Datasets:
manufernandezbur
/
tox_nontox_clustered_2025

Dataset card Data Studio Files
xet
Community
1
Unnamed: 0
int64
2
562k
Entry
stringlengths
6
10
Sequence
stringlengths
11
999
Protein names
stringlengths
5
558
Organism
stringclasses
392 values
Organism (ID)
int64
595
2.89M
Length
int64
11
999
Mass
int64
1.06k
118k
Keywords
stringlengths
4
380
⌀
Gene Ontology IDs
stringlengths
10
754
⌀
Protein existence
stringclasses
5 values
Annotation
float64
1
5
Subcellular location [CC]
stringlengths
30
2.26k
⌀
Signal peptide
stringclasses
677 values
Transmembrane
stringlengths
32
2.52k
⌀
Pfam
stringlengths
8
72
⌀
InterPro
stringlengths
10
180
⌀
PDB
stringlengths
5
2.65k
⌀
Taxonomic lineage
stringclasses
178 values
Gene Names
stringlengths
2
299
⌀
Toxin
bool
2 classes
species
stringclasses
111 values
cdhit_cluster
int64
0
4.65k
cdhit_rep
stringlengths
5
10
cdhit_rep_is_ref
bool
1 class
cdhit_pct_id
float64
177,867
C5MC60
MAPIPPTPAQDISILHPKVLLLSAGITTSLFLGYRFYTRYVRRVRTYLDLTPSIIENNKKLYGYVTRVGDGDNFRFYHTPGGLLMGWGWLRKIPTTRKELKDETLMIRLCGIDAPEGAHFGKPAQPFADDALNWLRGYVDGKYVTITPYSIDQYKRVVARAQIWKWTGKKDVSAEMLKTGYAIVYEGKAEAEFGDNEDWYRKLEAHSKRLRKGVWSLGKKLTTPGEFKRVHYRGE
Probable endonuclease LCL3 (EC 3.1.-.-)
Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast)
294,747
235
27,012
Calcium;Endonuclease;Hydrolase;Membrane;Metal-binding;Mitochondrion;Nuclease;Reference proteome;Transmembrane;Transmembrane helix
GO:0004519; GO:0005739; GO:0016020; GO:0046872
Inferred from homology
3
SUBCELLULAR LOCATION: Mitochondrion. Membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
null
TRANSMEM 15..37; /note="Helical"; /evidence="ECO:0000255"
PF00565;
IPR035437;IPR016071;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida tropicalis (species)
LCL3 CTRG_03652
false
Candida tropicalis
52
row_165126
false
null
399,708
C5M580
MKFSTILTALTAVIATVAGYETSGKPHTVDILIDYSIKETPELSQNDVANWVNGDKYTLEYVVSNNEETEIAVVGVTGQFKNPVTNQIVTNLTTGQVGPITVAPGESIKFEQIVDVDLMANNYELFPYVFVAHDDLIKVIPCRGQLTSVVDATISFFDPRLILLELVLLVTFGAAAYFIYEIWGKQYLKGTAPVKVPARKSGSTVSKKGASATASGFDESWIPEAHLKKNKKKA
Increased recombination centers protein 22-1
Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast)
294,747
234
25,521
Endoplasmic reticulum;Membrane;Reference proteome;Signal;Transmembrane;Transmembrane helix
GO:0005789
Inferred from homology
2
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
SIGNAL 1..19; /evidence="ECO:0000255"
TRANSMEM 162..182; /note="Helical"; /evidence="ECO:0000255"
PF03896;
IPR005595;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida tropicalis (species)
IRC22-1 CTRG_02058
false
Candida tropicalis
53
row_382309
false
null
399,716
C5M7I9
MAGKKKSKSDSVPLDLGNIKPLEKLQPVPKTRSSSITSIESADEPGTMKQVLLPPTIREFDELEQFEAFVRDETWDNEFDYFHGRLHYYPPFVMKACHDDVEKIKPTVNKNSKKFRRDLQHHIQKHLIKDLEKCCGYELNFGKGEVVETDSKVTWKFKDETDHGFSKEEEDMYDRHWRLELDVTCTNESAMVDVEYKSIPL
Respiratory growth induced protein 1
Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast)
294,747
201
23,515
Cell membrane;Membrane;Reference proteome
GO:0005886; GO:0006112
Inferred from homology
2
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
null
null
PF10843;
IPR022554;IPR038235;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida tropicalis (species)
RGI1 CTRG_01821
false
Candida tropicalis
54
row_382317
false
null
177,857
C5M5F1
MFLDLHPYTILVSIFIILLVKQIVGRIGKSTIQEFVWLLYLKISPNQAIKDYNTKKVELHEINKQKRSISAQDEYAKWTKLNRQADKLTSEIQKLNEEIRQSKASIDKLANVLLMVLTTLPIWVARIFFRKTHLFYLRSGIFPRYIEWVLALPFFPSGAVGLTVWMFAANSVIHNVISLVSFAFEKRVEKPVRQKK
Golgi to ER traffic protein 1 (Guided entry of tail-anchored proteins 1)
Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast)
294,747
196
22,878
Coiled coil;Endoplasmic reticulum;ER-Golgi transport;Golgi apparatus;Membrane;Reference proteome;Transmembrane;Transmembrane helix;Transport
GO:0000139; GO:0005789; GO:0016192; GO:0043495; GO:0043529; GO:0071816
Inferred from homology
3
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03113}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03113}. Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_03113}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03113}.
null
TRANSMEM 11..30; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03113"; TRANSMEM 115..135; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03113"; TRANSMEM 160..176; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03113"
PF04420;
IPR028945;IPR027538;IPR029012;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida tropicalis (species)
GET1 CTRG_01081
false
Candida tropicalis
55
row_165116
false
null
536,247
C5M9K8
MSSSFSSDASQYQAENTVNKLFSNILHTNISTTKSTTNANQLFAQHGSSVKKNKKNEAKRIKKNEERTKAFNKFVKYNYIKNKENKNESDKKYLSKLVRKNVNKLNSSSKIDDFEINEEFNIVSSELLDQIKPKNGKRLRKKLFRVNENDERAKEFNEKLQKGVISYPGLTPGLAPVDYNESDSE
Regulator of rDNA transcription 14
Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast)
294,747
185
21,293
Nucleus;Reference proteome;Transcription;Transcription regulation
GO:0005730
Inferred from homology
1
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
null
null
PF17075;
IPR031404;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida tropicalis (species)
RRT14 CTRG_02170
false
Candida tropicalis
56
row_516559
false
null
399,717
C5M7P6
MSKKKEKKFQESKISTRSYRSTTMLRHQIRRITTANRLLDELKTSKDIEKFLNNSTWSIKELLQQPLTNTTTKEVSSDVVTKMLKLSGLSDSQDIQNIRKSLNLQMMFINHLYDKSGNNAEKKVNDNNCMFRLLASDHIPQRPLDLDTLMDEINKLEPSEEKGEIGFGIKDLQRDSFVINKK
Glutamyl-tRNA(Gln) amidotransferase subunit F, mitochondrial (Glu-AdT subunit F) (EC 6.3.5.-)
Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast)
294,747
182
21,136
ATP-binding;Ligase;Membrane;Mitochondrion;Mitochondrion inner membrane;Nucleotide-binding;Protein biosynthesis;Reference proteome
GO:0005524; GO:0005743; GO:0030956; GO:0032543; GO:0050567; GO:0070681
Inferred from homology
2
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03151}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03151}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03151}.
null
null
PF20977;
IPR027499;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida tropicalis (species)
GTF1 CTRG_01878
false
Candida tropicalis
57
row_382318
false
null
177,855
C5M4J6
MNLRQQITQFLTLAYVFSSAFMLWKTLSVIANSHSPIVVVLSGSMEPAFQRGDILFLWNRENRQKVGDIVVYEIDGKSIPIVHRVLREHHNNEKQLLLTKGDNNAVDDLSLYAKKQQYLNQKEDLVGTVKGYLPFIGYVTILISENVYFKYGMLGLLGLSALFSNE
Signal peptidase complex catalytic subunit SEC11 (EC 3.4.21.89) (Signal peptidase I)
Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast)
294,747
166
18,912
Endoplasmic reticulum;Hydrolase;Membrane;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix
GO:0004252; GO:0005787; GO:0006465; GO:0045047
Inferred from homology
3
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P15367}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P15367}.
null
TRANSMEM 10..30; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255"
PF00717;
IPR036286;IPR019756;IPR015927;IPR019533;IPR001733;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida tropicalis (species)
SEC11 CTRG_00986
false
Candida tropicalis
58
row_165114
false
null
399,718
C5M8B9
MSTFLQSFKISQASDEYKQRRKTQMLKFFTASAITILTSRFAYRSTIARQYVPTLFQGNHSPPLSYNFTTDAAVAVATGTILCGSVSSMLVLGGFWILDVSNLGEFGWRMKEKLGGLEKEKHLGEMEMDEESRYIQDSLNDLLDGKYDFEEEGGNNSVA
Altered inheritance of mitochondria protein 11
Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast)
294,747
159
17,850
Membrane;Reference proteome;Transmembrane;Transmembrane helix
GO:0005739; GO:0016020
Inferred from homology
2
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
null
TRANSMEM 25..43; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 74..98; /note="Helical"; /evidence="ECO:0000255"
null
IPR038814;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida tropicalis (species)
AIM11 CTRG_02641
false
Candida tropicalis
59
row_382319
false
null
177,863
C5MAV2
MSGLPSSVAFGEEEEPDLLDKMWEKSKQQPLVPIGSLLTAGAVFLAARSMKRGEKVKTQIYFRYRIGFQLATLAALVLGGMYYGTETKEYKQSREEKLREKAKQREKLWIEELERRDAIIQARKQRLEESKKELRELAKQGFEEEQNSQQSQEKN
Respiratory supercomplex factor 1, mitochondrial
Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast)
294,747
155
18,016
Coiled coil;Membrane;Mitochondrion;Reference proteome;Transmembrane;Transmembrane helix
GO:0005743; GO:0010155; GO:0033617; GO:0097250; GO:0098803
Inferred from homology
3
SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000255|PROSITE-ProRule:PRU00836}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00836}.
null
TRANSMEM 31..48; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00836"; TRANSMEM 61..83; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00836"
PF04588;
IPR007667;IPR050355;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida tropicalis (species)
RCF1 AIM31 CTRG_03194
false
Candida tropicalis
60
row_165122
false
null
177,861
C5M799
MVKKVLLINGPNLNLLGTREPEKYGTTSLSDIEKAAIEQAQLKKNDSEVLTYQNNTEGFIIDRIHEARRQGVGFIVINAGAYTHTSVGIRDALLGTAIPFIEVHITNVHQREPFRHQSYLSDKAVAVICGLGVYGYTAAIEYALNY
Catabolic 3-dehydroquinase (cDHQase) (EC 4.2.1.10) (3-dehydroquinate dehydratase)
Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast)
294,747
146
16,161
Lyase;Quinate metabolism;Reference proteome
GO:0003855; GO:0019631; GO:0046279
Inferred from homology
3
null
null
null
PF01220;
IPR001874;IPR018509;IPR036441;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida tropicalis (species)
DQD1 CTRG_01731
false
Candida tropicalis
61
row_165120
false
null
399,704
C5M3K2
MQYLLVALSLFISLSSANLFDFLNNFNHGGGGRQQQQGARNPQEYENRILNSQCDQYLCPDTGLCVESPKFCPCPYPSSQIRCFLPDGRFVCISKPAGEGISDKYNDPKTNWKIDAKDDNIRDCGWVNRAWRGLV
Long chronological lifespan protein 2
Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast)
294,747
135
15,257
Reference proteome;Signal
GO:0036503
Inferred from homology
2
null
SIGNAL 1..17; /evidence="ECO:0000255"
null
null
IPR034543;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida tropicalis (species)
LCL2 CTRG_00641
false
Candida tropicalis
62
row_382305
false
null
399,734
C5MJD6
MSATLSAYRNALRATKVVFRHDLPILTAARTQIKENIRNNSNLKDTTEIEEAVKKLNDVSKFLISNIVQGEKQDDGKYFLNFHEKTELGDNESIKQGKKNLGSLAGKKGSSIRSCKD
Mitochondrial zinc maintenance protein 1, mitochondrial
Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast)
294,747
117
13,083
Chaperone;Mitochondrion;Reference proteome;Transit peptide
GO:0005759; GO:0034551; GO:0044183
Inferred from homology
2
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
null
null
null
IPR045298;IPR050435;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida tropicalis (species)
MZM1 CTRG_06179
false
Candida tropicalis
63
row_382335
false
null
399,714
C5M6H7
MSDEINETCKPQACAIQNCLMKNGYNESKCSYYIDELYKCCKKFYESNGSSASSVCCPKFNLLQLKLKQRELGQIDANLIDTKHG
Cx9C motif-containing protein 4, mitochondrial
Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast)
294,747
85
9,641
Disulfide bond;Mitochondrion;Reference proteome;Repeat
GO:0005758
Inferred from homology
2
SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000250}. Note=Imported into the mitochondria via the mitochondrial disulfide relay system. {ECO:0000250}.
null
null
PF08991;
IPR027179;IPR009069;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Fungi (kingdom), Dikarya (subkingdom), Ascomycota (phylum), saccharomyceta (clade), Saccharomycotina (subphylum), Pichiomycetes (class), Serinales (order), Debaryomycetaceae (family), Candida/Lodderomyces clade (clade), Candida (genus), Candida tropicalis (species)
CMC4 CTRG_01458
false
Candida tropicalis
64
row_382315
false
null
188,845
P04362
GAFIMPGTLWCGAGNAASDYSQLGTEKDTDMCCRDHDHC
Phospholipase A2 (PLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
Heloderma horridum horridum (Mexican beaded lizard)
8,552
39
4,179
Calcium;Direct protein sequencing;Hydrolase;Lipid degradation;Lipid metabolism;Secreted
GO:0004623; GO:0005576; GO:0006644; GO:0016042; GO:0050482
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted.
null
null
PF05826;
IPR016090;IPR036444;IPR033113;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Anguimorpha (infraorder), Neoanguimorpha (clade), Helodermatidae (family), Heloderma (genus), Heloderma horridum (species)
null
false
Heloderma horridum
0
row_175724
false
null
502,640
Q86108
MDFPNLVLSAKNSIQNVDSKDEKQKIIDQLISDIRGQNDGVIPDEVLSEIQQVAEINGLSFNYEKPVKQELLEQPDPTSVLSQEVFQIRTILSKTLFVDVEAEDYSVYIPDETSNLSPVQIDARPIQTYQPKALMYKDTAILPSNRDEVSDQYGADEILFDSHMFNDISQAQIRDFETYVLDKAMQIQSSLPNLDFVSSLDKEVNPFNVHNTLCLNFGQREYYNIIADRTNQSFQQRRQSVQFDNVVVDGVARRARVSLRLHPFDSQLLDIIRFNTIQDQPLADTMAEYQLVAADGFVATPRFRTDRDARLIADVRSRVMARLCELSPYFHRTRILSSMTDFNSLWKVNVFSSSIDNAKDAIYRMAEISFTVADATTSALSSVNIASAQQTLLVLLNMSLFRFEIEPVGSQSNFGAAVSAALMLVVFPTDEASMSNVTFDNLCNLVFNELIAWTVDRPTFVKRTGMTNAFEANVNIGGGNMTRDITAYMRFVLLRRPWAVFQRTYDDQYVADIMVPNIDEANVNDQSYMAINNLFSGLIQAAQRNPNPGRQIAATSFRKLLKSMKDSCCNRIMPLIRLMKYNVERIARIYRFFPYTADLVQRIPAFRDERIRIKVPVSGMLSIALGINKSPDVFDWYNLLRFADVIRTKNFAERQSLESIMVQALIRNDINPARSRKEYIQQNIKPATNVVASITKVPSATFTTILSDRMLNNEIRRTQSYIVVNRIRDAVRAAFEHVPTAEHGIAKGALLLPYPQNFQRSSVYVRKDNILYNAPVGVDRFSLDDLLNGRFYQGMVNRIQNMSPFVIAGPLQVRASNASAIDSVTSAYLTMSSPYDACVKPEDLRHNRIVQPPIVDFFSDSSITRPNTQFEQLMSKTSVFVIDAPKLIVQSDATVYNFDYRDIQLTTSVVDKLEFTSVKTPDVTLFNGMLVFED
Inner capsid protein VP2
Rotavirus B (isolate RVB/Rat/United States/IDIR/1984/G1P[X]) (RV-B) (Rotavirus B (isolate infectious diarrhea of infant rats))
28,877
934
106,015
Capsid protein;Inner capsid protein;RNA-binding;T=2 icosahedral capsid protein;Virion
GO:0003723; GO:0019013; GO:0039616; GO:0039625
Inferred from homology
2
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04123}. Note=Inner capsid protein. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. {ECO:0000255|HAMAP-Rule:MF_04123}.
