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Database: UniProt
Entry: W6N2Z7_CLOTY
LinkDB: W6N2Z7_CLOTY
Original site: W6N2Z7_CLOTY 
ID   W6N2Z7_CLOTY            Unreviewed;       466 AA.
AC   W6N2Z7;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   22-NOV-2017, entry version 18.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=CTDIVETGP_0858 {ECO:0000313|EMBL:CDL90788.1};
OS   Clostridium tyrobutyricum DIVETGP.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1408889 {ECO:0000313|EMBL:CDL90788.1, ECO:0000313|Proteomes:UP000019482};
RN   [1] {ECO:0000313|EMBL:CDL90788.1, ECO:0000313|Proteomes:UP000019482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DIVETGP {ECO:0000313|EMBL:CDL90788.1,
RC   ECO:0000313|Proteomes:UP000019482};
RA   Soggiu A., Piras C., Gaiarsa S., Sassera D., Roncada P., Bendixen E.,
RA   Brasca M., Bonizzi L.;
RT   "Draft Genome Sequence of Clostridium tyrobutyricum Strain DIVETGP,
RT   Isolated from Cow's Milk for Grana Padano Production.";
RL   Genome Announc. 3:213-215(2015).
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:CDL90788.1}.
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DR   EMBL; CBXI010000010; CDL90788.1; -; Genomic_DNA.
DR   RefSeq; WP_017895430.1; NZ_CBXI010000010.1.
DR   EnsemblBacteria; CDL90788; CDL90788; CTDIVETGP_0858.
DR   Proteomes; UP000019482; 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   PANTHER; PTHR28570; PTHR28570; 1.
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:CDL90788.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000019482};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:CDL90788.1};
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:UP000019482};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   466 AA;  52167 MW;  D7E22AB011553A8B CRC64;
     MAKDLQKKYD YAWDKYSKDD FKALFKISDE YKAFMSKCKT ERECTREFIK RAEVKGYKNI
     EELIKSNTKL NPGDKVYANN KDKTLALFVI GSKDIQEGMR ILGAHIDSPR LDLKQNPLYE
     DTDLALFDTH YYGGIKKYQW VTLPLAIHGI VIKKDGTKVD IVIGEDEDDP VVGISDLLIH
     LSADQMAKKA AKVIEGEDLN ILVGSIPVKD KDVKNRVKQN ILKILNKKYS IEEEDFVSAE
     IEVVPAGKAR DYGIDKSMVM AYGHDDKICA YTSFDAMMKI KNPDKTCVTL LVDKEEIGSV
     GATGMQSRFF ENTVAELIDL IGDYSDLKLR RALTNSKMLS SDVSAAFDPN YPSVMEKNNA
     AYFGKGVVFN KYTGARGKSG CNDANPEFIA EIRKVMDDNN VSWQTSELGK VDQGGGGTIA
     YILAEYNMQV IDCGIALHNM HAPWEVASKA DIYEAVKGYK AFLNEI
//
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