPLFDFLTELTLPDAISSGIAMVSIPSFRSHLASRATALLDQLRRDYLSGQRGAAPASPYLNKTRMVYEFVRLTLGVKMHGSENYARFAKGLGVEDETIGQNISRIHEAIRDGKMQAITVAMFA
|
Phenylalanine ammonia-lyase 2 (EC 4.3.1.24) (PoPAL2)
|
Pleurotus ostreatus (Oyster mushroom) (White-rot fungus)
| 5,322 | 747 | 79,946 |
Cytoplasm;Lyase;Phenylalanine catabolism;Phenylpropanoid metabolism
|
GO:0005737; GO:0006559; GO:0009800; GO:0045548
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
| null | null |
PF00221;
|
IPR001106;IPR024083;IPR008948;IPR022313;IPR005922;IPR023144;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Basidiomycota (phylum), Agaricomycotina (subphylum), Agaricomycetes (class), Agaricomycetidae (subclass), Agaricales (order), Pleurotineae (suborder), Pleurotaceae (family), Pleurotus (genus)
|
PAL2
| false |
479 |
A0A4Z3
|
MALEGLRAKKRLLWRLFLSAFGLLGLYHYWFKIFRLFEVFIPMGICPMAIMPLLKDNFTGVLRHWARPEVLTCTSWGAPIIWDETFDPHVAEREARRQNLTIGLTVFAVGRYLEKYLEHFLVSAEQYFMVGQNVVYYVFTDRPEAVPHVALGQGRLLRVKPVRREKRWQDVSMARMLTLHEALGGQLGREADYVFCLDVDQYFSGNFGPEVLADLVAQLHAWHFRWPRWMLPYERDKRSAAALSLSEGDFYYHAAVFGGSVAALLKLTAHCATGQQLDREHGIEARWHDESHLNKFFWLSKPTKLLSPEFCWAEEIGWRPEIHHPRLIWAPKEYALVRT
|
Alpha-1,3-galactosyltransferase 2 (EC 2.4.1.87) (Isoglobotriaosylceramide synthase) (iGb3 synthase) (iGb3S)
|
Rattus norvegicus (Rat)
| 10,116 | 339 | 39,548 |
Glycoprotein;Glycosyltransferase;Golgi apparatus;Manganese;Membrane;Metal-binding;Reference proteome;Signal-anchor;Transferase;Transmembrane;Transmembrane helix
|
GO:0001962; GO:0005794; GO:0005975; GO:0006688; GO:0016757; GO:0030259; GO:0031982; GO:0032580; GO:0046872; GO:0047276; GO:0071287
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:17206613, ECO:0000269|PubMed:18630988}; Single-pass type II membrane protein {ECO:0000269|PubMed:17206613, ECO:0000269|PubMed:18630988}. Note=Also found in numerous large vesicles throughout the cytoplasm of the soma.
| null |
TRANSMEM 12..31; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255"
|
PF03414;
|
IPR005076;IPR029044;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Glires (clade), Rodentia (order), Myomorpha (suborder), Muroidea (clade), Muridae (family), Murinae (subfamily), Rattus (genus)
|
A3galt2
| false |
480 |
A0A509ADH4
|
MRMSKLYKNKEKENEKPSNEPPIKQDSLKRMSSKFLGNSLNSFDLSGKLEQVDEYLKKYPFIIEFGYKLGIKPSYIVVFGGSALFISLVLGWGAALICNLVGFAYPAYQSFKAVESQGHAETKLWLTYWVVFSLFFFIEYLIDIILFWIPFYYVIKLLFLLYLYMPQVRGAETVYNYIIRPILLKHEKTIDDTVHKISQTATNHLNQFTGNIAEKLVQEGVRRRNV
|
Protein YOP1 homolog (PbYOP1)
|
Plasmodium berghei (strain Anka)
| 5,823 | 226 | 26,311 |
Endoplasmic reticulum;Membrane;Reference proteome;Transmembrane;Transmembrane helix
|
GO:0005789; GO:0007033; GO:1990809
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:32432369}; Multi-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 73..92; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q12402"; TRANSMEM 95..113; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q12402"; TRANSMEM 124..140; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q12402"; TRANSMEM 144..162; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q12402"
|
PF03134;
|
IPR004345;
| null |
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Aconoidasida (class), Haemosporida (order), Plasmodiidae (family), Plasmodium (genus), Plasmodium (Vinckeia) (subgenus), Plasmodium berghei (species)
|
YOP1 PBANKA_0414500
| false |
481 |
A0A509AFG4
|
MNQLCVERNLSISTAYIKSKPKKYIERIKKKKSSNKSIKSQHKFEGSKIANKNNELKDIKSKDPKHYENHINKNTKHKDILLKSKRSDNFKFSRRGFILSFTGNLEDFYNLSEEPLGKGTYGCVYKATDKLLKIQRAVKVVSKKKLKNIPRFRQEIDIMKNLDHPNVIKLLETFEDEEQIYLIMDLCTGGELFDKIIKKGSFVEMYASFIMKQIFSVLNYLHIRNICHRDIKPENFLFYDKSTESLIKIIDFGLAAYFNDIDYEMKTKAGTPYYVAPQVLTGCYDYKCDLWSAGVLFYIILCGYPPFYGESDHEILSMVKKGKYNFKGKEWNNISEEAKDLIKRCLTIDSGKRINASEALKHPWFKKKKGSFNLDVKMDIHVLENFKNYALLLKLQKLAMTIIAQQSNDYDLQQLKTVFLYLDEDGKGNITKNQLKKGLENSGLKLPQNFDVLLDQIDSDGSGRIDYTEFLAAALDRKHLSKKLIYCAFRVFDVDNDGEITTAELAHILYNGNKKGSITQKDVNQVKKMIQEVDKNNDGKIDFYEFCEMMKLKY
|
Calcium-dependent protein kinase 3 (EC 2.7.11.1) (PbCDPK3)
|
Plasmodium berghei (strain Anka)
| 5,823 | 554 | 64,328 |
ATP-binding;Calcium;Cytoplasm;Kinase;Magnesium;Metal-binding;Nucleotide-binding;Reference proteome;Repeat;Serine/threonine-protein kinase;Transferase
|
GO:0004674; GO:0005509; GO:0005524; GO:0005737; GO:0030335; GO:2000147
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16430692}.
