TRM6_YEAST
ID TRM6_YEAST Reviewed; 478 AA.
AC P41814; D6W1B8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6;
DE AltName: Full=General control non-derepressible protein 10;
DE Short=Protein GCD10;
DE AltName: Full=tRNA(m1A58)-methyltransferase subunit TRM6;
DE Short=tRNA(m1A58)MTase subunit TRM6;
GN Name=GCD10; Synonyms=TIF33, TRM6; OrderedLocusNames=YNL062C;
GN ORFNames=N2422;
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], FUNCTION IN TRANSLATIONAL REPRESSION,
RP AND RNA-BINDING.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7542616; DOI=10.1101/gad.9.14.1781;
RA Garcia-Barrio M.T., Naranda T., Vazquez De Aldana C.R., Cuesta R.,
RA Hinnebusch A.G., Hershey J.W., Tamame M.;
RT "GCD10, a translational repressor of GCN4, is the RNA-binding subunit of
RT eukaryotic translation initiation factor-3.";
RL Genes Dev. 9:1781-1796(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / FY1676;
RX PubMed=8533472; DOI=10.1002/yea.320111008;
RA Bergez P., Doignon F., Crouzet M.;
RT "The sequence of a 44 420 bp fragment located on the left arm of chromosome
RT XIV from Saccharomyces cerevisiae.";
RL Yeast 11:967-974(1995).
RN [3]
RP ERRATUM OF PUBMED:8533472.
RX PubMed=8904343;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<297::aid-yea940>3.0.co;2-d;
RA Bergez P., Doignon F., Crouzet M.;
RL Yeast 12:297-297(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [5]
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 [6]
RP FUNCTION AS A TRNA METHYLTRANSFERASE SUBUNIT, SUBUNIT, AND SUBCELLULAR
RP 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 [7]
RP FUNCTION AS A TRNA METHYLTRANSFERASE SUBUNIT.
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 IDENTIFICATION BY 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] {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: Substrate-binding subunit of tRNA (adenine-N(1)-)-
CC methyltransferase, which catalyzes the formation of N(1)-methyladenine
CC at position 58 (m1A58) in initiator methionyl-tRNA (PubMed:10779558,
CC PubMed:9851972). Also required for repression of GCN4 mRNA translation
CC by the upstream open reading frames (uORFs) under conditions of amino
CC acid sufficiency (PubMed:7542616). {ECO:0000269|PubMed:10779558,
CC ECO:0000269|PubMed:7542616, ECO:0000269|PubMed:9851972}.
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 P41814; P46959: GCD14; NbExp=3; IntAct=EBI-8995, EBI-7416;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9851972}.
CC -!- MISCELLANEOUS: Present with 2580 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRM6/GCD10 family. {ECO:0000305}.
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DR EMBL; X83511; CAA58501.1; -; Genomic_DNA.
DR EMBL; U12141; AAA99649.1; -; Genomic_DNA.
DR EMBL; Z71338; CAA95935.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10484.1; -; Genomic_DNA.
DR PIR; S51669; S51669.
DR RefSeq; NP_014337.3; NM_001182900.3.
DR PDB; 5EQJ; X-ray; 2.20 A; A=1-478.
DR PDB; 5ERG; X-ray; 2.20 A; A=1-478.
DR PDBsum; 5EQJ; -.
DR PDBsum; 5ERG; -.
DR AlphaFoldDB; P41814; -.
DR SMR; P41814; -.
DR BioGRID; 35761; 258.
DR ComplexPortal; CPX-1631; tRNA (adenine(58)-N(1))-methyltransferase complex.
DR DIP; DIP-3842N; -.
DR IntAct; P41814; 2.
DR MINT; P41814; -.
DR STRING; 4932.YNL062C; -.
DR iPTMnet; P41814; -.
DR MaxQB; P41814; -.
DR PaxDb; P41814; -.
DR PRIDE; P41814; -.
DR EnsemblFungi; YNL062C_mRNA; YNL062C; YNL062C.
DR GeneID; 855663; -.
DR KEGG; sce:YNL062C; -.
DR SGD; S000005006; GCD10.
DR VEuPathDB; FungiDB:YNL062C; -.
DR eggNOG; KOG1416; Eukaryota.
DR GeneTree; ENSGT00390000008327; -.
DR HOGENOM; CLU_010916_1_1_1; -.
DR InParanoid; P41814; -.
DR OMA; TFHNRTE; -.
DR BioCyc; MetaCyc:G3O-33092-MON; -.
DR BioCyc; YEAST:G3O-33092-MON; -.
DR BRENDA; 2.1.1.220; 984.
DR PRO; PR:P41814; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P41814; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030488; P:tRNA methylation; IDA:SGD.
DR DisProt; DP02050; -.
DR InterPro; IPR017423; TRM6.
DR PANTHER; PTHR12945; PTHR12945; 1.
DR Pfam; PF04189; Gcd10p; 1.
DR PIRSF; PIRSF038170; tRNA_m1A_mtfrase; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Repressor; RNA-binding;
KW tRNA processing.
FT CHAIN 1..478
FT /note="tRNA (adenine(58)-N(1))-methyltransferase non-
FT catalytic subunit TRM6"
FT /id="PRO_0000123558"
FT REGION 456..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT TURN 3..5
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 198..208
FT /evidence="ECO:0007829|PDB:5EQJ"
FT TURN 211..216
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 246..256
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 267..276
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 280..284
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 289..295
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 301..305
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 310..314
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 322..327
FT /evidence="ECO:0007829|PDB:5ERG"
FT HELIX 330..353
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 385..391
FT /evidence="ECO:0007829|PDB:5EQJ"
FT HELIX 393..404
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 409..423
FT /evidence="ECO:0007829|PDB:5EQJ"
FT STRAND 441..447
FT /evidence="ECO:0007829|PDB:5EQJ"
SQ SEQUENCE 478 AA; 54389 MW; 99790A1AACE88609 CRC64;
MNALTTIDFN QHVIVRLPSK NYKIVELKPN TSVSLGKFGA FEVNDIIGYP FGLTFEIYYD
GEEVSSDENR DSKPKNKIPI GKVRLLSQEI KDVNNDKDDG QSEPPLSIKE KSVSLELSSI
DSSATNQNLV NMGSKAQELT VEEIEKMKQE SLSSKEIIDK IIKSHKSFHN KTVYSQEKYV
NRKKQKFAKY FTVEYLSSSN LLQFLIDKGD IQRVLDMSQE SMGMLLNLAN IQSEGNYLCM
DETGGLLVYF LLERMFGGDN ESKSKGKVIV IHENEHANLD LLKFANYSEK FIKEHVHTIS
LLDFFEPPTL QEIQSRFTPL PKEEARALKG GKKNSYYRKL RWYNTQWQIL ELTGEFLYDG
LVMATTLHLP TLVPKLAEKI HGSRPIVCYG QFKETLLELA HTLYSDLRFL APSILETRCR
PYQSIRGKLH PLMTMKGGGG YLMWCHRVIP APEPVSENAT AADSSEKLAE HGAKKQKI
