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Database: UniProt
Entry: A0A0D2J5J0_9DELT
LinkDB: A0A0D2J5J0_9DELT
Original site: A0A0D2J5J0_9DELT 
ID   A0A0D2J5J0_9DELT        Unreviewed;       471 AA.
AC   A0A0D2J5J0;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   22-NOV-2017, entry version 11.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=X474_14420 {ECO:0000313|EMBL:KIX13384.1};
OS   Dethiosulfatarculus sandiegensis.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfarculales;
OC   Desulfarculaceae; Dethiosulfatarculus.
OX   NCBI_TaxID=1429043 {ECO:0000313|EMBL:KIX13384.1, ECO:0000313|Proteomes:UP000032233};
RN   [1] {ECO:0000313|EMBL:KIX13384.1, ECO:0000313|Proteomes:UP000032233}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SPR {ECO:0000313|EMBL:KIX13384.1,
RC   ECO:0000313|Proteomes:UP000032233};
RA   Davidova I.A., Callaghan A.V., Wawrik B., Pruitt S., Marks C.,
RA   Duncan K.E., Suflita J.M.;
RT   "Metagenomic analysis of a methanogenic consortium involved in long
RT   chain n-alkane degradation.";
RL   Submitted (NOV-2013) 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}.
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:KIX13384.1}.
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DR   EMBL; AZAC01000016; KIX13384.1; -; Genomic_DNA.
DR   EnsemblBacteria; KIX13384; KIX13384; X474_14420.
DR   PATRIC; fig|1429043.3.peg.3056; -.
DR   Proteomes; UP000032233; 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:KIX13384.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000032233};
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:UP000032233};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   471 AA;  51885 MW;  4F14A72E3AD6BFDA CRC64;
     MTEKQVEDLS QKLALESKSV WEEADQEARK EIFALADRYM EFLDKAKTER MAVQTIRELA
     EKNGFAPLDA KKNAKGYFAA YHEKVIFLFR PGKKPVSQGL RILGAHLDSP RLDLKGKPLY
     EDQDLAFLKT HYYGGIKKYH WLSRPLALHG VVCLENGETV EIHIGEDRDD PVFTVLDVLP
     HLSRNAQGKK KVADAFEAER MNILIGGLPL DAEKGKEKVK LAVLQLLHEK YGIKEEDFTS
     AELEAVPVGR ARHVGLDRSL IGGYGHDDRC CAYAALEAIF AATEPEVGSL VLLVDKEEIG
     SEGATGAQSL FLELFLAELL EKTGEKAEYL NVTKALTTSR AISGDVSGGF DPDYPEVHEK
     RNAAFLGKGI TLTKYTGSGG KYSASDANAE YVAWIRGVWN QAEVVWQAAG MGKIDEGGGG
     TIAKFLAKRG MEIVDAGPAL LAMHAPFEIM HKSDLYSTYQ AYKAFLEAKA K
//
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