| null | null |
PF13499;PF00069;
|
IPR050205;IPR011992;IPR018247;IPR002048;IPR011009;IPR000719;IPR017441;IPR008271;
| null |
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Aconoidasida (class), Haemosporida (order), Plasmodiidae (family), Plasmodium (genus), Plasmodium (Vinckeia) (subgenus), Plasmodium berghei (species)
|
CDPK3 PBANKA_0408200
| false |
482 |
A0A509AH51
|
MLNMVDQKKGINNGSSTGVINNINGKIKNEFIFMYLIAAGGFSCVYKIKKKKSNKFYALKKIKFSANESNYEKKVLLNLREIECLRKLKNHPNIVSMNDFWLEVVQTLSKSKRERRGRRKEQQREQMGDKRREKRQQQRREKRKEQNTNTKKRVLITLSDHKKKKLKHLSCPENALNISNITNNERNVLKKDNWKNLILLKNFKKEKHNYNFNHQIELNKYNIMCLWKILNQMCVCKNEKKNIESLLPEQLIKNFKNFLFEKYILAIYDDCSYLNNKNNKTFIFFNNNLGNILHYLWWSYLGKNGKEKKNDIFKLLKYVSDNIIKDNTNLYNIILEFRHSLIELSRFPSNELGNVILNMRIPPNGSCELSEYISNMAKINKLEIYRNKNTLEKFIFKINCNNFDVYKMWINFKNDIIYEGKDVYKEHRKINLKRKIIKKKDIWIKGKKEKHLKNTIGNKCIKKINIYYEKPIHVFVYKSLTYKRQKHHKLWRKHYNNKKNWKYCLNKHENSKKYILFSKICRLMKTQMNKFKREEKFEKKKKIAITNIKVNYNDFEQDISSFNIQIYNKKNKNQLINRIKEQYEQLSISLNPYKLTYENENILRYNEHNYLFGLKNDNEKENIYNAIYFLNFYIWIRREINEYAIISKKRQICQNSRNYQSKKKFYIKRHNQKTYFFENIIFYHYIIMLFLDIEKYKNKFVSLFQYNLYRKLLKISKRIVLMLHRIETNVICIFLLKHFEDYFIRKGIHIVQDKSDRSNKGDEIGIHKMVKIWKSMIAISLIFGKKMYKKKKNIFNFFIELFLNNIQINIFKKFEILYLIIYFYNYFEKSKQFDIEGIGDIIYVWLSLINLFYDDKGKCIKILSKIFAKLNKKLYYVYWGKLYIIMNWTTIVDTIFIRNVLSINREGNYYWVIIVLKMINYFVNVAYTLTRMDIFFIKVMIKFYTRIGSAAATNSVSKNSYNEIFNNIFTLNFMNYIIYNSYFENEKKNYDIYTKYAILFIYCFIIQAYYFDTLFNIRSLESNEIANNLFPGYNYSYKNILLFYERLGRVIKNSNNTKICKYMWRKFINMWSNSIVIKENIISCLTTSRHIYFNILMNFMKIYCLDNILHIKKKKKKMNTPIVLTSKNDLKKWKDCELTKNPKSVKKGILIKKKNRNNNKKYKKKLKETHFIYNIKKVLFKKLVNINIETILYEQNGQCYILVFGSVIKKKNGQIKVKDTKIVRDINIIRDYRIYFYNYLEYFYKNNAHISDNINLIYARKWPYNNKNAVKQFCPYFDKIKDGNRKDIVSLYGNKILVKQNFSKIGNKIKNKKNNLCKKKMRTQKSIYNSNYWREKKENKLLNGNVNIIKKYKSEKIKKKELENFFDNIVYSSENDDFKIIFENATNSNACSTVDLASPNELNTKRNNINKKLKFFKHKKNSKKQKNYKNHKSHKKIFFKSVNNANRFFVTNVEPNPIMSNNHQIADSNDIYNNFSIQKKYEYNHKNCGNIYNTKDCDENDSSYICFLINEHEGQVLSHRHKELYKNMLGMERGNILYRDNACKLKDDFSCLHDQCDNSMIKACGTNELIKESTKIKRENMDKINKMNEVNQHISLETLKYKCSFKKIDKNLIQNKKKIIIRKICQINKTFYFKYNKINDKKRIYFDSVLCKSERHKTYKKRNENIKVILLKTLKGESNEYVLTTYLTEIYSDNINDPFENSRKKINSNEIFYQKTFDMYCIEDEGEVYEEQKRVNKNNKKKKYINEMIKMDTIRTDFEDNFTNSYNKKCNILKMASNINNKNNSGKKERDIKRQFLITNKKKHENNIKIFYNLFKLEESNVNSNPQTNPYYETVIHDNEDNIFYCLYKYIQQQVYRYCNCDIDEYTSNCIDKNVNKWEWYGFIKENENYDKIKTEINSNSFYNCREKHNICNSYNSVYQLEFRKLGNASKEKNFEEKKKIIKIEFRKSFNNFKLPSLLCILKWDNFFKPHFIIRCDNFLHTYNIYFDFFILLMNLFHKGEGSNLYRFNSNKSIIYNPYLSHQIYMVTKYFISNVHKINNKLPIHLENDILEIYSYNRFLTIPNKCSFKNCGNDNNNYDQRSKKHYFTKCGILNTEKVKPSKKRRIGWDGQRQRKRKDIINTLNEENQNMFCKNKEKKEENYKKIDTNISQFSEKNPVSNIDNEKNKQNFIKNKKYKFNLYIRMEYCKDTIENYINRRTRINIKRNIEIINMIIMGLNYIHNNNIMHRDLKPSNIFISNNDIVKIGDFGLASYDYLDDHKINTTKEEEIQKDLIINKNCDKIFFCNKKKLFSNYNSVFPLENGQISDVHNTKGDYNESSISKSKKFAIQNKNRNLRSCKRIFQWWSTIGELNILSKNRRRLTKFKSGSNTIHIRKSTLDENIIVRHANKCHNLSFSQNREHIDRNRMKKCNIIKNHIIKSNKSEKMNISMNVFLRCTKTRRYFTDEDKSVETRKKCSKTSEEENGNICDTKKKKNDIGEKMDKNKIAAQKKKKKKENKHPIGRRSTNSSISSAIVVKRNAYCRLEIEKYFLSKSFQNCRSNKKKKYINIKTIKNKFCSASNKNFGAKWMRIYRKGLHHDDIQEKSADQTTEQMGGCNKTVASDFSSNLKNKKESINHTLGIGTKLYSAPEQLEGNKYTKSVDIFSLGLIIIDLFIKTETNMERTQILCNARERILPDLLIKKHPNVASLCKKMLSLDYKSRPTSAQLYNKIISAGDIFLPDKCP
|
Eukaryotic translation initiation factor 2-alpha kinase 2 (PbeIK2) (eIF2alpha kinase 2) (EC 2.7.11.1)
|
Plasmodium berghei (strain Anka)
| 5,823 | 2,724 | 327,427 |
ATP-binding;Coiled coil;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Protein synthesis inhibitor;Reference proteome;Serine/threonine-protein kinase;Transferase;Transmembrane;Transmembrane helix
|
GO:0004694; GO:0005524; GO:0010998; GO:0016020; GO:0017148; GO:0018105; GO:0085015
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 25..45; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 674..694; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 719..739; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 801..821; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 833..853; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 877..897; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 909..929; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 997..1017; /note="Helical"; /evidence="ECO:0000255"
|
PF00069;
|
IPR011009;IPR050660;IPR000719;IPR008271;
| null |
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Aconoidasida (class), Haemosporida (order), Plasmodiidae (family), Plasmodium (genus), Plasmodium (Vinckeia) (subgenus), Plasmodium berghei (species)
|
eIK2 PBANKA_0205800
| false |
483 |
A0A509AHB6
|
MGCNQSKSANDVRGNKVNHVNSKKKNNKREDTNDGEEIAINPGMYVRKKEGKIGESYFKVRKLGSGAYGEVLLCKEKNGHSEKAIKVIKKSQFDKGRYSDDNKNIEKFHEEIYNEISLLKSLDHPNIIKLFDVFEDKKYFYLVTEFYEGGELFEQIINRHKFDECDAANIMKQILSGICYLHKHNIVHRDIKPENILLENKNSLLNIKIVDFGLSSFFSKDYKLRDRLGTAYYIAPEVLKKKYNEKCDVWSCGVIMYILLCGYPPFGGQNDQDIIKKVEKGKYYFDFNDWKNISDEAKELIKLMLTYDYNKRCTAEEALNSRWIKKYANNINKSDQKTLCGALSNMRKFEGSQKLAQAAILFIGSKLTTLEERKELTDIFKKLDKNGDGQLDKKELIEGYNVLRNFKNELGELKNVEEEVDNILKEVDFDKNGYIEYSEFISVCMDKQILFSEERLRRAFNLFDTDKSGKITKEELANLFGLTSISEKTWNDVLGEADQNKDNMIDFDEFVSMMHKICDHKTF
|
Calcium-dependent protein kinase 1 (EC 2.7.11.1) (PbCDPK1)
|
Plasmodium berghei (strain Anka)
| 5,823 | 523 | 60,809 |
3D-structure;ATP-binding;Calcium;Cell membrane;Cell projection;Cilium;Cytoplasm;Flagellum;Host cell membrane;Host membrane;Kinase;Lipoprotein;Magnesium;Membrane;Metal-binding;Myristate;Nucleotide-binding;Palmitate;Phosphoprotein;Reference proteome;Repeat;Serine/threonine-protein kinase;Transferase
|
GO:0004674; GO:0005509; GO:0005524; GO:0005737; GO:0005886; GO:0020002; GO:0020005; GO:0031514; GO:0045727; GO:2000147
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P62344}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}. Cell membrane {ECO:0000269|PubMed:22817984}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}; Cytoplasmic side {ECO:0000250|UniProtKB:P62344}. Parasitophorous vacuole membrane {ECO:0000250|UniProtKB:P62344}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}. Cytoplasm {ECO:0000250|UniProtKB:A0A2I0BVG8}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:A0A2I0BVG8}. Host cell membrane {ECO:0000250|UniProtKB:P62344}; Lipid-anchor {ECO:0000250|UniProtKB:P62344}. Note=Calcium and/or autophosphorylation does not affect membrane localization. {ECO:0000250|UniProtKB:P62344}.