null
null
null
IPR007779;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus B (species), unclassified Rotavirus B (no rank)
null
false
Rotavirus B
0
row_483337
false
null
502,645
Q86195
MDSTVLVESAKTNIHGVDSKAEKQTIFDQLISDIKSQTDGQIPDEVLPDLQQLAEINGLTFEYKPKEKLSIMDHPDPTSVLSQDVFQIRTILSKTLFVDVENEDYSVYIPNDTAKLTPVLIDARPIQTYQPKALMHKDTAILPSHRDEISDQYGTDEILFDSHMFNDISQAQIRDFDTYILDKSIQIQNTLPNLEFISSLEKEVNPFNIHNTLCLNFGQKEYYNIIADRTNLSFQQRRQSVQFDNVIVDGVARTARVSLRLHPFDSQLLDIVRFNVIQDQPLADTLMEYQLVAADGFVATPKFRVDRDARLIADVRSPVMARLCELSPFFHRTRILSSMTDFTPLWKVNVFSSSIDNAKDAIYRMAEISFTVADATTSALASVNVASAQQTLLTLLNLSLFRFEIDPTGSQSNFGSAVSAALMLIVFPTDEQSMSNITFDNLCNLVFNELIAWTVDRPTFVKRTGMTNAFEANVNIGGGNMTRDIIAYMRFVLLRRPWAVFQRTYDDRYVSDIMVPNIDEANVNDQCYVAINNLFNGLIQAAQRNPNPGRQIAATSFRKLLKSMKDSCCNRIIPLIRLLKYNIERIARVYRFFPYTADLVHVIPAFRDERLRVKVPVSGMLSIALGINKAPDSFDWYNLLKFADVVRTKNFADQSLESIMVHALIRNDINPARSKKDYIQQNIKPATNVVASLSKLPSATFTTILADRMLNNEIRRTQSYVVTNRIRDAVRAAFEHVPTAEHGIAKGALLLPIPQNFQRSSVYVRKDNILYDPPVGVDRFNLSDLLDGRFYQGLINRVQNMAPFVISGPLQVKPSDASAIESVTSAYLTMSSPYDACVRPEDLRHNRVVHPPTVDYFSDASITRPNTQFEQLMSKTSVFVIDAPRLIVQNDATVYTFDYKDIQLTTSVVDKLEFTSVKTPDVTLFNGMLVYED
Inner capsid protein VP2
Rotavirus B (isolate RVB/Human/China/ADRV/1982) (RV-B) (Rotavirus B (isolate adult diarrhea rotavirus))
10,942
933
105,635
Capsid protein;Inner capsid protein;RNA-binding;T=2 icosahedral capsid protein;Virion
GO:0003723; GO:0019013; GO:0039616; GO:0039625
Inferred from homology
2
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04123}. Note=Inner capsid protein. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. {ECO:0000255|HAMAP-Rule:MF_04123}.
null
null
null
IPR007779;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus B (species)
null
false
Rotavirus B
1
row_483341
false
null
195,266
P15155
MLAYLRREWQSYGETVIAEGTFNSTSSDSSQSEKPIKTDGRYCYQAEIGRNAYSMDARGFMLGESDRHVDTTQFLPYTGYITDGIKYCNIEPPCGTLLRMHFDVSGDVSVDMHRVASIYVEVDSVTYDGSQYTIRGYRDRNLTATETQKKLIFYGFRKLGMIGMTGNGRVMLTSTIIQKISYKHQFTFQMHSESYVWGPCSGRIKTRVQGNDSRIIIYEQEDGFWKILKETLWIKLKPYFKPYGTMGGAFKNWLIDSGFEKHEYTYSYERDGQVVNATTVTYVKPTGKAGINQSWRPATDYNGQFTVLQPEDEFSVWYFEDKWQISQAIYAKNFQSDSQVEGELTNNGALIFKMNYIPSLAGITNKGGKVKYRYISGGFAQIDTSRHTGLAIILNFKCYGKKFYADNNNYPVDNALNPYICYIGDSYTLSGGTHYRQGACAGFAAGYDDEITEHDMTISYTVMKPSDPDFVTGGDNYGQTVTSDIERSIRDLQDQINSILAEMNIQQVTSAVFTAITNLGELPSLFSNITKVFNRAKDNIKKLRSRSNSDISPIGATKIIDKTTLETPQLSVINRMPEEYELGIIYNSMRTRKLIDERKHDFDTFAVATEMELPYISKVNTLTKEFKDYLKKPGLLSNDDVAVQIDPMNNRLSVLRRKYADIIEYKIDPELAHEVLSNMSNSATRSLFSLNVRKQIAMNNSFSEPTFSQIIDRMFDDGQLIDVLNNLNRETATELFDEFLTRIKSMLVKMS
Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
Rotavirus B (isolate RVB/Rat/United States/IDIR/1984/G1P[X]) (RV-B) (Rotavirus B (isolate infectious diarrhea of infant rats))
28,877
751
85,558
Capsid protein;Hemagglutinin;Host cell membrane;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Membrane;Outer capsid protein;Viral attachment to host cell;Viral penetration into host cytoplasm;Viral penetration via permeabilization of host membrane;Virion;Virus entry into host cell
GO:0016020; GO:0019062; GO:0020002; GO:0039624; GO:0039665; GO:0044168; GO:0044172
Inferred from homology
3
SUBCELLULAR LOCATION: [Outer capsid protein VP4]: Virion {ECO:0000255|HAMAP-Rule:MF_04125}. Host rough endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_04125}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04125}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|HAMAP-Rule:MF_04125}. Note=The outer layer contains 180 copies of VP4, grouped as 60 dimers. Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles. {ECO:0000255|HAMAP-Rule:MF_04125}.
null
null
null
IPR042546;IPR038017;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus B (species), unclassified Rotavirus B (no rank)
null
false
Rotavirus B
2
row_181949
false
null
215,114
Q04916
MLTYLRREWQSFGETVTIKNTFNAQEDNNQSGRKTDNRPVKTEGRYCYKADVNRSKYYHDVQGFSLGQSDLHIDPTQFIMYSGTISNGISYVNQAPSCVQLSLKFTPGNSSLIEDLHIEPYKVEVLKIEHVGNVSRATLLSDIVSLSIAQKKLLLYGFTQLGIQGLTGDVVSVETKRIPTPTQTNLLTIEDSMQCFTWDMNCANVRSTKQDSRLIIYEQEDGFWKIVTETLSIKVKPYFKAYGTMGGAFKNWLVDSGFEKYQHDLAYVRDGVTVNAHTITYVNPSGKAGLQQDWRPATDYNGQITVLQPGDGFSVWYYEDKWQINQAIYAKNFQSDTRAQGYLENVGTLKFKMNYIPAFAEIRNKPGKVNYAYLNGGFAQVDASGYTGMSIILNFVCTGERFYASDNNSRVDNKITPFISYIGDYYTLSGGDFYRQGCCAGFAAGYDDVSPEHGITVSYTVMKPSDPDFITGGENYGESITSDLEVSIRNLQDQINSIIAEMNIQQVTSAVFTAITNLGELPGLFSNITKVFSKTKEALSKLKSRKKTSPMPIAATSIIDKTTVDVPNLTIVNKMPEEYELGIIYNSMRTKKLIEQKKHDFSTFTVATEVKLPYISKATNFSDQFMTSISSRGITIGKSDIIQYDPMNNILSAMNRKNAQIINYKIDPDLAHEVLSQMSTNATRSLFSLNVRKQLHINNSFDTPTYGQLVERILDDGQLLDILGKLNPNSVEELFSEFLHRIQHQLREY
Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
Rotavirus B (isolate RVB/Human/China/ADRV/1982) (RV-B) (Rotavirus B (isolate adult diarrhea rotavirus))
10,942
749
84,362
Capsid protein;Hemagglutinin;Host cell membrane;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Membrane;Outer capsid protein;Viral attachment to host cell;Viral penetration into host cytoplasm;Viral penetration via permeabilization of host membrane;Virion;Virus entry into host cell
GO:0016020; GO:0019062; GO:0020002; GO:0039624; GO:0039665; GO:0044168; GO:0044172
Evidence at protein level
3
SUBCELLULAR LOCATION: [Outer capsid protein VP4]: Virion {ECO:0000255|HAMAP-Rule:MF_04125}. Host rough endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_04125}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04125}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|HAMAP-Rule:MF_04125}. Note=The outer layer contains 180 copies of VP4, grouped as 60 dimers. Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles. {ECO:0000255|HAMAP-Rule:MF_04125}.
null
null
null
IPR042546;IPR038017;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus B (species)
null
false
Rotavirus B
3
row_201266
false
null
417,035
P26015
MDLIETVNACVKLQKRVLGLAPNTNLNTAEQSVLNDYNALPSRVNGKTYALLNQIAVYTPYTINAPIISLAVRISTDDYDDMRSGIESILDVLAAAIRTEGSRPTRVIERRVLEQNVKQLVDDLRLKSLISDLSIANLAAVDTAMIQPEVIETENPLYADIIEQIVHRPNIGMNGGNIRATLGRWSGNKGVVTCMSGMDSEHRFTVELKTRTCGIINIVYIPTAGTILIPMPAGRNREGDLIDVSAEMMADDFAIDFMDDDKIIQTETGVGVYSFPMCNRIRFRINPWNTQKDDDNLGTVHMINWAQGTAPKQPAISFMFETRRTFTEGNYQHLSRCAPKAQYMMDTQFNDVSFTNRPAVDWNIQSLLTSNTQRVWCQKIAMLIAAFAAKI
Intermediate capsid protein VP6
Rotavirus B (isolate RVB/Human/China/ADRV/1982) (RV-B) (Rotavirus B (isolate adult diarrhea rotavirus))
10,942
391
43,671
Capsid protein;Intermediate capsid protein;Virion
GO:0005198; GO:0019031; GO:0019064; GO:0039626; GO:0046789
Inferred from homology
2
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04126}. Note=Component of the intermediate capsid. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. {ECO:0000255|HAMAP-Rule:MF_04126}.
null
null
null
IPR001385;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus B (species)
null
false
Rotavirus B
4
row_399286
false
null
432,559
Q01754
MDLIETVNACVGLQKRVLKLAPNTNLNTAGQSVLNDYNALASRVNGRTYALLDQTAVYTPYTVNAPIISLAVRISTDDYDDMRSGIDSILDILAAAIRTEGSRPTRVIERRVIEPNVKQLVEDLKLKSLTSEISIANMAAVDTALIQPEIIETENPLFADIIEQVIHRPNASMTGGNIRATLGRWSGNKGIVTCMSGMDSEHRFTVDFKTRTCGIINVVYAPTAGVIMIPMPTGRNREGHLIDVSAEMMAENFAIDFMDDDDIIQTETGVGVFSFPMCNRIRFRINPWDMQKHNDNLWTVNLANWPQGTSPRQPAISFLFETRRTFTEGDYQHLSRCAPKVQYMMDTIFPETAFTNRPVVDWNVQSLLTSSSQKTWCQKIAMLIAAYAAKI
Intermediate capsid protein VP6
Rotavirus B (isolate RVB/Rat/United States/IDIR/1984/G1P[X]) (RV-B) (Rotavirus B (isolate infectious diarrhea of infant rats))
28,877
391
43,646
Capsid protein;Intermediate capsid protein;Virion
GO:0005198; GO:0019031; GO:0019064; GO:0039626; GO:0046789
Evidence at transcript level
2
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04126}. Note=Component of the intermediate capsid. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. {ECO:0000255|HAMAP-Rule:MF_04126}.
null
null
null
IPR001385;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus B (species), unclassified Rotavirus B (no rank)
null
false
Rotavirus B
5
row_414294
false
null
477,387
Q5K037
MALDALASILETVLRNCGINEISRVTTKFEEALDDCGMKVDDWREAYYKERFPKRMTATTMASQIMNFEIENLQLRNKAWAEGADRKFRLLSSFEIGNKDGHTILVPKTRNAEILLANSTSDLKLSSFPSEAVAKLAEENEKMRKQIEHLREQQTSKSTATLCEALENMTERMKLIEREKETVRRMFLECDKTNQRLRKQIQICEEEATDRLVLVNSHHREEILIMKREIYRLQMENVTLKEQIDSIEQELDHSNRIVRGLANRAGLVVDEVDSGNETSDLSDDSDHDDHENSESDLEDMMDPGEDERIPRGGENPRRQARMLQMREEMERLHEDMEILNLNLDLDI
Non-structural protein 3 (NSP3) (NCVP4) (Non-structural RNA-binding protein 34) (NS34)
Rotavirus B (isolate RVB/Human/China/ADRV/1982) (RV-B) (Rotavirus B (isolate adult diarrhea rotavirus))
10,942
347
40,357
Coiled coil;Host cytoplasm;RNA-binding;Translation regulation
GO:0003723; GO:0006417; GO:0030430
Evidence at transcript level
2
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04090}.
null
null
null
IPR002873;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus B (species)
null
false
Rotavirus B
6
row_458487
false
null
557,574
Q86199
MEYHHFLSEILGKTDLLPKYMSNQLCNPAQSSRKPEKVSFLKYENSLRECPEMPGDSILISDICPLNHEHFCGGIHIPQQENTSPKGRLAHAAADKIIWPCGLKSIKINDRKIEGHIFVKCRCGNLYPTWIPGEENFFFITCCANDTATVKLGKTDGDKCQNCSKFNRWYFPGLGFNSDISQYKTQFFCPACTPIRDLVSNMTKFGSTVFRSPSYTDMLKNYVWKRNLPNNSETAFRALNSPFIQTSITAYSKIDVDVNSMTVTELVASVNRTWNTEFKIIPINRTKVVFKDYYRGKSIIFHDNDHLHNQILLTLTDWHFL
Non-structural protein 1, peptide 2 (NSP1 peptide 2) (NSP1-2)
Rotavirus B (isolate RVB/Human/China/ADRV/1982) (RV-B) (Rotavirus B (isolate adult diarrhea rotavirus))
10,942
321
36,877
null
null
Inferred from homology
1
null
null
null
null
null
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus B (species)
null
false
Rotavirus B
7
row_537572
false
null
557,582
Q86517
MEFNQFLKEASGKVDLVPIYMSNPSCNPIHSSRKPGKVSALKYDNPLKECPEIPGDSVLISDVCPFIHEHFCGGIHIPYQHNMRPKGRITHVSADKIVWPCGLRSIKLDGKLVVGHMFVKCRCGNMYPTWISGESDFFFITCCANDTPAIKIGLANGDKCQNCLRLKRWYNPGPGFKSGINHYIAPFFCPVCTPIRDLVSNMTRFGAVSFDSPDYAEMKRNYDWKRSYPNNCESAFRSLNSPLIQTLPTVCDTVCASSGTTVTEMIASINRSWCTGFKIIPINRTRVLLKDDYRGRIIEFQDNNHLHNQIMAAMTEWKFL
Non-structural protein 1, peptide 2 (NSP1 peptide 2) (NSP1-2)
Rotavirus B (isolate RVB/Rat/United States/IDIR/1984/G1P[X]) (RV-B) (Rotavirus B (isolate infectious diarrhea of infant rats))
28,877
320
36,220
null
null
Inferred from homology
1
null
null
null
null
null
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus B (species), unclassified Rotavirus B (no rank)
null
false
Rotavirus B
8
row_537579
false
null
284,604
Q86197
MTQSVSLSDFIVKTEDGYMPSDRECIALDRYLSKEQKELRETFKDGKNDRAALRIKMFLCPSPSRRFTQHGVVPMREIKTNTDMPSTLWTLVTDWLLNLLQDEENQEMFEDFISSKFPDVLASADKLARFAQRLEDRKDVLRKNFGKAMNAFGACFWAIKPTFATEGKCNVVRASDDSIILEFQPVPEYFRCGKSKATFYKLYPLSDEQPVNGMLALKAVAGNQFFMYHGHGHIRTVPYHELLTLSNHSLVKIKKRSKTFLNHHSQLNVVVNFSICSME
Non-structural protein 2 (NSP2) (EC 3.6.4.-) (NCVP3) (Non-structural RNA-binding protein 35) (NS35)
Rotavirus B (isolate RVB/Human/China/ADRV/1982) (RV-B) (Rotavirus B (isolate adult diarrhea rotavirus))
10,942
279
32,110
ATP-binding;Host cytoplasm;Hydrolase;Magnesium;Metal-binding;Nucleotide-binding;RNA-binding
GO:0003723; GO:0005524; GO:0016817; GO:0019079; GO:0030430; GO:0046872
Evidence at transcript level
3
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04089}. Note=Found in spherical cytoplasmic structures, called viral factories, that appear early after infection and are the site of viral replication and packaging. {ECO:0000255|HAMAP-Rule:MF_04089}.
null
null
null
IPR003668;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus B (species)
null
false
Rotavirus B
9
row_268812
false
null
415,734
P18570
MASLLLLVLAAAVTAQLNIVPSTHPEVCVLYADDHQADANKFNGNFTQIFHSYNSITLSFMSYSSSSYDVIDIISKYDLSSCNILAIDVFNASMDFNVFLQSTNNCSKYNANKVHHVKLPRGEEWFSYSKNLKFCPLSDSLIGMYCDTQLSDTYFEISTGGTYEVTDIPEFTQMGYTFHSSEEFYLCHRISSEAWLNYHLFYRDYDVSGVISKQVNWGNVWSGFKTFAQVLYKILDLFFNSKRNVEPRA
Outer capsid glycoprotein VP7
Rotavirus B (isolate RVB/Human/China/ADRV/1982) (RV-B) (Rotavirus B (isolate adult diarrhea rotavirus))
10,942
249
28,459
Calcium;Capsid protein;Disulfide bond;Glycoprotein;Host endoplasmic reticulum;Host-virus interaction;Metal-binding;Outer capsid protein;Signal;T=13 icosahedral capsid protein;Virion
GO:0016020; GO:0039621; GO:0039624; GO:0044166; GO:0046872
Inferred from homology
2
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04130}. Host endoplasmic reticulum lumen {ECO:0000255|HAMAP-Rule:MF_04130}. Note=The outer layer contains 780 copies of VP7, grouped as 260 trimers. Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles. {ECO:0000255|HAMAP-Rule:MF_04130}.
