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Database: UniProt
Entry: C9N0B3_9FUSO
LinkDB: C9N0B3_9FUSO
Original site: C9N0B3_9FUSO 
ID   C9N0B3_9FUSO            Unreviewed;       457 AA.
AC   C9N0B3;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   25-OCT-2017, entry version 36.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=GCWU000323_02269 {ECO:0000313|EMBL:EEX73600.1};
OS   Leptotrichia hofstadii F0254.
OC   Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae;
OC   Leptotrichia.
OX   NCBI_TaxID=634994 {ECO:0000313|EMBL:EEX73600.1, ECO:0000313|Proteomes:UP000006233};
RN   [1] {ECO:0000313|EMBL:EEX73600.1, ECO:0000313|Proteomes:UP000006233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0254 {ECO:0000313|EMBL:EEX73600.1,
RC   ECO:0000313|Proteomes:UP000006233};
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., Nelson J., Hou S., Wollam A., Pepin K.H., Johnson M.,
RA   Bhonagiri V., Nash W.E., Warren W., Chinwalla A., Mardis E.R.,
RA   Wilson R.K.;
RL   Submitted (SEP-2009) 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:EEX73600.1}.
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DR   EMBL; ACVB02000026; EEX73600.1; -; Genomic_DNA.
DR   RefSeq; WP_006805571.1; NZ_GG700633.1.
DR   ProteinModelPortal; C9N0B3; -.
DR   STRING; 634994.GCWU000323_02269; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; EEX73600; EEX73600; GCWU000323_02269.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   OrthoDB; POG091H01QL; -.
DR   Proteomes; UP000006233; 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   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:EEX73600.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006233};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EEX73600.1};
KW   Protease {ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:EEX73600.1};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   457 AA;  51832 MW;  DEE15B88CB752D94 CRC64;
     MTKENLWKNY TDEQKKVIFD FAEDYKKYLD SAKTEREFVD LTEKELKKNG FVNINEKSEL
     KKGDKIYFNN RNKNIIAVIV GNDIKSGINM IVSHVDSPRL DLKPNPIMEE EEFALLNTHY
     YGGIKKYQWA ATPLALHGVV FLKNGEKVTL SIGENYDEPV FSMPDILPHL SYNVQDERKA
     RDVIKGEELK LLFGNMPLND ENVNKKIKQF VLDKLKKDYG IEEDDFFTAE LEVVPAGKLR
     DVGLDKSMIG GYGQDDRICA YTSLRALFDI KKTEKTVMIY LTDKEEIGSE GSTSLKSTLP
     EYVVGKMLSL TEKNYNDQIL RETLWNSKAL SSDVTAALNP VFKSVHDVEN AARLSYGLAF
     AKYTGSRGKV MANDADAEFI QEIRQIFDKN EIKYQSGGFG KVDEGGGGTV AKFLAYYGIR
     TVDAGPALLS MHSLFEISSK ADLYETYRAY KVFFELD
//
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