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Database: UniProt
Entry: A0A3R7P5D9_PENVA
LinkDB: A0A3R7P5D9_PENVA
Original site: A0A3R7P5D9_PENVA 
ID   A0A3R7P5D9_PENVA        Unreviewed;       256 AA.
AC   A0A3R7P5D9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN   ORFNames=C7M84_020533 {ECO:0000313|EMBL:ROT61685.1};
OS   Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC   Penaeoidea; Penaeidae; Penaeus.
OX   NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT61685.1, ECO:0000313|Proteomes:UP000283509};
RN   [1] {ECO:0000313|EMBL:ROT61685.1, ECO:0000313|Proteomes:UP000283509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Muscle {ECO:0000313|EMBL:ROT61685.1};
RA   Zhang X., Yuan J., Li F., Xiang J.;
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ROT61685.1, ECO:0000313|Proteomes:UP000283509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Muscle {ECO:0000313|EMBL:ROT61685.1};
RA   Sun Y., Gao Y., Yu Y.;
RT   "The decoding of complex shrimp genome reveals the adaptation for benthos
RT   swimmer, frequently molting mechanism and breeding impact on genome.";
RL   Submitted (JAN-2019) 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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01211}.
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:ROT61685.1}.
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DR   EMBL; QCYY01004036; ROT61685.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R7P5D9; -.
DR   STRING; 6689.A0A3R7P5D9; -.
DR   EnsemblMetazoa; XM_027379201.1; XP_027235002.1; LOC113826331.
DR   Proteomes; UP000283509; Unassembled WGS sequence.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04280; ZnMc_astacin_like; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   InterPro; IPR034035; Astacin-like_dom.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001506; Peptidase_M12A.
DR   InterPro; IPR006026; Peptidase_Metallo.
DR   PANTHER; PTHR10127; DISCOIDIN, CUB, EGF, LAMININ , AND ZINC METALLOPROTEASE DOMAIN CONTAINING; 1.
DR   PANTHER; PTHR10127:SF780; ZINC METALLOPROTEINASE NAS-13; 1.
DR   Pfam; PF01400; Astacin; 1.
DR   PRINTS; PR00480; ASTACIN.
DR   SMART; SM00235; ZnMc; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51864; ASTACIN; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
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:UP000283509};
KW   Signal {ECO:0000256|RuleBase:RU361183};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT   CHAIN           23..256
FT                   /note="Metalloendopeptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT                   /id="PRO_5018381120"
FT   DOMAIN          56..255
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         158
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   256 AA;  28871 MW;  6EC300D21002E16E CRC64;
     MYLYHFSMLL VTLLAVVAVA GATPAVPRAA TAMYNPDLFQ GDIKGIAGQE PGKERAAILG
     EQYLWPGGVV PYVFGNSVNS YERSLIISAM DDFHARTCIR FVERTSQSNY IEIVSNDSGC
     WSYVGTIGGK QRVSLDSNGC MYKGTVIHEL MHAIGFYHEH CRNDRDYYVT IHYENVQAGM
     ESQFNKDTYW QYVGEGYNYE SIMHYGTYAF SVQWGVAKTI VPTDPNVILT EAYDKLQMAQ
     SDANQINNLY RNQCSF
//
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