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Database: UniProt
Entry: U2QHB0_9ACTN
LinkDB: U2QHB0_9ACTN
Original site: U2QHB0_9ACTN 
ID   U2QHB0_9ACTN            Unreviewed;       434 AA.
AC   U2QHB0;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   22-NOV-2017, entry version 19.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=HMPREF0682_0539 {ECO:0000313|EMBL:ERK55579.1};
OS   Propionibacterium acidifaciens F0233.
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Propionibacterium.
OX   NCBI_TaxID=553198 {ECO:0000313|EMBL:ERK55579.1, ECO:0000313|Proteomes:UP000017052};
RN   [1] {ECO:0000313|EMBL:ERK55579.1, ECO:0000313|Proteomes:UP000017052}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0233 {ECO:0000313|EMBL:ERK55579.1,
RC   ECO:0000313|Proteomes:UP000017052};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M.,
RA   Haft D.H., Methe B., Sutton G., Nelson K.E.;
RL   Submitted (AUG-2013) 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:ERK55579.1}.
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DR   EMBL; ACVN02000182; ERK55579.1; -; Genomic_DNA.
DR   EnsemblBacteria; ERK55579; ERK55579; HMPREF0682_0539.
DR   OrthoDB; POG091H01I4; -.
DR   Proteomes; UP000017052; 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:ERK55579.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000017052};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:ERK55579.1};
KW   Protease {ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:ERK55579.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017052};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   434 AA;  45874 MW;  101B5C2B96A816C3 CRC64;
     MRSGCAGAAW FNGAMADPTD FMTGFAQFIT AGPTSYHTAA VMAQGLAEAG FTRLDERQEW
     GSVAGRRFLV RGGALVAWVA PDGLDDDAGV RIVGTHTDSP ALTLKPSPSF VRAGWQQANV
     EVYGGPLLNS WLDRELGLAG RVVTLDGVER LVSTGPVLRV SQIAPHFDRG VNERLTIDRQ
     YELVPSYGLG DEPDIVEWVC SRAGVPAGEV AFGDIRVVPT QAPAVFGIGG EFFASARLDN
     LSSTYPAYRA IGETRPGRDI ALFVAFDHEE VGSGTASGAA GPLLSDVLAR IADGYGLGVD
     ARRALLARSS CISADASHAV NPNHTAKYDP LVQPAMNRGP ALKVNAQQRY ATDAISTALW
     ERACRAARVP HQVFVSNNDV ACGTTIGPLT AQRLGVPTVD VGVPILSMHS TREMCGTSDP
     EHLCAALRAH WAGA
//
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