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Database: UniProt
Entry: A6DND7_9BACT
LinkDB: A6DND7_9BACT
Original site: A6DND7_9BACT 
ID   A6DND7_9BACT            Unreviewed;       423 AA.
AC   A6DND7;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   07-JUN-2017, entry version 50.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=LNTAR_06554 {ECO:0000313|EMBL:EDM26885.1};
OS   Lentisphaera araneosa HTCC2155.
OC   Bacteria; Lentisphaerae; Lentisphaeria; Lentisphaerales;
OC   Lentisphaeraceae; Lentisphaera.
OX   NCBI_TaxID=313628 {ECO:0000313|EMBL:EDM26885.1, ECO:0000313|Proteomes:UP000004947};
RN   [1] {ECO:0000313|EMBL:EDM26885.1, ECO:0000313|Proteomes:UP000004947}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2155 {ECO:0000313|EMBL:EDM26885.1,
RC   ECO:0000313|Proteomes:UP000004947};
RX   PubMed=20363947; DOI=10.1128/JB.00208-10;
RA   Thrash J.C., Cho J.C., Vergin K.L., Morris R.M., Giovannoni S.J.;
RT   "Genome sequence of Lentisphaera araneosa HTCC2155T, the type species
RT   of the order Lentisphaerales in the phylum Lentisphaerae.";
RL   J. Bacteriol. 192:2938-2939(2010).
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:EDM26885.1}.
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DR   EMBL; ABCK01000013; EDM26885.1; -; Genomic_DNA.
DR   RefSeq; WP_007279376.1; NZ_ABCK01000013.1.
DR   ProteinModelPortal; A6DND7; -.
DR   STRING; 313628.LNTAR_06554; -.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; EDM26885; EDM26885; LNTAR_06554.
DR   eggNOG; ENOG4105DFM; Bacteria.
DR   eggNOG; COG1362; LUCA.
DR   OrthoDB; POG091H01I4; -.
DR   BioCyc; LARA313628:G11I7-2933-MONOMER; -.
DR   Proteomes; UP000004947; 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   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EDM26885.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000004947};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EDM26885.1};
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:UP000004947};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   423 AA;  46893 MW;  2F4A031076D28747 CRC64;
     MRDPQAESLL AYIDASPSPF HAVANTKEQL KAADFTELDE SDEWKLEAGG AYYVERSGGS
     IIAFRLPEIH KEVKFHIVGA HTDSPCFKMK PNAATSVGNY HQWGAETYGG LLKNSWLDRD
     LHLSGRLTLI INGEMVTKLV SLDSYQFRIP QLAIHLDDNR EALKLNAQQH LMPIFGLDKE
     QDLLQIILDE HKIKATSTEV AAFDLFLHDS QKSAFGGLND EFIYAPRLDN LAMCHASLEA
     LIKSKPHSAV SMAALFDHEE VGSVSDRGAC SSFLPAILER ISLSLKGERE AYLAALSRSY
     LLSADMAHAV HPNYAERHDK DHHPLINHGP VIKHNANQRY ATNSETAAYF NLLCQESGIM
     VQEFVSRNDC PCGSTIGPSV ASKLGIKTVD VGNPMLSMHS IREMAGSKDH AKMICVFEEF
     FCK
//
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