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Database: UniProt
Entry: F9N6S6_9FIRM
LinkDB: F9N6S6_9FIRM
Original site: F9N6S6_9FIRM 
ID   F9N6S6_9FIRM            Unreviewed;       468 AA.
AC   F9N6S6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   22-NOV-2017, entry version 25.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=HMPREF9200_0455 {ECO:0000313|EMBL:EGS33363.1};
OS   Veillonella sp. oral taxon 780 str. F0422.
OC   Bacteria; Firmicutes; Negativicutes; Veillonellales; Veillonellaceae;
OC   Veillonella.
OX   NCBI_TaxID=944564 {ECO:0000313|EMBL:EGS33363.1, ECO:0000313|Proteomes:UP000010295};
RN   [1] {ECO:0000313|EMBL:EGS33363.1, ECO:0000313|Proteomes:UP000010295}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0422 {ECO:0000313|EMBL:EGS33363.1,
RC   ECO:0000313|Proteomes:UP000010295};
RA   Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B.,
RA   Sutton G.G., Nelson K.E.;
RL   Submitted (JUN-2011) 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:EGS33363.1}.
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DR   EMBL; AFUJ01000055; EGS33363.1; -; Genomic_DNA.
DR   STRING; 944564.HMPREF9200_0455; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; EGS33363; EGS33363; HMPREF9200_0455.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   OrthoDB; POG091H01QL; -.
DR   BioCyc; VSP944564-HMP:GTWA-428-MONOMER; -.
DR   Proteomes; UP000010295; 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:EGS33363.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010295};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EGS33363.1};
KW   Protease {ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:EGS33363.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010295};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   468 AA;  51868 MW;  A01E9E2CECEA63FD CRC64;
     MKRKELSMER RNAWHEYTEE QLQEIDTLAT KYRHFLDHGK TERECVDQIV EAAEAAGYRN
     MDSVIKEGAT LKAGDKVYYV HMKKAVAMVN IGTEPIEQGM NILGAHIDSP RLDVKQNPFY
     VDSDLALLDT HYYGGIKKYQ WVTMPLAIHG VVVKRDGTVI NLAIGENPTD PVFCVTDLLP
     HLGQEQMEKK AAKVVEGEQL DLLIGSRPVK GELKDGVKAY VLQVLQEQYD FEEEDFLSAE
     LEIVPAGAAR ELGFDRSMII GYGQDDRVCA YTSLVAMLET ENVSRTTCTL LVDKEEIGSV
     GATGMQSRFF ENFMAEVLEA MGHTSPLAVR RTLSNSHMLS SDVSAGFDPL YASAFEKKNA
     AFLGRGVVFN KFTGSRGKSG SNDANAEYMA RIRHLMDQDN ISYQTAELGR VDLGGGGTIA
     YIMALYGMDV IDCGVAVLSM HSPWEVTSKA DIYEAKRCYL AFLAAKGE
//
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