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Database: UniProt
Entry: C4ZEZ6_AGARV
LinkDB: C4ZEZ6_AGARV
Original site: C4ZEZ6_AGARV 
ID   C4ZEZ6_AGARV            Unreviewed;       428 AA.
AC   C4ZEZ6;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-SEP-2017, entry version 51.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=EUBREC_2386 {ECO:0000313|EMBL:ACR76117.1};
OS   Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 /
OS   KCTC 5835 / VPI 0990) (Eubacterium rectale).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae.
OX   NCBI_TaxID=515619 {ECO:0000313|EMBL:ACR76117.1, ECO:0000313|Proteomes:UP000001477};
RN   [1] {ECO:0000313|EMBL:ACR76117.1, ECO:0000313|Proteomes:UP000001477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / VPI 0990
RC   {ECO:0000313|Proteomes:UP000001477};
RX   PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA   Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA   Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA   Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA   Hettich R.L., Gordon J.I.;
RT   "Characterizing a model human gut microbiota composed of members of
RT   its two dominant bacterial phyla.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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; CP001107; ACR76117.1; -; Genomic_DNA.
DR   RefSeq; WP_012743211.1; NC_012781.1.
DR   ProteinModelPortal; C4ZEZ6; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; ACR76117; ACR76117; EUBREC_2386.
DR   KEGG; ere:EUBREC_2386; -.
DR   HOGENOM; HOG000253244; -.
DR   KO; K01267; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000001477; 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:ACR76117.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001477};
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:UP000001477};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   428 AA;  47713 MW;  8574A6829C7C96BF CRC64;
     MKQEKLFDLL KAAVSPCECV KAAKQELLEN GFEEIDYTGD WKLVRGGRYV LNHHDTTMFA
     FTVGSGYNKK DMVRIAAAHT DYPYLRIKPN PDFMTNSYAQ VNVEVYGGPI LNTWFDRPLG
     VAGRVAIKSE DVFNPRMVLY RSKKPVMIIP NLAIHMNRDV NKGVGINNQV DLMPVLDSIT
     EDEMTTDYFL SFLARELSVE KSDIIDFELN TFCMEEPCFV GVNDTMISSP RIDNQSSCRA
     LLDAIEDGNR ADGINIIALF DHEEIGSNSK QGAASIMLHD MLRRILRNMD LSENEIDESI
     YDAMLLSVDV AHALHPNKKE KMDITNMPVM GKGFCIKQAC SQSYATDAQA IAILCQLCDE
     KGIPYQRFVN RSDSRGGSTL GSIAGTLLPV KTVDIGIPIL AMHSACELMG VRDMKALSDC
     VTAFFGYH
//
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