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Database: UniProt
Entry: M3VB99_9ACTN
LinkDB: M3VB99_9ACTN
Original site: M3VB99_9ACTN 
ID   M3VB99_9ACTN            Unreviewed;       434 AA.
AC   M3VB99;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   22-NOV-2017, entry version 20.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=GM1_013_00260 {ECO:0000313|EMBL:GAC79893.1};
OS   Gordonia malaquae NBRC 108250.
OC   Bacteria; Actinobacteria; Corynebacteriales; Gordoniaceae; Gordonia.
OX   NCBI_TaxID=1223542 {ECO:0000313|EMBL:GAC79893.1, ECO:0000313|Proteomes:UP000035009};
RN   [1] {ECO:0000313|EMBL:GAC79893.1, ECO:0000313|Proteomes:UP000035009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 108250 {ECO:0000313|EMBL:GAC79893.1,
RC   ECO:0000313|Proteomes:UP000035009};
RA   Yoshida I., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA   Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia malaquae NBRC 108250.";
RL   Submitted (FEB-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:GAC79893.1}.
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DR   EMBL; BAOP01000013; GAC79893.1; -; Genomic_DNA.
DR   RefSeq; WP_008378532.1; NZ_BAOP01000013.1.
DR   MEROPS; M18.002; -.
DR   EnsemblBacteria; GAC79893; GAC79893; GM1_013_00260.
DR   OrthoDB; POG091H01I4; -.
DR   BioCyc; GMAL1223542:G1194-1838-MONOMER; -.
DR   Proteomes; UP000035009; 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   Complete proteome {ECO:0000313|Proteomes:UP000035009};
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:UP000035009};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   434 AA;  46138 MW;  1832EF42A8DAF4C9 CRC64;
     MAVNTSATAA GLGDFIDASP SPFHVCATVA AELDAAGYVR VFEDRPWSTT VRGYVIRGGS
     IIAWDASVLE GLSSYAPQPF RIVGGHTDSP NLRVKQNPDR TAAGLSTVAL EPYGGAWLNS
     WLDRDLGLSG RLAYNDGGRV AHTLVRIDEP VLRVPQLAIH LSDDRKGVHL DPQRHVDGIR
     GVGESQPLLE YVADRAGVDP DAVLGWELMT HDVTPSRIIG SAGDLLSAPR LDNQGTCYAG
     LRALLDVPRL RSGGEDGQPR GIAMLALFDH EEVGSGSERG ASSDFLVTVC ERIVGGLGGD
     RDEFLRIMAS SICASGDMAH ATHPNYSERH EPSHHIAVNG GPVLKVNQNL RYASDAIGEA
     EFALACRDAG VPLQRYIHRA DLPCGSTIGP LTATRTGLLT VDVGAPQLAM HSCRELMGAD
     DVAMYSAALA AFLR
//
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