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UniProtKB - A6MFK7 (FAXD1_DEMVE)

Entry version 82 (07 Oct 2020)
Sequence version 1 (24 Jul 2007)
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Protein

Venom prothrombin activator vestarin-D1

Gene
N/A
Organism
Demansia vestigiata (Lesser black whip snake) (Demansia atra)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Snake prothrombin activator that attacks the hemostatic system of prey. This protein is functionally similar to blood coagulation factor Xa (By similarity).By similarity

Miscellaneous

Is classified in the group D of snake venom prothrombin activators, since it requires the mammalian factor Va for maximal activity for the cleavage of prothrombin.
In contrast to blood coagulation factors that circulate as inactive zymogen in plasma, venom prothrombin activators are always found in the active form in the venom.

Caution

Lacks the Cys residue in position 255 that is replaced by a Gly residue, resulting of a loss a disulfide bond. This may contribute to a probable lower procoagulant activity.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin. EC:3.4.21.6

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei270Charge relay systemBy similarity1
Active sitei315Charge relay systemBy similarity1
Active sitei412Charge relay systemBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionBlood coagulation cascade activating toxin, Hemostasis impairing toxin, Hydrolase, Protease, Prothrombin activator, Serine protease, Toxin
LigandCalcium

Protein family/group databases

MEROPS protease database

More...MEROPSi		S01.396

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Venom prothrombin activator vestarin-D1 (EC:3.4.21.6)
Short name:
vPA
Alternative name(s):
Venom coagulation factor Xa-like protease
Cleaved into the following 2 chains:
Vestarin-D1 light chain
Vestarin-D1 heavy chain
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiDemansia vestigiata (Lesser black whip snake) (Demansia atra)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri412038 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Lepidosauria › Squamata › Bifurcata › Unidentata › Episquamata › Toxicofera › Serpentes › Colubroidea › Elapidae › Notechinae › Demansia

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 20Sequence analysisAdd BLAST20
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000040989421 – 40By similarityAdd BLAST20
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_500025411141 – 181Vestarin-D1 light chainAdd BLAST141
PropeptideiPRO_0000409895182 – 228Activation peptideBy similarityAdd BLAST47
ChainiPRO_0000409896229 – 473Vestarin-D1 heavy chainAdd BLAST245

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei464-carboxyglutamatePROSITE-ProRule annotation1
Modified residuei474-carboxyglutamatePROSITE-ProRule annotation1
Modified residuei544-carboxyglutamatePROSITE-ProRule annotation1
Modified residuei564-carboxyglutamatePROSITE-ProRule annotation1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi57 ↔ 62By similarity
Modified residuei594-carboxyglutamatePROSITE-ProRule annotation1
Modified residuei604-carboxyglutamatePROSITE-ProRule annotation1
Modified residuei654-carboxyglutamatePROSITE-ProRule annotation1
Modified residuei664-carboxyglutamatePROSITE-ProRule annotation1
Modified residuei694-carboxyglutamatePROSITE-ProRule annotation1
Modified residuei724-carboxyglutamatePROSITE-ProRule annotation1
Modified residuei754-carboxyglutamatePROSITE-ProRule annotation1
Disulfide bondi90 ↔ 101By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi92O-linked (Hex...) serineBy similarity1
Disulfide bondi95 ↔ 110By similarity
Disulfide bondi112 ↔ 121By similarity
Disulfide bondi129 ↔ 140By similarity
Disulfide bondi136 ↔ 149By similarity
Disulfide bondi151 ↔ 164By similarity
Disulfide bondi172 ↔ 335Interchain (between light and heavy chains)PROSITE-ProRule annotation
Disulfide bondi235 ↔ 240By similarity
Glycosylationi273N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi383 ↔ 397By similarity
Disulfide bondi408 ↔ 436By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		A6MFK7

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed by the venom gland.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Heterodimer of a light chain and a heavy chain; disulfide-linked.

By similarity

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		A6MFK7

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini41 – 86GlaPROSITE-ProRule annotationAdd BLAST46
Domaini86 – 122EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini129 – 164EGF-like 2PROSITE-ProRule annotationAdd BLAST36
Domaini229 – 460Peptidase S1PROSITE-ProRule annotationAdd BLAST232

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase S1 family. Snake venom subfamily.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Family and domain databases

Conserved Domains Database

More...CDDi		cd00190, Tryp_SPc, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.40.10.10, 2 hits
4.10.740.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR017857, Coagulation_fac-like_Gla_dom
IPR001881, EGF-like_Ca-bd_dom
IPR000742, EGF-like_dom
IPR000152, EGF-type_Asp/Asn_hydroxyl_site
IPR018097, EGF_Ca-bd_CS
IPR035972, GLA-like_dom_SF
IPR000294, GLA_domain
IPR012224, Pept_S1A_FX
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR001314, Peptidase_S1A
IPR001254, Trypsin_dom
IPR018114, TRYPSIN_HIS
IPR033116, TRYPSIN_SER