| null | null |
PF13499;PF00069;
|
IPR050205;IPR011992;IPR018247;IPR002048;IPR011009;IPR000719;IPR017441;IPR008271;
|
3Q5I;
|
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Aconoidasida (class), Haemosporida (order), Plasmodiidae (family), Plasmodium (genus), Plasmodium (Vinckeia) (subgenus), Plasmodium berghei (species)
|
CDPK1 PBANKA_0314200
| false |
484 |
A0A509AJA5
|
MKSITFFVFNICSILALLSHCEDNDIYSFDIVNETNWLKIAKNIFKGKSPSNFTIIPFNNTGSSNDNESNKEESVLLIRKKIKSNKNHDSSIISGDTVNGDISDLNYTASNFSDNSEDIEDNQKYPTTSYNSFNHLNSNIAFNEESEYIEINSESDLENKIKDINIKSNLEENNTMNESGKVDSKYELTGDEKCGKSLKLGNISNQTNQETITQSLSVGEILCIDLEGNAGTGYLWVLLGIHKDEPIINPENFPTKLTKKSFFSEEISVTQPKKYKIDEHDSSKNVNREIESPEQKESDSKPKKPQMQLLGGPDRMRSVIKGHKPGKYYIVYSYYRPFSPTSGANTKIIYVTVQ
|
Falstatin (Cysteine protease inhibitor) (PbICP)
|
Plasmodium berghei (strain Anka)
| 5,823 | 354 | 39,974 |
3D-structure;Cytoplasmic vesicle;Host cytoplasm;Protease inhibitor;Reference proteome;Secreted;Signal;Thiol protease inhibitor
|
GO:0004869; GO:0005576; GO:0020009; GO:0030133; GO:0030430
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20361051}. Cytoplasmic vesicle, secretory vesicle, microneme {ECO:0000269|PubMed:20361051}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:20361051}. Host cytoplasm {ECO:0000269|PubMed:20361051}. Parasitophorous vacuole lumen {ECO:0000269|PubMed:20361051}. Note=During the asexual blood stage, localizes to the parasitophorous vacuole (PV) and to exomembrane structures beyond the limits of the PV (By similarity). Localizes to punctate peripheral structures in schizonts and rings (By similarity). Released after host erythrocyte rupture (By similarity). Secreted by gliding sporozoites (PubMed:20361051). Localizes partially with micronemes at the apical pole of sporozoites (PubMed:20361051). Released into the host cytoplasm by sporozoites (PubMed:20361051). During the host liver stage and in late schizont and cytomere stages, localizes mainly to the PV, but is also present in the parasite cytoplasm (PubMed:20361051). After completion of daughter parasite development, localizes to the host hepatocyte cytoplasm following the rupture of the PV membrane (PubMed:20361051). {ECO:0000250|UniProtKB:Q8I333, ECO:0000269|PubMed:20361051}.
|
SIGNAL 1..21; /evidence="ECO:0000255"
| null |
PF12628;
|
IPR036331;IPR024321;
|
3PNR;
|
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Aconoidasida (class), Haemosporida (order), Plasmodiidae (family), Plasmodium (genus), Plasmodium (Vinckeia) (subgenus), Plasmodium berghei (species)
|
ICP PBANKA_0813000
| false |
485 |
A0A509AKL0
|
MDDDEIIPKKNHPSNERNKKKAILSHEDFTGEDSLMENHLELRDKLTEDIVTIKASLKNNLVCSTLNENEILALSNYMQFFVFKSGDMVIKQGEKGSYFFIINSGKFDVYVNDKKVKTLTKGSSFGEAALIHNTQRSATIKAGTNGTLWGVQRSTFRATLKQLSNRNFNENRSFIDSVSVFDMLTEAQKNMITNACVIQNFKPGETIVKQGDYGDVLYILKDGKATVYINDEEIRVLEKGSYFGERALLYDEPRSATIIAKEVTSCASICRKLLNVVLGNLQVVLFRNIMTEALQQSEIFKQISPDQLNDLADTAIVRDYPANYNILHKDKIKSVKYIIVLEGKVELFLDDESIGILTRGKSFGDQYVLNQKQKFKHTLKSLEVCKIALITESCLADCLGNNNIDASIDYNNKKSIIKKMYIFRYLTDKQCNLLIEAFKTTRYEEGDYIIQEGEVGSRFYIIKAGEVEIVKNNKRLRTLGKNDYFGERALIYDEPRTASVISTVNNLECWYVDKSVFLQIIEGPMLAHLEERIKMQDTKVEMSELLTERIIGRGTFGIVKLVLHEPTKIRYALKCVSKKSIIELNQQNNIKLEREITAENDHPFIIRLVRTFKDSKYFYFLTELVTGGELYDAIRKLGLLSRSQAQFYLGSIILAIEYLHERSIVYRDLKPENILLDKQGYVKLIDFGCAKKIHGRSYTLVGTPHYMAPEVILGKGYGCTVDIWAFGVCLYEFICGPLPFGNDQEDQLEIFRDILTGQLTFPDYVTDTDSINLIKRLLCRLPQGRIGCSINGFKDIKENSFFADFDWDRLAGRLLEPPLISKSETYAEDIDVKQIEQEEEDNANTEIDDENWDIDF
|
cGMP-dependent protein kinase (EC 2.7.11.12) (PbPKG)
|
Plasmodium berghei (strain Anka)
| 5,823 | 856 | 97,901 |
ATP-binding;cGMP;cGMP-binding;Cytoplasm;Endoplasmic reticulum;Kinase;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Reference proteome;Serine/threonine-protein kinase;Transferase
|
GO:0004691; GO:0004692; GO:0005524; GO:0005789; GO:0005952; GO:0030553; GO:0046872
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19779564, ECO:0000269|PubMed:27425827}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8I719}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8I719}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8I719}. Note=Predominantly localizes to the cytoplasm during schizogony. {ECO:0000250|UniProtKB:Q8I719}.
| null | null |
PF00027;PF00069;
|
IPR000961;IPR002374;IPR018488;IPR000595;IPR018490;IPR011009;IPR000719;IPR017441;IPR014710;IPR008271;IPR035014;
| null |
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Aconoidasida (class), Haemosporida (order), Plasmodiidae (family), Plasmodium (genus), Plasmodium (Vinckeia) (subgenus), Plasmodium berghei (species)
|
PKG PBANKA_1008200
| false |
486 |
A0A509ALD0
|
MEIPNEEIKFLKKEDIKNINLNGMNKKERYEIWKKIPKVELHCHLDLTFSGKFFLKWVRKYNLQPNMTDDQVLDHYLFTKEGKSLAEFIRKAISVSDIYRDYDILEDLAKWAVIEKYKEGVVLMEFRYSPTFVSSSHGLDIELIHKAFVKGIKNATEMLNNKIYVALICISDTGHSAASIKHSGDFAIKHKHDFVGFDHGGREIDLKDHKDVYHSVRNHGLHLTVHAGEDATLPNLNTLYTAINILNVERIGHGIRVSESEELIELVKKNNILLEVCPISNLLLNNVKSMDTHPIRKLFDAGVKVSVNSDDPGMFLTDINDNYEKLYIHLNFTLEEFMTMNNWALEKSFVNDDIKSKLKTMYF
|
Adenosine deaminase (EC 3.5.4.4) (S-methyl-5'-thioadenosine deaminase) (EC 3.5.4.31)
|
Plasmodium berghei (strain Anka)
| 5,823 | 363 | 41,989 |
Hydrolase;Metal-binding;Purine salvage;Reference proteome;Zinc
|
GO:0004000; GO:0005829; GO:0006154; GO:0006166; GO:0009168; GO:0009897; GO:0043103; GO:0046103; GO:0046872; GO:0060169; GO:0090614
|
Evidence at protein level
| 5 | null | null | null |
PF00962;
|
IPR006650;IPR001365;IPR006330;IPR032466;
| null |
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Aconoidasida (class), Haemosporida (order), Plasmodiidae (family), Plasmodium (genus), Plasmodium (Vinckeia) (subgenus), Plasmodium berghei (species)
|
ADA PBANKA_0513600
| false |
487 |
A0A509AM03
|
MRTVFIYACIISLVLRTIPAHNDLMSKEKENKEKDVHKIIEDLRFLEKVDAILENSNMTIDDVKADADAYNPDEDAPKEELNKIEMEKKKAEEEAKNSKKKILERYLLDEKKKKSLRLIVSENHATSPSFFEESLIQEDFMSFIQSKGEIVNLKNLKSMIIELNSDMTDKELEAYITLLKKKGAHVESDELVGADSIYVDIIKDAVKRGDTSINFKKMQSNMLEVENKTYEKLNNNLKKSKNSYKKSFFNDEYRNLQWGLDLARLDDAQEMITTNSVETTKICVIDSGIDYNHPDLKGNIYVNLNELNGKEGIDDDNNGIIDDIYGVNYVNNTGDPWDDHNHGSHVSGIISAIGNNSIGVVGVNPSSKLVICKALDDKKLGRLGNIFKCIDYCINKKVNIINGSFSFDEYSTIFSSTIEYLARLGILFVVSSSNCSHPPSSIPDITRCDLSVNSKYPSVLSTQYDNMVVVANLKKKINGEYDISINSFYSDIYCQVSAPGANIYSTASRGSYMELSGTSMAAPHVAGIASIILSINPDLTYKQVVNILKNSVVKLSSHKNKIAWGGYIDILNAVKNAISSKNSYIRFQGIRMWKSKKRN
|
Subtilisin-like protease 1 (EC 3.4.21.62) (PbSUB1)
|
Plasmodium berghei (strain Anka)
| 5,823 | 599 | 67,314 |
Calcium;Coiled coil;Cytoplasmic vesicle;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Protease;Reference proteome;Secreted;Serine protease;Signal;Zymogen
|
GO:0004252; GO:0005576; GO:0006508; GO:0030133
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8I0V0}. Parasitophorous vacuole lumen {ECO:0000250|UniProtKB:Q8I0V0}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:30941868}. Note=At the schizont stage, in merozoites, localizes to dense secretory granules called exonemes (PubMed:24348254). Just prior to egress secreted into the parasitophorous vacuole (By similarity). In male gametocytes, localizes to secretory organelles called male osmiophilic bodies (PubMed:30941868). {ECO:0000250|UniProtKB:Q8I0V0, ECO:0000269|PubMed:24348254, ECO:0000269|PubMed:30941868}.
