TRM1_SCHPO
ID TRM1_SCHPO Reviewed; 548 AA.
AC Q9P804; O74566;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase;
DE EC=2.1.1.216;
DE AltName: Full=tRNA 2,2-dimethylguanosine-26 methyltransferase;
DE AltName: Full=tRNA(guanine-26,N(2)-N(2)) methyltransferase;
DE AltName: Full=tRNA(m(2,2)G26)dimethyltransferase;
GN Name=trm1; ORFNames=SPBC25D12.05;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=10611485; DOI=10.1016/s0014-5793(99)01679-8;
RA Niederberger C., Graub R., Costa A., Desgres J., Schweingruber M.E.;
RT "The tRNA N2,N2-dimethylguanosine-26 methyltransferase encoded by gene trm1
RT increases efficiency of suppression of an ochre codon in
RT Schizosaccharomyces pombe.";
RL FEBS Lett. 464:67-70(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Dimethylates a single guanine residue at position 26 of most
CC tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43140, Rhea:RHEA-COMP:10359, Rhea:RHEA-COMP:10360,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=2.1.1.216;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00958};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Nuclear/cytoplasmic compartments. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Trm1 family. {ECO:0000255|PROSITE-ProRule:PRU00958}.
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DR EMBL; AJ224000; CAA11801.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA20101.2; -; Genomic_DNA.
DR PIR; T39993; T39993.
DR PIR; T46565; T46565.
DR RefSeq; NP_596547.1; NM_001022468.2.
DR AlphaFoldDB; Q9P804; -.
DR SMR; Q9P804; -.
DR BioGRID; 277130; 13.
DR STRING; 4896.SPBC25D12.05.1; -.
DR iPTMnet; Q9P804; -.
DR MaxQB; Q9P804; -.
DR PaxDb; Q9P804; -.
DR EnsemblFungi; SPBC25D12.05.1; SPBC25D12.05.1:pep; SPBC25D12.05.
DR GeneID; 2540604; -.
DR KEGG; spo:SPBC25D12.05; -.
DR PomBase; SPBC25D12.05; trm1.
DR VEuPathDB; FungiDB:SPBC25D12.05; -.
DR eggNOG; KOG1253; Eukaryota.
DR HOGENOM; CLU_010862_4_1_1; -.
DR InParanoid; Q9P804; -.
DR OMA; YRVSYSH; -.
DR PhylomeDB; Q9P804; -.
DR BRENDA; 2.1.1.216; 5613.
DR PRO; PR:Q9P804; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0031965; C:nuclear membrane; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IDA:PomBase.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0002940; P:tRNA N2-guanine methylation; IMP:PomBase.
DR Gene3D; 3.30.56.70; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002905; Trm1.
DR InterPro; IPR042296; tRNA_met_Trm1_C.
DR PANTHER; PTHR10631; PTHR10631; 1.
DR Pfam; PF02005; TRM; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00308; TRM1; 1.
DR PROSITE; PS51626; SAM_MT_TRM1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..548
FT /note="tRNA (guanine(26)-N(2))-dimethyltransferase"
FT /id="PRO_0000147677"
FT DOMAIN 30..470
FT /note="Trm1 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00958"
FT REGION 523..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 322
FT /note="S -> T (in Ref. 1; CAA11801)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 60297 MW; E0DD19178A6B4959 CRC64;
MYEANMLRLS QRISNAVNHF STAMMSGASA SLTEGSAIIP FSNPNEVFYN PVQQFNRDLS
VTAIRAWSET RSKKIVAKSH HRHQLLDQNS ELSQENLTKC DTTHDFEKNC SEKTDSTSAD
NIAGFTILEA LSATGLRSIR YAKELPNVKR ILANDLLENA VKTIEKNVNY NNVSDIVIPN
KGDANAVMHM NKFHYDVIDL DPYGSAAPFL DAAVQSVSKD GLLCITCTDS AVLAGNAYPE
KCFSNYGGSS LRSNFCHEQA VRHLLYAIAA SAAKYGRAIK PLLSLSIDFY FRVFVQIKAK
PVLVKNLQSQ SLLIYHCSGC GSFAEQPLGK TSPGRLPGTT KFSNASGPPV SANCEHCGYV
HHVGGPLWGG PLHDAEFLKK MRAIAEDLDP EVYGTKRRIL GMLALADEEL PDVPFYFVLS
QICSVLRSQS PPQNIFVSAL LNAGYRVSGS HAKSNAIKTN APWSFVWDVL RSWIKDHPVK
LENISKTSAG AAILEKTPTA EVDFTFRPDS EFASKKEGYT RYQMNPTENW GPKSKPGKRT
IAEVDSKS
