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Database: UniProt
Entry: A0A162DJ74_9FLAO
LinkDB: A0A162DJ74_9FLAO
Original site: A0A162DJ74_9FLAO 
ID   A0A162DJ74_9FLAO        Unreviewed;       389 AA.
AC   A0A162DJ74;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Peptidase M12A domain-containing protein {ECO:0000259|PROSITE:PS51864};
GN   ORFNames=AWE51_22805 {ECO:0000313|EMBL:KZS41238.1};
OS   Aquimarina aggregata.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Aquimarina.
OX   NCBI_TaxID=1642818 {ECO:0000313|EMBL:KZS41238.1, ECO:0000313|Proteomes:UP000076715};
RN   [1] {ECO:0000313|EMBL:KZS41238.1, ECO:0000313|Proteomes:UP000076715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RZW4-3-2 {ECO:0000313|EMBL:KZS41238.1,
RC   ECO:0000313|Proteomes:UP000076715};
RA   Wang Y.;
RT   "The draft genome sequence of Aquimarina sp. RZW4-3-2.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PROSITE-ProRule:PRU01211};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC       ProRule:PRU01211};
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:KZS41238.1}.
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DR   EMBL; LQRT01000006; KZS41238.1; -; Genomic_DNA.
DR   RefSeq; WP_066312577.1; NZ_LQRT01000006.1.
DR   AlphaFoldDB; A0A162DJ74; -.
DR   STRING; 1642818.AWE51_22805; -.
DR   OrthoDB; 8455098at2; -.
DR   Proteomes; UP000076715; 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   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 2.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
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; ZINC METALLOPROTEINASE NAS-29; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01211};
KW   Metalloprotease {ECO:0000256|PROSITE-ProRule:PRU01211};
KW   Protease {ECO:0000256|PROSITE-ProRule:PRU01211};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076715};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01211}.
FT   DOMAIN          98..288
FT                   /note="Peptidase M12A"
FT                   /evidence="ECO:0000259|PROSITE:PS51864"
FT   ACT_SITE        192
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         191
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         195
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT   BINDING         201
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ   SEQUENCE   389 AA;  43151 MW;  2A49E48CB66C0004 CRC64;
     MKTKNLINLA KVSALSLGLF FTSCSNESIE DLPEETGGEQ EQLVDKYFKG DLIQVEDIGN
     NTFKFGDVLF DSAQLSDEIV AYDANPEPGA GLSSDPKLGL AGGVRKWPNN TIIYVLDNSL
     SSNQRQVTFD AMDEWKNKTN IRFKERTNES FYVTIRNSGA QCNCASASLG VQGTRGTINM
     GVRTGFGVMT HEIGHTLGYL HEQNRSDRDQ FVRIFPENIQ DGAISQFRVD NNSVNPGRFD
     VESIMIYSSF TFSKNGQPVM LELDGSRIPF RSRLSAGDIA GTNQLYPGGD GGDGGGDTDT
     CEGVDEWVRG RQYTVGDRVT YRGSLYERDF SRWNRIKECD ATTPQDICEG VAAYNRGTRY
     RAGDRVTFQG FLYELQSNGR WSNLGQCAN
//
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