ID   TR112_SCHPO             Reviewed;         126 AA.
AC   Q09723;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 120.
DE   RecName: Full=Multifunctional methyltransferase subunit trm112;
DE   AltName: Full=eRF1 methyltransferase subunit trm112;
DE            Short=eRF1 MTase subunit trm112;
DE   AltName: Full=tRNA methyltransferase 112 homolog;
GN   Name=trm112; ORFNames=SPAC31A2.02;
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   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- FUNCTION: Acts as an activator of both rRNA/tRNA and protein
CC       methyltransferases. Together with methyltransferase mtq2, required for
CC       the methylation of eRF1 on 'Gln-182'. Together with methyltransferase
CC       trm11, required for the formation of 2-methylguanosine at position 10
CC       (m2G10) in tRNA. Together with methyltransferase bud23, required for
CC       the formation of a 7-methylguanine in 18S rRNA. Involved in biogenesis
CC       of both 40S and 60S ribosomal subunits (By similarity).
CC       {ECO:0000250|UniProtKB:P53738}.
CC   -!- SUBUNIT: Heterodimer of mtq2-trm112, forming the eRF1
CC       methyltransferase. Trm112 is necessary for the solubility and activity
CC       of the catalytic subunit mtq2. Interacts with trm11; required for full
CC       tRNA methyltransferase activity. Interacts with bud23; required for
CC       full rRNA methyltransferase activity. Interacts with rcm1, nop2, trm9
CC       and lys9 (By similarity). {ECO:0000250|UniProtKB:P53738}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the TRM112 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA90460.1; -; Genomic_DNA.
DR   PIR; S58099; S58099.
DR   RefSeq; NP_592914.1; NM_001018315.2.
DR   AlphaFoldDB; Q09723; -.
DR   SMR; Q09723; -.
DR   BioGRID; 278203; 67.
DR   STRING; 4896.SPAC31A2.02.1; -.
DR   MaxQB; Q09723; -.
DR   PaxDb; Q09723; -.
DR   EnsemblFungi; SPAC31A2.02.1; SPAC31A2.02.1:pep; SPAC31A2.02.
DR   GeneID; 2541708; -.
DR   KEGG; spo:SPAC31A2.02; -.
DR   PomBase; SPAC31A2.02; trm112.
DR   VEuPathDB; FungiDB:SPAC31A2.02; -.
DR   eggNOG; KOG1088; Eukaryota.
DR   HOGENOM; CLU_086140_0_0_1; -.
DR   InParanoid; Q09723; -.
DR   OMA; NMLTSKC; -.
DR   PhylomeDB; Q09723; -.
DR   Reactome; R-SPO-156581; Methylation.
DR   Reactome; R-SPO-72764; Eukaryotic Translation Termination.
DR   PRO; PR:Q09723; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0035657; C:eRF1 methyltransferase complex; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0043528; C:tRNA (m2G10) methyltransferase complex; ISO:PomBase.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0018364; P:peptidyl-glutamine methylation; ISO:PomBase.
DR   GO; GO:2000765; P:regulation of cytoplasmic translation; ISO:PomBase.
DR   GO; GO:0070476; P:rRNA (guanine-N7)-methylation; IBA:GO_Central.
DR   GO; GO:0030488; P:tRNA methylation; ISO:PomBase.
DR   InterPro; IPR039127; Trm112.
DR   InterPro; IPR005651; Trm112-like.
DR   PANTHER; PTHR12773; PTHR12773; 1.
DR   Pfam; PF03966; Trm112p; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Nucleus; Reference proteome.
FT   CHAIN           1..126
FT                   /note="Multifunctional methyltransferase subunit trm112"
FT                   /id="PRO_0000215804"
FT   DOMAIN          2..122
FT                   /note="TRM112"
SQ   SEQUENCE   126 AA;  14075 MW;  209418E5DCB76B1A CRC64;
     MKLLTANFLN CSNKKCTSSP EAFPLDVVDA KLAIQQLELK PEFLIGIMPR IDWNALLKTT
     RQLGNYSLPD EKPDLVDDSD EVLLKSLHNV LLETEITEGK MVCGNCGHVY PIFEGIPNML
     LSESEI