TRM61_YEAST
ID TRM61_YEAST Reviewed; 383 AA.
AC P46959; D6VW61;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRM61;
DE EC=2.1.1.220;
DE AltName: Full=General control non-derepressible protein 14;
DE Short=Protein GCD14;
DE AltName: Full=tRNA(m1A58)-methyltransferase subunit TRM61;
DE Short=tRNA(m1A58)MTase subunit TRM61;
GN Name=GCD14; Synonyms=TRM61; OrderedLocusNames=YJL125C; ORFNames=J0710;
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=S288c / GRF88;
RA Cuesta R.;
RL Thesis (1996), University of Salamanca, Spain.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8948101;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1471::aid-yea30>3.0.co;2-4;
RA Cziepluch C., Kordes E., Pujol A., Jauniaux J.-C.;
RT "Sequencing analysis of a 40.2 kb fragment of yeast chromosome X reveals 19
RT open reading frames including URA2 (5' end), TRK1, PBS2, SPT10, GCD14,
RT RPE1, PHO86, NCA3, ASF1, CCT7, GZF3, two tRNA genes, three remnant delta
RT elements and a Ty4 transposon.";
RL Yeast 12:1471-1474(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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 [5]
RP FUNCTION AS A TRNA METHYLTRANSFERASE, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9851972; DOI=10.1101/gad.12.23.3650;
RA Anderson J., Phan L., Cuesta R., Carlson B.A., Pak M., Asano K.,
RA Bjoerk G.R., Tamame M., Hinnebusch A.G.;
RT "The essential Gcd10p-Gcd14p nuclear complex is required for 1-
RT methyladenosine modification and maturation of initiator methionyl-tRNA.";
RL Genes Dev. 12:3650-3662(1998).
RN [6]
RP FUNCTION IN TRANSLATIONAL REPRESSION.
RX PubMed=9539420; DOI=10.1093/genetics/148.3.1007;
RA Cuesta R., Hinnebusch A.G., Tamame M.;
RT "Identification of GCD14 and GCD15, novel genes required for translational
RT repression of GCN4 mRNA in Saccharomyces cerevisiae.";
RL Genetics 148:1007-1020(1998).
RN [7]
RP FUNCTION AS A TRNA METHYLTRANSFERASE.
RX PubMed=10779558; DOI=10.1073/pnas.090102597;
RA Anderson J., Phan L., Hinnebusch A.G.;
RT "The Gcd10p/Gcd14p complex is the essential two-subunit tRNA(1-
RT methyladenosine) methyltransferase of Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:5173-5178(2000).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [11] {ECO:0007744|PDB:5EQJ, ECO:0007744|PDB:5ERG}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).
RX PubMed=27582183; DOI=10.1038/srep32562;
RA Wang M., Zhu Y., Wang C., Fan X., Jiang X., Ebrahimi M., Qiao Z., Niu L.,
RA Teng M., Li X.;
RT "Crystal structure of the two-subunit tRNA m(1)A58 methyltransferase TRM6-
RT TRM61 from Saccharomyces cerevisiae.";
RL Sci. Rep. 6:32562-32562(2016).
CC -!- FUNCTION: Catalytic subunit of tRNA (adenine-N(1)-)-methyltransferase,
CC which catalyzes the formation of N(1)-methyladenine at position 58
CC (m1A58) in initiator methionyl-tRNA (PubMed:10779558, PubMed:9851972).
CC GCD14 is also required for repression of GCN4 mRNA translation by the
CC upstream open reading frames (uORFs) under conditions of amino acid
CC sufficiency (PubMed:9539420). {ECO:0000269|PubMed:10779558,
CC ECO:0000269|PubMed:9539420, ECO:0000269|PubMed:9851972}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(58) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methyladenosine(58) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43152, Rhea:RHEA-COMP:10365, Rhea:RHEA-COMP:10366,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.220;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00952};
CC -!- SUBUNIT: Heterotetramer; composed of two copies of TRM6/GCD10 and two
CC copies of TRM61/GCD14. {ECO:0000269|PubMed:27582183,
CC ECO:0000305|PubMed:9851972}.
CC -!- INTERACTION:
CC P46959; P41814: GCD10; NbExp=3; IntAct=EBI-7416, EBI-8995;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9851972}.