|
SIGNAL 1..20; /evidence="ECO:0000255"
| null |
PF00082;PF18213;
|
IPR000209;IPR036852;IPR023827;IPR022398;IPR023828;IPR050131;IPR015500;IPR041089;
| null |
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Aconoidasida (class), Haemosporida (order), Plasmodiidae (family), Plasmodium (genus), Plasmodium (Vinckeia) (subgenus), Plasmodium berghei (species)
|
SUB1 PBANKA_1107100
| false |
488 |
A0A509AMC3
|
MYNKGINICLNEDNKCIILLHIIFNKCIVSFVASHILVEGKICFLNRIKNSKIFRRFGNINNHRRNNVKEYYKFVGRINKGKEKRNKCRIKLHRFYEYAKSYILKQIKWVLNKSKYIYFNIIYHLKTICYLKNAFFLQYTQRKYFSQNIENYIINSLPKHIQSFNPIKWSYYNNNEYASNYIIINNLNFIKYKNKYEKQYDIEMEEDINCKGANDIFYNSYNYCNNNNSNSKCDEKIEKNIVDKNIENKYNIKEYDKTNKSILFPIEEEFKKIIQIENNIERNYMVPNESNKNILYNIKNILEKIRNIEAISNINNYIDMKNTIESYKLNPDKCKEILHKDKDFRNKSKLCLSCFHNIIHKIIYYSKMENISFSDMYKQLLTNYNNTSCEYCNLINNSINSNNDFLSLYNDKNMYNWKNCEKNKFETLENEISCWNFNSSYGNHFQHIQKNSKIYRRILNEENEKAFNNIVGRNEMENDELYKRIHTENNYANQFTENNVDFGVYSDLREYNNGNEKYMLDENEMDQIIDEEVKKQEKNQNLNNMDFNNVNKKYNQLKDDNIIIFNKNNMHNNLYSNGLNDSNLEKNNILFPYEKYNNLDKNEMNLTKYSQNKQFYGQYKYDEAIYKYDLIVLDTSGYIYKVSTDGTYHWKYRIVKNIQYYINYEEENKIENYYNAFKKNNGKINMTHKDILRKNDYEQYHKLKLRAMKKLQYNNFIDVFNSNYKKNYPTYLNEQITEKDDIYKKKNYNYEKSKKKSKNKNAMKKLLSDYSGDLFYVDENNEAIPININIKDVVNNSPFKSTLFPNILFIGSRQSSIVNLDFDTGYVIKKYEENYDDLVKEKQKALPNKYEKFINKNSNVLHDKLEKYLDHSIDINDKNYYVNEEKDDLDKDYTIIDGKVAENNQQLDNIDLYNNEIETENNNGINHLLLIDGKGQIEEQSPNNGNKIIKGDVSNMTDECGTENCLSKHSKEEIEIANNKFNKNNKDKLLIQRTKIKNKKHFLMGKWYMNISNNNLLNINSSVLGINKKKRNSKKGENRNKKRKTQKRQLQISLVKWVIKAVDETSLKQKWITSWVDVGSIFITDSHKQDLSFINSLIDIDGNKLILRTLENNKVNKPYNNTISKNIEDAERNELEFASENYKNDIPNEIDEHNNKMGRNMNKLNSNIKSKIFIFSKEISSVFALQYKSKTNIFTLDTILKQNEKLFPEYDNIKPYSYNLLNLKNNSNALLLPFSSSNDYLKNNDKKNLPWNFNYDENGTNANNSIAFQNYNNFIVQRLNNISINITSIEKDLRYLLLSIIFVFDKHKKIPMNYIFQMKTLLHEYQKTKQKFMICLRGLNHNKNINIFSNHNDIRDTDIKHYGYNDYDYINKEMDAIDEPIHICEYTNKFIDLSFEGKEKCIDYCSMLNIWDKIFNNYTNHDDCLLLSNLYRILNSTYPLTNKDFNRIIDGIFLKNNESMLIKRRRKPNEGSRNHDLTEFSSQKHKKSWYWNIFYAITLVIVIPFIFIYRLFKKQTNNKNNNKIIMRKKKITDYDEDSNDTYDDELLNIDKVLLKRNKRKLANILKENGISSLNKTELEKYMKKSLKKAQDIEQLTLVDILARHARDSDSDSNFYDIHDGKYNLYPYYYSGQESKYSLPNMHYIDLSKSNSGETNKYDLNGNNLFYMHRRRAASQDVTYKQSFIVKKRVRSNYKLGNKYNKRNYTDYEKDKKNSSIKERNINEKAFDKSDFINFLKNFNKKFMKKNPFVDHLMKNNKTDSNNEFNNDNKEKSKYLYNEKYNLNSADEENKSPYAKKYSDEKKNRSKSSKYIENTQSNNNDNTNGNMNVGNHINNDKMNNKGSSARNLSIIQTSHIPYDAPLADFLENGRFTRTFQNISLIGQGGFGSVYKVSHRLEPGSPTYAVKFIYLKVSSLDNVNSRRYFREIAANRDIYSKHVVRYYTWWCEEPQFLPMDIIPKEIQNTLKKNKDPFKKVCNKNKKDNDYSSDCTVSSGENNKFDLKNYKKVITKKNSPKLKFYSDNDTPYNKRKNINQKNSFLNDKNLSDNIYIIENNKKKKKKKKKKKKIIYKEKKKGNIGINEDNKYSTFYEQNNPNNFSSTLQEYDPFGYGYLSENERDLIVFADNDESNGSGHSKKNDNDERKSLNNQNGIYNTGGDISKNGNVIHDDSNMLACQQSDKNSMTIKNTQGTSINGTINRNTISDETGTQGTNNNPKYSIDYHIDAIVKPKGESFTWVEKSPSNKYKKDSLDIINRNRKLIEEKNKKEKGQEKEKYKLKMNGELEKKENANKIKYYKKKNVGPEFSIVLLLQMEFCKGFTLRRWLDRSSRSDKPLYFTYGDKNTNHPLEFDLFKQLIKGLKDIHSTCFIHRDLKPENIFVDLDTYILKIGDLGLVRFIEEKKRENDLNNIDNFKDNIYTEINHNTITSQISLKGQMIGTPGYTAPEGGALCDEKADIYSAALILLELLCPRFNTIMERYKTLNDFRNYYTVPDYVKIHLNPWYILMLQMSKPNPADRPSAADLYNKIKVLLDPHLTDFTFSFNDINNDDLEYTGNRNVINSTNPNGDIKENVNQNNLVDDKGNNNIINGNEVDH
|
Eukaryotic translation initiation factor 2-alpha kinase PK4 (eIF2alpha kinase PK4) (EC 2.7.11.1) (Protein kinase PK4) (PbPK4)
|
Plasmodium berghei (strain Anka)
| 5,823 | 2,591 | 306,873 |
ATP-binding;Endoplasmic reticulum;Kinase;Membrane;Nucleotide-binding;Phosphoprotein;Protein synthesis inhibitor;Reference proteome;Serine/threonine-protein kinase;Transferase;Transmembrane;Transmembrane helix
|
GO:0004694; GO:0005524; GO:0005634; GO:0005789; GO:0010998; GO:0017148; GO:0018105; GO:0018107
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29241041}; Multi-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 17..37; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1489..1509; /note="Helical"; /evidence="ECO:0000255"
|
PF00069;
|
IPR050339;IPR011009;IPR000719;IPR008271;
| null |
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Aconoidasida (class), Haemosporida (order), Plasmodiidae (family), Plasmodium (genus), Plasmodium (Vinckeia) (subgenus), Plasmodium berghei (species)
|
PK4 PBANKA_1126900
| false |
489 |
A0A509APT1
|
MKVTFGNEYIKNFLGEFIGTFVLMFLGEGTTANHFAVPIKNDWLRLCIGWGLGVFFGILISAKLSGAHLNLAVTVGLSTIKKFNYKQIPLYFAGQLLGALSATASVYGLYYGFVSDQTIPKFSWETGKHANVHIASAFMHEFILTGILLLIILSVTDENICGKFHVLKVSSIVGLAIICIGISFGGNTGFALNPSRDLGARILSAIAYGFEAFTRDKCYFWIPLIAPIIGSIIFCQIYDKIVAPLVVISEHDKGALEI
|
Aquaglyceroporin (PbAQP) (Aquaporin-1)
|
Plasmodium berghei (strain Anka)
| 5,823 | 258 | 28,141 |
Cell membrane;Membrane;Reference proteome;Transmembrane;Transmembrane helix;Transport
|
GO:0005886; GO:0006833; GO:0015204; GO:0015250; GO:0015254; GO:0015793; GO:0044002; GO:0071918
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17284593, ECO:0000269|PubMed:29330527}; Multi-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 17..37; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 46..66; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 88..108; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 134..154; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 172..192; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 218..238; /note="Helical"; /evidence="ECO:0000255"
|
