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   27-MAR-2024, entry version 142.
DE   RecName: Full=tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase {ECO:0000305};
DE            EC=2.1.1.205 {ECO:0000255|HAMAP-Rule:MF_03162, ECO:0000305|PubMed:25404562};
DE   AltName: Full=2'-O-ribose RNA methyltransferase TRM7 homolog {ECO:0000255|HAMAP-Rule:MF_03162};
GN   Name=trm7 {ECO:0000312|PomBase:SPAC4F10.03c}; 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).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=25404562; DOI=10.1261/rna.047639.114;
RA   Guy M.P., Phizicky E.M.;
RT   "Conservation of an intricate circuit for crucial modifications of the
RT   tRNAPhe anticodon loop in eukaryotes.";
RL   RNA 21:61-74(2015).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=29596413; DOI=10.1371/journal.pgen.1007288;
RA   Han L., Guy M.P., Kon Y., Phizicky E.M.;
RT   "Lack of 2'-O-methylation in the tRNA anticodon loop of two
RT   phylogenetically distant yeast species activates the general amino acid
RT   control pathway.";
RL   PLoS Genet. 14:e1007288-e1007288(2018).
CC   -!- FUNCTION: Methylates the 2'-O-ribose of nucleotides at positions 32 and
CC       34 of the tRNA anticodon loop of substrate tRNAs (PubMed:25404562).
CC       Requires trm732 for methylation of the cytidine at position 32 of the
CC       anticodon loop of substrate tRNAs (PubMed:25404562). Requires trm734
CC       for methylation of the nucleotide at position 34 of the anticodon loop
CC       of substrate tRNAs (PubMed:25404562). Methylates tRNA(Phe)
CC       (PubMed:25404562). {ECO:0000269|PubMed:25404562}.
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         ECO:0000305|PubMed:25404562};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03162}.
CC   -!- DISRUPTION PHENOTYPE: Loss of methylation of the 2'-O-ribose of
CC       cytidine at position 32 and guanosine at position 34 of the tRNA
CC       anticodon loop of tRNA(Phe) (PubMed:25404562). Increases occurrence of
CC       1-methylguanosine residue at position 37 in the tRNA anticodon loop of
CC       tRNA(Phe) and decreases occurrence of wybutosine at this position
CC       (PubMed:25404562). Leads to activation of the general amino acid
CC       control (GAAC) response (PubMed:29596413). Slow cell population growth
CC       (PubMed:25404562). Abolishes spore germination (PubMed:25404562).
CC       {ECO:0000269|PubMed:25404562, ECO:0000269|PubMed:29596413}.
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; 284812.O36015; -.
DR   MaxQB; O36015; -.
DR   PaxDb; 4896-SPAC4F10-03c-1; -.
DR   EnsemblFungi; SPAC4F10.03c.1; SPAC4F10.03c.1:pep; SPAC4F10.03c.
DR   GeneID; 2543625; -.
DR   KEGG; spo:SPAC4F10.03c; -.
DR   PomBase; SPAC4F10.03c; trm7.
DR   VEuPathDB; FungiDB:SPAC4F10.03c; -.
DR   eggNOG; KOG1099; Eukaryota.
DR   HOGENOM; CLU_009422_1_2_1; -.
DR   InParanoid; O36015; -.
DR   OMA; FIVCLNF; -.
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:1904047; F:S-adenosyl-L-methionine binding; ISS:UniProtKB.
DR   GO; GO:0106339; F:tRNA (cytidine(32)-2'-O)-methyltransferase activity; IMP:PomBase.
DR   GO; GO:0106340; F:tRNA (guanine(34)-2'-O)-methyltransferase activity; IMP:PomBase.
DR   GO; GO:0016423; F:tRNA (guanine) methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0106050; F:tRNA 2'-O-methyltransferase activity; ISO:PomBase.
DR   GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0002181; P:cytoplasmic translation; ISS:UniProtKB.
DR   GO; GO:0030488; P:tRNA methylation; IMP:PomBase.
DR   GO; GO:0002130; P:wobble position ribose methylation; ISS:UniProtKB.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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; RIBOSOMAL RNA METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10920:SF12; TRNA (CYTIDINE(32)_GUANOSINE(34)-2'-O)-METHYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF01728; FtsJ; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN           1..285
FT                   /note="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
//