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Database: UniProt
Entry: A0A210PQU2_MIZYE
LinkDB: A0A210PQU2_MIZYE
Original site: A0A210PQU2_MIZYE 
ID   A0A210PQU2_MIZYE        Unreviewed;       396 AA.
AC   A0A210PQU2;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN   ORFNames=KP79_PYT23677 {ECO:0000313|EMBL:OWF38855.1};
OS   Mizuhopecten yessoensis (Japanese scallop) (Patinopecten yessoensis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae;
OC   Mizuhopecten.
OX   NCBI_TaxID=6573 {ECO:0000313|EMBL:OWF38855.1, ECO:0000313|Proteomes:UP000242188};
RN   [1] {ECO:0000313|Proteomes:UP000242188}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PY_sf001 {ECO:0000313|Proteomes:UP000242188};
RX   PubMed=28812685; DOI=10.1038/s41559-017-0120;
RA   Wang S., Zhang J., Jiao W., Li J., Xun X., Sun Y., Guo X., Huan P.,
RA   Dong B., Zhang L., Hu X., Sun X., Wang J., Zhao C., Wang Y., Wang D.,
RA   Huang X., Wang R., Lv J., Li Y., Zhang Z., Liu B., Lu W., Hui Y., Liang J.,
RA   Zhou Z., Hou R., Li X., Liu Y., Li H., Ning X., Lin Y., Zhao L., Xing Q.,
RA   Dou J., Li Y., Mao J., Guo H., Dou H., Li T., Mu C., Jiang W., Fu Q.,
RA   Fu X., Miao Y., Liu J., Yu Q., Li R., Liao H., Li X., Kong Y., Jiang Z.,
RA   Chourrout D., Li R., Bao Z.;
RT   "Scallop genome provides insights into evolution of bilaterian karyotype
RT   and development.";
RL   Nat. Ecol. Evol. 1:120-120(2017).
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:OWF38855.1}.
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DR   EMBL; NEDP02005553; OWF38855.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A210PQU2; -.
DR   EnsemblMetazoa; XM_021521892.1; XP_021377567.1; LOC110465798.
DR   OrthoDB; 2961753at2759; -.
DR   Proteomes; UP000242188; 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:SF850; METALLOENDOPEPTIDASE; 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   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:UP000242188};
KW   Signal {ECO:0000256|RuleBase:RU361183};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01211, ECO:0000256|RuleBase:RU361183}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT   CHAIN           26..396
FT                   /note="Metalloendopeptidase"
FT                   /evidence="ECO:0000256|RuleBase:RU361183"
FT                   /id="PRO_5033113928"
FT   DOMAIN          168..378
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   ACT_SITE        271
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         270
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         274
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         280
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   396 AA;  44896 MW;  397C347A3EBDAC38 CRC64;
     MKNLTLMRTV LVYLLLWLHI GTTIGQLPTQ SSPALRRLLS RLVTDVDSLF KIVKLFKSLN
     HNSASSSRTN QDIVPIDQII EEAEDPAASI KAEPSYIEKE NAFKLEGDIM MTVDQFTDMQ
     THISFDLLED AVAMMLNTTD RITSVQTLMN EISAGARSGR PSSRVKRAAR RDPNRLWPDA
     VMPVRIASSG FSAFDRWTIQ RAMMRISEQT CICFRIIDNE VADSGIPHVQ IVDGSGCSSY
     VGVTTRSRGR QNSQDLTLNS KCRTFRVATH ELLHALGLFH EQSRPDRDFF VKINSSNIRS
     GMERNFQKFS RRTINSRGIP YDYTSIMHYS NRAFSKDGTF TIEPIPAINR FWYLNIIGRS
     TAMSEGDVQA LRLMYNCPST PSTQPTCADY PYMFPY
//
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