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Database: UniProt
Entry: A0A096ANS7_9FIRM
LinkDB: A0A096ANS7_9FIRM
Original site: A0A096ANS7_9FIRM 
ID   A0A096ANS7_9FIRM        Unreviewed;       442 AA.
AC   A0A096ANS7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   22-NOV-2017, entry version 13.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=HMPREF0872_01670 {ECO:0000313|EMBL:KGF48326.1};
OS   Veillonella montpellierensis DNF00314.
OC   Bacteria; Firmicutes; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=1401067 {ECO:0000313|EMBL:KGF48326.1, ECO:0000313|Proteomes:UP000029628};
RN   [1] {ECO:0000313|EMBL:KGF48326.1, ECO:0000313|Proteomes:UP000029628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DNF00314 {ECO:0000313|EMBL:KGF48326.1,
RC   ECO:0000313|Proteomes:UP000029628};
RA   McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA   Sutton G., Nelson K.E.;
RL   Submitted (JUL-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:KGF48326.1}.
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DR   EMBL; JRNT01000005; KGF48326.1; -; Genomic_DNA.
DR   RefSeq; WP_038151298.1; NZ_JRNT01000005.1.
DR   EnsemblBacteria; KGF48326; KGF48326; HMPREF0872_01670.
DR   Proteomes; UP000029628; 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:KGF48326.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029628};
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:UP000029628};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   442 AA;  48787 MW;  3313DCE5F40BA637 CRC64;
     MKSPISLQDE KVVFDTVQEL LGYVKHCTSP QQTVSHSISI LESNGFVELG LGESWHLTSG
     NYYINVYGTT LIAFHIGTQY RHNLRIASAH TDFPAIRVKP NPLVIVSEYG KLNVEMYGGL
     ILHTWLDRPL GASGTVILKG ENPFDVREVT IDSNRPIAII PSLAIHMNRH VNEGIALQRQ
     KEMLPIIMMK GSTKDSEYDQ WLDFLAGEAQ CNPDDILSFE VTLYPTEDGT TVGLYDEFIS
     APRLDNLTSC KACLSGILEA SENDVNGIRL IALFDNEEVG SCTKQGGASM MLPNVLERIY
     RSLGLAKDEL DMDMAEGFMI SSDVAHGLHP NYPEKNDITN EPILNRGIVL KVAASQSYAN
     DAKSIGIVKS LCEIEDIPYQ YFVNRSDIPG GSTVGSISST MLPMRTMDVG VPIWAMHSAR
     ETMGTLDQYS LESLMRLFIG GN
//
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