ID A0A0V1N8Z0_9BILA Unreviewed; 460 AA.
AC A0A0V1N8Z0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Zinc metalloproteinase {ECO:0000256|PIRNR:PIRNR036365};
GN Name=hch-1 {ECO:0000313|EMBL:KRZ80500.1};
GN ORFNames=T10_6926 {ECO:0000313|EMBL:KRZ80500.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ80500.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ80500.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ80500.1};
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 ECO:0000256|PIRNR:PIRNR036365}.
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:KRZ80500.1}.
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DR EMBL; JYDO01000002; KRZ80500.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1N8Z0; -.
DR STRING; 268474.A0A0V1N8Z0; -.
DR Proteomes; UP000054843; 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 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 PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR PANTHER; PTHR10127:SF850; METALLOENDOPEPTIDASE; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 1.
DR PIRSF; PIRSF036365; Astacin_nematoda; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS01180; CUB; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW 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|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR036365};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PIRNR:PIRNR036365};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|PIRNR:PIRNR036365,
FT ECO:0000256|RuleBase:RU361183"
FT CHAIN 23..460
FT /note="Zinc metalloproteinase"
FT /evidence="ECO:0000256|PIRNR:PIRNR036365,
FT ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5006773952"
FT DOMAIN 114..310
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 343..460
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT ACT_SITE 207
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 460 AA; 52539 MW; 2A9FDA4A5B9A97A5 CRC64;
MASVKLNVIY LLMFLFFNGY KSKHSLRSFQ YKNNATMFST SELFRMELQS QAGFNETTVN
AYFQFMENVR NATLQTNPEE NSNLFEGDIL LTVEQMKVME KKIFKNSSDA DTLRGMVTGN
AFSRWKRTIP YSINTRSGVN TNAVERGIKQ WEKITCLKFV RQDNHPTEDY IEFFKGSGCY
SYVGKIGGKQ PISIGTGCES VGIVCHEIGH ALGVWHEQNR PDRDKFINVH HGNIKPHALS
NFYRLTNNIA LVNVIPFDYG SQMLYGPRAF AINNNRNTIS ALDVNYRSTL GQRDFPSFYD
AKTINLIYCN DLCKPLECEF DGYADPKNCS TCRCPVGLAG PYCKEALPTN YDCGKINIEI
ETSPWTINKS GQGKCHWLFK TTPQAKIELQ LVNFKFPCQI TCSRSFISVQ YGNSMANSPA
RFCCYERNKI IVSKSNYMLI SYYGRSTDFV TFIVKKHEMQ
//