SIGNAL 1..15; /evidence="ECO:0000255|HAMAP-Rule:MF_04130"
null
PF05868;
IPR008818;IPR001963;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus B (species)
null
false
Rotavirus B
10
row_398029
false
null
417,923
P30889
MTTMLLLLVVAALANGQLTILPHEESQICFLQPDNPGFDFDGNFTNIFRDYASVKISSFTYKAQDADIVEILNVDRDRSCTILAIYIADSTLDFNTFLQSENECVKYAASKKHYIKLPRDREYFALAKNLSFCPLNDDLIGIYCDTQLETTYFSVARSSNYDVTDIPEFTELGYVFHSNDHFYICERKSEGNWIDYQLFYQNDAPLGTVSQRVNWGNVWSNVKTVAQMVYKILDIFFGKRNIEPRA
Outer capsid glycoprotein VP7
Rotavirus B (isolate RVB/Rat/United States/IDIR/1984/G1P[X]) (RV-B) (Rotavirus B (isolate infectious diarrhea of infant rats))
28,877
246
28,319
Calcium;Capsid protein;Disulfide bond;Glycoprotein;Host endoplasmic reticulum;Host-virus interaction;Metal-binding;Outer capsid protein;Signal;T=13 icosahedral capsid protein;Virion
GO:0016020; GO:0039621; GO:0039624; GO:0044166; GO:0046872
Inferred from homology
2
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04130}. Host endoplasmic reticulum lumen {ECO:0000255|HAMAP-Rule:MF_04130}. Note=The outer layer contains 780 copies of VP7, grouped as 260 trimers. Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles. {ECO:0000255|HAMAP-Rule:MF_04130}.
SIGNAL 1..16; /evidence="ECO:0000255|HAMAP-Rule:MF_04130"
null
PF05868;
IPR008818;IPR001963;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus B (species), unclassified Rotavirus B (no rank)
null
false
Rotavirus B
11
row_400158
false
null
417,924
P30890
MAEASEFNFNLRRKSRAVTASRRVKEEVKEKQKMDDSKSQVVDVDSVSVYSHESSRSNYSDAYEKLKREPVVEESNDARYRTFEFSEDEETFKPANKMSDKSQRNSKSKHTEGLECSDTVLEKISELTLEIEKVKQMNQPITVDAAFNMTLRNVDNLTTRQKQALVNSIINSMN
Non-structural protein 5 (NSP5) (NS26)
Rotavirus B (isolate RVB/Rat/United States/IDIR/1984/G1P[X]) (RV-B) (Rotavirus B (isolate infectious diarrhea of infant rats))
28,877
174
20,057
Glycoprotein;Host cytoplasm;Nucleotide-binding;RNA-binding
GO:0000166; GO:0000287; GO:0003723; GO:0016887; GO:0019079; GO:0030430
Inferred from homology
2
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04092}. Note=Found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. {ECO:0000255|HAMAP-Rule:MF_04092}.
null
null
PF17580;
IPR002512;IPR020244;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus B (species), unclassified Rotavirus B (no rank)
null
false
Rotavirus B
12
row_400159
false
null
415,735
P18571
MAEASEFNFTIKRKQRTMSDRRTREDTKQKKIEEKSDIDLVDSASVYSQESSRSNYSDAYDKLKREPMVEESNDAKYRNFEFSEDEEVHRPSSKASDKSYREMKRKHDDINTSDSILEKLSELNLEIEKIKQMNQPITIDAAFNMILRNVDNLTIRQKQALINAIVNSMN
Non-structural protein 5 (NSP5) (NS26)
Rotavirus B (isolate RVB/Human/China/ADRV/1982) (RV-B) (Rotavirus B (isolate adult diarrhea rotavirus))
10,942
170
19,938
Glycoprotein;Host cytoplasm;Nucleotide-binding;RNA-binding
GO:0000166; GO:0000287; GO:0003723; GO:0016887; GO:0019079; GO:0030430
Inferred from homology
2
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04092}. Note=Found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. {ECO:0000255|HAMAP-Rule:MF_04092}.
null
null
PF17580;
IPR002512;IPR020244;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus B (species)
null
false
Rotavirus B
13
row_398030
false
null
557,581
Q86516
MGNRQSSAQLNSHLTQISSQHSNLYISDSKTSTFQTQHIILVAGVGIIVALFILLVCSCVLNCYLCNKFKRENGIQSISKRSLRQSRPSPNLYVQPVMQSNPFIKEARESICSEV
Non-structural protein 1, peptide 1 (NSP1 peptide 1) (NSP1-1)
Rotavirus B (isolate RVB/Rat/United States/IDIR/1984/G1P[X]) (RV-B) (Rotavirus B (isolate infectious diarrhea of infant rats))
28,877
115
12,845
Host membrane;Membrane;Transmembrane;Transmembrane helix
GO:0016020; GO:0033644
Inferred from homology
1
SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
null
TRANSMEM 39..59; /note="Helical"; /evidence="ECO:0000255"
null
null
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus B (species), unclassified Rotavirus B (no rank)
null
false
Rotavirus B
14
row_537578
false
null
557,573
Q86198
MGNRQSSAQLNSHLTHINSQNSNLFISDSKTAVFHTQHILLAAGVGIIATLLVLLLCSCVLNCYLCRRLKRTNGVSSLLERNLRQNGSSAKIYVKPVMQSSTIIEEA
Non-structural protein 1, peptide 1 (NSP1 peptide 1) (NSP1-1)
Rotavirus B (isolate RVB/Human/China/ADRV/1982) (RV-B) (Rotavirus B (isolate adult diarrhea rotavirus))
10,942
107
11,726
Host membrane;Membrane;Transmembrane;Transmembrane helix
GO:0016020; GO:0033644
Inferred from homology
1
SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
null
TRANSMEM 39..59; /note="Helical"; /evidence="ECO:0000255"
null
null
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus B (species)
null
false
Rotavirus B
15
row_537571
false
null
205,981
P59170
MRTLWIVAVWLVGVEGNLYQFGKMIKNKTGKPAMFSYSAYGCYCGWGGQGKPQDPSDRCCFLHDCCYTRVNNCSPKMTLYSYRFENGDIICGDNDPCRKAVCECDREAAICLGENVNTYDEKYRFYSSSYCTEEESEKC
Acidic phospholipase A2 4 (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
Echis carinatus sochureki (Saw-scaled viper)
124,223
139
15,895
Calcium;Disulfide bond;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Secreted;Signal
GO:0005509; GO:0005543; GO:0005576; GO:0006644; GO:0016042; GO:0042130; GO:0047498; GO:0050482
Evidence at transcript level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..16; /evidence="ECO:0000250"
null
PF00068;
IPR001211;IPR033112;IPR016090;IPR036444;IPR033113;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Echis (genus), Echis carinatus (species)
null
false
Echis carinatus
0
row_192428
false
null
545,061
P69174
MAKPARRKCKICKEWFHPAFSNQWWCCPEHGTQLALERRSKEREKAEKAAEKKRRREEQKQKDKLKIRKLALKPRSYWIKQAQQAVNAFIRERDRDLPCISCGTLTSAQWDAGHYRTTAAAPQLRFDERNIHKQCVVCNQHKSGNLVPYRVELINRIGQEAVDEIESNHNRHRWTVEECRAIKAKYQQKLKDLRNSRSEAA
Protein ninG
Escherichia phage 933W (Bacteriophage 933W)
10,730
201
23,790
Reference proteome
null
Inferred from homology
1
null
null
null
PF05766;
IPR008713;
null
Viruses (no rank), Duplodnaviria (realm), Heunggongvirae (kingdom), Uroviricota (phylum), Caudoviricetes (class), Sepvirinae (subfamily), Traversvirus (genus), Traversvirus tv933W (species)
ninG L0097
false
Traversvirus tv933W
0
row_525303
false
null
208,674
P68920
MSRKLRYGLSAAVLALIAAGASAPEILDQFLDEKEGNHTTAYRDGAGIWTICRGATRVDGKPVIPGMKLSKEKCDRVNAIERDKALAWVEKNIKVPLTEPQKAGIASFCPYNIGPGKCFPSTFYRRINAGDRKGACEAIRWWIKDGGRDCRIRSNNCYGQVSRRDQESALACWGIDR
SAR-endolysin (EC 3.2.1.17) (Endolysin) (Lysis protein) (Lysozyme) (Muramidase)
Escherichia phage 933W (Bacteriophage 933W)
10,730
177
19,607
Antimicrobial;Bacteriolytic enzyme;Cytolysis;Glycosidase;Host cell inner membrane;Host cell lysis by virus;Host cell membrane;Host membrane;Hydrolase;Membrane;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Viral release from host cell
GO:0003796; GO:0009253; GO:0016020; GO:0016998; GO:0020002; GO:0031640; GO:0042742
Inferred from homology
3
SUBCELLULAR LOCATION: Host cell inner membrane {ECO:0000255|HAMAP-Rule:MF_04136}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04136}; Periplasmic side {ECO:0000255|HAMAP-Rule:MF_04136}. Note=Secreted as a signal-anchored, membrane-tethered, inactive endolysin which is subsequently refolded, activated and released by membrane depolarization driven by the pinholin. {ECO:0000255|HAMAP-Rule:MF_04136}.
null
TRANSMEM 1..23; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255"
PF00959;
IPR051018;IPR034690;IPR002196;IPR023346;IPR023347;IPR043688;
null
Viruses (no rank), Duplodnaviria (realm), Heunggongvirae (kingdom), Uroviricota (phylum), Caudoviricetes (class), Sepvirinae (subfamily), Traversvirus (genus), Traversvirus tv933W (species)
R L0108
false
Traversvirus tv933W
1
row_195083
false
null
313,143
Q9XJJ6
MNRVLCVVIIVLAVGYGALWLATNHYRDNALTYKAQRDKKARELEQANATITDMQVRQRDVAALDAKYSRELADARAENETLRADVAAGRKRLRINATCSGTVREATGTSGVDNATGPRLADTAERDYFILRERLITMQKQLEGTQKYINEQCR
Spanin, inner membrane subunit (i-spanin) (Lysis protein Rz)
Escherichia phage 933W (Bacteriophage 933W)
10,730
154
17,320
Coiled coil;Cytolysis;Disulfide bond;Host cell inner membrane;Host cell lysis by virus;Host cell membrane;Host membrane;Membrane;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Viral release from host cell
GO:0016020; GO:0020002; GO:0044659
Inferred from homology
3
SUBCELLULAR LOCATION: Host cell inner membrane {ECO:0000255|HAMAP-Rule:MF_04137}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04137}; Periplasmic side {ECO:0000255|HAMAP-Rule:MF_04137}.
null
TRANSMEM 4..24; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255"
PF03245;
IPR004929;
null
Viruses (no rank), Duplodnaviria (realm), Heunggongvirae (kingdom), Uroviricota (phylum), Caudoviricetes (class), Sepvirinae (subfamily), Traversvirus (genus), Traversvirus tv933W (species)
Rz
false
Traversvirus tv933W
2
row_296646
false
null
427,367
P68922
MRDIRQVLERWGAWAANNYEDVTWSPIAAGFKGLIPEKVKSRPQCCDDDAMVICGCIARLYRNNRDLHDLLVDYYVLGETFMALARKHGCSDTCIGKRLHKAEGIVEGMLMMLGVRLEMDRYVERELPGGRTSVFYQRKNSLRS
Antitermination protein Q
Escherichia phage 933W (Bacteriophage 933W)
10,730
144
16,532
DNA-binding;Reference proteome;Transcription;Transcription regulation;Transcription termination
GO:0003677; GO:0006353; GO:0060567
Inferred from homology
2
null
null
null
PF06530;
IPR010534;
null
Viruses (no rank), Duplodnaviria (realm), Heunggongvirae (kingdom), Uroviricota (phylum), Caudoviricetes (class), Sepvirinae (subfamily), Traversvirus (genus), Traversvirus tv933W (species)
Q L0099
false
Traversvirus tv933W
3
row_409449
false
null
545,063
P69176
MTFTVKTIPDMLVEAYENQTEVARILNCSRNTVRKYTGDKEGKRHAIVNGVLMVHRGWGKDTDA
Protein ninH
Escherichia phage 933W (Bacteriophage 933W)
10,730
64
7,266
Reference proteome
null
Inferred from homology
1
null
null
null
PF06322;
IPR010454;
null
Viruses (no rank), Duplodnaviria (realm), Heunggongvirae (kingdom), Uroviricota (phylum), Caudoviricetes (class), Sepvirinae (subfamily), Traversvirus (genus), Traversvirus tv933W (species)
ninH L0098
false
Traversvirus tv933W
4
row_525305
false
null
562,291
Q9ZWX5
MRRQQRSITDIICENCKYLPTKRGIQKFSFEQNTMMSVQGGLSSLSDSQLTCIFKYCTLQRACV
Protein ninE
Escherichia phage 933W (Bacteriophage 933W)
10,730
64
7,387
null
null
Inferred from homology
1
null
null
null
PF05322;
IPR007986;
null
Viruses (no rank), Duplodnaviria (realm), Heunggongvirae (kingdom), Uroviricota (phylum), Caudoviricetes (class), Sepvirinae (subfamily), Traversvirus (genus), Traversvirus tv933W (species)
ninE
false
Traversvirus tv933W
5
row_542262
false
null
526,308
Q9XJJ7
MRELKMKLCVLMLPLVVSACGSTPPAPVPCVKPPAPPAWIMQPAPDWQTPLNGIISSSERG
Spanin, outer membrane subunit (o-spanin) (Outer membrane lipoprotein Rz1)
Escherichia phage 933W (Bacteriophage 933W)
10,730
61
6,509
Cytolysis;Disulfide bond;Host cell lysis by virus;Host cell outer membrane;Host membrane;Lipoprotein;Membrane;Palmitate;Reference proteome;Signal;Viral release from host cell
GO:0016020; GO:0020002; GO:0044659
Inferred from homology
2
SUBCELLULAR LOCATION: Host cell outer membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Periplasmic side {ECO:0000250}.
SIGNAL 1..19; /evidence="ECO:0000250"
null
PF06085;
IPR010346;
null
Viruses (no rank), Duplodnaviria (realm), Heunggongvirae (kingdom), Uroviricota (phylum), Caudoviricetes (class), Sepvirinae (subfamily), Traversvirus (genus), Traversvirus tv933W (species)
Rz1 L109
false
Traversvirus tv933W
6
row_506669
false
null
210,986
P84987
NNCPLDWLPMNGLCYKIFNQLKTWEDAEMFCRKYKPGCHLASFHLYGESLEIAEYISDYHKGQDNVWIGLWDKKKDFSWEWTDRSCIDYLNWNKNQPDHYKNKEFCVELVSLSGYRLWNDQVCESKDAFLCQCKF
C-type Lectin CRL (CTL)
Crotalus ruber ruber (Red diamond rattlesnake)
8,736
135
16,274
Calcium;Direct protein sequencing;Disulfide bond;Lectin;Metal-binding;Secreted
GO:0005576; GO:0030246; GO:0046872
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17251046}.
null
null
PF00059;
IPR001304;IPR016186;IPR050111;IPR018378;IPR016187;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Crotalus (genus), Crotalus ruber (species)
null
false
Crotalus ruber
0
row_197296
false
null
211,567
P92492
PIAGSMVLAAILLKLGGYGIIRMMQILPTTKTDMFLPFVVLALWGAILANLTCLQQTDLKSLIAYSSISHMGLVVAAIIIQTPWGLSGAMALMIAHGFTSSALFCLANTTYERTHTRILILTRGLHNILPMATTWWLLTNLMNIAVPPTMNFTGELLIMSALFNWCPTTIIMLGLSMLITASYSLHMFLSTQMGPTLLNNQTEPTHSREHLLMILHLIPLMMISMKPELVI
NADH-ubiquinone oxidoreductase chain 4 (EC 7.1.1.2) (NADH dehydrogenase subunit 4)
Agkistrodon contortrix contortrix (Southern copperhead)
8,713
231
25,465
Electron transport;Membrane;Mitochondrion;NAD;Respiratory chain;Translocase;Transmembrane;Transmembrane helix;Transport;Ubiquinone
GO:0008137; GO:0015990; GO:0031966; GO:0042773; GO:0048039
Inferred from homology
3
SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
null
TRANSMEM 1..21; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 34..54; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 63..85; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 89..111; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 128..148; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 156..176; /note="Helical"; /evidence="ECO:0000255"
PF00361;
IPR003918;IPR001750;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Agkistrodon (genus), Agkistrodon contortrix (species)
MT-ND4 MTND4 NADH4 ND4
false
Agkistrodon contortrix
0
row_197811
false
null
211,618
P92845
YINYKNMSHQHMLTLFNLLPVGSNISIWWNFGSMLLTCLMIQIATGFFLAIHYTANINLAFSSIIHISRDVPYGWIMQNTHAIGASLFFICIYIHIARGIYYGSYLNKEVWLSGTTLLIILMATAFFGYVLPWGQMSFWAATVITNLLTAIPYLGTTLTTWLWGGYAINDPTLTRFFALHFILPFAIISMSSIHILLLHNEGSNNPLGTNSDID
Cytochrome b (Complex III subunit 3) (Complex III subunit III) (Cytochrome b-c1 complex subunit 3) (Ubiquinol-cytochrome-c reductase complex cytochrome b subunit)
Agkistrodon contortrix contortrix (Southern copperhead)
8,713
214
24,168
Electron transport;Heme;Iron;Membrane;Metal-binding;Mitochondrion;Mitochondrion inner membrane;Respiratory chain;Transmembrane;Transmembrane helix;Transport;Ubiquinone
GO:0005743; GO:0006122; GO:0008121; GO:0046872
Inferred from homology
3
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00157}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00157}.
