(data stored in ACNUC7421 zone)

SWISSPROT: TRMB_RHOPS

ID   TRMB_RHOPS              Reviewed;         256 AA.
AC   Q13EL3;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 76.
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=RPD_0236;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP000283; ABE37476.1; -; Genomic_DNA.
DR   SMR; Q13EL3; -.
DR   STRING; 316057.RPD_0236; -.
DR   EnsemblBacteria; ABE37476; ABE37476; RPD_0236.
DR   KEGG; rpd:RPD_0236; -.
DR   eggNOG; ENOG4105CZ1; Bacteria.
DR   eggNOG; COG0220; LUCA.
DR   HOGENOM; HOG000073969; -.
DR   KO; K03439; -.
DR   OMA; PDPWHKS; -.
DR   BioCyc; RPAL316057:RPD_RS01195-MONOMER; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000001818; 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; Q13EL3.
DR   SWISS-2DPAGE; Q13EL3.
KW   Complete proteome; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN         1    256       tRNA (guanine-N(7)-)-methyltransferase.
FT                                /FTId=PRO_0000288215.
FT   ACT_SITE    159    159       {ECO:0000250}.
FT   BINDING      85     85       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01057}.
FT   BINDING     110    110       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01057}.
FT   BINDING     137    137       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01057}.
FT   BINDING     159    159       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01057}.
FT   BINDING     163    163       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01057}.
FT   BINDING     195    195       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01057}.
SQ   SEQUENCE   256 AA;  29350 MW;  94486706E0E2607E CRC64;
     MITIDRRVQT KCSVLGRHKQ VFIDMNETVH HQGSFFGRRK GHKLRAHQAD LVDNLLPHLA
     LDIELPAPDA LAELFDAPVE AVRLEIGFGG GEHLIAEALA HPEIGFIGAE PYVNGMAKIL
     ARIEDQNIRN VRLFAGDAAE LMAWLPARAL KRIDLIHPDP WPKRRHWKRR FVQDSMIGAM
     ARALIDGGEF RFVSDIDSYN AWTLAHLLRA PEFDWTAERA DDWRKPWSGY TMTRYGRKAE
     REGRRASYLR FRRIAA
//

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