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Database: UniProt
Entry: F5YE89_TREAZ
LinkDB: F5YE89_TREAZ
Original site: F5YE89_TREAZ 
ID   F5YE89_TREAZ            Unreviewed;       486 AA.
AC   F5YE89;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   05-JUL-2017, entry version 31.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=TREAZ_0238 {ECO:0000313|EMBL:AEF81505.1};
OS   Treponema azotonutricium (strain ATCC BAA-888 / DSM 13862 / ZAS-9).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
OX   NCBI_TaxID=545695 {ECO:0000313|EMBL:AEF81505.1, ECO:0000313|Proteomes:UP000009222};
RN   [1] {ECO:0000313|Proteomes:UP000009222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-888 / DSM 13862 / ZAS-9
RC   {ECO:0000313|Proteomes:UP000009222};
RA   Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA   Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X.,
RA   Lucey K., Ballor N.R., Ottesen E., Rosenthal R., Allen A.,
RA   Leadbetter J.R., Paulsen I.T.;
RT   "Complete sequence of Treponema azotonutricium strain ZAS-9.";
RL   Submitted (DEC-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}.
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DR   EMBL; CP001841; AEF81505.1; -; Genomic_DNA.
DR   STRING; 545695.TREAZ_0238; -.
DR   MEROPS; M18.004; -.
DR   EnsemblBacteria; AEF81505; AEF81505; TREAZ_0238.
DR   KEGG; taz:TREAZ_0238; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   OMA; YQWVTIP; -.
DR   OrthoDB; POG091H01QL; -.
DR   BioCyc; TAZO545695:GHPL-2028-MONOMER; -.
DR   Proteomes; UP000009222; Chromosome.
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:AEF81505.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000009222};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:AEF81505.1};
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:UP000009222};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   486 AA;  53285 MW;  5B6347F9ECCA285E CRC64;
     MKYPENEENE ENMPAKSADE KKTPGQKLAE KLFFNPKNCW EGVDEKIEKA IEVFARSYKE
     MLNKGKTERE FTSAAIDLLQ KKGFMDIDSA SAKKFSPGAK VYRSIKGKAL VAAVLGKRPL
     KEGLNILGAH VDSPRIDLKP SPLYEDTDFA FLDTHYYGGI KKYQWTAIPL AMHGVFIDSK
     GKTINVRLGE DEDDPVFTIT DLLPHLAREQ MQKKASEAVE GEDLDILVGS KPFKDEKVKE
     KVKLAILSIL NEQYGIDEQS FAGAEIELVP AFKARDLGLD RSMIGAYGHD DRCCAYPALR
     ALMDFASETP EKTAVCYLSD KEEIGSMGNT GAQSRGFENF VAALSGEGDL RSCLANSAML
     SADVNAAYDP AYAGVFDKKN SSFMGKGLIL SKYTGSGGKY GASDANAEFC SKVQALMNKN
     KIPWQFGELG KVDKGGGGTI ALHAAKLGME VLDCGIPVLS MHSPFEVISK VDLYYCYKGY
     VAFLKD
//
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