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Database: UniProt
Entry: E7N899_9ACTO
LinkDB: E7N899_9ACTO
Original site: E7N899_9ACTO 
ID   E7N899_9ACTO            Unreviewed;       458 AA.
AC   E7N899;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   07-JUN-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=HMPREF9057_01006 {ECO:0000313|EMBL:EFW27598.1};
OS   Actinomyces sp. oral taxon 171 str. F0337.
OC   Bacteria; Actinobacteria; Actinomycetales; Actinomycetaceae;
OC   Actinomyces.
OX   NCBI_TaxID=706439 {ECO:0000313|EMBL:EFW27598.1, ECO:0000313|Proteomes:UP000005722};
RN   [1] {ECO:0000313|EMBL:EFW27598.1, ECO:0000313|Proteomes:UP000005722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0337 {ECO:0000313|EMBL:EFW27598.1,
RC   ECO:0000313|Proteomes:UP000005722};
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-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:EFW27598.1}.
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DR   EMBL; AECW01000134; EFW27598.1; -; Genomic_DNA.
DR   RefSeq; WP_009394979.1; NZ_GL637771.1.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; EFW27598; EFW27598; HMPREF9057_01006.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000005722; 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:EFW27598.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005722};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EFW27598.1};
KW   Protease {ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:EFW27598.1};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   458 AA;  47640 MW;  C30B7999142D40A8 CRC64;
     MTDAASTPAS VPPGRRSGAL AADAVTGETL WDDDAYTDSL IDFVTASPSS YHAATEVARR
     LDAAGFTRAD ETVSWEGGLP RRGYVIRDGA IAAWALPEAL PAGAGMRIVG AHTDSPALKL
     KPSAAVVRSG WQLINAEVYG GPLLASFLDR ELGLAGRLTS RDGAVHLVRT GPIARVCQIA
     PHLDRAVNDT LHLDRQTHLL PLWSLAGPDA APDAVEAHLC EIAGIDAAEL AGHDVLTYPT
     QAPARFGRDG EFLASSRLDN LSSVHAGLAA LETLAVVGAE PIEPVILVAF DHEEVGSDTR
     SGAGGPFLET LLRRLAAALG IKGDAVDALL ARSTCVSADA GHSVHPAYAH LHDPVVQPLI
     NHGPLLKINA QQRYATDAVG AAIWARACAA AGVPSQEFVS NNAVPCGSTI GPITATRLGI
     TTVDVGVPLL SMHSAREMCG VKDGPWLAQA LHAYWQGA
//
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