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00008, EGF, 1 hit
PF00594, Gla, 1 hit
PF00089, Trypsin, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF001143, Factor_X, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00722, CHYMOTRYPSIN
PR00001, GLABLOOD

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00181, EGF, 2 hits
SM00179, EGF_CA, 1 hit
SM00069, GLA, 1 hit
SM00020, Tryp_SPc, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50494, SSF50494, 1 hit
SSF57630, SSF57630, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00010, ASX_HYDROXYL, 1 hit
PS00022, EGF_1, 1 hit
PS01186, EGF_2, 2 hits
PS50026, EGF_3, 1 hit
PS01187, EGF_CA, 1 hit
PS00011, GLA_1, 1 hit
PS50998, GLA_2, 1 hit
PS50240, TRYPSIN_DOM, 1 hit
PS00134, TRYPSIN_HIS, 1 hit
PS00135, TRYPSIN_SER, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

A6MFK7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAPQLLLCLI QTFLWSLPEA ESNVFLKSNV ANRFLQRTKR ANSGFEEIYP 
        60         70         80         90        100
ANFERECVEE RCSKEEAREV FEDDEKTEAF WTVYVDGDQC LSNPCHYGGT 
       110        120        130        140        150
CKDGIGSYTC TCLAGYEGKN CEHDLLKSCR VDNGNCWHFC KPVQNDTQCS 
       160        170        180        190        200
CAEGYRLGDN GFSCIAEGEF SCGRNIKSRN KREASLPDFQ TDFSDDYDAI 
       210        220        230        240        250
DENNLIETVQ SQSATLLKKS DNPNPDIRIV NGLDCKLGEC PWQAVLIDEK 
       260        270        280        290        300
GTAFGGGTIL SPYFVLTAAH CINKTKSIAV VVGQVDISRK ETRRLLSVDK 
       310        320        330        340        350
VYTHPKYVHV TNDYDIAIIQ LKTPIQFSEN VVPACLPTAD FANHVLMKQD 
       360        370        380        390        400
FGIVSGFGRI EEKGPTSNIL KVVMVPYVDR HTCILSTKIP ITRNMFCAGY 
       410        420        430        440        450
GNQPEDACEG DSGGPHITAY KDTHFLTGIV SWGEGCGRDG KYGIYTKVSN 
       460        470 
FLPWIKTIMR RKQPSTESST GRL
Length:473
Mass (Da):52,732
Last modified:July 24, 2007 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4C625C1975A8FBEC
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
DQ917518 mRNA Translation: ABK63547.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ917518 mRNA Translation: ABK63547.1

3D structure databases

SMRiA6MFK7
ModBaseiSearch...

Protein family/group databases

MEROPSiS01.396

Proteomic databases

PRIDEiA6MFK7

Family and domain databases

CDDicd00190, Tryp_SPc, 1 hit
Gene3Di2.40.10.10, 2 hits
4.10.740.10, 1 hit
InterProiView protein in InterPro
IPR017857, Coagulation_fac-like_Gla_dom
IPR001881, EGF-like_Ca-bd_dom
IPR000742, EGF-like_dom
IPR000152, EGF-type_Asp/Asn_hydroxyl_site
IPR018097, EGF_Ca-bd_CS
IPR035972, GLA-like_dom_SF
IPR000294, GLA_domain
IPR012224, Pept_S1A_FX
IPR009003, Peptidase_S1_PA
IPR043504, Peptidase_S1_PA_chymotrypsin
IPR001314, Peptidase_S1A
IPR001254, Trypsin_dom
IPR018114, TRYPSIN_HIS
IPR033116, TRYPSIN_SER
PfamiView protein in Pfam
PF00008, EGF, 1 hit
PF00594, Gla, 1 hit
PF00089, Trypsin, 1 hit
PIRSFiPIRSF001143, Factor_X, 1 hit
PRINTSiPR00722, CHYMOTRYPSIN
PR00001, GLABLOOD
SMARTiView protein in SMART
SM00181, EGF, 2 hits
SM00179, EGF_CA, 1 hit
SM00069, GLA, 1 hit
SM00020, Tryp_SPc, 1 hit
SUPFAMiSSF50494, SSF50494, 1 hit
SSF57630, SSF57630, 1 hit
PROSITEiView protein in PROSITE
PS00010, ASX_HYDROXYL, 1 hit
PS00022, EGF_1, 1 hit
PS01186, EGF_2, 2 hits
PS50026, EGF_3, 1 hit
PS01187, EGF_CA, 1 hit
PS00011, GLA_1, 1 hit
PS50998, GLA_2, 1 hit
PS50240, TRYPSIN_DOM, 1 hit
PS00134, TRYPSIN_HIS, 1 hit
PS00135, TRYPSIN_SER, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFAXD1_DEMVE
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: A6MFK7
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: July 24, 2007
Last modified: October 7, 2020
This is version 82 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
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