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
//