CC -!- MISCELLANEOUS: Present with 7220 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. TRM61 family. {ECO:0000255|PROSITE-ProRule:PRU00952}.
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DR EMBL; Z54149; CAA90863.1; -; Genomic_DNA.
DR EMBL; Z49400; CAA89420.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08677.1; -; Genomic_DNA.
DR PIR; S56906; S56906.
DR RefSeq; NP_012410.1; NM_001181558.1.
DR PDB; 5EQJ; X-ray; 2.20 A; B=1-383.
DR PDB; 5ERG; X-ray; 2.20 A; B=1-383.
DR PDBsum; 5EQJ; -.
DR PDBsum; 5ERG; -.
DR AlphaFoldDB; P46959; -.
DR SMR; P46959; -.
DR BioGRID; 33631; 319.
DR ComplexPortal; CPX-1631; tRNA (adenine(58)-N(1))-methyltransferase complex.
DR DIP; DIP-5421N; -.
DR IntAct; P46959; 17.
DR MINT; P46959; -.
DR STRING; 4932.YJL125C; -.
DR iPTMnet; P46959; -.
DR MaxQB; P46959; -.
DR PaxDb; P46959; -.
DR PRIDE; P46959; -.
DR EnsemblFungi; YJL125C_mRNA; YJL125C; YJL125C.
DR GeneID; 853317; -.
DR KEGG; sce:YJL125C; -.
DR SGD; S000003661; GCD14.
DR VEuPathDB; FungiDB:YJL125C; -.
DR eggNOG; KOG2915; Eukaryota.
DR GeneTree; ENSGT00940000154239; -.
DR HOGENOM; CLU_025402_4_0_1; -.
DR InParanoid; P46959; -.
DR OMA; VVYPKDA; -.
DR BioCyc; MetaCyc:G3O-31576-MON; -.
DR BioCyc; YEAST:G3O-31576-MON; -.
DR BRENDA; 2.1.1.220; 984.
DR PRO; PR:P46959; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P46959; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IDA:SGD.
DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0030488; P:tRNA methylation; IDA:SGD.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR014816; tRNA_MeTrfase_Gcd14.
DR PANTHER; PTHR12133; PTHR12133; 1.
DR Pfam; PF08704; GCD14; 1.
DR PIRSF; PIRSF017269; GCD14; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51620; SAM_TRM61; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; S-adenosyl-L-methionine; Transferase;
KW tRNA processing.
FT CHAIN 1..383
FT /note="tRNA (adenine(58)-N(1))-methyltransferase catalytic
FT subunit TRM61"
FT /id="PRO_0000087437"
FT BINDING 94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:27582183,
FT ECO:0000312|PDB:5ERG"
FT BINDING 121..124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:27582183,
FT ECO:0000312|PDB:5ERG"
FT BINDING 139
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:27582183,
FT ECO:0000312|PDB:5ERG"
FT BINDING 144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 168..169
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:27582183,
FT ECO:0000312|PDB:5ERG"
FT BINDING 203
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:27582183,
FT ECO:0000312|PDB:5ERG"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 27..32
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:5EQJ"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 142..154
FT /evidence="ECO:0007829|PDB:5EQJ"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 211..216
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 224..232
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 249..267
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 271..283
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 341..347
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 371..375
FT /evidence="ECO:0007829|PDB:5EQJ"
SQ SEQUENCE 383 AA; 43920 MW; A8402DF77A628FD3 CRC64;
MSTNCFSGYK DLIKEGDLTL IWVSRDNIKP VRMHSEEVFN TRYGSFPHKD IIGKPYGSQI
AIRTKGSNKF AFVHVLQPTP ELWTLSLPHR TQIVYTPDSS YIMQRLNCSP HSRVIEAGTG
SGSFSHAFAR SVGHLFSFEF HHIRYEQALE EFKEHGLIDD NVTITHRDVC QGGFLIKKGD
TTSYEFGNNE TAASLNANVV FLDLPAPWDA IPHLDSVISV DEKVGLCCFS PCIEQVDKTL
DVLEKYGWTD VEMVEIQGRQ YESRRQMVRS LNDALERLRD IKRHKLQGVE RRKRMFNNTI
DSNDEKVGKR NEDGVPLTEK AKFNPFGKGS RIKEGDSNYK WKEVTKMEAE IKSHTSYLTF
AFKVVNRSRD DEKVNEILRS TEK
