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Database: UniProt
Entry: G9YHU8_9FIRM
LinkDB: G9YHU8_9FIRM
Original site: G9YHU8_9FIRM 
ID   G9YHU8_9FIRM            Unreviewed;       425 AA.
AC   G9YHU8;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   07-JUN-2017, entry version 28.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=HMPREF0080_01232 {ECO:0000313|EMBL:EHM40378.1};
OS   Anaeroglobus geminatus F0357.
OC   Bacteria; Firmicutes; Negativicutes; Veillonellales; Veillonellaceae;
OC   Anaeroglobus.
OX   NCBI_TaxID=861450 {ECO:0000313|EMBL:EHM40378.1, ECO:0000313|Proteomes:UP000005481};
RN   [1] {ECO:0000313|EMBL:EHM40378.1, ECO:0000313|Proteomes:UP000005481}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0357 {ECO:0000313|EMBL:EHM40378.1,
RC   ECO:0000313|Proteomes:UP000005481};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B.,
RA   Courtney L., Fronick C., Harrison M., Strong C., Farmer C.,
RA   Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C.,
RA   Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (AUG-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:EHM40378.1}.
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DR   EMBL; AGCJ01000046; EHM40378.1; -; Genomic_DNA.
DR   RefSeq; WP_006790208.1; NZ_JH417588.1.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; EHM40378; EHM40378; HMPREF0080_01232.
DR   PATRIC; fig|861450.3.peg.1147; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000005481; 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:EHM40378.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005481};
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:UP000005481};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   425 AA;  46454 MW;  31C2129089331B16 CRC64;
     MNIYQENLIT LIKAGTSPFH VVREGKKRLE KHGFTCLESR EKWSLQRGGK YYLSCYDTTL
     IAFTVGENPA ESLRLAAAHT DFPCLRVKPS PETADKGYGR INIEPYGSII RHTWLDTPLS
     LAGKVVLKGA APFAPETVYI DPKKALFIIP EAAIHMNRDV NESASFNMQK EMLPLMTLTG
     EDTASTYFIN YLASLCEAES DDVLAYDLNL YPLSEAVFMG LHDEFIAAPR LDNLTSVSAC
     LSGITEADTA GIRMALFFDN EEVGSTTKQG AASMIIPDLL KRIYENLGFD REEYSRQCAG
     AFLLSMDAAH AYHPNYPEKN DITNFPLLNG GVVLKQAANQ TYAGDAEAVA AIKGLADSLG
     IKRQSFVNRS DMRGGSTLGS LLSANVPVRT ADIGIPLLSM HSSFETMGAD DQECLTGLAT
     AFLSR
//
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