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Database: UniProt
Entry: I0XBE1_9SPIO
LinkDB: I0XBE1_9SPIO
Original site: I0XBE1_9SPIO 
ID   I0XBE1_9SPIO            Unreviewed;       449 AA.
AC   I0XBE1;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   07-JUN-2017, entry version 26.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=MSI_03860 {ECO:0000313|EMBL:EID85957.1};
OS   Treponema sp. JC4.
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
OX   NCBI_TaxID=1124982 {ECO:0000313|EMBL:EID85957.1, ECO:0000313|Proteomes:UP000002967};
RN   [1] {ECO:0000313|EMBL:EID85957.1, ECO:0000313|Proteomes:UP000002967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JC4 {ECO:0000313|EMBL:EID85957.1,
RC   ECO:0000313|Proteomes:UP000002967};
RX   PubMed=22815447; DOI=10.1128/JB.00754-12;
RA   Rosewarne C.P., Cheung J.L., Smith W.J., Evans P.N., Tomkins N.W.,
RA   Denman S.E., O Cuiv P., Morrison M.;
RT   "Draft genome sequence of Treponema sp. strain JC4, a novel spirochete
RT   isolated from the bovine rumen.";
RL   J. Bacteriol. 194:4130-4130(2012).
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:EID85957.1}.
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DR   EMBL; AJGU01000002; EID85957.1; -; Genomic_DNA.
DR   RefSeq; WP_009103090.1; NZ_AJGU01000002.1.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; EID85957; EID85957; MSI_03860.
DR   PATRIC; fig|1124982.3.peg.391; -.
DR   OrthoDB; POG091H01QL; -.
DR   BioCyc; TSP1124982:G12ON-383-MONOMER; -.
DR   Proteomes; UP000002967; 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:EID85957.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002967};
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:UP000002967};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   449 AA;  49215 MW;  70E5EE9E06B64AAB CRC64;
     MNEKLIEDYK NFLDKGKTER ECVQEIIKLA QAKGYKDISE FDSLKKGDKV YITKMNKAVA
     LFEIGSGSIE KGMNILGAHI DSPRLDAKQN PLYEKDNITY LNTHYYGGIK KYQWTTLPLA
     IHGVVCKKDG TLVNVVIGED ESDPVFCISD ILPHLAQEQV QKKASEFITG EDLDLIMGAS
     VPVKKDAPKD EKKDAKEKSK KLVLELLKEK YGIEENDFNS AELEIVPAGK ARDLGLDRSM
     ILGYGQDDRS CAFTSLEALL DSQAGERTNC CLCVDKEEIG SVGATGMASN LFENMVSEII
     ARTEKSYSEL TLRRCLANSN MLSSDVNAAY DPMNAGLYDK ENASLLGGGI AFQKFTGSRG
     KSGASDANPE FIAKVRAAMD GVNVSYQMAE LGKVDQGGGG TIAYHAAKYG MNVLDAGVAV
     LSMHAPWEIT HKEDLSQIYE GYKAFLKIN
//
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