null
TRANSMEM 31..51; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"; TRANSMEM 75..96; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P00157"; TRANSMEM 111..131; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P00157"; TRANSMEM 176..196; /note="Helical"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
PF00033;
IPR005797;IPR027387;IPR048259;IPR016174;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Agkistrodon (genus), Agkistrodon contortrix (species)
MT-CYB COB CYTB MTCYB
false
Agkistrodon contortrix
1
row_197862
false
null
465,666
Q45UF9
MEVIEKLETIRETLNDTKDKKDFQKIHDELVQYLDGIDPLTIDDDKWNEILKLFKIIIVKLKNSTIKTTSLENELTQHEKKRTVKEVEKVEEDMKVDVANDNSKPTLMDKVLQVSSQPNNPYSADVLQIRTILSKTLFVDTDSEAYSLYVPESQKLDVSPITIELTTIEKYQPKVNILKQAVIVPSQNPLLADTYGAPEILFSTDFFDDITSNSSEGLQLYFFDKAYKLKKELPNLPFLSSLDKDVNPLNPLNSVCKSFGQEKYYDMVMDRTDRGLDARRAAMQFDNVIVDAQNRTVQFNVRMHPFDLQLLRISQQFAEPMQDLAPVVREYMMLGADGYVLTQKTRLDRDQQLIANRRSVVFDRMCELSGPLYRSRIVHSMRMMSKLWRTNVFRTSLEDEITKIYAAAEVSMVSIDATTSALSTINIASAEQTLNALLNMSFFRCELDLIGSQSSFGAAMSAMIALMILPTDQENMDDEVFDVLCNLVYNELIAWAADRPVFVRRAGATNAFRQFVNAGLNRDITNYMRFVLLRRPWLPLYNSRDVRRNAHVLVPNVDLANINDQVYVAINSFLNGIIEASRRNPNPNKTISANSFRKLMKNMRDICVNRLMPVIRLIRYNVERIGMILHMLPYSADIFDINRNLRDERLRIKIPMSGFLSLVMGITKAPDAFDWSQVLNFADDVRKMDYAEAISIEDSASVAIMRNDANRATSKKEIFISEVKPPTPTVASIQKIPSATLTAMFSDRQLINLIRDTHSFRVIREIAVALQAAFDNSPTSQHGVGKGAVLHPVPQNFGRSSQFVRRDNILLQRPAGIQQFTIEDLKQGRYFQGLMAQIRARQPIIVNGPIPLRISDAAEIEQVTLAFLTMNSPYDAYIDPRDLKQQKLLTDREVDLFIDQNPARPNDEFDNVMARTSVFIIDAPRAIVPINPQRLNFPYHDIMVTDSVTKFIEFTVALTPDLQLFNGLLVFEQ
Inner capsid protein VP2
Rotavirus X (strain RVX/Human/China/NADRV-J19/1997/GXP[X]) (RV ADRV-N) (Rotavirus (isolate novel adult diarrhea rotavirus-J19))
335,103
973
111,047
Capsid protein;Inner capsid protein;Reference proteome;RNA-binding;T=2 icosahedral capsid protein;Virion
GO:0003723; GO:0019013; GO:0039616; GO:0039625
Inferred from homology
2
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04123}. Note=Inner capsid protein. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. {ECO:0000255|HAMAP-Rule:MF_04123}.
null
null
null
IPR007779;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus H (species)
null
false
Rotavirus H
0
row_447022
false
null
245,921
Q45UF8
MSLRSLLITTEAVGETTQTSDHQTSFSTRTYNEINDRPSLRIEKDGEKAYCFKNLDPVRYDTRMGEYPFDYGGQSTENNQLQFDLFTKDLKADTDIDLSDDVKDDLKRQIMEYYQQGYRAIFLVRPQNQEQHYIASYSSTNLNFTSQPSIGVNLSILNKIQENKLYIYSTQPHIPSVGCEMIAKIFRTDIDNENSLINYSAPVTVTISVTKATFGDTFVCNHPNMNYQDLIPTMTKNSIYHDVKRITKIHEYINSKKKKKNSTSKIGGIQIAESKDGFWKILTKNYQIKLKFGVEGYGVMGGTFGNWLIDSGFKTVETNYEYQRNGKTINATTVASVKPSRKCGTRSPVFGQLQFSGEMMVLSHNDILTVFYTEREWALSNAIYAKNFATDFKRQFEITAQSDELLVRTNVVPHTIKNTPGKALMEYSHGGFGQIDTSDYTGMALTFRFRCISEDLPEGYYDRDKALAFANVGLTSFQDRQEANGTYWVYNTSTVGFGSCYPKKEFEYDINVTYTTLLPSDPEFTTGGTNYAQSVTAVLEESFINLQNQVNEMLTRMNISDLTSGVMSVFSVATSFPQILDGISDLLKAASSAFKKVKGKVGSVAKRLRGKRYVRLFDENVSIEETPRFLDSIRSSRRPSILSNMFNDDETFTALHTLASRTNSVASDVTYLQPIITTRIANSTPPVIAPASSVTYAKLKDISKIINAEIDPKSIMEFNQISNTISILDSTKKLAQYAVDPDIIDGILNKMVGGHARSLFSLKVRKHLLDAVEKDAFVKYNYHDLMGKLLNDRELLDITNNLSSQKQFELAKEFRDLLINALA
Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
Rotavirus X (strain RVX/Human/China/NADRV-J19/1997/GXP[X]) (RV ADRV-N) (Rotavirus (isolate novel adult diarrhea rotavirus-J19))
335,103
823
92,912
Capsid protein;Hemagglutinin;Host cell membrane;Host endoplasmic reticulum;Host membrane;Host-virus interaction;Membrane;Outer capsid protein;Reference proteome;Viral attachment to host cell;Viral penetration into host cytoplasm;Viral penetration via permeabilization of host membrane;Virion;Virus entry into host cell
GO:0016020; GO:0019062; GO:0020002; GO:0039624; GO:0039665; GO:0044168; GO:0044172
Inferred from homology
3
SUBCELLULAR LOCATION: [Outer capsid protein VP4]: Virion {ECO:0000255|HAMAP-Rule:MF_04125}. Host rough endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_04125}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04125}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|HAMAP-Rule:MF_04125}. Note=The outer layer contains 180 copies of VP4, grouped as 60 dimers. Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles. {ECO:0000255|HAMAP-Rule:MF_04125}.
null
null
PF17477;
IPR042546;IPR035330;IPR038017;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus H (species)
null
false
Rotavirus H
1
row_231368
false
null
245,920
Q45UF7
MAKLIIINSEKGEKVETHEDIFKLSNLQQREIYAITNERTKSILLNQTFYTILDIENEPKDKVAFDSYNSLFPTSIFSYSRQDRLFGTCNHVLDNNIHYSFALFDSMVDNLSTYLPNDWNIIKISDSIDYPIGNDLLFYVFDNLVHMTIDQFVNSEEKQMNTVPKCKESQDKIKEVFTDIMSHLYMPAIDYDPQSYNYRVSRREIGNLVRDQVFSLVKGHIHLIGPEMESLRNIIMFLHAGNSITFHTIDTSTKSSYIKELEFNKKTKLTMASVLVNQRKNMNNFFKGLIRHYITYGIPRKVYYIGAYPSYWLELITWVPFNIVAYDPKYRRVDNDKIIWYDRLFDRNDIETIESKSYIYIDIRTDVRNLDTTKKQRIFKEEDDMIVDMAIKLASKQCTVMFKRKIFPGNNMSFGDPLFHPKLTQLGREYYNCITTIVSPSVYKESELYSLLLSARSNNVSNYVYGGSKFDQFSIVNCNSTVVALYSLSNTVNSLKTIEHAIKYNHIITFPHRTDRGDWRNIEELDNSSPFQNRKRQLEFEDWSIDPKNYVMKFRCEMVSESVFLQLGHSRALIPDLYNHMISLRMEMPLFYSDRFFSHIGIRQPSIFKRDSYMTSRLSAYISRQLTHSINLSVLKRNHFEGYSGHLIAIETSFSSLVFTMSPYRWLIRAKKLLTKNKMRDKFKIGDGQPHTREEFENTYDYLKINRLVNSTFRSLLLD
Protein VP3 [Includes: mRNA guanylyltransferase (EC 2.7.7.50); mRNA (guanine-N(7))-methyltransferase (EC 2.1.1.56)]
Rotavirus X (strain RVX/Human/China/NADRV-J19/1997/GXP[X]) (RV ADRV-N) (Rotavirus (isolate novel adult diarrhea rotavirus-J19))
335,103
719
84,711
GTP-binding;Methyltransferase;mRNA capping;mRNA processing;Multifunctional enzyme;Nucleotide-binding;Nucleotidyltransferase;Reference proteome;RNA-binding;S-adenosyl-L-methionine;Transferase;Virion
GO:0003723; GO:0004482; GO:0004484; GO:0005525; GO:0016032; GO:0019013
Inferred from homology
3
SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=Attached inside the inner capsid as a minor component. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging (Potential). {ECO:0000305}.
null
null
PF06929;
IPR011181;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus H (species)
null
false
Rotavirus H
2
row_231367
false
null
465,665
Q45UF5
MDLIETINAVVELQHRVRNLSPNTNIYQDGQTTINDYNAIASRCNGKVYNLRDQIAQLSPFQVHMPVIPISTILSTDDHETMSAGIESLFDVLAAAIRTEGSRQNRAVVTKSIEPEVLKAVLDIGIRSQFSENPYANMLQVDTAKMEQQLEPIDDPLASQRINMLAAGGATNNTGGGYHALVGRATGKTGIITIIQGRPGAVTFNLNMKVPCSGVLSLTLLPAPGVIQLSLGNQPPNNIPVHAECVDVSTVFTEGDIVIRFELAGRVVGNANKLGTLNFPLCDRISITIEPWNANKQNNANANFNNWPAGTAQRQPTISLFVNIINASSLIDYETHSKYLAGATYLMGTTFSEDSFIASPPNVVWTMSSLLSGAPPQYIHWTRKIACMIAAFSCKI
Intermediate capsid protein VP6
Rotavirus X (strain RVX/Human/China/NADRV-J19/1997/GXP[X]) (RV ADRV-N) (Rotavirus (isolate novel adult diarrhea rotavirus-J19))
335,103
396
42,922
Capsid protein;Intermediate capsid protein;Reference proteome;Virion
GO:0005198; GO:0019031; GO:0019064; GO:0039626; GO:0046789
Inferred from homology
2
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04126}. Note=Component of the intermediate capsid. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. {ECO:0000255|HAMAP-Rule:MF_04126}.
null
null
null
IPR001385;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus H (species)
null
false
Rotavirus H
3
row_447021
false
null
551,273
Q45UF6
MMSIQRAAQINRQFDYMSIKELWMAKFPLHKPGDCLDMFKNGDYTGPTMGCIQKTKASKKNTIFHIKSDFNSTEYDEPPISGFKMFTQHCCQRIDEHFCGALHPVISNIEFEHNQLKTRPQVASELNLFIPCGIKNLKIESGEKSTWIVGTKFRKCMCLKPVIVAATIIGTPINKNLITFCSSDYIQVIVNRNREGSCGICMGNVSTYEACGNWTNETWGEEFSLDLKLCYKCTPVAFIFSLMMSTGHKPYVSKKQFEENRRKWERVLNYKICKENLDSHLACANHENVYKSIKKYEFFDSVWVYHLANSSWVRDLTRECIESNPGPNYIQLLNEHSQRYGFVQPTYEIIAVVSDGHHSYQCTCYYKDMKTQSTGPSKKNAKHQAAEQMFRHQCF
Non-structural protein 1 (NSP1)
Rotavirus X (strain RVX/Human/China/NADRV-J19/1997/GXP[X]) (RV ADRV-N) (Rotavirus (isolate novel adult diarrhea rotavirus-J19))
335,103
395
45,649
Reference proteome;RNA-binding
GO:0003723
Predicted
1
null
null
null
PF00035;
IPR014720;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus H (species)
null
false
Rotavirus H
4
row_531331
false
null
245,919
Q45UF4
MVSIKVSLADFIVKTEEGWIPSDNCPALDRFKTKTEKELLDSIKKEGADRASIRKQLFLTSISNKRLTQLGGVPVRDIRTSTTIPSSTRNLITDWLLNIFNDEESGEEVESAIASKYPDIFCSADKISRVAQRLENRRDRVHEDGFRILSATMLAIDSDIATEGKCEIVRATEDAIIAKFEPVSEHLCIGNPRGVFYKAFPIKKEQPMVYGVKALLGISNRDFIMNHGHGHLRTVPYSEINNAVRSFAKKNEAEIKRIRSDSLSPNAGEKFINMCDMLLQKEKIETVIAKIMKSDKN
Non-structural protein 2 (NSP2) (EC 3.6.4.-) (NCVP3) (Non-structural RNA-binding protein 35) (NS35)
Rotavirus X (strain RVX/Human/China/NADRV-J19/1997/GXP[X]) (RV ADRV-N) (Rotavirus (isolate novel adult diarrhea rotavirus-J19))
335,103
297
33,433
ATP-binding;Host cytoplasm;Hydrolase;Magnesium;Metal-binding;Nucleotide-binding;Reference proteome;RNA-binding
GO:0003723; GO:0005524; GO:0016817; GO:0019079; GO:0030430; GO:0046872
Inferred from homology
3
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04089}. Note=Found in spherical cytoplasmic structures, called viral factories, that appear early after infection and are the site of viral replication and packaging. {ECO:0000255|HAMAP-Rule:MF_04089}.
null
null
null
IPR003668;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus H (species)
null
false
Rotavirus H
5
row_231366
false
null
482,019
Q5Y9A9
MAELVCDALATLTRNTYGDNDESAKFCRMFRTMIRDSGLYGNIENWRAAFYRERLPKRMSHSTVSIQLDNLEREVLKIRAEGFCQGYTRKERTLNAFDLSDDGKGNTIIKPTTHLSSIILQNSYNSAFKLPKIPDGLLEKTRYELEEEKKNNDILKQKIKELENTISQLENYENEAKASQFVLEHLKFTNESLKIQRDEAQICLIGLCNKFGLQCEIDNSIHVTESDKKGKRKGRKNRRIEVSFGAPGHDLTEQISTLSDVE
Non-structural protein 3 (NSP3) (NCVP4) (Non-structural RNA-binding protein 34) (NS34)
Rotavirus X (strain RVX/Human/China/NADRV-J19/1997/GXP[X]) (RV ADRV-N) (Rotavirus (isolate novel adult diarrhea rotavirus-J19))
335,103
262
30,118
Coiled coil;Host cytoplasm;Reference proteome;RNA-binding;Translation regulation
GO:0003723; GO:0006417; GO:0030430
Inferred from homology
2
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04090}.
null
null
null
IPR002873;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus H (species)
null
false
Rotavirus H
6
row_463053
false
null
465,664
Q45UF2
MLLFIILSVGVDAISYIQNDRSNDLCIVYEMTSFGTSFNNANDSLVKLHKHMGLKYEVCKIESNANALTQMQKCNCIYDDTPQIVVFTNFKKSSLKTLIGTENKCELLPQTTIYTPTVDIESEYFIYGNDVKICYLDKNLLGIGCDATDTTSWLDLDAGLPTNHALDIPEITSDGFKLFAKYSDSFLCQRLMDEPKKQIQFYAEVDNVPSNDVIESSRSWASVWKVVKTVLHFTYHILDLFYGNRRATARMIEHSPLG
Outer capsid glycoprotein VP7
Rotavirus X (strain RVX/Human/China/NADRV-J19/1997/GXP[X]) (RV ADRV-N) (Rotavirus (isolate novel adult diarrhea rotavirus-J19))
335,103
258
29,265
Calcium;Capsid protein;Glycoprotein;Host endoplasmic reticulum;Host membrane;Membrane;Outer capsid protein;Reference proteome;T=13 icosahedral capsid protein;Transmembrane;Transmembrane helix;Virion
GO:0016020; GO:0039621; GO:0039624; GO:0044169
Inferred from homology
2
SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host rough endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}; Lumenal side {ECO:0000305}. Note=Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles (By similarity). {ECO:0000250}.
null
TRANSMEM 1..?13; /note="Helical"; /evidence="ECO:0000255"
PF05868;
IPR008818;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus H (species)
null
false
Rotavirus H
7
row_447020
false
null
465,663
Q45UF0
MSEVPRFELRSKRKIGKKQKVDIFGDKDDESMLQIDCETDSLISESVSSTHSYEDYSKAYKELTLETPADVNDSASTIVDSVCEESWYDKTIKDEQTKEDKKTDKKLKRIEKVKENNQNDSMSLQIAQLSLRIQRIESETKLKTLDSAYNTIITQADNLTTPQKKSLISAILATMR
Non-structural protein 5 (NSP5) (NS26)
Rotavirus X (strain RVX/Human/China/NADRV-J19/1997/GXP[X]) (RV ADRV-N) (Rotavirus (isolate novel adult diarrhea rotavirus-J19))
335,103
176
20,138
Glycoprotein;Host cytoplasm;Nucleotide-binding;Reference proteome;RNA-binding
GO:0000166; GO:0000287; GO:0003723; GO:0016887; GO:0019079; GO:0030430
Inferred from homology
2
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04092}. Note=Found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. {ECO:0000255|HAMAP-Rule:MF_04092}.
null
null
PF17580;
IPR002512;IPR020244;
null
Viruses (no rank), Riboviria (realm), Orthornavirae (kingdom), Duplornaviricota (phylum), Resentoviricetes (class), Reovirales (order), Sedoreoviridae (family), Rotavirus (genus), Rotavirus H (species)
null
false
Rotavirus H
8
row_447019
false
null
291,520
Q8JGT9
MIVFILLSLAAVLRQSFGNVDFNSESPRNPGKQQEIVNIHNSFRRSVRPTARNMLKMEWYSEAASNAERWAYQCAYDHSPRSSRILNGIQCGENIFMASDPWAWTSIIQDWYDEYRNFVYGVGANPPDSVTGHYTQIVWYKSYLVGCAAAYCPSSLYNYFYVCQYCPAGNIQGSTSTPYASGPTCADCPSNCDNGLCTNPCTHKDDYNNCNSLVSDCQSDWDKSHCPATCFCKNKII
Cysteine-rich venom protein tigrin (CRVP) (Cysteine-rich secretory protein RHA1) (CRISP-RHA1)
Rhabdophis tigrinus tigrinus (Tiger keelback snake)
193,080
237
26,697
Direct protein sequencing;Disulfide bond;Secreted;Signal
GO:0005576
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted.