PF00230;
|
IPR023271;IPR000425;IPR050363;
| null |
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Aconoidasida (class), Haemosporida (order), Plasmodiidae (family), Plasmodium (genus), Plasmodium (Vinckeia) (subgenus), Plasmodium berghei (species)
|
AQP PBANKA_0915600
| false |
490 |
A0A509APX1
|
MKETDKIKSEVLNLMQLDGKREHINKNNKLYRKVIINPTSEDDLQKFCKNYFRIYQFSLYNFIRRLISLDAVIVYTLFMTVYIFSEISQGITKKYLFVDTAISLFLNIGILVVIESLFELKLLKDIKNANSQHYLRIVPKMSYFEKVMTKDIKVGNIIRVFQGEEFPADVVILYSKKNTNAVVDSFKIDGLYNKSIKYPVEKYKIDRDYLKMLSEINGVIKCELPNKNVFCFQGTYKLDKHPRSLHLSYENFALQSSILKGAEYIDGVVVYTGADTKKNLNIPRKIEENMTFCIKMNNVVYYLIFMYILFVLLSIIIKAIFYRKGKLLENSNDTFFTVLEDFIGLYILVLPVMLYSEKSLIYIIQSLKIERDTRMNKDENSNNTKVFNKNKNDALGTVDIIATARNGVLVNKKEILVSCTINNVLYSKKKFIISDEFLKLPSLNILDAERTNVSELLNLDERIFKDPENIFFPSRDFNNFLKILGNNTNPIYDPINGDFSKILKEIYRNYLNEEFLYKKIKLSSSVKSLLDNGYNQFLEDCESSYDCKEIIEDGLKNNEQSEKIEEFILGICACNRIIIYNEKFGDIEMKDNINEKSTSEHMNYDKDREVENIESENKYAVDSDGEENMNTIEHEDICLFNTSKNIGFHIYCYKKCLFFYNLKNICKEYYIICFHDFLRSNNYTMCILKNKKELDKGILYIRGYDFNILPYLCKNKNDINKIKKTIKIHTANYLKVILICKKNITNEDIAKYIYLKSVRSKFSFKFFDIIKTFFLYDLECIGIIGLKNDLNDGVVETFNDINNFDIRSWIFTNDSSKNTYLTALQCNLITPNSNLFIINFLNPDHSDEETVANYLFNNFLFSMENMKSRSYAIAINEMSLKNIMRSRYALKVFLCIIMRATVVLFCKLNNETKGKIISKFLSYTTPKLTVLGVGSTLNDAYLLKNTTISVCLTLNKQVNALYSISDYAMEEFKYVGELLILGRLNRFSLCRAFLWIIYLKVMIGSFYFFHNFDNFFSGSSISSILYSQTAFAIFHYSLIVAFASYEIDIPYKFIRNFPYIYQLARRKYFLNNTIIFLNIVESIFSSFISYYILRGNLFNLITHRKFTFHIFVLNFFLISEKILLFSKTWHIFFFIMTIIIVSILFIYINIYTLVDCLITGKCEFSLFDPEDSYFWISLLPILYINFIIDKFMKFVKNKIYPDITYHLSNTLKIETQEKFATNNKREEVITDKNIEKLAPVPKSYIIKEDNAYYGKSKKNKYIFDTLRKIIDIKIKYRNQQLNLEYKTYEKRNKLKLRIIILLLFIIFLITFTIQIIISKFIEKKLHSLSYLTVIYYIVAVLYLIKILIRNKTNYTYFYIIGKLLLVIGYLLEISENSVNNIINMLVTYSFTVCYIFFISFKILEGLVMCIIILSIAIWVYYHKNNNLNAMCTDFCDNPYTSLDNLEYINISCICKQQIFTFLICTLSFTLICLFMKYYEIYYLKKKFLTRYKQKVNLGKQIEILHTMLPSFLVEYLLVSDPKADGIMVGKNISGEDRGIISVIFCDIDDFQTMVSTLEPHTLVQTLDNLYLYFDKCIKYFNCIKIETVFESYLAASGLSEKKNNCVHKIKYDTKCAIKMAIAQLSAKYYISYKVLDTLSNNKDSNSIFPIESKYIYKNISLRIGIHTGKAISGVIGSVKPQYSLFGDTVNTASRMKSTSLKDHIHVSYDTYKYLKDDKTLVWKERSIFIKGKGEMKTYLLVDILDNSKKDHTKALEESTSSIFRSNDEIVNKSELITKEKEFDKIEMPDKSEIIDETKKIFKKSEKPSTKKKKIKKENAKEKNINIKMKEMGEILNNYDKEKVYNCNKSDDGSNSIGQNDFLYSTKNYNYKKSKYLDLERLSTNKSFRRNVLAYNFESPINLPPKIGDNTKRNYDSDNFFTSPYIIDKNEKDEIRDTTNKALYIKKSKNIINRMREDSIDFKDEFSKENDKIKEYIKERITYRQKVTPNYFNFNNMSKYSNAFKKKKKKKKDIQKKYTYRQKTSFYNFLNKNDIINYNYSSEFEYFIDPKMKNKKPINFNNLFAKIYKKKLSLLNIKNEPINIKKKNIKNKSRDRIIFSSRRDEEHDDNQKMNKKLFSRTYAQKAEQTSHENIFTEMINDNFLKKEDKEQCEIRNENRCPTVFLIKRNKTTININKNRVLKRIFKDIITRKKIKRNRILKNKKLNYVNKNDNLGKKYEILNNICLVHKRAMTFVQYNTEDEEKKRTKRFHKNDEIFGSDMNISRNLNGSNSNIQNINRRSKNKAEDDLFIRNKVNLNNIKNNINLRKNIYKTDERGMQYNDLKGYDKKKNTEENNEDKEKKIEYDSNENIKNGFPKNEDKMIMKKRMISKRISFYSLKEYEKGDSFKSYDNSSCGIKSKKTNSIISDEEMNEYFNYNTEFNSNRNKNKQNKEFSLASKVNNIFKNIFKKNYISDKLKSGKYNTMSNSKSGQTNITTDNKKSQIKKNGDVNKANTNVSNKNSDFVTNFDNYNKNILKKLTSTLQINRKTSYFNRFYYKFKDEELEEEYTREYYQEIINIDLTKKLIIIFVISELILSLCNVIELSYYENKETPNDFIVIIWLIRSIYLFTITFIWLLLKTKLKEYKDNSSKMMWTTFILNIFLSSWGIIMIDLACIHYSNLVGNSRERSIFFMKDATELIISMQLIFVKNMLFKHKFFFFVFFFVFLMYSFFKLFVIHVCELRICCSILLILSINILYFWYSEYLDRTQYIIKRKRNRMERTSHDFLTRILPRQVLEEYQNDNLQLTYKHEKIAFLFADIVGFTKWSKTAAPKNVLKLLQKLISKIDKDTIKLGLYKLFTIGDAYVATSQPNASITDQTEAADGIISIFKLAKLILHNINTIKIQFNKHDFNMRIGLHYGSCVGGIIGSVRIRYDMWGLDVLIANHIESNGIPGEIVCSEQFKNFFLENEPHAKLNFWHYKTISINDKDIKIYVVEDKNYEEDYDPKIINYETLLKLREQNKVKG
|
Guanylate cyclase beta (PfGCbeta) (EC 4.6.1.2) (Guanylyl cyclase beta)
|
Plasmodium berghei (strain Anka)
| 5,823 | 3,004 | 354,776 |
cGMP biosynthesis;Glycoprotein;Lyase;Magnesium;Membrane;Metal-binding;Reference proteome;Transmembrane;Transmembrane helix
|
GO:0004383; GO:0005886; GO:0035556; GO:0045332; GO:0046872; GO:0140326; GO:2000147
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 67..87; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 95..115; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 301..321; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 335..355; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 992..1012; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1023..1043; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1073..1093; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1106..1126; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1131..1151; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1172..1192; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1298..1318; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1328..1348; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1354..1374; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1395..1415; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1458..1478; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 1501..1521; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 2564..2584; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 2595..2615; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 2635..2655; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 2668..2688; /note="Helical"; /evidence="ECO:0000305"; TRANSMEM 2696..2716; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 2723..2743; /note="Helical"; /evidence="ECO:0000255"
|
PF00211;PF16212;
