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Database: UniProt
Entry: A0A0Q4HD21_9MICO
LinkDB: A0A0Q4HD21_9MICO
Original site: A0A0Q4HD21_9MICO 
ID   A0A0Q4HD21_9MICO        Unreviewed;       425 AA.
AC   A0A0Q4HD21;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   25-OCT-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=ASE68_06465 {ECO:0000313|EMBL:KQM82939.1};
OS   Agromyces sp. Leaf222.
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Agromyces.
OX   NCBI_TaxID=1735688 {ECO:0000313|EMBL:KQM82939.1, ECO:0000313|Proteomes:UP000050813};
RN   [1] {ECO:0000313|EMBL:KQM82939.1, ECO:0000313|Proteomes:UP000050813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf222 {ECO:0000313|EMBL:KQM82939.1,
RC   ECO:0000313|Proteomes:UP000050813};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQM82939.1, ECO:0000313|Proteomes:UP000050813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf222 {ECO:0000313|EMBL:KQM82939.1,
RC   ECO:0000313|Proteomes:UP000050813};
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:KQM82939.1}.
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DR   EMBL; LMKQ01000001; KQM82939.1; -; Genomic_DNA.
DR   RefSeq; WP_055856431.1; NZ_LMKQ01000001.1.
DR   EnsemblBacteria; KQM82939; KQM82939; ASE68_06465.
DR   Proteomes; UP000050813; 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:KQM82939.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000050813};
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:UP000050813};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   425 AA;  44770 MW;  FEC42CFA217F9C3A CRC64;
     MPLVDRDAHI EDLSAFIRES PSSYHAAVAV ADRLVAAGFE RLDERDEWPA GPGRRVVVRD
     GAVIAWVQPE AATATSPYRI IGAHTDSPSF KLKPGASTSS EGVLQAGVEV YGGPLLNSWL
     DRELELAGRL VTADGTEHLV RTGALLRIPQ LAIHLDREVN KGLTLDRQRH LQPIWGSGAA
     GDVLAHLAGI AGLHADEIAG HDVLVADTAA PTRFGLDDVF FAAGRQDNLT SVHAGLVALL
     AAGDDAASDH VSVLAAFDHE ELGSESRSGA SGPFLVDVLA RIAGGLGADE HDRRRAFASS
     WLLSSDAGHA VHPNYPERHD PVNRPHLGDG PLLKLNANQK YATDAHGSAL WARACEQAGV
     RFQPFVSNNA IPCGSTIGPL SATRLGIRTV DVGTPLLSMH SARELSHVDD LAALAAAATA
     FLTPA
//
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