TRM11_YEAST
ID TRM11_YEAST Reviewed; 433 AA.
AC Q12463; D6W1U4;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=tRNA (guanine(10)-N2)-methyltransferase;
DE EC=2.1.1.214;
DE AltName: Full=tRNA [Gm10] methyltransferase;
DE AltName: Full=tRNA guanosine-2'-O-methyltransferase TRM11;
DE AltName: Full=tRNA methylase 11;
GN Name=TRM11; OrderedLocusNames=YOL124C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896265;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1013::aid-yea980%3e3.0.co;2-5;
RA Casamayor A., Khalid H., Balcells L., Aldea M., Casas C., Herrero E.,
RA Arino J.;
RT "Sequence analysis of a 13.4 kbp fragment from the left arm of chromosome
RT XV reveals a malate dehydrogenase gene, a putative Ser/Thr protein kinase,
RT the ribosomal L25 gene and four new open reading frames.";
RL Yeast 12:1013-1020(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TRM112, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF ASP-215 AND ASP-291.
RX PubMed=15899842; DOI=10.1128/mcb.25.11.4359-4370.2005;
RA Purushothaman S.K., Bujnicki J.M., Grosjean H., Lapeyre B.;
RT "Trm11p and Trm112p are both required for the formation of 2-
RT methylguanosine at position 10 in yeast tRNA.";
RL Mol. Cell. Biol. 25:4359-4370(2005).
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.
CC {ECO:0000269|PubMed:15899842}.
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 Evidence={ECO:0000269|PubMed:15899842};
CC -!- SUBUNIT: Interacts with TRM112. {ECO:0000269|PubMed:15899842}.
CC -!- INTERACTION:
CC Q12463; P53738: TRM112; NbExp=4; IntAct=EBI-30471, EBI-28520;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15899842}.
CC -!- MISCELLANEOUS: Present with 2020 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM11 methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00959}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U41293; AAC49469.1; -; Genomic_DNA.
DR EMBL; Z74866; CAA99143.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10660.1; -; Genomic_DNA.
DR PIR; S63447; S63447.
DR RefSeq; NP_014517.1; NM_001183378.1.
DR AlphaFoldDB; Q12463; -.
DR SMR; Q12463; -.
DR BioGRID; 34251; 182.
DR ComplexPortal; CPX-778; TRM11-TRM112 tRNA (m2G10) methyltransferase complex.
DR DIP; DIP-6751N; -.
DR IntAct; Q12463; 1.
DR MINT; Q12463; -.
DR STRING; 4932.YOL124C; -.
DR MaxQB; Q12463; -.
DR PaxDb; Q12463; -.
DR PRIDE; Q12463; -.
DR EnsemblFungi; YOL124C_mRNA; YOL124C; YOL124C.
DR GeneID; 853996; -.
DR KEGG; sce:YOL124C; -.
DR SGD; S000005484; TRM11.
DR VEuPathDB; FungiDB:YOL124C; -.
DR eggNOG; KOG2671; Eukaryota.
DR GeneTree; ENSGT00390000018131; -.
DR HOGENOM; CLU_029646_3_0_1; -.
DR InParanoid; Q12463; -.
DR OMA; MWMPTAN; -.
DR BioCyc; MetaCyc:G3O-33520-MON; -.
DR BioCyc; YEAST:G3O-33520-MON; -.
DR BRENDA; 2.1.1.214; 984.
DR PRO; PR:Q12463; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12463; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043528; C:tRNA (m2G10) methyltransferase complex; IPI:SGD.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IDA:SGD.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030488; P:tRNA methylation; IDA:SGD.
DR GO; GO:0006400; P:tRNA modification; TAS:Reactome.
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 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..433
FT /note="tRNA (guanine(10)-N2)-methyltransferase"
FT /id="PRO_0000270922"
FT MUTAGEN 215
FT /note="D->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:15899842"
FT MUTAGEN 291
FT /note="D->A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:15899842"
SQ SEQUENCE 433 AA; 50073 MW; 61B291029D55263D CRC64;
MKKYLLYMVQ VHLNFRRAEL ESLADLYNLS IDFSQYDANS PFFIVELEND QQAKDWIKRS
ILTRGIYEYW GQGTTLDELH KDIQRQSNFE QDLQLKFKHS TFKFEFECYK GNSKAKRVEQ
IETFRYLGFE GKIDMKHPQE VFTVIEEYTP ISENVGGKTP TRIYFGRQVQ MSNRSAMEKY
DLKKRPYKGT TSFEAELSLV SANIAQVKPG TIMYDPFAGT GSFLVAGGHF GSLVIGSDID
GRMIRGKGAQ VNISANFKKY GESSQFLDVL TMDFTNNALR NNLVIDTILC DPPYGIRESI
KVLGAKDPER FLGKEDMEID GEKAYLRRDY IPTKKPYALD SLLDDLLQYS SERLPIGGRL
AFWMPTANDA NIETIVPMHE NLELKYNCVQ EFNKWSRRLL VYINRGSTFN GSSNHGIKRS
KDNFRERYFN NFN
