ID   TRMB_CAEEL              Reviewed;         256 AA.
AC   Q23126;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 56.
DE   RecName: Full=tRNA (guanine-N(7)-)-methyltransferase;
DE            EC=2.1.1.33;
DE   AltName: Full=tRNA(m7G46)-methyltransferase;
GN   ORFNames=W02B12.10;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at
CC       position 46 (m7G46) in tRNA (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-
CC       homocysteine + tRNA containing N(7)-methylguanine.
CC   -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. TrmB
CC       family.
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DR   EMBL; Z66521; CAA91400.1; -; Genomic_DNA.
DR   PIR; T26090; T26090.
DR   RefSeq; NP_496448.1; -.
DR   UniGene; Cel.14230; -.
DR   Ensembl; W02B12.10; Caenorhabditis elegans.
DR   GeneID; 174753; -.
DR   KEGG; cel:W02B12.10; -.
DR   NMPDR; fig|6239.3.peg.7486; -.
DR   WormBase; WBGene00012205; W02B12.10.
DR   WormPep; W02B12.10; CE03770.
DR   OMA; Q23126; PDPHFKQ.
DR   BRENDA; 2.1.1.33; 672.
DR   NextBio; 885350; -.
DR   ArrayExpress; Q23126; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IEA:EC.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009792; P:embryonic development ending in birth or eg...; IMP:WormBase.
DR   GO; GO:0006400; P:tRNA modification; ISS:UniProtKB.
DR   InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase.
DR   PANTHER; PTHR23417:SF1; Methyltransf_4; 1.
DR   Pfam; PF02390; Methyltransf_4; 1.
DR   TIGRFAMs; TIGR00091; CHP91; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Methyltransferase; Nucleus; RNA-binding;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT   CHAIN         1    256       tRNA (guanine-N(7)-)-methyltransferase.
FT                                /FTId=PRO_0000171433.
FT   REGION       97     98       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   REGION      132    133       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   REGION      230    232       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   ACT_SITE    155    155       By similarity.
FT   BINDING      74     74       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING     152    152       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
SQ   SEQUENCE   256 AA;  30041 MW;  4F4FAF58CB25FD24 CRC64;
     MDITPALTEM ELDHKPTCET VPGLPQKKHY RQRAHSNPHS DHDIEYPLTP NHMDWTKYYG
     DYTKGRQVDF ADIGCGYGGL LMRLSPKYPD NLMIGMEIRV KVSDYVNEKI QALRKHHAEA
     GHYRNVAVLR SNAMKYMPNY FHKGQLSKMF FLFPDPHFKN KKHKWRIITP TLLSEYAYVL
     REGGIIYTIT DVKDLHEWMV KHLSEHPLFE RLTEEEMKKD PIVEMLFEST EEGQKVTRND
     GGKWPAIFRR LPNPAL
//