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   08-NOV-2023, entry version 178.
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}.
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; 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; 259.
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; 4932-YNL062C; -.
DR   PeptideAtlas; P41814; -.
DR   EnsemblFungi; YNL062C_mRNA; YNL062C; YNL062C.
DR   GeneID; 855663; -.
DR   KEGG; sce:YNL062C; -.
DR   AGR; SGD:S000005006; -.
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; TRCRPYQ; -.
DR   OrthoDB; 22535at2759; -.
DR   BioCyc; MetaCyc:G3O-33092-MONOMER; -.
DR   BioCyc; YEAST:G3O-33092-MONOMER; -.
DR   BRENDA; 2.1.1.220; 984.
DR   BioGRID-ORCS; 855663; 4 hits in 10 CRISPR screens.
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; TRANSLATION INITIATION FACTOR EIF3-RELATED; 1.
DR   PANTHER; PTHR12945:SF0; TRNA (ADENINE(58)-N(1))-METHYLTRANSFERASE NON-CATALYTIC SUBUNIT TRM6; 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
//