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Database: UniProt
Entry: A0A0Q9NJX5_9MICC
LinkDB: A0A0Q9NJX5_9MICC
Original site: A0A0Q9NJX5_9MICC 
ID   A0A0Q9NJX5_9MICC        Unreviewed;       441 AA.
AC   A0A0Q9NJX5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   22-NOV-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=ASG77_19060 {ECO:0000313|EMBL:KRE76741.1};
OS   Arthrobacter sp. Soil762.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=1736401 {ECO:0000313|EMBL:KRE76741.1, ECO:0000313|Proteomes:UP000051715};
RN   [1] {ECO:0000313|EMBL:KRE76741.1, ECO:0000313|Proteomes:UP000051715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil762 {ECO:0000313|EMBL:KRE76741.1,
RC   ECO:0000313|Proteomes:UP000051715};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE76741.1, ECO:0000313|Proteomes:UP000051715}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil762 {ECO:0000313|EMBL:KRE76741.1,
RC   ECO:0000313|Proteomes:UP000051715};
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:KRE76741.1}.
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DR   EMBL; LMSG01000005; KRE76741.1; -; Genomic_DNA.
DR   RefSeq; WP_056342671.1; NZ_LMSG01000005.1.
DR   EnsemblBacteria; KRE76741; KRE76741; ASG77_19060.
DR   Proteomes; UP000051715; 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:KRE76741.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000051715};
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:UP000051715};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   441 AA;  46002 MW;  F08EB356DAA89E3D CRC64;
     MPSRTSAAAS SAVDHIQDLG AYVSASPSSF HAVHEAARRL DKAGFTGLDE RESWAGGAGS
     FYLVRDGALI AWVVPENAGP TTGFNILGAH TDSPSFKLKP KPTTGAFGWL QAGVEVYGGP
     LLNSWLDREL RLAGRLVLLD GTEHLTATGP LLRFPQLAVH LDRAVNDGLT LDKQRHMNPV
     WGLGNPADFD LLAVLASHVP GASVDPARIG GYDVVIADTQ APAVFGANGE FFASGRLDNL
     SATHAGLAAL IAHSSAASGG AAGGPIAILA AFDHEEIGSN SRSGACGPIL EDVLVRVSDG
     LGATVSQRRQ ALAASFCVSA DAGHAVHPNY PERHDPANHP VLNGGPLLKI NANQRYATDA
     PGAAFWARLC GEAKVPYQEF VSNNVMPCGS TIGPLTATRM GIRTVDVGVP LLSMHSAREL
     CGVADPHRLA TVTELFFQTA M
//
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