(data stored in ACNUC7421 zone)

SWISSPROT: TRMB_PSEAB

ID   TRMB_PSEAB              Reviewed;         244 AA.
AC   Q02U31;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   08-MAY-2019, entry version 68.
DE   RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057};
DE            EC=2.1.1.33 {ECO:0000255|HAMAP-Rule:MF_01057};
DE   AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057};
DE   AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057};
GN   Name=trmB {ECO:0000255|HAMAP-Rule:MF_01057};
GN   OrderedLocusNames=PA14_05000;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at
CC       position 46 (m7G46) in tRNA. {ECO:0000255|HAMAP-Rule:MF_01057}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-
CC         methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:42708, Rhea:RHEA-COMP:10188, Rhea:RHEA-
CC         COMP:10189, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74480; EC=2.1.1.33;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01057};
CC   -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01057}.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. TrmB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01057}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABJ15348.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; CP000438; ABJ15348.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_015502217.1; NC_008463.1.
DR   SMR; Q02U31; -.
DR   EnsemblBacteria; ABJ15348; ABJ15348; PA14_05000.
DR   KEGG; pau:PA14_05000; -.
DR   HOGENOM; HOG000073968; -.
DR   KO; K03439; -.
DR   BioCyc; PAER208963:G1G74-416-MONOMER; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01057; tRNA_methyltr_TrmB; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR   PANTHER; PTHR23417; PTHR23417; 1.
DR   Pfam; PF02390; Methyltransf_4; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00091; TIGR00091; 1.
DR   PROSITE; PS51625; SAM_MT_TRMB; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q02U31.
DR   SWISS-2DPAGE; Q02U31.
KW   Complete proteome; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN         1    244       tRNA (guanine-N(7)-)-methyltransferase.
FT                                /FTId=PRO_0000288203.
FT   REGION      222    225       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01057}.
FT   ACT_SITE    149    149       {ECO:0000250}.
FT   BINDING      74     74       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01057}.
FT   BINDING      99     99       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01057}.
FT   BINDING     126    126       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01057}.
FT   BINDING     149    149       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01057}.
FT   BINDING     153    153       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01057}.
FT   BINDING     185    185       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01057}.
SQ   SEQUENCE   244 AA;  27525 MW;  E7DFE8529BE6FF56 CRC64;
     MSDTPQSPAQ GSLAEHDEAR PMRTVKSFVM RAGRMTEGQQ RGLDLGWPKF GLELSDEVQD
     FDAIFGRQAP RTFEIGFGMG HSTLEMAAAA PDIDFIGVEV HKPGVGALLN GLLTQGLGNV
     RVYSCDALEV LRHCVADASL DRLLLFFPDP WHKKRHHKRR IVQPEFAELV RRKLKVGGVL
     HMATDWEPYA EHMLDVMSAA PGYRNQAEDG RFVARPQERP VTKFERRGER LGHGVWDLKF
     ERID
//

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