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Database: UniProt
Entry: A0A0Q9R8F8_9MICC
LinkDB: A0A0Q9R8F8_9MICC
Original site: A0A0Q9R8F8_9MICC 
ID   A0A0Q9R8F8_9MICC        Unreviewed;       426 AA.
AC   A0A0Q9R8F8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   25-OCT-2017, entry version 9.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=ASH00_04755 {ECO:0000313|EMBL:KRF08988.1};
OS   Arthrobacter sp. Soil782.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=1736410 {ECO:0000313|EMBL:KRF08988.1, ECO:0000313|Proteomes:UP000053496};
RN   [1] {ECO:0000313|EMBL:KRF08988.1, ECO:0000313|Proteomes:UP000053496}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil782 {ECO:0000313|EMBL:KRF08988.1,
RC   ECO:0000313|Proteomes:UP000053496};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRF08988.1, ECO:0000313|Proteomes:UP000053496}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil782 {ECO:0000313|EMBL:KRF08988.1,
RC   ECO:0000313|Proteomes:UP000053496};
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:KRF08988.1}.
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DR   EMBL; LMSO01000001; KRF08988.1; -; Genomic_DNA.
DR   RefSeq; WP_056545512.1; NZ_LMSO01000001.1.
DR   EnsemblBacteria; KRF08988; KRF08988; ASH00_04755.
DR   Proteomes; UP000053496; 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   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:KRF08988.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053496};
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:UP000053496};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   426 AA;  45286 MW;  2353C7823BBC03D2 CRC64;
     MTAAHAHIAD LGAYVAASPS SFHAAHEGAI RLQAAGFSQL HEDDPWDGGP GRFYVIRDGA
     LIAWIAPSTA TETTGFHILG AHTDSPSFKL KPKPTIGRHG WLQAGVEIYG GPLLNSWLDR
     ELALAGRLVT HDGAEHLVHT GPLLRFPQLA IHLDRAVNDG LKLDKQQHMN PVWGLGDPGR
     ADLLQLLAVD ADLEAAEIGG FDVVVADTQQ PRVFGADGEF FASGRLDNLS SVHAGITALI
     QATKNDAGGA PIAVLAAFDH EEVGSGSRSG ASGPFLEDIL HRISTGLGAG AEQRRRAFAS
     SFCVSSDAGH AVHPNYAERH DPANHPVLNG GPLLKINANQ RYTTDAPGAA YWARLCRDAG
     APYQEFVSNN VMPCGSTIGP LTATRLGIRT VDVGVPLLSM HSARELCGVE DPYQLTRVMQ
     RFFTVS
//
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