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Database: UniProt
Entry: E2SNI9_9FIRM
LinkDB: E2SNI9_9FIRM
Original site: E2SNI9_9FIRM 
ID   E2SNI9_9FIRM            Unreviewed;       458 AA.
AC   E2SNI9;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   22-NOV-2017, entry version 29.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=HMPREF0983_02710 {ECO:0000313|EMBL:EFP60900.1};
OS   Erysipelotrichaceae bacterium 3_1_53.
OC   Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae.
OX   NCBI_TaxID=658659 {ECO:0000313|EMBL:EFP60900.1, ECO:0000313|Proteomes:UP000006223};
RN   [1] {ECO:0000313|EMBL:EFP60900.1, ECO:0000313|Proteomes:UP000006223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3_1_53 {ECO:0000313|EMBL:EFP60900.1,
RC   ECO:0000313|Proteomes:UP000006223};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Young S.K., Pearson M., Zeng Q.,
RA   Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z.,
RA   Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heilman E., Heiman D., Howarth C., Jen D., Larson L., Mehta T.,
RA   Neiman D., Park D., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA   Allen-Vercoe E., Strauss J., Sibley C., Daigneault M., Haas B.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Erysipelotrichaceae bacterium strain 3_1_53.";
RL   Submitted (JUL-2010) 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:EFP60900.1}.
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DR   EMBL; ACTJ01000063; EFP60900.1; -; Genomic_DNA.
DR   STRING; 658659.HMPREF0983_02710; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; EFP60900; EFP60900; HMPREF0983_02710.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   Proteomes; UP000006223; 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:EFP60900.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006223};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EFP60900.1};
KW   Protease {ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:EFP60900.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006223};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   458 AA;  50884 MW;  C1AC953D807321E0 CRC64;
     MRENAWKKYD EAGLKEVFDY CEGYKKYISD CKTERECVSE SIRIAQAYGY RNLEDVIRNK
     ETLKSGDKVY ANNMGKGLAL FLIGEEPMSN GFNILGAHVD SPRLDIKQNP LYEDKEFAML
     DTHYYGGIKK YQWVTLPLAL HGVVVKKDGT MITLNIGEDD NDPIVGISDL LVHLSADQMS
     KKASNVIEGE DLNVTLGSMP LNGEEKDAVK ANILKLLKET YDFEEDDFVS AEIEVVPAGK
     ARDYGLDRSM IAGYGHDDRI CAYTSMMAQL ETEAVKRTAV TLLVDKEEVG SIGATGQHSR
     FFENTVAEVM DRMGEYSELN VRRALKNSKM LSSDVSAAFD PNYAAVNEEK NSAFMGHGLV
     FNKYTGSRGK GGCNDANAEY MAELRNIMDS ENVTFQTAEL GKVDQGGGGT IAYILAQYNM
     EVIDSGIALH NMHAPWEIAS KIDIWEATKG YKAFLKHA
//
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