TRM11_SCHPO
ID TRM11_SCHPO Reviewed; 469 AA.
AC O94636;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=tRNA (guanine(10)-N2)-methyltransferase;
DE EC=2.1.1.214;
DE AltName: Full=tRNA guanosine-2'-O-methyltransferase TRM11;
DE Short=tRNA methylase 11;
GN Name=trm11; ORFNames=SPBC16D10.02;
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: Catalytic subunit of an S-adenosyl-L-methionine-dependent
CC tRNA methyltransferase complex that mediates the methylation of the
CC guanosine nucleotide at position 10 (m2G10) in tRNAs. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(10) in tRNA + S-adenosyl-L-methionine = H(+) + N(2)-
CC methylguanosine(10) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43128, Rhea:RHEA-COMP:10355, Rhea:RHEA-COMP:10357,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.214;
CC -!- SUBUNIT: Interacts with trm112. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM11 methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00959}.
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DR EMBL; CU329671; CAB38506.2; -; Genomic_DNA.
DR PIR; T39566; T39566.
DR RefSeq; NP_596497.2; NM_001022418.2.
DR AlphaFoldDB; O94636; -.
DR STRING; 4896.SPBC16D10.02.1; -.
DR iPTMnet; O94636; -.
DR MaxQB; O94636; -.
DR PaxDb; O94636; -.
DR PRIDE; O94636; -.
DR EnsemblFungi; SPBC16D10.02.1; SPBC16D10.02.1:pep; SPBC16D10.02.
DR GeneID; 2540011; -.
DR KEGG; spo:SPBC16D10.02; -.
DR PomBase; SPBC16D10.02; trm11.
DR VEuPathDB; FungiDB:SPBC16D10.02; -.
DR eggNOG; KOG2671; Eukaryota.
DR HOGENOM; CLU_029646_3_0_1; -.
DR InParanoid; O94636; -.
DR OMA; MWMPTAN; -.
DR PhylomeDB; O94636; -.
DR PRO; PR:O94636; -.
DR Proteomes; UP000002485; Chromosome II.
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:0043528; C:tRNA (m2G10) methyltransferase complex; IC:PomBase.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; ISO:PomBase.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0002940; P:tRNA N2-guanine methylation; IC:PomBase.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR000241; RNA_methylase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016691; tRNA_mtfrase_TRM11.
DR Pfam; PF01170; UPF0020; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
DR PROSITE; PS51627; SAM_MT_TRM11; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Nucleus; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..469
FT /note="tRNA (guanine(10)-N2)-methyltransferase"
FT /id="PRO_0000316241"
SQ SEQUENCE 469 AA; 53590 MW; 1521A6DF8B7C5A08 CRC64;
MSVYLLHLAS THAHFHLPEL ETLAKIENVE FWLIPKSEYL NVAFKSDKSR NQALFSHAIK
EFQDSISPND ATTQNPFMLA VVNSNEDARR WIRRSIFCKG IYEIYCIGDS FTRLHEKMKE
LNPAPWDSFK HNSSYKFTFE TFGTRRTMKE QLSIISDFEY MQLQGPVSMH NPQHVFTVLE
NRRNNVEGPK VYFGHWCGSG SRDAIDTFDL KQRSYIGITS FDAELSLVTA QMAMAAPGKL
IYDPFVGTGS FLYTCSFFGA HTLGSDIDGR QMRGKNGRSI KSNFRQYKLS PFFLDTFTGD
VTNCPLRKNL LLDAIVCDPP YGVRAGAKKI AKCSQRPPKE SSSTGNHYPK LEQYQISDMV
YDIICFASDR LVDGGRLVLW LPTITEEYGI DDIPSHPYLS LIYNSIQPFT HWSRRLLTFQ
RLPRAHDSKS LNLLPKINNK TPSHHNFREK YFSSAGRASA STKFSPVLE
