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Database: UniProt
Entry: A0A0J8Y2W6_9GAMM
LinkDB: A0A0J8Y2W6_9GAMM
Original site: A0A0J8Y2W6_9GAMM 
ID   A0A0J8Y2W6_9GAMM        Unreviewed;       465 AA.
AC   A0A0J8Y2W6;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   07-JUN-2017, entry version 9.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=AB733_04025 {ECO:0000313|EMBL:KMV31914.1};
OS   Photobacterium swingsii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=680026 {ECO:0000313|EMBL:KMV31914.1, ECO:0000313|Proteomes:UP000037287};
RN   [1] {ECO:0000313|EMBL:KMV31914.1, ECO:0000313|Proteomes:UP000037287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAIM 1393 {ECO:0000313|EMBL:KMV31914.1,
RC   ECO:0000313|Proteomes:UP000037287};
RX   PubMed=20228205; DOI=10.1099/ijs.0.019687-0;
RA   Gomez-Gil B., Roque A., Rotllant G., Peinado L., Romalde J.L.,
RA   Doce A., Cabanillas-Beltran H., Chimetto L.A., Thompson F.L.;
RT   "Photobacterium swingsii sp. nov., isolated from marine organisms.";
RL   Int. J. Syst. Evol. Microbiol. 61:315-319(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KMV31914.1}.
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DR   EMBL; LELC01000002; KMV31914.1; -; Genomic_DNA.
DR   RefSeq; WP_048897587.1; NZ_LELC01000002.1.
DR   EnsemblBacteria; KMV31914; KMV31914; AB733_04025.
DR   PATRIC; fig|680026.4.peg.981; -.
DR   Proteomes; UP000037287; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001948; Peptidase_M18.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KMV31914.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000037287};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|RuleBase:RU004386};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   465 AA;  52066 MW;  010F690DBD3E8E90 CRC64;
     METLKFTNGW LDLDKKRIDE INLFNEGYKH FLDQGKTERQ CVTVSIAQAE QHGFRPISEF
     EQLVAGDKVY FINRHKNVVL AIIGQRPISE GIRYVVSHID SPRLDLKPSP VYEKCELALM
     RTHYYGGIKK YQWASRPLAL HGIVVTKSGR KVDIAIGEDD SDPVFTIPDL LPHLDRKVQR
     ERKADEVLKG EELQIVVGSV PMTFDDEKIK DTVKHHVLTK LFEKYEISEP DFISAELMLV
     PAGKARDVGL DHGIIGAYGQ DDRICAYTSL EAIFDIDTPE QTAVCFLVDK EEIGSTGATG
     LESRYLEFFT GELLVRQAGG QYNDQMLRRC LWQSYALSSD VNAGLNPLFE SVHDAQNASK
     LGYGLVLTKY TGHGGKVASN DADAEYVAAL RRIFDDTEIK WQTGLLGKVD EGGGGTVAKY
     LAHYGINTID AGAAILSMHS PFELSSKFDV HELYRAYKAF YMQAL
//
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