TRM7_SCHPO
ID TRM7_SCHPO Reviewed; 285 AA.
AC O36015;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03162};
DE EC=2.1.1.205 {ECO:0000255|HAMAP-Rule:MF_03162};
DE AltName: Full=2'-O-ribose RNA methyltransferase TRM7 homolog {ECO:0000255|HAMAP-Rule:MF_03162};
GN ORFNames=SPAC4F10.03c;
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 [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: Methylates the 2'-O-ribose of nucleotides at positions 32 and
CC 34 of the tRNA anticodon loop of substrate tRNAs. {ECO:0000255|HAMAP-
CC Rule:MF_03162}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cytidine(32)/guanosine(34) in tRNA + 2 S-adenosyl-L-methionine
CC = 2'-O-methylcytidine(32)/2'-O-methylguanosine(34) in tRNA + 2 H(+) +
CC 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:42396, Rhea:RHEA-
CC COMP:10246, Rhea:RHEA-COMP:10247, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74445, ChEBI:CHEBI:74495, ChEBI:CHEBI:82748;
CC EC=2.1.1.205; Evidence={ECO:0000255|HAMAP-Rule:MF_03162};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03162}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. RNA methyltransferase RlmE family. TRM7 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03162}.
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DR EMBL; CU329670; CAB11724.1; -; Genomic_DNA.
DR PIR; T38807; T38807.
DR RefSeq; NP_594746.1; NM_001020173.2.
DR AlphaFoldDB; O36015; -.
DR SMR; O36015; -.
DR BioGRID; 280039; 1.
DR STRING; 4896.SPAC4F10.03c.1; -.
DR MaxQB; O36015; -.
DR PaxDb; O36015; -.
DR EnsemblFungi; SPAC4F10.03c.1; SPAC4F10.03c.1:pep; SPAC4F10.03c.
DR GeneID; 2543625; -.
DR KEGG; spo:SPAC4F10.03c; -.
DR PomBase; SPAC4F10.03c; -.
DR VEuPathDB; FungiDB:SPAC4F10.03c; -.
DR eggNOG; KOG1099; Eukaryota.
DR HOGENOM; CLU_009422_1_2_1; -.
DR InParanoid; O36015; -.
DR OMA; GLHDMDI; -.
DR PhylomeDB; O36015; -.
DR PRO; PR:O36015; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0008173; F:RNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0106339; F:tRNA (cytidine 32-2'-O)-methyltransferase activity; IMP:PomBase.
DR GO; GO:0106340; F:tRNA (guanosine 32-2'-O)-methyltransferase activity; IMP:PomBase.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IMP:PomBase.
DR GO; GO:0002130; P:wobble position ribose methylation; ISO:PomBase.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01547; RNA_methyltr_E; 1.
DR HAMAP; MF_03162; RNA_methyltr_E_TRM7; 1.
DR InterPro; IPR028590; RNA_methyltr_E_TRM7.
DR InterPro; IPR002877; RNA_MeTrfase_FtsJ_dom.
DR InterPro; IPR015507; rRNA-MeTfrase_E.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR10920:SF12; PTHR10920:SF12; 1.
DR Pfam; PF01728; FtsJ; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..285
FT /note="Putative tRNA (cytidine(32)/guanosine(34)-2'-O)-
FT methyltransferase"
FT /id="PRO_0000155589"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162"
FT BINDING 53
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162"
FT BINDING 55
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162"
FT BINDING 99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162"
FT BINDING 124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03162"
SQ SEQUENCE 285 AA; 31466 MW; 1B279F7F6C385A9C CRC64;
MGRSSKDKRD AYYRLAKEQG WRARSAFKLL QLNEQFNLFE GAKRVVDLCA APGSWSQVLS
RELLKNIDTS IAADEKPMIV AVDLQPMAPI DGVCTLQLDI THPNTLSIIL SHFGNEPADL
VVSDGAPDVT GLHDLDEYIQ AQILLAAFNL AVCVLKPGGK FVAKIFRGRD VSLLYSQLRL
MFRKVSCAKP RSSRASSIES FVVCEDFNPP SNFQPDLTKP LCVIDPTNAH EIAPFIACGD
LDGYDADATY PVEINMKKAT LDVIQPPTAP PYKRAIELKH SKMMS