|
IPR001054;IPR023298;IPR008250;IPR036412;IPR023214;IPR029787;IPR032630;
| null |
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Aconoidasida (class), Haemosporida (order), Plasmodiidae (family), Plasmodium (genus), Plasmodium (Vinckeia) (subgenus), Plasmodium berghei (species)
|
GCbeta PBANKA_1136700
| false |
491 |
A0A509AQ68
|
MAHVITRINAREILDSRGNPTVEVDLETTLGIFRAAVPSGASTGIYEALELRDNDKSRYLGKGVQQAIKNINEIIAPKLIGLDCREQKKIDNMMVQELDGSKTEWGWSKSKLGANAILAISMAICRAGAAANKTSLYKYLAQLAGKNTEKMILPVPCLNVINGGSHAGNKLSFQEFMIVPVGAPSFKEAMRYGAEVYHTLKSEIKKKYGIDATNVGDEGGFAPNILNAHEALDLLVASIKKAGYENKVKIAMDVAASEFYNIETKTYDLDFKTPNNDKSLVKTGQELVDLYIELVKKYPIISIEDPFDQDDWENYAKLTEAIGKDVQIVGDDLLVTNPTRIEKALEKKACNALLLKVNQIGSITEAIEACLLSQKNNWGVMVSHRSGETEDVFIADLVVALRTGQIKTGAPCRSERNAKYNQLFRIEESLGANGSFAGDKFRLQLN
|
Enolase (EC 4.2.1.11)
|
Plasmodium berghei (strain Anka)
| 5,823 | 446 | 49,026 |
Acetylation;Cell membrane;Cytoplasm;Cytoskeleton;Glycolysis;Isopeptide bond;Lyase;Magnesium;Membrane;Metal-binding;Nucleus;Phosphoprotein;Reference proteome;Ubl conjugation;Vacuole
|
GO:0000015; GO:0000287; GO:0004634; GO:0005634; GO:0005773; GO:0005856; GO:0005886; GO:0006096; GO:0009986
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21949403}. Nucleus {ECO:0000269|PubMed:21949403}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:W7JLR6}. Cell surface {ECO:0000269|PubMed:21949403, ECO:0000269|PubMed:24474798}. Cell membrane {ECO:0000250|UniProtKB:Q7RA60}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000250|UniProtKB:Q7RA60}. Vacuole {ECO:0000250|UniProtKB:Q8IJN7}. Note=Partially localizes to the nucleus in rings and trophozoites. Localization to the nucleus and food vacuole is higher in early and mid-stage trophozoites compared to the late-stage trophozoites and schizonts (By similarity). In the nucleus, localizes to heterochromatin region (By similarity). In rings, nuclear localization is dependent on the actin cytoskeleton (By similarity). Localizes to the cell surface of merozoites (By similarity). In gametocytes, predominantly localizes to the actin cytoskeleton (By similarity). In the trophozoite food vacuole, colocalizes with hemozoin, a product of heme detoxification (By similarity). In sporozoites, localizes to punctate structures beneath the cell membrane (By similarity). Localizes to the cell surface of ookinetes, especially on the apical pellicle complex that is involved in invasion (PubMed:21949403, PubMed:24474798). When phosphorylated at Thr-339, localizes to the cytoskeleton (By similarity). When phosphorylated at Ser-42, localizes to the cytoplasm (By similarity). When ubiquitinated at Lys-138, acetylated at Lys-133 and Lys-375 and phosphorylated at Tyr-139, localizes to the food vacuole (By similarity). When triubiquitinated at Lys-138, appears to colocalize with hemozoin in the food vacuole (By similarity). {ECO:0000250|UniProtKB:Q7RA60, ECO:0000250|UniProtKB:Q8IJN7, ECO:0000250|UniProtKB:W7JLR6, ECO:0000269|PubMed:21949403, ECO:0000269|PubMed:24474798}.
| null | null |
PF00113;PF03952;
|
IPR000941;IPR036849;IPR029017;IPR020810;IPR020809;IPR020811;
| null |
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Aconoidasida (class), Haemosporida (order), Plasmodiidae (family), Plasmodium (genus), Plasmodium (Vinckeia) (subgenus), Plasmodium berghei (species)
|
ENO PBANKA_1214300
| false |
492 |
A0A509AQE6
|
MCEHKANNKNDGEFVNLKEKNENNHCGNTKSTIADCDDDYSIITLCTKCLSTKTEVNKNKIILDSKALKDSRTKRRSSVNINIDILNNNLNLSPYFDRSQIVQETILMNNDDLEKLYELDKYKLGKGSYGNVVKAINKKTGQAKAIKIIDKKRINNIERLKREILIMKQMDHPNIIKLYEVYEDNEKLYLVLELCTGGELFDKIVKHGSFSEYETYKIMKQIFSALAYCHSKNIIHRDLKPENILYVDSSDDSPIQIIDWGFASKCMNNHNLKSVVGTPYYIAPEILKGKYDKKCDIWSSGVIMYILLCGYPPFNGKNNDDILKKVKKGEFVFDSNYWSKISLDAKELICECLNYNYKERIDVHKIVNHKWFIKFKNYNHITINKHLSKELIEKFKKFHKLCKIKKLAITCIAYQLNKKKFGKMKKTFEAFDHNGDGVLTISEIFQCLKVGDNEIDRDLYYLLKQLDTDGNGLIDYTEFLAACLDHSILEQDAVCRNAFKIFDANGDGIITKDELLNVLSFSNDQMPFSKEIIENVIKEVDANNDGYIDYDEFYKMMSGRQS
|
Calcium-dependent protein kinase 5 (EC 2.7.11.1) (PbCDPK5)
|
Plasmodium berghei (strain Anka)
| 5,823 | 562 | 65,108 |
ATP-binding;Calcium;Cell membrane;Cytoplasm;Cytoplasmic vesicle;Kinase;Lipoprotein;Magnesium;Membrane;Metal-binding;Nucleotide-binding;Palmitate;Phosphoprotein;Reference proteome;Repeat;Serine/threonine-protein kinase;Transferase
|
GO:0004674; GO:0005509; GO:0005524; GO:0005886; GO:0031410; GO:0033163; GO:2000147
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A0A5K1K8H0}. Cytoplasmic vesicle, secretory vesicle, microneme membrane {ECO:0000250|UniProtKB:A0A5K1K8H0}; Peripheral membrane protein {ECO:0000250|UniProtKB:A0A5K1K8H0}; Cytoplasmic side {ECO:0000250|UniProtKB:A0A5K1K8H0}. Cell membrane {ECO:0000250|UniProtKB:A0A5K1K8H0}; Peripheral membrane protein {ECO:0000250|UniProtKB:A0A5K1K8H0}; Cytoplasmic side {ECO:0000250|UniProtKB:A0A5K1K8H0}. Note=During the late stages of schizogony, localizes to the cytoplasm in immature daughter merozoites, co-localizes with AMA1 to a subset of micronemes and to the apical region in maturing daughter merozoites, and near the plasma membrane in mature daughter and free merozoites. {ECO:0000250|UniProtKB:A0A5K1K8H0}.
