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Database: UniProt
Entry: A0A0Q5E8G1_9MICO
LinkDB: A0A0Q5E8G1_9MICO
Original site: A0A0Q5E8G1_9MICO 
ID   A0A0Q5E8G1_9MICO        Unreviewed;       427 AA.
AC   A0A0Q5E8G1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   07-JUN-2017, entry version 8.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=ASF68_11380 {ECO:0000313|EMBL:KQQ52859.1};
OS   Plantibacter sp. Leaf314.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Plantibacter.
OX   NCBI_TaxID=1736333 {ECO:0000313|EMBL:KQQ52859.1, ECO:0000313|Proteomes:UP000051200};
RN   [1] {ECO:0000313|EMBL:KQQ52859.1, ECO:0000313|Proteomes:UP000051200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ52859.1,
RC   ECO:0000313|Proteomes:UP000051200};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ52859.1, ECO:0000313|Proteomes:UP000051200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ52859.1,
RC   ECO:0000313|Proteomes:UP000051200};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQQ52859.1}.
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DR   EMBL; LMOB01000001; KQQ52859.1; -; Genomic_DNA.
DR   RefSeq; WP_056010283.1; NZ_LMOB01000001.1.
DR   EnsemblBacteria; KQQ52859; KQQ52859; ASF68_11380.
DR   Proteomes; UP000051200; 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:KQQ52859.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000051200};
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:UP000051200};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   427 AA;  44908 MW;  455C37C9BB6A0469 CRC64;
     MDSVAHITDL ADFIVASPTS YHAVAESARR LEAARFTRLL ETESWDGGGG RFFVEREGAI
     IAWVQPEGAT PTTPFRILGS HTDSPSFKLK PKPTIGAHGW LQAGVEVYGG PLLNSWLDRE
     LELAGRLVTL DGTVHLVRTG PFLRIPQLAV HLDRAVNDGL VLDRQHHLQP VYGVGELAHA
     DVLAHLAKIA GIDPTAIAGY DVLVADTQEP RRFGLDGQLF AAGRMDNLTS VHAGLAALLA
     AGDGGATDEA DHISVFAAFD HEELGSSSTS GASGPFLDDV LTRIGAGLGA TTAERLQAYA
     GSWCLSADAG HAIHPNYPER HDPTNRPIAG GGPLLKINAN QRYATDALGA ALWARSCAAA
     GVTSQDFVSN NTVPCGSTIG PLTATRLGIR TVDVGTPLLS MHSARELCHI DDPAALSAAV
     QAFFRGA
//
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