SIGNAL 1..18; /evidence="ECO:0000269|PubMed:12047379"
null
PF00188;PF08562;
IPR018244;IPR014044;IPR035940;IPR042076;IPR001283;IPR013871;IPR034117;IPR003582;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Colubridae (family), Natricinae (subfamily), Rhabdophis (genus), Rhabdophis tigrinus (species)
null
false
Rhabdophis tigrinus
0
row_275560
false
null
346,110
A7X4J4
MQARVFLLLLGVILLGMMGPMVSAQDGKAGSCPDVNQPIPPLGVCKTTCATDSNCPDIQKCCKNGCGHMSCTRPST
Waprin-Rha1
Rhabdophis tigrinus tigrinus (Tiger keelback snake)
193,080
76
7,912
Antibiotic;Antimicrobial;Disulfide bond;Secreted;Signal
GO:0005576; GO:0030414; GO:0042742; GO:0044278
Inferred from homology
2
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:17855442}.
SIGNAL 1..24; /evidence="ECO:0000255"
null
PF00095;
IPR036645;IPR008197;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Colubridae (family), Natricinae (subfamily), Rhabdophis (genus), Rhabdophis tigrinus (species)
null
false
Rhabdophis tigrinus
1
row_329234
false
null
299,030
Q90WA0
MSSGGLLLLLGLLTLWEVLTPVSSKDRPELCELPPDTGPCRVRFPSFYYNPDEQKCLEFIYGGCEGNANNFITKEECESTCAA
Kunitz-type serine protease inhibitor textilinin-2 (Txln-2)
Pseudonaja textilis textilis (Eastern brown snake)
169,397
83
9,179
Direct protein sequencing;Disulfide bond;Protease inhibitor;Secreted;Serine protease inhibitor;Signal
GO:0004867; GO:0005615
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10847427}.
SIGNAL 1..24; /evidence="ECO:0000305|PubMed:10847427"
null
PF00014;
IPR002223;IPR036880;IPR020901;IPR050098;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Pseudonaja (genus), Pseudonaja textilis (species)
null
false
Pseudonaja textilis
0
row_282917
false
null
376,678
B5L5Q1
MSSGGLLLLLGLLTLWEVLTPVSSKDRPKFCELLPDTGSCEDFTGAFHYSTRDRECIEFIYGGCGGNANNFKTLEECESTCAA
Kunitz-type serine protease inhibitor textilinin-7 (Txln-7)
Pseudonaja textilis textilis (Eastern brown snake)
169,397
83
9,031
Disulfide bond;Protease inhibitor;Secreted;Serine protease inhibitor;Signal
GO:0004867; GO:0005615
Inferred from homology
2
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..24; /evidence="ECO:0000255"
null
PF00014;
IPR002223;IPR036880;IPR020901;IPR050098;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Pseudonaja (genus), Pseudonaja textilis (species)
null
false
Pseudonaja textilis
1
row_359414
false
null
514,927
Q90W96
MSSGGLLLLLGLLTLWEVLTPVSSKDRPKFCELPADIGPCDDFTGAFHYSPREHECIEFIYGGCKGNANNFNTQEECESTCAA
Kunitz-type serine protease inhibitor textilinin-6 (Txln-6)
Pseudonaja textilis textilis (Eastern brown snake)
169,397
83
9,060
Disulfide bond;Protease inhibitor;Secreted;Serine protease inhibitor;Signal
GO:0004867; GO:0005576
Evidence at transcript level
2
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..24; /evidence="ECO:0000255"
null
PF00014;
IPR002223;IPR036880;IPR020901;IPR050098;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Pseudonaja (genus), Pseudonaja textilis (species)
null
false
Pseudonaja textilis
2
row_495453
false
null
514,929
Q90W98
MSSGGLLLLLGLLTLWEVLTPVSSKDHPKFCELPADTGSCKGNVPRFYYNADHHQCLKFIYGGCGGNANNFKTIEECKSTCAA
Kunitz-type serine protease inhibitor textilinin-4 (Txln-4)
Pseudonaja textilis textilis (Eastern brown snake)
169,397
83
8,983
Disulfide bond;Protease inhibitor;Secreted;Serine protease inhibitor;Signal
GO:0004867; GO:0005615
Evidence at transcript level
2
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..24; /evidence="ECO:0000255"
null
PF00014;
IPR002223;IPR036880;IPR020901;IPR050098;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Pseudonaja (genus), Pseudonaja textilis (species)
null
false
Pseudonaja textilis
3
row_495455
false
null
514,930
Q90W99
MSSGGLLLLLGLLTLWEVLTPVSSKDRPNFCKLPAETGRCNAKIPRFYYNPRQHQCIEFLYGGCGGNANNFKTIKECESTCAA
Kunitz-type serine protease inhibitor textilinin-3 (Txln-3)
Pseudonaja textilis textilis (Eastern brown snake)
169,397
83
9,158
Disulfide bond;Protease inhibitor;Secreted;Serine protease inhibitor;Signal
GO:0004867; GO:0005576
Evidence at transcript level
2
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..24; /evidence="ECO:0000255"
null
PF00014;
IPR002223;IPR036880;IPR020901;IPR050098;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Hydrophiinae (subfamily), Pseudonaja (genus), Pseudonaja textilis (species)
null
false
Pseudonaja textilis
4
row_495456
false
null
308,760
Q9MLJ6
MSNQHILLTSNLLPVGSNISTWWNFGSMLLTCLILQITTGFFLAIHYTANINLAFSSVIHITRDVPHGWIMQNLHAIGASMFFICIYIHIARGLYYGLYLNKEVWLSGTALLILLMATAFFGYVLPWGQMSFWAATVITNLLTAIPYLGSALTTWLWGGFSINDPTLTRFFALHFILPFTIISMSSIHIILLHNEGSNNPLGTNPDIDKIPFHPYHSYKDMLMITIMITFMLLILSFSPDLMNDPENYSKANPLITPQHIKPEWYFLFAYGILRSIPNKLGGTLALFMSIAILMTAPFTHTSYTRSMSFRPLTQTMFWILIATFITITWTATKPVEPPFISISQVTSIIYFSFFIINPLLGWVENKLSTLNN
Cytochrome b (Complex III subunit 3) (Complex III subunit III) (Cytochrome b-c1 complex subunit 3) (Ubiquinol-cytochrome-c reductase complex cytochrome b subunit)
Dendroaspis polylepis polylepis (Black mamba)
8,620
372
42,203
Electron transport;Heme;Iron;Membrane;Metal-binding;Mitochondrion;Mitochondrion inner membrane;Respiratory chain;Transmembrane;Transmembrane helix;Transport;Ubiquinone
GO:0005743; GO:0006122; GO:0008121; GO:0045275; GO:0046872
Inferred from homology
3
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00157}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00157}.
null
TRANSMEM 25..45; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P00157"; TRANSMEM 69..90; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P00157"; TRANSMEM 105..125; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P00157"; TRANSMEM 170..190; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P00157"; TRANSMEM 218..238; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P00157"; TRANSMEM 280..300; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P00157"; TRANSMEM 312..332; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P00157"; TRANSMEM 339..358; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P00157"
PF00032;PF00033;
IPR005798;IPR036150;IPR005797;IPR027387;IPR030689;IPR048260;IPR048259;IPR016174;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Dendroaspis (genus), Dendroaspis polylepis (species)
MT-CYB COB CYTB MTCYB
false
Dendroaspis polylepis
0
row_292404
false
null
308,763
Q9MLJ9
MSNQHTLLMSNLLPVGSNISTWWNFGSMLLTCLMLQITTGFFLAIHYTANINLAFSSVIHITRDVPYGWIMQNLHAISASMFFICIYIHIARGLYYGLYLNKEVWLSGTALLITLMATAFFGYVLPWGQMSFWAATVITNLLTAIPYLGTMLTTWLWGGFSINDPTLTRFFALHFILPFAIMALSSIHIILLHNEGSNNPLGTNSDIDKIPFHPYHSYKDMLMFTSMITLLFITLSFSPDLLNYPENFSKANPLVTPQHIKPEWYFLFAYGILRSIPNKLGGALALLMSVMILTTVPFTHTSYTRSMMFRPLSQILFWTLMATFITITWTASKPVEPPFISISQTTSIFYFSFFITIPLLGWTENKIMMMNN
Cytochrome b (Complex III subunit 3) (Complex III subunit III) (Cytochrome b-c1 complex subunit 3) (Ubiquinol-cytochrome-c reductase complex cytochrome b subunit)
Naja annulata annulata (Banded water cobra) (Boulengerina annulata annulata)
8,610
372
42,392
Electron transport;Heme;Iron;Membrane;Metal-binding;Mitochondrion;Mitochondrion inner membrane;Respiratory chain;Transmembrane;Transmembrane helix;Transport;Ubiquinone
GO:0005743; GO:0006122; GO:0008121; GO:0045275; GO:0046872
Inferred from homology
3
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00157}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00157}.
null
TRANSMEM 25..45; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P00157"; TRANSMEM 69..90; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P00157"; TRANSMEM 105..125; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P00157"; TRANSMEM 170..190; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P00157"; TRANSMEM 218..238; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P00157"; TRANSMEM 280..300; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P00157"; TRANSMEM 312..332; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P00157"; TRANSMEM 339..358; /note="Helical"; /evidence="ECO:0000250|UniProtKB:P00157"
PF00032;PF00033;
IPR005798;IPR036150;IPR005797;IPR027387;IPR030689;IPR048260;IPR048259;IPR016174;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Elapidae (family), Elapinae (subfamily), Naja (genus), Naja annulata (species)
MT-CYB COB CYTB MTCYB
false
Naja annulata
0
row_292407
false
null
338,413
A5X2X1
MSSGGLLLLLGFLTLWAELTPVSGQDPPRFCSLPAETGECRGRIPRFYYNSASKQCEQFFYSGCGGNANNFETKDQCHYTCVEKPGVCPPRPQQQGQEGKNCENDWKCPGQQKCCRYRGKTECKDAVFEKFASTTRTPTSIGSTPVGSSVPT
Fused toxin protein
Sistrurus catenatus edwardsii (Desert massasauga) (Crotalophorus edwardsii)
8,762
152
16,710
Disulfide bond;Protease inhibitor;Pyrrolidone carboxylic acid;Secreted;Serine protease inhibitor;Signal
GO:0004867; GO:0005615
Evidence at transcript level
2
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..24; /evidence="ECO:0000250"
null
PF00014;PF00095;
IPR036645;IPR002223;IPR036880;IPR020901;IPR050098;IPR008197;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Sistrurus (genus), Sistrurus catenatus (species)
null
false
Sistrurus catenatus
0
row_321611
false
null
424,326
P59866
VTMGYIKDGDGKKIAKKKNKNGRKHVEIDLNKVG
Non-cysteinic peptide Bs 10 (Bs10) (Non-disulfide-bridged peptide 2.1) (NDBP-2.1)
Hottentotta tamulus sindicus (Scorpion) (Buthus sindicus)
42,519
34
3,783
Direct protein sequencing;Secreted
GO:0005576
Evidence at protein level
2
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10048185}.
null
null
null
null
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Chelicerata (subphylum), Arachnida (class), Scorpiones (order), Buthida (parvorder), Buthoidea (superfamily), Buthidae (family), Mesobuthus (genus), Hottentotta tamulus (species)
null
false
Hottentotta tamulus
0
row_406441
false
null
500,212
Q7YWA8
MKNYSKNATHLITVLLFSFVVILLIIPSKCEAVSNDMQPLEARSADLIPEPRYIIDVPPRCPPGSKFIKNRCRVIVP
Secapin
Vespa velutina nigrithorax (Hornet)
202,809
77
8,678
Disulfide bond;Secreted;Signal
GO:0005576
Evidence at transcript level
2
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..32; /evidence="ECO:0000255"
null
PF17521;
IPR020128;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Mandibulata (clade), Pancrustacea (clade), Hexapoda (subphylum), Insecta (class), Dicondylia (clade), Pterygota (subclass), Neoptera (infraclass), Endopterygota (cohort), Hymenoptera (order), Apocrita (suborder), Aculeata (infraorder), Vespoidea (superfamily), Vespidae (family), Vespinae (subfamily), Vespa (genus), Vespa velutina (species)
null
false
Vespa velutina
0
row_480936
false
null
500,214
Q7YWB0
MKNYSKNATYLITVLLFSFVAMLLIIPSKCEAVSNDMQPLEARTADLVQQPRYIIDVPPRCPPGSKFVHKRCRVIVP
Secapin
Apis cerana cerana (Oriental honeybee)
94,128
77
8,733
Disulfide bond;Secreted;Signal
GO:0005576
Evidence at transcript level
2
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..32; /evidence="ECO:0000255"
null
PF17521;
IPR020128;
null
cellular organisms (no rank), Eukaryota (domain), Opisthokonta (clade), Metazoa (kingdom), Eumetazoa (clade), Bilateria (clade), Protostomia (clade), Ecdysozoa (clade), Panarthropoda (clade), Arthropoda (phylum), Mandibulata (clade), Pancrustacea (clade), Hexapoda (subphylum), Insecta (class), Dicondylia (clade), Pterygota (subclass), Neoptera (infraclass), Endopterygota (cohort), Hymenoptera (order), Apocrita (suborder), Aculeata (infraorder), Apoidea (superfamily), Anthophila (clade), Apidae (family), Apinae (subfamily), Apini (tribe), Apis (genus), Apis cerana (species)
null
false
Apis cerana
0
row_480938
false
null
800
R4NNL0
MIQVLLVIICLAVFPYQGSSIILESGNVNDYEVVYLQKVTAMNKGAVKQPEQKYEDTMQYEFKVNGEPVILHLEKNKDLFSEDYSETHYSPDGREITTNPPVEDHCYYHGRIQNDADSTASISACNGLKGHFQLRGETYFIEPLKIPDSEAHAVYKYENVEKEDEAPKTCGVTQTNWESDELIKKASQLNLTPEQQRYLNSPKYIKLVIVADYIMFLKYGRSLITIRTRIYEIVNLLNVIYRVLNIYIALVGLEIWNNGDKINVLPEAKVTLDLFGKWRETDLLNRRKHDNAQLLTGINFNGPTAGLGYLGSMCNPQYSAGIVQDHNKVNFLVALAMAHEMGHNLGMDHDGIQCTCGAKSCIMSGTLSCEASIRFSNCSQEEHRKYLINKMPQCILNKPLKTDIVSPAVCGNYLVELGEDCDCGSPRDCQNPCCNAATCKLTPGSQCADGECCDQCKFGRAGTVCRPANGECDVSDVCTGQSAECPTDQFQRNGHPCQNNNGYCYNGTCPILGKQCISLFGASATVAQDACFQFNRLGNEYGYCRKENGRKIPCAPQDVKCGRLYCFDNLPEHKNPCQIYYTPRDENKGMVDPGTKCGDGMACSSNGQCVDVNTAY
Zinc metalloproteinase-disintegrin-like protein H3 (EC 3.4.24.-) (H3 metalloproteinase 1) (Hemorrhagin 3) (P-IIIc metalloproteinase H3) (Snake venom metalloproteinase) (SVMP) (VaH3)
Vipera ammodytes ammodytes (Western sand viper)
8,705
616
68,546
Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin;Zinc;Zymogen
GO:0004222; GO:0005576; GO:0005886; GO:0006508; GO:0046872; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23321470}.
SIGNAL 1..20; /evidence="ECO:0000255"
null
PF08516;PF00200;PF01562;PF01421;
IPR006586;IPR018358;IPR001762;IPR036436;IPR024079;IPR001590;IPR002870;IPR034027;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Vipera (genus), Vipera ammodytes (species)
null
true
Vipera ammodytes
0
row_750
false
null
2
A0A0B4U9L8
MLQVLLVTICLAVFPYQGSSIILESGNVNDYEVVYPQKLTALLKGAIQQPEQKYEDAMQYEFKVNGKPVVLHLEKNKGLFSEDYSETHYSPDGREITTNPPVEDHCYYHGHIQNDAHLTASISACNGLKGHFQLRGETYLIEPLKIPDSEAHAVYKYENVEKEDEGPKKCGVTQTNWKSDEPIKASQFILTPEQRAYMNANKYIKLAIVVDNVMFRKYTGNFTAIRTRIYEIVNTLNLIYTILNIHIALVFLEIWSKGDSINVQSVVDVTLNSFGEWRERDLLNRKRHDNAQLLTGINFNGDTIGFGFVGSMCIPKKSVGIVQDHSKTHLLVATTMAHELGHNLGINHDGDSCTCQANSCIMAAKLSHQPSYQFSDCSINELWMYLISHTPRCILNEPLTTDVVSPAVCGNYVVEEGEECDCGSLWYCRNPCCDAATCKLKPGAECGDGVCCYQCRFVTAGTVCRPARSECDIPEYCSGQSVECPMDHIQKNGKPCLMNHGYCYNGRCPIMIHQCIALWGPGTTVSSDVCFQRNESGQGYSYCRRENNQNIPCAPQDVKCGRLYCKFHNVNTLPCNFKYSDFAPDYGLVDHGTKCGDGKVCNSNRQCVDVNTAY
Zinc metalloproteinase-disintegrin-like protein F1 (EC 3.4.24.-) (Fibrinogenase 1) (Metalloproteinase F1) (P-IIIa metalloproteinase F1) (Snake venom metalloproteinase) (SVMP) (VaF1)
Vipera ammodytes ammodytes (Western sand viper)
8,705
614
68,745
Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin;Zinc;Zymogen
GO:0004222; GO:0005576; GO:0005886; GO:0006508; GO:0008237; GO:0008270; GO:0035738; GO:0043245; GO:0044468; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25549999}.