| null | null |
PF13499;PF00069;
|
IPR050205;IPR011992;IPR018247;IPR002048;IPR011009;IPR000719;IPR008271;
| null |
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Aconoidasida (class), Haemosporida (order), Plasmodiidae (family), Plasmodium (genus), Plasmodium (Vinckeia) (subgenus), Plasmodium berghei (species)
|
CDPK5 PBANKA_1351500
| false |
493 |
A0A509AST0
|
MKLLGNSKYFFVVLLLCISVFLNGQEILDEIKYSEEVCNEQIDLHILLDGSGSIGHSNWISHVIPMLTTLVDNLNISRDEINISMTLFSTYARELVRLKRYGSTSKASLRFIIAQLQNNYSPHGTTNLTSALLNVDNLIQKKMNRPNAIQLVIILTDGIPNNLKKSTTVVNQLKKKDVNVAIIGVGAGVNNMFNRILVGCGKLGPCPYYSYGSWDQAQTMIKPFLSKVCQEVEKVALCGKWEEWSECSTTCDNGTKIRKRKVLHPNCAGEMTAPCKVRDCPPKPVAPPVIPIKVPDVPVKPVEPIEPAEPAEPAEPAEPAEPAEPAEPAEPAEPAEPAEPAEPAEPAEPAEPAEPAEPAEPAEPAKPAEPAEPAEPAEPAEPVNPDNPILPIKPEEPSGGAEPLNPEVENPFIIPDEPIEPIIAPGAVPDKPIIPEESNELPNNLPESPSDSQVEYPRPNDNGDNSNNTINSNKNIPNKHVPPTDDNPYKGQEERIPKPHRSNDEYIYYNNANNNDKLEPEIPSKDYEENKSKKQSKSNNGYKIAGGIIGGLAIIGCIGVGYNFIAGSSAAAMAGEAAPFEDVMADDEKGIVENEQFKLPEDNDWN
|
Thrombospondin-related anonymous protein (Thrombospondin-related adhesive protein) (PbTRAP)
|
Plasmodium berghei (strain Anka)
| 5,823 | 606 | 65,959 |
3D-structure;Cell membrane;Cytoplasm;Membrane;Reference proteome;Signal;Transmembrane;Transmembrane helix
|
GO:0005737; GO:0005886
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11927544, ECO:0000269|PubMed:9041516}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:9041516}.
|
SIGNAL 1..24; /evidence="ECO:0000255"
|
TRANSMEM 544..564; /note="Helical"; /evidence="ECO:0000255"
|
PF00090;PF00092;
|
IPR050525;IPR000884;IPR036383;IPR002035;IPR036465;
|
2EPH;2PC4;
|
cellular organisms (no rank), Eukaryota (domain), Sar (clade), Alveolata (clade), Apicomplexa (phylum), Aconoidasida (class), Haemosporida (order), Plasmodiidae (family), Plasmodium (genus), Plasmodium (Vinckeia) (subgenus), Plasmodium berghei (species)
|
TRAP PBANKA_1349800
| false |
494 |
A0A517FNB9
|
MEGLLLLLPTAIIALYLYISLIRRSRKKHNLPPGSDGWPFLGETFSYLKPHSAISIGRFMEDHISRYGKIYRSNLFGEPTIVSADAELNRFVLQNEGRLFECSYPRSIGGILGKWSMLVLVGDMHRDMRMISLNFMSAARLRTRLMPEVERQTLLVLRSWREGSTFSAQEEAKKFTFNLMAKHIMSMDPGEPETEMLRREYITFMKGVVSAPLNFPGTPYWKALKSRSSILAVIERKMEERIGRRDRGDGGVEDDDLLGWAMNQSNLLKEQILDLLLSLLFAGHETSSMALALAIYFLESCPEAVRDLRDEHLAISMSGKEGECGLSWDQYKQMEFTHCVINESLRLGNVVRFVHRKAIQDVQYKGYDIPCGWKVLPVFAAVHLDSTLYSDPHRFNPWRWQSSSSKTTAANFMPYGGGLRLCTGSELAKLEMAVFLHHLVLNYQWKLAEPEQAFAYPFLDFPKGLQIKVRAIT
|
Cholesterol 22-monohydroxylase CYP90B52 (EC 1.14.14.-) (Cytochrome P450 CYP90B52) (PpCYP90B52)
|
Paris polyphylla (Daiswa polyphylla)
| 49,666 | 473 | 54,036 |
Brassinosteroid biosynthesis;Cholesterol metabolism;Iron;Lipid biosynthesis;Lipid metabolism;Membrane;Metal-binding;Oxidoreductase;Steroid biosynthesis;Steroid metabolism;Sterol metabolism;Transmembrane;Transmembrane helix
|
GO:0004497; GO:0005506; GO:0006694; GO:0008203; GO:0010268; GO:0016020; GO:0016132; GO:0016705; GO:0020037
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 2..22; /note="Helical"; /evidence="ECO:0000255"
|
PF00067;
|
IPR001128;IPR002401;IPR036396;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), Liliopsida (clade), Petrosaviidae (subclass), Liliales (order), Melanthiaceae (family), Paris (genus)
|
CYP90B52
| false |
495 |
A0A517FNC5
|
MAPVVILFFLFPTLLVLVVAVLGLRGGDDSWKKRGLKVPPGSMGWPLLGETIAFRRLHPCTSLGEYMEEHVNKYGKIYRSNLFGAPTIVSADAELNRFVLMNDERLFEPCFPKSVADILGHTSMLVLTGEMHRYMKSLSVNFMGIARLRNNFLGDSELYITQNFNRWKENIPFPAKEEACKVTFNLMVKNILSLNPGEPESEHLRKLYMSFMKGVVAIPLNLPGTAYKKAIQSRATILKMIEKLMEERIRNKKAGTDKIGEADLLGFILEQSNLDAEQFGDLLLGLLFGGHETSATAITLVIYFLYDCPKAVDHLREEHLGIVRAKKARGEPPALTWDDYKQMEFSQCVVSETLRLGNIIKFVHRKAKTDVQFKGYDIPKGWSVIPVFAAAHLDPSVYENPQKFDPWRWQTISTGTARIDNYMPFGQGLRNCAGLELAKMEIVVFLHHLTLNFDWEMAEPDHPLAYAFPDFPKGLPIKVRRLALK
|
Cholesterol 16,22-dihydroxylase CYP90G4 (EC 1.14.14.-) (Cytochrome P450 CYP90G4) (PpCYP90G4) (Protein DWARF 4 homolog) (PpDWF4) (Steroid 22-alpha-hydroxylase CYP90G4) (EC 1.14.14.-)
|
Paris polyphylla (Daiswa polyphylla)
| 49,666 | 485 | 54,979 |
Cholesterol metabolism;Heme;Iron;Lipid biosynthesis;Lipid metabolism;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Steroid biosynthesis;Steroid metabolism;Sterol metabolism;Transmembrane;Transmembrane helix
|
GO:0004497; GO:0005506; GO:0006694; GO:0008203; GO:0010268; GO:0016020; GO:0016132; GO:0016135; GO:0016705; GO:0020037
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 4..24; /note="Helical"; /evidence="ECO:0000255"
|
PF00067;
|
IPR001128;IPR017972;IPR002401;IPR036396;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), Liliopsida (clade), Petrosaviidae (subclass), Liliales (order), Melanthiaceae (family), Paris (genus)
|
CYP90G4 DWF4
| false |
496 |
A0A517FNC6
|
MSDSDITFYCLSSILSVLLIFIFILIKRKQAKPKLNLPPGKMGWPFLGETIGYLKPYSATTLGEFMDQHIARYGKIYKSKLFGEPAIVSADAGLNRFILQNEGKLFECSYPRSIGGILGKWSMLVLVGDMHRDMRLISLNFLSHARLRTHLLKEVEKHTRLVISSWKENSTFAAQDEAKKFTFNLMAEHIMSLQPGKIETEKLKKEYVTFMKGVVSAPLNFPGTAYWKALKSRGTILKFIEGKMEERIKRMKEGNENLEEDDLLNWVLKHSNLSTEQILDLILSLLFAGHETSSVSIALAIYFLPGCPQAILQLREEHKEIARAKKQAGETELTWEDYKKMEFTHCVVNETLRLGNVVRFLHRKALKDVRYKGYDIPCGWKVLPVIAAVHLDPLLFDQPQHFNPWRWQNNGNCPNFSGASSNSNNIFLPFGGGPRLCAGSELAKLEMAVFIHHLILNYHWELTDNNDQAFAYPFVDFPKGLQIRVQSHSLI
|
Cholesterol 22-monohydroxylase CYP90B51 (EC 1.14.14.-) (Cytochrome P450 CYP90B51) (PpCYP90B51)
|
Trigonella foenum-graecum (Fenugreek)
| 78,534 | 491 | 56,049 |
