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Database: UniProt
Entry: K6T208_9CLOT
LinkDB: K6T208_9CLOT
Original site: K6T208_9CLOT 
ID   K6T208_9CLOT            Unreviewed;       465 AA.
AC   K6T208;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   22-NOV-2017, entry version 23.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=A370_03876 {ECO:0000313|EMBL:EKQ53188.1};
OS   Clostridium sp. Maddingley MBC34-26.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1196322 {ECO:0000313|EMBL:EKQ53188.1, ECO:0000313|Proteomes:UP000001325};
RN   [1] {ECO:0000313|EMBL:EKQ53188.1, ECO:0000313|Proteomes:UP000001325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Maddingley MBC34-26 {ECO:0000313|Proteomes:UP000001325};
RX   PubMed=23405323;
RA   Rosewarne C.P., Greenfield P., Li D., Tran-Dinh N., Bradbury M.I.,
RA   Midgley D.J., Hendry P.;
RT   "Draft Genome Sequence of Clostridium sp. Maddingley, Isolated from
RT   Coal-Seam Gas Formation Water.";
RL   Genome Announc. 1:E00081-12(2013).
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:EKQ53188.1}.
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DR   EMBL; ALXI01000117; EKQ53188.1; -; Genomic_DNA.
DR   MEROPS; M18.004; -.
DR   PATRIC; fig|1196322.3.peg.3788; -.
DR   Proteomes; UP000001325; 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:EKQ53188.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001325};
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:UP000001325};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   465 AA;  51765 MW;  006EE68FDF43FC1B CRC64;
     MKNEKKDLSK NAWNKYNDKQ VKEIFDFCEG YKNFMSKCKT ERECVKEVIS LAEAQGYKDL
     YEIIKSKKKL KPGDKVYANN KGKAIALFIV GKEPMENGLK ILGAHIDSPR LDLKQNPLYE
     DSELVLLDTH YYGGIKKYQW VTLPLALHGV VAKKDGTVID ICIGEDENDP VVGVSDLLIH
     LAGDQMGKKA DKVVEGEDLN VLVGSMPLKG SEKDAVKANI LKLLKDKYDF EEEDFLSAEI
     EVVPAGKARD YGLDRSMVMA YGHDDRVCSY TSLMAMFEIK ETDKTCCCLL VDKEEVGSIG
     ATGMHSRFFE NIVSEIIDKI DGYTELKFRR CLTNSKMLSS DVSAAYDPNY PSVMEKKNAA
     FFGKGMVFNK YTGARGKAGS NDASAEYMAE LRSIMEKHDV SIQTAELGKV DAGGGGTIAY
     ILAQYNMEVI DCGVALHNMH APWEVASKVD IYETMKGYKA FLIEA
//
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