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Database: UniProt
Entry: A0A081N7A1_9GAMM
LinkDB: A0A081N7A1_9GAMM
Original site: A0A081N7A1_9GAMM 
ID   A0A081N7A1_9GAMM        Unreviewed;       434 AA.
AC   A0A081N7A1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   22-NOV-2017, entry version 11.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=GZ77_07935 {ECO:0000313|EMBL:KEQ14324.1};
OS   Endozoicomonas montiporae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Endozoicomonas.
OX   NCBI_TaxID=1027273 {ECO:0000313|EMBL:KEQ14324.1, ECO:0000313|Proteomes:UP000028006};
RN   [1] {ECO:0000313|EMBL:KEQ14324.1, ECO:0000313|Proteomes:UP000028006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 24815 {ECO:0000313|EMBL:KEQ14324.1,
RC   ECO:0000313|Proteomes:UP000028006};
RA   Neave M.J., Apprill A., Voolstra C.R.;
RT   "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:KEQ14324.1}.
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DR   EMBL; JOKG01000002; KEQ14324.1; -; Genomic_DNA.
DR   RefSeq; WP_034874175.1; NZ_JOKG01000002.1.
DR   EnsemblBacteria; KEQ14324; KEQ14324; GZ77_07935.
DR   Proteomes; UP000028006; 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   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KEQ14324.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000028006};
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   Reference proteome {ECO:0000313|Proteomes:UP000028006};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   434 AA;  48008 MW;  7F71A8F75E761CCD CRC64;
     MSQTPSLQQN FNQNLVEFLR ESPTPYHAVK NMVAKLEQHG FVQLNESQAW QLKDNGRYYV
     TRNDSSIVAF TNGNHQQGFR MVGGHTDFPC LKVKPQPELH KHQYLQLAVE VYGGALLNPW
     FDRDLSIAGR VFYIDTAGEL KSSLINYRKA VAYIPSLAIH LDREANKKRS VNPQTDIPPI
     LCQLGKDEKA DFRALLKEQL AEEGVTDVTE VLEYDLSFYD TQGAAIIGLK DEFIVSQSLD
     NLLSCYVGMT AMIEALDNSS APMVLVCNDH EECGSQSATG AQGPMLKTIL HRVAGSTEAL
     AQAIARSMII SADNAHGVHP NYADRHEGNH QPLLNKGAVL KINANQRYAS NDETCALFGL
     LCREAGADYQ YFVTRTDLAC GSTIGPLTAG ELGIRTLDIG LPTFGMHSIR ETAGTRDAFQ
     LNQVLQRFFA KDQI
//
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