Brassinosteroid biosynthesis;Cholesterol metabolism;Heme;Iron;Lipid biosynthesis;Lipid metabolism;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Steroid biosynthesis;Steroid metabolism;Sterol metabolism;Transmembrane;Transmembrane helix
|
GO:0004497; GO:0005506; GO:0006694; GO:0008203; GO:0010268; GO:0016020; GO:0016132; GO:0016705; GO:0020037
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
| null |
TRANSMEM 6..26; /note="Helical"; /evidence="ECO:0000255"
|
PF00067;
|
IPR001128;IPR017972;IPR002401;IPR036396;
| null |
cellular organisms (no rank), Eukaryota (domain), Viridiplantae (kingdom), Streptophyta (phylum), Streptophytina (subphylum), Embryophyta (clade), Tracheophyta (clade), Euphyllophyta (clade), Spermatophyta (clade), Magnoliopsida (class), Mesangiospermae (clade), eudicotyledons (clade), Gunneridae (clade), Pentapetalae (clade), rosids (clade), fabids (clade), Fabales (order), Fabaceae (family), Papilionoideae (subfamily), 50 kb inversion clade (clade), NPAAA clade (clade), Hologalegina (clade), IRL clade (clade), Trifolieae (tribe), Trigonella (genus)
|
CYP90B51
| false |
497 |
A0A571BEE2
|
MSIPRFLKVTYGAYDNYIPVSELSKKSWNQQYFSLAFPKPPRPGKKRRSLPSQLQNNTAPVIDEEKLGVHRPPLWMHRSLMRISERPSVYLAARKGLIPKPLHFGKGESKSVGTHKSLASEKTKKEVKMKKDGFEAKEKTALKTDKEGSPKPAKKNIPRDSQKDKGRVSSDSEGEKAGVKKGSKKVKNTPKGKDSASESEGEKAGSKKEAKTTKKGSKDKVSATESGGEKAGSKKEAKATKKGSKDKVSGTESGGEKAGSKKEAKTTKKESKDKVSATESGGEKAGSKKEAKDDKKDATSSQETLLSTAADKDGKKKEEKPVKQSSKSKDTVKDSASEKGDEKKEDKKEGKKEKKKKDGEGKEGGKKEKKDKKDKKDKKDKKDKKDKKDKKEKDKKDKKDKKDKKDKKDKKDKKDKKDKKAK
|
Cylicin-2 (Cylicin II)
|
Mus musculus (Mouse)
| 10,090 | 422 | 46,653 |
Alternative splicing;Cytoplasm;Cytoskeleton;Developmental protein;Differentiation;Reference proteome;Repeat;Spermatogenesis
|
GO:0001675; GO:0005200; GO:0007283; GO:0007338; GO:0033150; GO:0098727; GO:1905198; GO:1905199
|
Evidence at transcript level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, perinuclear theca, calyx {ECO:0000269|PubMed:38013430}. Cytoplasm, cytoskeleton, perinuclear theca {ECO:0000269|PubMed:38013430}. Note=Localizes to the subacrosomal layer of the perinuclear theca in round and elongating spermatids. Localizes to the calyx, also known as post-acrosomal region, in spermatozoa. {ECO:0000269|PubMed:38013430}.
| null | null |
PF15241;
|
IPR026189;IPR029354;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Deuterostomia (clade), Chordata (phylum), Craniata (subphylum), Vertebrata (clade), Gnathostomata (clade), Teleostomi (clade), Euteleostomi (clade), Sarcopterygii (superclass), Dipnotetrapodomorpha (clade), Tetrapoda (clade), Amniota (clade), Mammalia (class), Theria (clade), Eutheria (clade), Boreoeutheria (clade), Euarchontoglires (superorder), Glires (clade), Rodentia (order), Myomorpha (suborder), Muroidea (clade), Muridae (family), Murinae (subfamily), Mus (genus), Mus (subgenus)
|
Cylc2
| false |
498 |
A0A5B8NIM2
|
MDAAVDLLDPSKALNLKHIRQQLIRMEDTITFQLIERVQFPLNRTVYEPGAVKIPNSNLSFLDWTLREREKTDSLIRRYQSPDEHPFFPDALLKPILQPLIYPKILHRNNINLNDKIKKYFTDQVLPSICHDFGREDRGEQAENYGSTVTADIQCLQTLSRRIHFGKWVAESKYIDDPQGFAKLIKAGDRQAIGKAITKPAVELQVLERIRLKSRTYSTDPCESDDPEPKINVDAVVAMYRDCVIPLTKEVEIDYLMQRLSD
|
Chorismate mutase (EC 5.4.99.5) (EqCMU)
|
Erysiphe quercicola (Hevea powdery mildew)
| 425,177 | 262 | 30,282 |
Amino-acid biosynthesis;Aromatic amino acid biosynthesis;Cytoplasm;Host cytoplasm;Isomerase;Phenylalanine biosynthesis;Secreted;Tyrosine biosynthesis;Virulence
|
GO:0004106; GO:0005576; GO:0005737; GO:0006571; GO:0009094; GO:0030430; GO:0046417; GO:0140502
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:33010586}. Secreted {ECO:0000305|PubMed:33010586}. Host cytoplasm {ECO:0000305|PubMed:33010586}. Note=Appears to be secreted despite an apparent lack of a secretory signal. {ECO:0000305|PubMed:33010586}.
| null | null |
PF01817;
|
IPR036263;IPR008238;IPR037039;IPR002701;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Pezizomycotina (subphylum), leotiomyceta (clade), sordariomyceta (clade), Leotiomycetes (class), Erysiphales (order), Erysiphaceae (family), Erysiphe (genus)
|
CMU
| false |
499 |
A0A5E4M3Q4
|
MSVCVSPLVQATILMTEESLTCPQCPKSFSSTKLLQQHQQMFHTDKSVLLSLKSTDAPVGMDRAFICETCGKAFRFRSNLAEHRSVHTALKPYVCKFCGKSSRLKGNLTKHILKHHKKEQNEAIAKDDIIVKKAPKIVTKDNGPTTNGSTPTTSTATPSVITVSSALASSNGHNNNNNNHAVNNNLRTIKMELEDPDYNLIAKSAPTPVVSKIVATHTVTPRSRPTPKDIKEILETIAPSVGVSETPEEMCLLPKDASSESDRSVLISLGFDFGSTLSLNHQQLQQVVRELKGELSISPDTVQSDHSDDFEQDSPPPMAIANISTVGGEATLAAMIVAATNASGQRGDGTPDSTDTQKGCSPQRELSPESDPSTSSGDSCPSPPKMLHCKECGTLVRKSSHLPIHMTMSHGYPPPLVAAPVEEKPAPEQPVNASSLHNELRVISNAICELKAQQAATPRVEQALTYIDSRVGKLERSLETALNSIYTLVQLQTGMTSSVNRLREDSTKNFSDLKTRMEMSLSPIKPFQQRFSRERSSSSSVERSPSRERSRSPL
|
Zinc finger protein syd-9 (Synapse defective protein 9)
|
Caenorhabditis elegans
| 6,239 | 554 | 60,211 |
Alternative splicing;Metal-binding;Nucleus;Reference proteome;Repeat;Zinc;Zinc-finger
|
GO:0000977; GO:0000981; GO:0005634; GO:0006357; GO:0008270; GO:0016607
|
Evidence at protein level
| 5 |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16803962}. Nucleus speckle {ECO:0000269|PubMed:16803962}.
| null | null |
PF00096;
|
IPR050888;IPR036236;IPR013087;
| null |
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Nematoda (phylum), Chromadorea (class), Rhabditida (order), Rhabditina (suborder), Rhabditomorpha (infraorder), Rhabditoidea (superfamily), Rhabditidae (family), Peloderinae (subfamily), Caenorhabditis (genus)
|
syd-9 tag-239 ztf-10 ZK867.1
| false |
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