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Entry version 24 (07 Nov 2018)
Sequence version 1 (29 Apr 2015)
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Protein

Zinc metalloproteinase dpy-31

Gene

dpy-31

Organism
Teladorsagia circumcincta (Brown stomach worm) (Ostertagia circumcincta)
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

Metalloprotease which cleaves the carboxyl terminus of procollagens to mature collagens. Probably involved in cuticular collagen maturation.By similarity

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+PROSITE-ProRule annotationNote: Binds 1 zinc ion per subunit.PROSITE-ProRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by marimastat and tripeptide hydroxamic acids (PubMed:26546217). Inhibited by 1,10-phenanthroline (PubMed:25736599).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi245Zinc; via tele nitrogen; catalyticPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei246PROSITE-ProRule annotation1
Metal bindingi249Zinc; via tele nitrogen; catalyticPROSITE-ProRule annotation1
Metal bindingi255Zinc; via tele nitrogen; catalyticPROSITE-ProRule annotation1

<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

GO - Biological processi

<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 functionHydrolase, Metalloprotease, Protease
LigandMetal-binding, Zinc

<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_and_taxonomy_section">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:
Zinc metalloproteinase dpy-31By similarity (EC:3.4.24.-2 Publications)
Alternative name(s):
Nematode astacin 35By similarity
Procollagen C-proteinaseBy similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:dpy-31Imported
Synonyms:nas-35By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiTeladorsagia circumcincta (Brown stomach worm) (Ostertagia circumcincta)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri45464 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaStrongylidaTrichostrongyloideaHaemonchidaeTeladorsagia

<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 provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3739251

<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 – 24Sequence analysisAdd BLAST24
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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_000044224725 – 150By similarityAdd BLAST126
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_5005111502151 – 614Zinc metalloproteinase dpy-31Sequence analysisAdd BLAST464

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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>Glycosylationi190N-linked (GlcNAc...) asparaginePROSITE-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 bondi193 ↔ 348PROSITE-ProRule annotation
Disulfide bondi216 ↔ 237PROSITE-ProRule annotation
Disulfide bondi352 ↔ 372PROSITE-ProRule annotation
Disulfide bondi374 ↔ 383PROSITE-ProRule annotation
Disulfide bondi394 ↔ 422PROSITE-ProRule annotation
Glycosylationi461N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi525 ↔ 556PROSITE-ProRule annotation
Disulfide bondi529 ↔ 561PROSITE-ProRule annotation
Disulfide bondi541 ↔ 546PROSITE-ProRule annotation

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

<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_and_domains_section">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>Domaini150 – 349Peptidase M12APROSITE-ProRule annotationAdd BLAST200
Domaini344 – 384EGF-likePROSITE-ProRule annotationAdd BLAST41
Domaini394 – 510CUBPROSITE-ProRule annotationAdd BLAST117
Domaini513 – 562TSP type-1PROSITE-ProRule annotationAdd BLAST50

Keywords - Domaini

EGF-like domain, Signal

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00041 CUB, 1 hit
cd04280 ZnMc_astacin_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.20.100.10, 1 hit
2.60.120.290, 1 hit
3.40.390.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR034035 Astacin-like_dom
IPR000859 CUB_dom
IPR013032 EGF-like_CS
IPR024079 MetalloPept_cat_dom_sf
IPR017050 Metallopeptidase_nem
IPR001506 Peptidase_M12A
IPR006026 Peptidase_Metallo
IPR035914 Sperma_CUB_dom_sf
IPR000884 TSP1_rpt
IPR036383 TSP1_rpt_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01400 Astacin, 1 hit
PF00431 CUB, 1 hit
PF00090 TSP_1, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF036365 Astacin_nematoda, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00480 ASTACIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00042 CUB, 1 hit
SM00209 TSP1, 1 hit
SM00235 ZnMc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49854 SSF49854, 1 hit
SSF82895 SSF82895, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51864 ASTACIN, 1 hit
PS01180 CUB, 1 hit
PS00022 EGF_1, 1 hit
PS01186 EGF_2, 1 hit
PS50092 TSP1, 1 hit
PS00142 ZINC_PROTEASE, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

