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