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Database: UniProt
Entry: W2BVS7_9FIRM
LinkDB: W2BVS7_9FIRM
Original site: W2BVS7_9FIRM 
ID   W2BVS7_9FIRM            Unreviewed;       469 AA.
AC   W2BVS7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   22-NOV-2017, entry version 16.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=HMPREF0378_0420 {ECO:0000313|EMBL:ETJ98937.1};
OS   Eubacterium nodatum ATCC 33099.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Clostridiales Family XIII. Incertae Sedis.
OX   NCBI_TaxID=1161902 {ECO:0000313|EMBL:ETJ98937.1, ECO:0000313|Proteomes:UP000018868};
RN   [1] {ECO:0000313|EMBL:ETJ98937.1, ECO:0000313|Proteomes:UP000018868}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33099 {ECO:0000313|EMBL:ETJ98937.1,
RC   ECO:0000313|Proteomes:UP000018868};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M.,
RA   Haft D.H., Methe B., Sutton G., Nelson K.E.;
RL   Submitted (DEC-2013) 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:ETJ98937.1}.
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DR   EMBL; AZKM01000028; ETJ98937.1; -; Genomic_DNA.
DR   RefSeq; WP_051404120.1; NZ_AZKM01000028.1.
DR   EnsemblBacteria; ETJ98937; ETJ98937; HMPREF0378_0420.
DR   PATRIC; fig|1161902.3.peg.1579; -.
DR   OrthoDB; POG091H01QL; -.
DR   Proteomes; UP000018868; 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:ETJ98937.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018868};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ETJ98937.1};
KW   Protease {ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:ETJ98937.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018868};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   469 AA;  51855 MW;  4CA17DFEAA458033 CRC64;
     MQNTNTWEKY SEVQLKDCEK FCKGYMDFLS TCKTERECVS KIVSDIEEAG YLPLDEKIKK
     HVKLKAGDKV YAVNMDKAVV MFNIGEESIE NGLNILGAHI DSPRMDVKQN PLYEEGGFAY
     LDTHYYGGIK KYQWVAMPLA LHGVVIKKNG DRVNISIGES TDDPVFFVSD LLIHLAQEQM
     DKKAAKVIEG EALDIIVGNK PILIKEEEVK DKDKDKVKQA ILEILCKNYD FDEGDFVSAE
     LEVVPAGAAR EAGLDRSMIL SYGQDDRVCS YTSYKAMLEV PRVNRTACCI LVDKEEIGSV
     GATGMQSKFF ENTVAEVIGL MGEYSELTLK RALAASTMLS SDVSSAYDPT YKSSFDSKNV
     AFLGNGMVFN KFTGARGKSG SNDANAEYLA HLREILDSEN VNFQTAELGR VDLGGGGTIA
     YILALYGMNV IDSGVAVLNM HAPWEATSKA DVYETKRGYV AFLKKAKRV
//
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