A0A0C5PRQ1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSLLRCTTLL LVVVAIALPP CILGYSLHDG SRLDDFLTES AADRRPRRPT
60 70 80 90 100
TAAQRRLMGL TEEQYKTVHF YLNKLKELGN QRHPEGYDKD TTKDEADKWR
110 120 130 140 150
KRMRDDIEGE LLNPEEYGRH FEGDIILFPE QAKQIYENAL KTGQRRVKRK
160 170 180 190 200
FIGSDLRRWD PTRPIVYSFD GSHTSREQRI IELALEHWHN ITCLNFVRND
210 220 230 240 250
NANSGNRIVF TDVDGCASNV GRHPLGEEQL VSLAPECIRL GVIAHEVAHA
260 270 280 290 300
LGFWHEQSRP DRDQFVNVRW ENIDKDSKGQ FLKEDPDDVD NAGVPYDYGS
310 320 330 340 350
IMHYRSKAFS RYDDLYTIST FVTDYQKTIG QRDQLSFNDI RLMNKIYCSN
360 370 380 390 400
VCSRKLPCQR GGYTDPRRCD RCRCPDGFTG QFCEQVMPGY GAVCGGRIQV
410 420 430 440 450
NGGWTKFSSP GYPREFKEGQ ECSWLLVAPH GQVVEMQFIG EFEMYCKVRH
460 470 480 490 500
SLCMDYVEVR NSTDFANTGM RYCCYGTPST SIRSATTDLV VLFRSFYRGG
510 520 530 540 550
RGFEARARAL PANGQWASWS PWTPCTASCG ACGSRMRTRV CSHGACAGEP
560 570 580 590 600
VENQVCNTHP CNGLCAHKKT EDGECGGFLA LLRGVRCKQE RTVMEPCENA
610
CCPGFSVVGG RCVR
Length:614
Mass (Da):69,695
Last modified:April 29, 2015 - 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:iBEB519E319F787C9
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
KM272923 Genomic DNA Translation: AJQ21780.1

<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
KM272923 Genomic DNA Translation: AJQ21780.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Chemistry databases

ChEMBLiCHEMBL3739251

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd00041 CUB, 1 hit
cd04280 ZnMc_astacin_like, 1 hit
Gene3Di2.20.100.10, 1 hit
2.60.120.290, 1 hit
3.40.390.10, 1 hit
InterProiView protein in InterPro
IPR034035 Astacin-like_dom
IPR000859 CUB_dom
IPR013032 EGF-like_CS
IPR024079 MetalloPept_cat_dom_sf
IPR017050 Metallopeptidase_nem
IPR001506 Peptidase_M12A
IPR006026 Peptidase_Metallo
IPR035914 Sperma_CUB_dom_sf
IPR000884 TSP1_rpt
IPR036383 TSP1_rpt_sf
PfamiView protein in Pfam
PF01400 Astacin, 1 hit
PF00431 CUB, 1 hit
PF00090 TSP_1, 1 hit
PIRSFiPIRSF036365 Astacin_nematoda, 1 hit
PRINTSiPR00480 ASTACIN
SMARTiView protein in SMART
SM00042 CUB, 1 hit
SM00209 TSP1, 1 hit
SM00235 ZnMc, 1 hit
SUPFAMiSSF49854 SSF49854, 1 hit
SSF82895 SSF82895, 1 hit
PROSITEiView protein in PROSITE
PS51864 ASTACIN, 1 hit
PS01180 CUB, 1 hit
PS00022 EGF_1, 1 hit
PS01186 EGF_2, 1 hit
PS50092 TSP1, 1 hit
PS00142 ZINC_PROTEASE, 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 nameiNAS35_TELCI
<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: A0A0C5PRQ1
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 22, 2017
Last sequence update: April 29, 2015
Last modified: November 7, 2018
This is version 24 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)
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