SIGNAL 1..20; /evidence="ECO:0000255"
null
PF08516;PF00200;PF01562;PF01421;
IPR006586;IPR018358;IPR001762;IPR036436;IPR024079;IPR001590;IPR002870;IPR034027;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Vipera (genus), Vipera ammodytes (species)
null
true
Vipera ammodytes
1
row_2
false
null
805
V5TBK6
MIQPLLVVTCLVVFPYQVSSIILESGNVNDYEVVYPQKVTSLPKGAVQQPEQKYEDTMQYEFKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGREITTNPPVEDHCYYHGHIQNEADSTASISACNGLKGHFKLQGETYLIEPLKIPESEAHAVYKYENIEKEDEAPKMCGVTETNWESDEPIRKASQLVATSEQRRNIQKYIELVIVVDNVMFRKYTGNSTAIRTRIYEIVNTLNVVFRNVHIFVALVGIEIWNKKDQIKVKSAESVTLDLFGDWREKDLLRRKRHDNAQLLTGIDLNEQTLGIAPMSGMCKPKSSVGLIQDYCKSYLLVAIVMAHELGHNLGMDHDDGNCICREMPCIMSPEAGSKPAFYFSDCSWNQYQKFRNDIKSKCIDNKPLKTDIVSPAFCGNYFVEEGEECDCGFPGNCRNPCCNATTCKLTPGSECGDGECCDQCRIQTAGTECRPAWDECDVPEYCTGQSAECPTDVLQRNGQPCKNNNGYCYNGVCPILTNQCISLFGSSVTVAPDRCFNNNLQGTENFHCGMENGRYIKCKPQDKKCGRLFCVEPPTGGGINCKSIRSEGDPDHGMVDLGTKCADGKVCNSNRQCVDVNTAY
Zinc metalloproteinase-disintegrin-like protein H4 subunit A (EC 3.4.24.-) (Hemorrhagin 4 subunit A) (Metalloproteinase H4-A) (P-III metalloproteinase H4 subunit A) (Snake venom metalloproteinase) (SVMP) (VaH4-A)
Vipera ammodytes ammodytes (Western sand viper)
8,705
614
68,662
Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Platelet aggregation inhibiting toxin;Protease;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin;Zinc;Zymogen
GO:0004222; GO:0005576; GO:0005886; GO:0006508; GO:0046872; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24269369}.
SIGNAL 1..20; /evidence="ECO:0000255"
null
PF08516;PF00200;PF01562;PF01421;
IPR006586;IPR018358;IPR001762;IPR036436;IPR024079;IPR001590;IPR002870;IPR034027;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Vipera (genus), Vipera ammodytes (species)
null
true
Vipera ammodytes
2
row_754
false
null
294
P0DI84
DRNPLEECFRETDYEEFLEIARNGLKKTSNPKHVVVVGAGMSGLSAAYVLAGAGHKVTVLEASERAGGRVRTHRNSKEGWYANLGPMRIPEKHRIVREYIRKFGLNLNEFSQENDNAWYFIKNIRKRVGEVNKDPGLLKYPVKPSEEGKSAGQLYEESLGSAVKDLKRTNCSYILNKYDTYSTKEYLIKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVGGMDQLPTSMYRAIEEKVKFNARVIKIQQNANQVTVTYQTPEKDTSSNTADYVIVCTTSRAARRIQFEPPLPPKKQHALRSVHYRSGTKIFLTCSSKFWEDDGIHGGKSTTDLPSRFIYYPNHNFSTGVGVIIAYGIGDDANFFQALKFKDCADIVFNDLSLIHQLPKEEIQSFCYPSMIQKWSLDKYAMGAITTFTPYQFQRFSEALTAPQGRIFFAGEYTAEAHGWIDSTIKSGLTAARDVNRASEQ
L-amino-acid oxidase (LAO) (VAA-LAAO I) (EC 1.4.3.2)
Vipera ammodytes ammodytes (Western sand viper)
8,705
484
54,748
3D-structure;Antibiotic;Antimicrobial;Apoptosis;Cytolysis;Disulfide bond;FAD;Flavoprotein;Glycoprotein;Hemolysis;Hemostasis impairing toxin;Metal-binding;Oxidoreductase;Secreted;Toxin;Zinc
GO:0001716; GO:0005576; GO:0006915; GO:0009063; GO:0031640; GO:0042742; GO:0046872; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18931435}.
null
null
PF01593;
IPR002937;IPR036188;IPR001613;IPR050281;
3KVE;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Vipera (genus), Vipera ammodytes (species)
null
true
Vipera ammodytes
3
row_278
false
null
29
A0A6B7FMR5
MIQVLLVIICLAVFPYQVSSIILESGNINNYEVVYPQKVTALPKGAIQQLEQKYEDAMQYQFKVKGEPVVLHLEKNKDFFPEDYSETHYSPDDREITTNPPVEDHCYYYGHIQNDADSTASISACNGLKGYFTLRGVTYLIEPLKIPESEAHAIYKYENVEKEDEDPKKCEFRRAGTECRPARSECDVAEYCTGQSAECPTDVFHSNGKPCLNNFGYCYNGNCPIMYHQCYALFGPNATVGQDGCFEWNKKGESYFYCRKENDVPIPCAPEDIKCGRLFCELIKNTCKYDYSEDPDYGMVDHGTKCGDGKVCINRHCVDVTTAY
Disintegrin-like/cysteine-rich protein MPIII-3 (D'C protein MPIII-3) (Metalloproteinase-like protein of class P-III MPIII-3) (Snake venom metalloproteinase precursor-derived protein MPIII-3) (SVMP precursor-derived protein MPIII-3) (Snake venom metalloproteinase-like) (SVMP-like) (Vaa-MPIII-3) (VaaMPIII-3)
Vipera ammodytes ammodytes (Western sand viper)
8,705
324
36,837
Calcium;Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Metal-binding;Platelet aggregation inhibiting toxin;Secreted;Signal;Toxin
GO:0005576; GO:0005886; GO:0046872; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31017792, ECO:0000269|PubMed:35448841}.
SIGNAL 1..20; /evidence="ECO:0000255"
null
PF08516;PF00200;PF01562;
IPR006586;IPR001762;IPR036436;IPR002870;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Vipera (genus), Vipera ammodytes (species)
null
true
Vipera ammodytes
4
row_25
false
null
826
A0A1I9KNP0
MVLIRVLANLLVLQLSYAQKSSELVIGGDECNINEHPFLVALHTARSKRFYCAGTLINQEWVLTAARCDRKNIRIILGVHSKNVPNEDEQMRVPKEKFFCLSSKTYTRWDKDIMLIRLKRPVNDSTHIAPLSLPSSPPSVGSVCRIMGWGTITTTKVTYPDVPHCADINMFDYSVCQKVYRKLPEKSRTLCAGILQGGIDSCKVDNGGPLICNGQIQGIVSWGGYPCAQPHKPALYTNVFDYTDWIQSIIAGNITATCPP
Vaa serine proteinase homolog 1 (VaaSPH-1) (Enzymatically inactive serine proteinase-like protein SPH-1) (Snake venom serine protease homolog)
Vipera ammodytes ammodytes (Western sand viper)
8,705
260
28,928
Blood coagulation cascade inhibiting toxin;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Pharmaceutical;Secreted;Serine protease homolog;Signal;Toxin
GO:0004252; GO:0005576; GO:0006508; GO:0030141; GO:0090729
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30235482}.
SIGNAL 1..18; /evidence="ECO:0000255"
null
PF00089;
IPR009003;IPR043504;IPR001314;IPR001254;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Vipera (genus), Vipera ammodytes (species)
null
true
Vipera ammodytes
5
row_775
false
null
482
P67863
MAAYLLAVAILFCIQGWPSGTVQGQVRPFLEVHERSACQARETLVPILQEYPDEISDIFRPSCVAVLRCSGCCTDESLKCTPVGKHTVDLQIMRVNPRTQSSKMEVMKFTEHTACECRPRRKQGEPDGPKEKPRRGGVRARFPFV
Snake venom vascular endothelial growth factor toxin vammin (svVEGF) (VEGF-F)
Vipera ammodytes ammodytes (Western sand viper)
8,705
145
16,307
3D-structure;Direct protein sequencing;Disulfide bond;Growth factor;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin
GO:0001666; GO:0001938; GO:0002040; GO:0005172; GO:0005615; GO:0008083; GO:0016020; GO:0038084; GO:0042056; GO:0045766; GO:0048010; GO:0050930; GO:0060754; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14600159, ECO:0000269|PubMed:15542594}.
SIGNAL 1..24; /evidence="ECO:0000255"
null
PF00341;
IPR029034;IPR023581;IPR000072;IPR050507;
1WQ8;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Vipera (genus), Vipera ammodytes (species)
null
true
Vipera ammodytes
6
row_446
false
null
181
P00626
MRTLWIVAVCLIGVEGSLLEFGMMILGETGKNPLTSYSFYGCYCGVGGKGTPKDATDRCCFVHDCCYGNLPDCSPKTDRYKYHRENGAIVCGKGTSCENRICECDRAAAICFRKNLKTYNYIYRNYPDFLCKKESEKC
Basic phospholipase A2 ammodytoxin A (AtxA) (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase)
Vipera ammodytes ammodytes (Western sand viper)
8,705
138
15,531
3D-structure;Blood coagulation cascade inhibiting toxin;Calcium;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Host cytoplasm;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Neurotoxin;Presynaptic neurotoxin;Secreted;Signal;Toxin
GO:0005509; GO:0005543; GO:0005576; GO:0006644; GO:0016042; GO:0042130; GO:0047498; GO:0050482; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18261469}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:18261469}.
SIGNAL 1..16; /evidence="ECO:0000269|PubMed:3986212"
null
PF00068;
IPR001211;IPR033112;IPR016090;IPR036444;IPR033113;
3G8G;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Vipera (genus), Vipera ammodytes (species)
null
true
Vipera ammodytes
7
row_168
false
null
381
P17935
MRILWIVAVCLIGVEGSVIEFGKMIQEETDKNPLTSYSFYGCHCGLGNKGKPKDATDRCCFVHSCCYAKLPDCSPKTNRYEYHRENGAIVCGSSTPCKKQICECDRAAAICFRENLKTYNKKYKVYLRFKCKGVSEKC
Basic phospholipase A2 homolog ammodytin L (AMDL) (AtnL) (svPLA2 homolog)
Vipera ammodytes ammodytes (Western sand viper)
8,705
138
15,636
3D-structure;Direct protein sequencing;Disulfide bond;Myotoxin;Neurotoxin;Presynaptic neurotoxin;Secreted;Signal;Toxin
GO:0005509; GO:0005543; GO:0005576; GO:0006644; GO:0016042; GO:0042130; GO:0047498; GO:0050482; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1765075, ECO:0000269|PubMed:2101000}.
SIGNAL 1..16; /evidence="ECO:0000269|PubMed:1765075"
null
PF00068;
IPR001211;IPR033112;IPR016090;IPR036444;IPR033113;
3DIH;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Vipera (genus), Vipera ammodytes (species)
null
true
Vipera ammodytes
8
row_352
false
null
210
P04084
NLFQFGDMILQKTGKEAVHSYAIYGCYCGWGGQGRAQDATDRCCFAQDCCYGRVNDCNPKTATYTYSFENGDIVCGDNDLCLRAVCECDRAAAICLGENVNTYDKNYEYYSISHCTEESEQC
Acidic phospholipase A2 homolog vipoxin A chain (svPLA2 homolog) (Acidic phospholipase A2 inhibitor vipoxin A chain) (Vipoxin acidic component) (VAC) (Vipoxin non-toxic component)
Vipera ammodytes meridionalis (Eastern sand viper)
73,841
122
13,639
3D-structure;Direct protein sequencing;Disulfide bond;Neurotoxin;Postsynaptic neurotoxin;Secreted;Toxin
GO:0005509; GO:0005543; GO:0005576; GO:0006644; GO:0016042; GO:0042130; GO:0047498; GO:0050482; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted.
null
null
PF00068;
IPR001211;IPR033112;IPR016090;IPR036444;
1AOK;1JLT;1Q5T;1VPI;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Vipera (genus), Vipera ammodytes (species)
null
true
Vipera ammodytes
9
row_197
false
null
367
P14420
NLFQFAKMINGKLGAFSVWNYISYGCYCGWGGQGTPKDATDRCCFVHDCCYGRVRGCNPKLAIYSYSFKKGNIVCGKNNGCLRDICECDRVAANCFHQNKNTYNKNYKFLSSSRCRQTSEQC
Basic phospholipase A2 vipoxin B chain (svPLA2) (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase) (Vipoxin toxic component)
Vipera ammodytes meridionalis (Eastern sand viper)
73,841
122
13,828
3D-structure;Calcium;Cytolysis;Direct protein sequencing;Disulfide bond;Hemolysis;Hemostasis impairing toxin;Hydrolase;Lipid degradation;Lipid metabolism;Metal-binding;Neurotoxin;Platelet aggregation inhibiting toxin;Postsynaptic neurotoxin;Secreted;Toxin
GO:0005509; GO:0005543; GO:0005576; GO:0006644; GO:0016042; GO:0031640; GO:0042130; GO:0047498; GO:0050482; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted.
null
null
PF00068;
IPR001211;IPR033112;IPR016090;IPR036444;IPR033113;
1AOK;1JLT;1RGB;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Vipera (genus), Vipera ammodytes (species)
null
true
Vipera ammodytes
10
row_340
false
null
3,269
P0C6A5
NSANPCCDPVTCKPRRGEHCVSGPCCRNCKFLNAGTICRYARGDDMNDYCTGVTSDCPRNPYKS
Disintegrin VA6
Vipera ammodytes ammodytes (Western sand viper)
8,705
64
7,023
Cell adhesion impairing toxin;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Platelet aggregation inhibiting toxin;Secreted;Toxin
GO:0005576; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12667142}.
null
null
PF00200;
IPR018358;IPR001762;IPR036436;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Vipera (genus), Vipera ammodytes (species)
null
true
Vipera ammodytes
11
row_3152
false
null
3,306
P0C8J5
AFCCPSGWSAYDQNCY
Snaclec factor X-activator 2 light chain 2 (VAFXA-II LC2)
Vipera ammodytes ammodytes (Western sand viper)
8,705
16
1,815
Blood coagulation cascade activating toxin;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Metal-binding;Secreted;Toxin
GO:0005576; GO:0046872; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted.
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), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Vipera (genus), Vipera ammodytes (species)
LC2
true
Vipera ammodytes
12
row_3188
false
null
1,430
P0C8I7
LVSVSPAFNGNYFVE
Factor X-activator 1 heavy chain (VAFXA-I HC) (EC 3.4.24.-) (Snake venom metalloproteinase) (SVMP)
Vipera ammodytes ammodytes (Western sand viper)
8,705
15
1,643
Blood coagulation cascade activating toxin;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Toxin;Zinc;Zymogen
GO:0005576; GO:0006508; GO:0008237; GO:0046872; GO:0090729
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted.
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), Sauropsida (clade), Sauria (clade), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Viperinae (subfamily), Vipera (genus), Vipera ammodytes (species)
null
true
Vipera ammodytes
13
row_1369
false
null
1,683
P24419
MLILNGFSSATLALITPPFLPKGGKALSQSGPDGLASITLPLPISAERGFAPALALHYSSGGGNGPFGVGWSCATMSIARRTSHGVPQYNDSDEFLGPDGEVLVQTLSTGDAPNPVTCFAYGDVSFPQSYTVTRYQPRTESSFYRLEYWVGNSNGDDFWLLHDSNGILHLLGKTAAARLSDPQAASHTAQWLVEESVTPAGEHIYYSYLAENGDNVDLNGNEAGRDRSAMRYLSKVQYGNATPAADLYLWTSATPAVQWLFTLVFDYGERGVDPQVPPAFTAQNSWLARQDPFSLYNYGFEIRLHRLCRQVLMFHHFPDELGEADTLVSRLLLEYDENPILTQLCAARTLAYEGDGYRRAPVNNMMPPPPPPPPPMMGGNSSRPKSKWAIVEESKQIQALRYYSAQGYSVINKYLRGDDYPETQAKETLLSRDYLSTNEPSDEEFKNAMSVYINDIAEGLSSLPETDHRVVYRGLKLDKPALSDVLKEYTTIGNIIIDKAFMSTSPDKAWINDTILNIYLEKGHKGRILGDVAHFKGEAEMLFPPNTKLKIESIVNCGSQDFASQLSKLRLSDDATADTNRIKRIINMRVLNS
Mono(ADP-ribosyl)transferase SpvB (mADPRT) (mART) (EC 2.4.2.31) (65 kDa virulence protein) (NAD(+)--arginine ADP-ribosyltransferase) (Toxin SpvB)
Salmonella dublin
98,360
593
65,614
Glycosyltransferase;NAD;NADP;Nucleotide-binding;Nucleotidyltransferase;Plasmid;Secreted;Toxin;Transferase;Virulence
GO:0000166; GO:0005576; GO:0005737; GO:0016779; GO:0090729; GO:0106274
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted. Note=Secreted via the type III secretion system 2 (SPI-2 T3SS).
