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Database: UniProt
Entry: D9R8L8_CLOSW
LinkDB: D9R8L8_CLOSW
Original site: D9R8L8_CLOSW 
ID   D9R8L8_CLOSW            Unreviewed;       428 AA.
AC   D9R8L8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   07-JUN-2017, entry version 45.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   OrderedLocusNames=Closa_3217 {ECO:0000313|EMBL:ADL05747.1};
OS   Clostridium saccharolyticum (strain ATCC 35040 / DSM 2544 / NRCC 2533
OS   / WM1).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae.
OX   NCBI_TaxID=610130 {ECO:0000313|EMBL:ADL05747.1, ECO:0000313|Proteomes:UP000001662};
RN   [1] {ECO:0000313|EMBL:ADL05747.1, ECO:0000313|Proteomes:UP000001662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35040 / DSM 2544 / NRCC 2533 / WM1
RC   {ECO:0000313|Proteomes:UP000001662};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA   Mikhailova N., Mouttaki H., Lin L., Zhou J., Hemme C.L., Woyke T.;
RT   "Complete sequence of Clostridium saccharolyticum WM1.";
RL   Submitted (JUL-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}.
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DR   EMBL; CP002109; ADL05747.1; -; Genomic_DNA.
DR   RefSeq; WP_013273817.1; NC_014376.1.
DR   ProteinModelPortal; D9R8L8; -.
DR   STRING; 610130.Closa_3217; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; ADL05747; ADL05747; Closa_3217.
DR   KEGG; csh:Closa_3217; -.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   HOGENOM; HOG000253244; -.
DR   KO; K01267; -.
DR   OMA; CFDHEEI; -.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000001662; 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:ADL05747.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001662};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ADL05747.1};
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:UP000001662};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   428 AA;  46502 MW;  02DF3393F5572343 CRC64;
     MNHMEQLETL IAASVSPYHC IMAAADQLLS AGFQELPLAE PWELTRGGSY YINVFDSTLI
     AFSVGEVLDV IPTLKLAASH TDWPCLKVKP SPEVTSLEYG KLNVEVYGGP LLGTWFDRPL
     SMAGKVCVAG PSPMMPETIL VDFSRPLLTV PNLAIHMNRD ANDGVAINPQ VDMLPLIARI
     TDELSKEDFF LEALAKEAGV KKEDILDYEI CIYNWEKGTL LGLQNEFYSA PRLDNLTSVQ
     ACLNGITAGP CKNGLHVIAL YDNEEIGSHT KQGAASALME RILEKICLSL GYSRETFLNI
     LMNGFLLSLD VAHAIHPNHG EKCDIKNQIL MGDGVAIKLA SSQAYATDAS STGVIEGICR
     KNHIPYKKFS NRSDVKGGST LGSISSALLT MRTVDAGVPI LAMHSAREVM GAKDQEALVK
     LTEAFFQA
//
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