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Database: UniProt
Entry: A0A0Q5MHC6_9MICO
LinkDB: A0A0Q5MHC6_9MICO
Original site: A0A0Q5MHC6_9MICO 
ID   A0A0Q5MHC6_9MICO        Unreviewed;       432 AA.
AC   A0A0Q5MHC6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   07-JUN-2017, entry version 7.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=ASF89_14920 {ECO:0000313|EMBL:KQR62060.1};
OS   Frigoribacterium sp. Leaf172.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
OC   Frigoribacterium.
OX   NCBI_TaxID=1736285 {ECO:0000313|EMBL:KQR62060.1, ECO:0000313|Proteomes:UP000051720};
RN   [1] {ECO:0000313|EMBL:KQR62060.1, ECO:0000313|Proteomes:UP000051720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf172 {ECO:0000313|EMBL:KQR62060.1,
RC   ECO:0000313|Proteomes:UP000051720};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQR62060.1, ECO:0000313|Proteomes:UP000051720}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf172 {ECO:0000313|EMBL:KQR62060.1,
RC   ECO:0000313|Proteomes:UP000051720};
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:KQR62060.1}.
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DR   EMBL; LMPB01000006; KQR62060.1; -; Genomic_DNA.
DR   RefSeq; WP_055816339.1; NZ_LMPB01000006.1.
DR   EnsemblBacteria; KQR62060; KQR62060; ASF89_14920.
DR   Proteomes; UP000051720; 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:KQR62060.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000051720};
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:UP000051720};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   432 AA;  44930 MW;  81F3E455A32FE8DE CRC64;
     MTSSRPHLDD LARFITASPS SFHAAAEAAR RLDEAGFDRL DETAVWPSGP GARYIVRDGA
     VVAWIEPARA HATTPFRVVG AHTDSPGFKL KPKSTTGTRG WVQAGVEVYG GPLFNSWLDR
     DLEFAGRLVT RQGETRLVRT GPLLRIPQLA VHLDRGVNSE GLTLDPQRHL NPVVGAGPLD
     QADVLGHLAA LAGLDPADVT GYDVVVADTA PPARLGLSGE LFAAGRMDNL TSTHAGLVAL
     IETATSSGGA GAELDHVAVL AAFDHEEVGS ATPSGAAGPL LEDVLARVSD GLGATATDHR
     RALAASWCLS ADAGHAVHPN YPERHDPANQ PIVNGGPLLK INANQRYATD GLGAAEWSRA
     CEQAGVPFQE FVSNNSVPCG STIGPITATR LGIRTIDVGV PLLGMHSARE LCGADDPGHL
     SRAAAAFLAP AA
//
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