null
null
PF03496;PF03534;
IPR003540;IPR003284;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Salmonella (genus), Salmonella enterica (species), Salmonella enterica I (subspecies)
spvB vsdC
true
Salmonella enterica
0
row_1612
false
null
349
P0DUJ8
MARFNAAFTRIKIMFSRIRGLISCQSNTQTIAPTLSPPSSGHVSFAGIDYPLLPLNHQTPLVFQWFERNPDRFGQNEIPIINTQKNPYLNNIINAAIIEKERIIGIFVDGDFSKGQRKALGKLEQNYRNIKVIYNSDLNYSMYDKKLTTIYLENITKLEAQSASERDEVLLNGVKKSLEDVLKNNPEETLISSHNKDKGHLWFDFYRNLFLLKGSDAFLEAGKPGCHHLQPGGGCIYLDADMLLTDKLGTLYLPDGIAIHVSRKDNHVSLENGIIAVNRSEHPALIKGLEIMHSKPYGDPYNDWLSKGLRHYFDGSHIQDYDAFCDFIEFKHENIIMNTSSLTASSWR
Protein-arginine N-acetylglucosaminyltransferase SseK2 (Arginine GlcNAcyltransferase SseK2) (EC 2.4.1.-) (Salmonella secreted effector K2)
Salmonella typhimurium (strain SL1344)
216,597
348
39,566
3D-structure;Glycosyltransferase;Host Golgi apparatus;Manganese;Metal-binding;Secreted;Toxin;Transferase;Virulence
GO:0005576; GO:0030145; GO:0044177; GO:0090729; GO:0106362
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8ZNP4}. Host Golgi apparatus {ECO:0000269|PubMed:32432056, ECO:0000269|PubMed:32974215}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000250|UniProtKB:Q8ZNP4}.
null
null
PF24688;
null
5H61;5H62;5H63;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Salmonella (genus), Salmonella enterica (species), Salmonella enterica I (subspecies), Salmonella typhimurium (no rank)
sseK2 SL1344_2113
true
Salmonella enterica
1
row_323
false
null
2,191
Q8ZNP4
MARFNAAFTRIKIMFSRIRGLISCQSNTQTIAPTLSPPSSGHVSFAGIDYPLLPLNHQTPLVFQWFERNPDRFGQNEIPIINTQKNPYLNNIINAAIIEKERIIGIFVDGDFSKGQRKALGKLEQNYRNIKVIYNSDLNYSMYDKKLTTIYLENITKLEAQSASERDEVLLNGVKKSLEDVLKNNPEETLISSHNKDKGHLWFDFYRNLFLLKGSDAFLEAGKPGCHHLQPGGGCIYLDADMLLTDKLGTLYLPDGIAIHVSRKDNHVSLENGIIAVNRSEHPALIKGLEIMHSKPYGDPYNDWLSKGLRHYFDGSHIQDYDAFCDFIEFKHENIIMNTSSLTASSWR
Protein-arginine N-acetylglucosaminyltransferase SseK2 (Arginine GlcNAcyltransferase SseK2) (EC 2.4.1.-) (Salmonella secreted effector K2)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
99,287
348
39,566
Glycosyltransferase;Host Golgi apparatus;Manganese;Metal-binding;Reference proteome;Secreted;Toxin;Transferase;Virulence
GO:0005576; GO:0043657; GO:0044177; GO:0046872; GO:0090729; GO:0106362
Inferred from homology
4
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15322005}. Host Golgi apparatus {ECO:0000269|PubMed:28069818}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000269|PubMed:15322005}.
null
null
PF24688;
null
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Salmonella (genus), Salmonella enterica (species), Salmonella enterica I (subspecies), Salmonella typhimurium (no rank)
sseK2 STM2137
true
Salmonella enterica
2
row_2107
false
null
9
A0A0H3NK84
MIPPLNRYVPALSKNELVKTVTNRDIQFTSFNGKDYPLCFLDEKTPLLFQWFERNPARFGKNDIPIINTEKNPYLNNIIKAATIEKERLIGIFVDGDFFPGQKDAFSKLEYDYENIKVIYRNDIDFSMYDKKLSEIYMENISKQESMPEEKRDCHLLQLLKKELSDIQEGNDSLIKSYLLDKGHGWFDFYRNMAMLKAGQLFLEADKVGCYDLSTNSGCIYLDADMIITEKLGGIYIPDGIAVHVERIDGRASMENGIIAVDRNNHPALLAGLEIMHTKFDADPYSDGVCNGIRKHFNYSLNEDYNSFCDFIEFKHDNIIMNTSQFTQSSWARHVQ
Protein-arginine N-acetylglucosaminyltransferase SseK1 (Arginine GlcNAcyltransferase SseK1) (EC 2.4.1.-) (Salmonella secreted effector K1)
Salmonella typhimurium (strain SL1344)
216,597
336
38,836
3D-structure;Glycoprotein;Glycosyltransferase;Host cytoplasm;Manganese;Metal-binding;Secreted;Toxin;Transferase;Virulence
GO:0005576; GO:0030145; GO:0030430; GO:0033668; GO:0044164; GO:0090729; GO:0106362
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9L9J3}. Host cytoplasm, host cytosol {ECO:0000305|PubMed:32432056}. Note=Secreted via type III secretion systems 1 and 2 (SPI-1 and SPI-2 T3SS). {ECO:0000250|UniProtKB:Q9L9J3}.
null
null
PF24688;
null
5H60;7YM5;7YM7;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Salmonella (genus), Salmonella enterica (species), Salmonella enterica I (subspecies), Salmonella typhimurium (no rank)
sseK1 SL1344_4096
true
Salmonella enterica
3
row_8
false
null
348
P0DUJ7
MFSRVRGFLSCQNYSHTATPAITLPSSGSANFAGVEYPLLPLDQHTPLLFQWFERNPSRFGENQIPIINTQQNPYLNNIINAAIIEKERTIGVLVDGNFSAGQKKALAKLEKQYENIKVIYNSDLDYSMYDKKLSDIYLENIAKIEAQPANVRDEYLLGEIKKSLNEVLKNNPEESLVSSHDKRLGHVRFDFYRNLFLLKGSNAFLEAGKHGCHHLQPGGGCIYLDADMLLTGKLGTLYLPDGIAVHVSRKGNSMSLENGIIAVNRSEHPALKKGLEIMHSKPYGDPYIDGVCGGLRHYFNCSIRHNYEEFCNFIEFKHEHIFMDTSSLTISSWR
Protein-arginine N-acetylglucosaminyltransferase SseK3 (Arginine GlcNAcyltransferase SseK3) (EC 2.4.1.-) (Salmonella secreted effector K3)
Salmonella typhimurium (strain SL1344)
216,597
335
37,890
3D-structure;Glycoprotein;Glycosyltransferase;Host Golgi apparatus;Lipid-binding;Manganese;Metal-binding;Secreted;Toxin;Transferase;Virulence
GO:0005576; GO:0008289; GO:0030145; GO:0043657; GO:0044177; GO:0052040; GO:0090729; GO:0106362
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21445262}. Host Golgi apparatus {ECO:0000269|PubMed:26394407, ECO:0000269|PubMed:32432056, ECO:0000269|PubMed:32504010, ECO:0000269|PubMed:32974215}. Note=Secreted via type III secretion system 2 (SPI-2 T3SS) (PubMed:21445262). Localizes to host Golgi apparatus via lipid-binding (PubMed:32504010). {ECO:0000269|PubMed:21445262, ECO:0000269|PubMed:32504010}.
null
null
PF24688;
null
6CGI;6DUS;6EYR;6EYT;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Salmonella (genus), Salmonella enterica (species), Salmonella enterica I (subspecies), Salmonella typhimurium (no rank)
sseK3 SL1344_1928
true
Salmonella enterica
4
row_322
false
null
2,190
Q8Z727
MTGIFAEQTVEVVKSAIETADGALDLYNKYLDQVIPWKTFDETIKELSRFKQEYSQEASVLVGDIKVLLMDSQDKYFEATQTVYEWCGVVTQLLSAYILLFDEYNEKKASAQKDILIRILDDGVKKLNEAQKSLLTSSQSFNNASGKLLALDSQLTNDFSEKSSYFQSQVDRIRKEAYAGAAAGIVAGPFGLIISYSIAAGVIEGKLIPELNNRLKTVQNFFTSLSATVKQANKDIDAAKLKLATEIAAIGEIKTETETTRFYVDYDDLMLSLLKGAAKKMINTCNEYQQRHGKKTLFEVPDV
Hemolysin E (Cytotoxin ClyA) (Silent hemolysin SheA)
Salmonella typhi
90,370
303
33,790
Cytolysis;Disulfide bond;Hemolysis;Host cell membrane;Host membrane;Membrane;Periplasm;Secreted;Toxin;Transmembrane;Transmembrane helix;Virulence
GO:0005576; GO:0016020; GO:0019836; GO:0020002; GO:0042597; GO:0044179; GO:0090729; GO:0140911
Inferred from homology
4
SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Periplasm {ECO:0000250}. Host cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Exported from the cell by outer membrane vesicles. Also found in the periplasmic space (By similarity). {ECO:0000250}.
null
TRANSMEM 179..199; /note="Helical"; /evidence="ECO:0000255"
PF06109;
IPR027018;
null
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Salmonella (genus), Salmonella enterica (species), Salmonella enterica I (subspecies)
hlyE clyA sheA STY1498 t1477
true
Salmonella enterica
5
row_2106
false
null
4,784
Q8Z6A7
MKKPVFFLLTMIICSYISFACANISDYKVMTWNLQGSSASTESKWNVNVRQLLSGTAGVDILMVQEAGAVPTSAVPTGRHIQPFGVGIPIDEYTWNLGTTSRQDIRYIYHSAIDVGARRVNLAIVSRQRADNVYVLRPTTVASRPVIGIGLGNDVFLTAHALASGGPDAAAIVRVTINFFRQPQMRHLSWFLAGDFNRSPDRLENDLMTEHLERVVAVLAPTEPTQIGGGILDYGVIVDRAPYSQRVEALRNPQLASDHYPVAFLARSC
Cytolethal distending toxin subunit B homolog (CDT B) (Deoxyribonuclease CdtB) (EC 3.1.-.-)
Salmonella typhi
90,370
269
29,560
3D-structure;Endonuclease;Hydrolase;Nuclease;Secreted;Signal;Toxin;Virulence
GO:0004519; GO:0005576; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Secreted. Note=Localized to the nucleus of infected cells.
SIGNAL 1..22; /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
null
PF03372;
IPR003539;IPR036691;IPR005135;
4K6L;6VX4;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Salmonella (genus), Salmonella enterica (species), Salmonella enterica I (subspecies)
cdtB STY1886 t1111
true
Salmonella enterica
6
row_4560
false
null
3,802
P0DW66
MPYVYANAKALQDTEKVGNHHQCVELIQHYIRVGQASTWQQGAAVFGNKNIEVGTVIATFVNGRYPNHNSGNHAAFFLGQDTGGIWVMDQWKDDIAKPRVSKRYIRKLHNGSVRSDGTYIRMSNNAEAYFIVE
Type VI secretion amidase effector 2 protein (Tae2) (EC 3.4.-.-) (Peptidoglycan endopeptidase Tae2)
Salmonella typhi
90,370
133
15,000
3D-structure;Cell wall biogenesis/degradation;Host periplasm;Hydrolase;Secreted;Toxin
GO:0005576; GO:0016787; GO:0016998; GO:0044229; GO:0071555; GO:0090729
Evidence at protein level
3
SUBCELLULAR LOCATION: Host periplasm {ECO:0000305|PubMed:22607806}. Secreted {ECO:0000305|PubMed:22607806}. Note=Delivered to the target cell periplasm by the SPI-6 type 6 secretion system (T6SS). {ECO:0000305|PubMed:22607806}.
null
null
null
IPR047746;
6WIN;
cellular organisms (no rank), Bacteria (domain), Pseudomonadati (kingdom), Pseudomonadota (phylum), Gammaproteobacteria (class), Enterobacterales (order), Enterobacteriaceae (family), Salmonella (genus), Salmonella enterica (species), Salmonella enterica I (subspecies)
tae2 t2586
true
Salmonella enterica
7
row_3652
false
null
341
P0DQQ4
GLKEPVQPQVSCRYRCNETFSRMASGCSCDDKCTERQACCSDYEDTCVLPTQSWSCSKLRCGEKRIANVLCSCSEDCLEKKDCCTDYKTICKGETSWLKDKCASSGATQCPAGFEQSPLILFSMDGFRAGYLENWDSLMPNINKLKTCGTHAKYMRAVYPTKTFVNHYTIATGLYPESHGIIDNNIYDVNLNLNFSLSSSTARNPAWWGGQPIWHTATYQGLKAATYFWPGSEVKINGSYPTIFKNYDKSIPFEARVTEVLKWLDLPKAKRPDFFTLYIEEPDTTGHKYGPVSGEIIKALQMADRTLGMLMEGLKQRNLHNCVNLILLADHGMEEISCDRLEYMANYFDNVDFFMYEGPAPRIRSKNVPKDFYTFDSEGIVKNLTCRKPKQYFKAYLSKDLPKRLHYANNIRIDKVNLMVDQQWMAVRDKKFTRCKGGTHGYDNEFKSMQAIFLAHGPGFNEKNEVTSFENIEVYNLMCDLLKLKPAPNDGTHGSLNHLLKNPFYTPSPAKEQSSPLSCPFGPVPSPDVSGCKCSSITELEKVNQRLNLNNQAKTESEAHNLPYGRPQVLQNHSKYCLLHQAKYISAYSQDILMPLWSSYTIYRSTSTSVPPSASDCLRLDVRIPAAQSQTCSNYQPDLTITPGFLYPPNFNSSNFEQYDALITSNIVPMFKGFTRLWNYFHTTLIPKYARERDGLNVISGPIFDYNYDGHFDSYDTIKQHVSNTKIPIPTHYFVVLTSCENQINTPLNCLGPLKVLSFILPHRPDNSESCADTSPENLWVEERIQIHTARVRDVELLTGLNFYSGLKQPLPETLQLKTFLPIFVNPVN
Venom phosphodiesterase CdcPDE (PDE) (EC 3.6.1.-)
Crotalus durissus collilineatus (Brazilian rattlesnake)
221,569
829
94,154
Direct protein sequencing;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Metal-binding;Platelet aggregation inhibiting toxin;Repeat;Secreted;Toxin
GO:0003676; GO:0005576; GO:0009143; GO:0046872; GO:0047429; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33636276}.
null
null
PF01223;PF01663;PF01033;
IPR017850;IPR044929;IPR001604;IPR020821;IPR044925;IPR002591;IPR036024;IPR001212;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Crotalus (genus), Crotalus durissus (species)
null
true
Crotalus durissus
0
row_318
false
null
1,997
Q2QA02
MIQVLLVTICLAALPYQGSSIILESGNVNDYEIVYPRKVTALPKGAVQPKYEDAMQYELKVNGEPVVLYLEKNKQLFSKDYSETHYSPDGREITTYPLVEDHCYYHGRIENDADSTASISACNGLKGHFKLQGEMYLIEPLKLSNSEAHAVYKYENVEKEDEAPKMCGVTQNWKSYEPIKKASQLVVTAEHQKYNPFRFVELVLVVDKAMVTKNNDDLDKIKTRMYELANTVNEIYRYMYIHVALVGLEIWSNEDKITVKPEAGYTLNAFGEWRKTDLLTRKKHDNAQLLTAIDLDRVIGLAYVGSMCHPKRSTGIIQDYSPINLVVAVIMAHEMGHNLGIHHDSGYCSCGDYACIMRPEISPEPSTFFSNCSYFDCWDFIMNQNPECIVNEPLGTDIISPPVCGNELLEVGEECDCGTPENCQNECCDAATCKLKSGSQCGHGDCCEQCKFSKSGTECRASMSECDPAEHCTGQSSECPADVFHKNGQPCLDNYGYCYNGNCPIMYHQCYDLFGADVYEAEDSCFERNQKGNYYGYCRKENGNKIPCAPEDVKCGRLYCKDNSPGQNNPCKMFYSNEDEHKGMVLPGTKCADGKVCSNGHCVDVATAY
Zinc metalloproteinase-disintegrin-like (EC 3.4.24.-) (Snake venom metalloproteinase) (SVMP)
Crotalus durissus durissus (Central American rattlesnake)
31,150
609
68,291
Calcium;Disulfide bond;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Toxin;Zinc;Zymogen
GO:0004222; GO:0005576; GO:0005886; GO:0006508; GO:0046872; GO:0090729
Evidence at transcript level
4
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..20; /evidence="ECO:0000255"
null
PF08516;PF00200;PF01562;PF01421;
IPR006586;IPR018358;IPR001762;IPR036436;IPR024079;IPR001590;IPR002870;IPR034027;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Crotalus (genus), Crotalus durissus (species)
null
true
Crotalus durissus
1
row_1916
false
null
76
C0HJE7
MNVFFMFSLLFLAALGSCAHDRNPLEECFRETDYEEFLEIARNGLTVTSNPKHVVIVGAGMAGLSAAYVLAGAGHQVTVLEASERVGGRVRTYRKKDWYANLGPMRLPTKHRIVREYIRKFGLQLNEFFQENENAWYFIKNIRKRVREVKNNPGILEYPVKPSEEGKSAAQLYVESLRKVVKELKRTNCKYILDKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFGYEKRFDEIVGGMDQLPTSMYEAIKEKVQVHFNARVIEIQQNDRETKVTYQTSANEMSSVTADYVIVCTTSRAARRIKFEPPLPPKKAHALRSVHYRSGTKIFLTCKRKFWEDDGIRGGKSTTDLPSRFIYYPNHNFTSGVGVIIAYGIGDDANFFQALDFKDCADIVINDLSLIHQLPKEDIQTFCRPSMIQRWSLDKYAMGGITTFTPYQFQHFSEALTAPFKRIYFAGEYTAQFHGWIDSTIKSGLTAARDVNRASENPSGIHLSNDNEF
L-amino acid oxidase bordonein-L (LAAO) (LAO) (EC 1.4.3.2)
Crotalus durissus terrificus (South American rattlesnake)
8,732
516
58,919
Antibiotic;Antimicrobial;Apoptosis;Cytolysis;Direct protein sequencing;Disulfide bond;FAD;Flavoprotein;Glycoprotein;Hemostasis impairing toxin;Oxidoreductase;Platelet aggregation inhibiting toxin;Secreted;Signal;Toxin
GO:0005576; GO:0006915; GO:0009063; GO:0031640; GO:0042742; GO:0090729; GO:0106329
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26273287}.
