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Database: UniProt
Entry: A0A0V1C191_TRISP
LinkDB: A0A0V1C191_TRISP
Original site: A0A0V1C191_TRISP 
ID   A0A0V1C191_TRISP        Unreviewed;       716 AA.
AC   A0A0V1C191;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
DE   Flags: Fragment;
GN   Name=dpy-31 {ECO:0000313|EMBL:KRY42936.1};
GN   ORFNames=T01_11220 {ECO:0000313|EMBL:KRY42936.1};
OS   Trichinella spiralis (Trichina worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6334 {ECO:0000313|EMBL:KRY42936.1, ECO:0000313|Proteomes:UP000054776};
RN   [1] {ECO:0000313|EMBL:KRY42936.1, ECO:0000313|Proteomes:UP000054776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS3 {ECO:0000313|EMBL:KRY42936.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC         ECO:0000256|RuleBase:RU361183};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRY42936.1}.
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DR   EMBL; JYDH01000002; KRY42936.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1C191; -.
DR   Proteomes; UP000054776; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00041; CUB; 1.
DR   CDD; cd04280; ZnMc_astacin_like; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 1.
DR   InterPro; IPR034035; Astacin-like_dom.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR017050; Metallopeptidase_nem.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR   PANTHER; PTHR10127:SF813; ZINC METALLOPROTEINASE DPY-31; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF00090; TSP_1; 1.
DR   PIRSF; PIRSF036365; Astacin_nematoda; 2.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00209; TSP1; 1.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
DR   PROSITE; PS01180; CUB; 1.
DR   PROSITE; PS50092; TSP1; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU01211}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|PROSITE-
KW   ProRule:PRU01211};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW   ECO:0000256|RuleBase:RU361183};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054776};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT   DOMAIN          254..453
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   DOMAIN          497..613
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   REGION          72..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..223
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        350
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         349
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         359
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   DISULFID        297..452
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRY42936.1"
SQ   SEQUENCE   716 AA;  81865 MW;  EE62527D9621C92F CRC64;
     LDFIHLLIYF QHPLPPSLPP SLSVHHSLFV QDLPKIIFSH LLLPNKTVMQ ISSLLLSLIC
     LIDIHCHAEN ADEHHRQQRS TEVVKQKPGR DLLAADVDNP TSDLIDSDIR KKAFTFGQTK
     QQRDRINFIL KQMEQLMLSN VKMERLAVAD TKSMVPSLEK RISNQIEANL YQSEDSFHRR
     LQDQRKNASN SSIDYLKHKP HKEQPGRFMD SDPHGKSPEE SGSHYEGDIV LTPEQAEELY
     SSLVHKNDRR QKRKFIALNA RHWDSSVPID YSFDGSHTSK QERLIELALK HWENVTCLRF
     RRRFDTPKGN RIIFTDVDGC ASNVGRNPMK EPQYVSLSLD CMKLGVIAHE VAHALGFWHE
     QSRPDRDRFV NVVWRNIDEG SLAQFLKEQT REVDSKGIPY DYGSIMHYRS KAFAKNGDLY
     TLLTNVQNYQ RTIGQRDHLS FNDIRLMNQI YCSHVCTPLN CQRGGYTDPK KCSRCRCPDG
     FTGKLCEIVM PGFDANCGGL VAVKSRWHYF SSPNYPKAFK AGQECSWLFR ASDGLRVELE
     FIERFDIYCK AEHSLCMDYI EIRNSSDFAN TGMRLCCHNI PKQRIYSSTT DMLVLFRSFY
     RSGLGFRARV RAVPPSGEWE KWGEWSPCSV SCGGCGVQTR QRKCPKDSLC AGESTSVQSC
     GNVPCEKCKE EKLVSVSCGL WGLFRCEAMQ SVEVPCKEKC CTGYTVVNGV CEPVIL
//
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