SIGNAL 1..18; /evidence="ECO:0000255"
null
PF01593;
IPR002937;IPR036188;IPR050281;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Crotalus (genus), Crotalus durissus (species)
null
true
Crotalus durissus
2
row_70
false
null
95
C0L2T8
MIQVLLVTICLAAFPYQGSSIILESGNVNDYEVIYPRKVTALPKGAVQPKYEDTMQYELKVNGQPVVLHLEKNKGLFSKDYSETHYSPDGRKITTNPSVEDHCYYHGRIENDADSTASISACNGLKGHFKLQGEMYIIEPLELSDSEDHAVFKLENVEKEDEAPKMCGVTQNWESNEPIKKASHLNLNPEHQRYVEIVIVVDHGMFTKYNGDSDKIRQRVHQMVNIMKESYRYMYIDISLAGIEIWSNKDLINVQPAAPNTLKSFGEWRETDLPKRKSHDNAQLLTSIDFNGQTIGIANIGAICDPKPSTRVVQDHSKINLRVALTMTHELSHNLGIHHDTGSCSCSGYSCIMSPVISDEPSKYFSDCSYIQCWNFIMNQKPQCILKKPLRTDTVSTPVSGNELLEARIECDCGSIENPCCYATTCKLRPGSQCAEGMCCDQCRFMKKGTVCRVSLVNKNDDTCTGQSADCPRNVLYG
Zinc metalloproteinase/disintegrin (Metalloproteinase PII) (MPII) [Cleaved into: Snake venom metalloproteinase (SVMP) (EC 3.4.24.-); Disintegrin Cdc]
Crotalus durissus collilineatus (Brazilian rattlesnake)
221,569
478
53,639
Cell adhesion impairing toxin;Collagen degradation;Direct protein sequencing;Disulfide bond;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Signal;Toxin;Zinc;Zymogen
GO:0004222; GO:0005576; GO:0005886; GO:0006508; GO:0030574; GO:0046872; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: [Snake venom metalloproteinase]: Secreted {ECO:0000305|PubMed:19230843}.; SUBCELLULAR LOCATION: [Disintegrin Cdc]: Secreted {ECO:0000269|PubMed:30377432}.
SIGNAL 1..20; /evidence="ECO:0000255"
null
PF00200;PF01562;PF01421;
IPR018358;IPR001762;IPR036436;IPR024079;IPR001590;IPR002870;IPR034027;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Crotalus (genus), Crotalus durissus (species)
MPII
true
Crotalus durissus
3
row_89
false
null
4,494
Q076D1
EQQRYLNAKKYVKLFLVADYIMYLKYGRNLTAVRTRMYDIDNVITPIYHRMNIHVALVGLEIWSNTDKIIVQSSADVTLDLFAKWRATDLLSRKSHDNAQLLTGINFNGPTAGLGYLGGICNTMYSAGIVQDHSKIHDLVAIAIAHEMGHNLGMDHDKDTCTCGTRPCIMAGALSCEASFLFSDCSQKDHQEFLIKNMPQCILKKPLKTDVVSPAVCGNYFVEVGEECDCGPPRTCRDPCCDAATCKLRQGAQCAEGLCCDQCRFKGAGTECRAAKDECDMADVCTGRSTECTDRFQRNGQPCKNNNGYCYNGKCPIMADQCIALFGPGATVSQDACFQFNREGNHYGYCRKEQNTKIACEPQDVKCGRLYCFPNSPENKNPCNIYYSPNDEDKGMVLPGTKCADGKACSNGQCVDVNTPY
Zinc metalloproteinase-disintegrin-like crotastatin (EC 3.4.24.-) (Snake venom metalloprotease) (SVMP) (Vascular apoptosis-inducing protein-like) (VAP-like)
Crotalus durissus terrificus (South American rattlesnake)
8,732
421
46,565
Apoptosis;Calcium;Cell adhesion impairing toxin;Disulfide bond;Fibrinogenolytic toxin;Glycoprotein;Hemorrhagic toxin;Hemostasis impairing toxin;Hydrolase;Metal-binding;Metalloprotease;Protease;Secreted;Toxin;Zinc
GO:0004222; GO:0005576; GO:0005886; GO:0006508; GO:0006915; GO:0046872; GO:0090729
Evidence at transcript level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
null
null
PF08516;PF00200;PF01421;
IPR006586;IPR018358;IPR001762;IPR036436;IPR024079;IPR001590;IPR034027;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Crotalus (genus), Crotalus durissus (species)
null
true
Crotalus durissus
4
row_4295
false
null
910
B0FXM1
MVLIRVLANLLILQLSYAQKSSELVIGGDECNINEHNFLVALYEYWSQSFLCGGTLINGEWVLTAAHCDRKHILIYVGVHDRSVQFDKEQRRFPKEKYFFNCRNNFTKWDKDIMLIRLNKPVSYSEHIAPLSLPSSPPIVGSVCRVMGWGTIKSPQETLPDVPHCANINLLDYEVCRTAHPQFRLPATSRILCAGVLEGGIDTCHRDSGGPLICNGEFQGIVSWGDGPCAQPDKPALYSKVFDHLDWIQNIIAGSETVNCPS
Thrombin-like enzyme gyroxin B1.3 (SVTLE gyroxin B1.3) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP)
Crotalus durissus terrificus (South American rattlesnake)
8,732
262
29,347
Blood coagulation cascade activating toxin;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Ion channel impairing toxin;Potassium channel impairing toxin;Protease;Secreted;Serine protease;Signal;Toxin;Voltage-gated potassium channel impairing toxin
GO:0004252; GO:0005576; GO:0006508; GO:0015459; GO:0030141; GO:0090729
Evidence at transcript level
4
SUBCELLULAR LOCATION: Secreted.
SIGNAL 1..18; /evidence="ECO:0000255"
null
PF00089;
IPR009003;IPR043504;IPR001314;IPR001254;IPR018114;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Crotalus (genus), Crotalus durissus (species)
null
true
Crotalus durissus
5
row_857
false
null
911
B0FXM2
MVLIRVLANLLILQLSYAQKSSELVIGGDECNINEHNFLVALYEYWSQSFLCGGTLINGEWVLTAAHCDRTHFLIYVGVHDRSVQFDKEQRRFPKEKYFFNCGNNFTKWDKDIMLIRLNKPVRNNEHIAPLSLPSSPPSVGSVCRVMGWGQTTSPQNTLPDVPHCANINLLDYEVCRTALPQLRLPATSRILCAGVLEGGIDTCNRDSGGPLICNGEFQGIVFWGPDPCAQPDKPALYSKVFDHLDWIQSIIAGNTIVNCPP
Thrombin-like enzyme gyroxin B1.4 (SVTLE gyroxin B1.4) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP)
Crotalus durissus terrificus (South American rattlesnake)
8,732
262
29,262
Blood coagulation cascade activating toxin;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Signal;Toxin
GO:0004252; GO:0005576; GO:0006508; GO:0030141; GO:0090729
Evidence at transcript level
4
SUBCELLULAR LOCATION: Secreted.
SIGNAL 1..18; /evidence="ECO:0000255"
null
PF00089;
IPR009003;IPR043504;IPR001314;IPR001254;IPR018114;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Crotalus (genus), Crotalus durissus (species)
null
true
Crotalus durissus
6
row_858
false
null
4,539
Q2QA04
MVLIRVLANLLILQLSYAQKSSELVIGGDECNINEHRSLALVYITSGFLCGGTLINKEWVLTAAHCDRGDILVLLGVHRLKDVQTGVSKDVQTRVAKEKFICPNRKKDDEKDKDIMLIRMDSPVNISTHIAPLSLPSNPPSVGSVCRIMGWGAITSPNVTLPGVPHCADINIFDYEVCRAAKPELPVTSRTLCAGILEGGKGSCDGDSGGPLICNGEIQGIVSWGGDICAQPREPEPYTKVFDYTEWIQSIIAGNTDATCPP
Snake venom serine protease (SVSP) (EC 3.4.21.-)
Crotalus durissus durissus (Central American rattlesnake)
31,150
262
28,271
Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Signal;Toxin;Zymogen
GO:0004252; GO:0005576; GO:0006508; GO:0030141; GO:0090729
Evidence at transcript level
3
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..18; /evidence="ECO:0000255"
null
PF00089;
IPR009003;IPR043504;IPR001314;IPR001254;IPR018114;IPR033116;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Crotalus (genus), Crotalus durissus (species)
null
true
Crotalus durissus
7
row_4340
false
null
912
B0FXM3
MVLIRVLANLLILQLSYAQKSSELVIGGDECNINEHRLLAIVYTNSSQCAGTLINQEWVLTAAHCDGENMDIYLGVHNESVQYDDEEGRVAAEKFFCLSSRNYTKWDKDIMLIRLNIPVRNSTHIAPLSLPSSPPSVGSVCRVMGWGTITSPNETYPDVPHCANINLFDYEVCLAAYPEFGLPATSRTLCAGIQQGGKDTCGSDSGGSLICNGQFQGIVSWGDNPCAQPHKPALYTKVLDDTEWIQSIIAGNTAVTCPP
Thrombin-like enzyme gyroxin B1.7 (SVTLE gyroxin B1.7) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP)
Crotalus durissus terrificus (South American rattlesnake)
8,732
259
28,184
Blood coagulation cascade activating toxin;Disulfide bond;Glycoprotein;Hemostasis impairing toxin;Hydrolase;Protease;Secreted;Serine protease;Signal;Toxin
GO:0004252; GO:0005576; GO:0006508; GO:0030141; GO:0090729
Evidence at transcript level
4
SUBCELLULAR LOCATION: Secreted.
SIGNAL 1..18; /evidence="ECO:0000255"
null
PF00089;
IPR009003;IPR043504;IPR001314;IPR001254;IPR018114;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Crotalus (genus), Crotalus durissus (species)
null
true
Crotalus durissus
8
row_859
false
null
2,236
Q9DEZ9
MSMLCYTLIIAFLIGIWAAPKSEDNVPLGSPATSDLSDTSCAKTHEALKTSRNIDQHYPAPKKAEDQEFGSAANIIVDPKLFQKRRFQSPRVLFSTQPPPLSRDEQSVDNANSLNRNIRAKREDHPVHKRGEYSVCDSVNVWVANKTTATDIRGNLVTVMVDVNINNNVYKQYFFETKCRNPNPVPTGCRGIDARHWNSYCTTTNTFVKALTMEGNQASWRFIRIDSACVCVISRKNENFG
Venom nerve growth factor (v-NGF) (vNGF)
Crotalus durissus terrificus (South American rattlesnake)
8,732
241
27,119
Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Growth factor;Lipid-binding;Metalloenzyme inhibitor;Metalloprotease inhibitor;Protease inhibitor;Secreted;Signal;Toxin
GO:0005163; GO:0005615; GO:0007169; GO:0008021; GO:0008083; GO:0008191; GO:0008289; GO:0021675; GO:0030424; GO:0030425; GO:0038180; GO:0043524; GO:0048812; GO:0050804; GO:0090729
Evidence at transcript level
4
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P61898}.
SIGNAL 1..18; /evidence="ECO:0000255"
null
PF00243;
IPR029034;IPR020408;IPR002072;IPR020425;IPR019846;IPR020433;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Crotalus (genus), Crotalus durissus (species)
null
true
Crotalus durissus
9
row_2152
false
null
12
A0A0S4FKT4
VIGGDECNINEHNFLVALYEYWSQSFLCGGTLINGEWVLTAAHCDRKHILIYVGVHDRSVQFDKEQRRFPKEKYFFNCRNNFTKWDKDIMLIRLNKPVSYSEHIAPLSLPSSPPIVGSVCRVMGWGTIKSPQETLPDVPHCANINLLDYEVCRTAHPQFRLPATIRILCAGVLEGGIDTCHRDSGGPLICNGEFQGIVSWGDGSCAQPDKPALYSKVFDHLDWIQNIIAGSETVNCPS
Thrombin-like enzyme collinein-1 (SVTLE collinein-1) (EC 3.4.21.-) (Fibrinogen-clotting enzyme) (Snake venom serine protease) (SVSP)
Crotalus durissus collilineatus (Brazilian rattlesnake)
221,569
238
26,664
Blood coagulation cascade activating toxin;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Hydrolase;Ion channel impairing toxin;Potassium channel impairing toxin;Protease;Secreted;Serine protease;Toxin;Voltage-gated potassium channel impairing toxin
GO:0004252; GO:0005615; GO:0006508; GO:0015459; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26227411}.
null
null
PF00089;
IPR009003;IPR043504;IPR001314;IPR050127;IPR001254;IPR018114;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Crotalus (genus), Crotalus durissus (species)
null
true
Crotalus durissus
10
row_11
false
null
620
Q2PE51
MFVSRLAASGLLLLALLAVSLDGKPLQQWSQRWPHLEIPPLVVQNWKSPTQLQARESPAGGTTALREELSLGPEAALDTPPAGPDGGPRGSKAAAAAPQRLSKSKGASATSAASRDLRTDGKQARQNWGRLVSPDHHSAAGGGGGGGGGARRLKGLAKKRAGNGCFGLKLDRIGSMSGLGC
Bradykinin-potentiating and C-type natriuretic peptides (Angiotensin converting enzyme inhibitor-CNP) (ACEI-CNP) (BPP-CNP) [Cleaved into: Bradykinin-potentiating peptide-1 (BPP-1); Bradykinin-potentiating peptide-2 (BPP-2); Bradykinin inhibitor peptide homolog (Cdc peptide) (Novel peptide); C-type natriuretic peptide (CNP)]
Crotalus durissus collilineatus (Brazilian rattlesnake)
221,569
181
18,514
Cleavage on pair of basic residues;Direct protein sequencing;Disulfide bond;Hypotensive agent;Metalloenzyme inhibitor;Metalloprotease inhibitor;Protease inhibitor;Pyrrolidone carboxylic acid;Secreted;Signal;Toxin;Vasoactive;Vasodilator
GO:0005179; GO:0005576; GO:0006182; GO:0007168; GO:0008217; GO:0030414; GO:0042311; GO:0090729
Evidence at protein level
5
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16979945}.
SIGNAL 1..23; /evidence="ECO:0000255"
null
PF00212;
IPR000663;IPR030480;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Crotalus (genus), Crotalus durissus (species)
null
true
Crotalus durissus
11
row_580
false
null
1,310
O93426
MGRFIFVSFGLLVLFLSLSGTGAGLHCPSDWYYYDQHCYRIFNEEMNWEDAEWFCTKQAKGAHLVSIKSAKEADFVAWMVTQNIEESFSHVSIGLRVQNKEKQCSTKWSDGSSVSYDNLLDLYITKCSLLKKETGFRKWFVASCIGKIPFVCKFPPQC
Snaclec convulxin subunit alpha (CVX-alpha)
Crotalus durissus terrificus (South American rattlesnake)
8,732
158
18,141
3D-structure;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Platelet aggregation activating toxin;Secreted;Signal;Toxin
GO:0005576; GO:0090729
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted.
SIGNAL 1..23; /evidence="ECO:0000269|PubMed:9153205, ECO:0000269|PubMed:9657980"
null
PF00059;
IPR001304;IPR016186;IPR050111;IPR016187;
1UMR;1UOS;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Crotalus (genus), Crotalus durissus (species)
null
true
Crotalus durissus
12
row_1251
false
null
7,269
Q719L9
MGRFIFVSFGLLVVFLSLSGTGADFDCPSGWSAYDQYCYRVIKQLKTWEDAEWFCTKQAKGAHLVSVESAGEADFVAQLVAENIKQNKYYVWIGLRIQNKGQQCSTKWSDGSSVNYENLLKSYSKKCFGLKKETEFLQWYNTDCEEKNLFVCKFPPQR
Snaclec crotocetin-1 (CRC1)
Crotalus durissus terrificus (South American rattlesnake)
8,732
158
18,199
Disulfide bond;Hemostasis impairing toxin;Secreted;Signal;Toxin
GO:0005576; GO:0090729
Evidence at transcript level
2
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
SIGNAL 1..23; /evidence="ECO:0000250"
null
PF00059;
IPR001304;IPR016186;IPR050111;IPR018378;IPR016187;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Crotalus (genus), Crotalus durissus (species)
null
true
Crotalus durissus
13
row_6990
false
null
1,311
O93427
MGRFIFVSFGLLVVFLSLSGSEAGFCCPSHWSSYDRYCYKVFKQEMTWADAEKFCTQQHTGSHLVSFHSTEEVDFVVKMTHQSLKSTFFWIGANNIWNKCNWQWSDGTKPEYKEWHEEFECLISRTFDNQWLSAPCSDTYSFVCKFEA
Snaclec convulxin subunit beta (CVX-beta)
Crotalus durissus terrificus (South American rattlesnake)
8,732
148
17,403
3D-structure;Direct protein sequencing;Disulfide bond;Hemostasis impairing toxin;Platelet aggregation activating toxin;Secreted;Signal;Toxin
GO:0005576; GO:0090729
Evidence at protein level
4
SUBCELLULAR LOCATION: Secreted.
SIGNAL 1..23; /evidence="ECO:0000269|PubMed:9153205, ECO:0000269|PubMed:9657980"
null
PF00059;
IPR001304;IPR016186;IPR050111;IPR018378;IPR016187;
1UMR;1UOS;
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), Lepidosauria (class), Squamata (order), Bifurcata (clade), Unidentata (clade), Episquamata (clade), Toxicofera (clade), Serpentes (infraorder), Colubroidea (superfamily), Viperidae (family), Crotalinae (subfamily), Crotalus (genus), Crotalus durissus (species)
null
true
Crotalus durissus
14
row_1252
false
null