TRM82_YEAST
ID TRM82_YEAST Reviewed; 444 AA.
AC Q03774; D6VSE5;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit TRM82 {ECO:0000255|HAMAP-Rule:MF_03056};
DE AltName: Full=Transfer RNA methyltransferase 82 {ECO:0000255|HAMAP-Rule:MF_03056};
GN Name=TRM82 {ECO:0000255|HAMAP-Rule:MF_03056}; OrderedLocusNames=YDR165W;
GN ORFNames=YD8358.19;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP CHARACTERIZATION.
RX PubMed=12403464; DOI=10.1017/s1355838202024019;
RA Alexandrov A., Martzen M.R., Phizicky E.M.;
RT "Two proteins that form a complex are required for 7-methylguanosine
RT modification of yeast tRNA.";
RL RNA 8:1253-1266(2002).
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, AND INTERACTION WITH TRM8.
RX PubMed=15811913; DOI=10.1261/rna.2030705;
RA Alexandrov A., Grayhack E.J., Phizicky E.M.;
RT "tRNA m7G methyltransferase Trm8p/Trm82p: evidence linking activity to a
RT growth phenotype and implicating Trm82p in maintaining levels of active
RT Trm8p.";
RL RNA 11:821-830(2005).
RN [7]
RP FUNCTION.
RX PubMed=16387656; DOI=10.1016/j.molcel.2005.10.036;
RA Alexandrov A., Chernyakov I., Gu W., Hiley S.L., Hughes T.R.,
RA Grayhack E.J., Phizicky E.M.;
RT "Rapid tRNA decay can result from lack of nonessential modifications.";
RL Mol. Cell 21:87-96(2006).
RN [8]
RP FUNCTION.
RX PubMed=17382321; DOI=10.1016/j.febslet.2007.03.023;
RA Matsumoto K., Toyooka T., Tomikawa C., Ochi A., Takano Y., Takayanagi N.,
RA Endo Y., Hori H.;
RT "RNA recognition mechanism of eukaryote tRNA (m7G46) methyltransferase
RT (Trm8-Trm82 complex).";
RL FEBS Lett. 581:1599-1604(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP FUNCTION, PATHWAY, AND MUTAGENESIS OF LYS-223.
RX PubMed=26416026; DOI=10.1186/s13059-015-0779-x;
RA Shaheen R., Abdel-Salam G.M., Guy M.P., Alomar R., Abdel-Hamid M.S.,
RA Afifi H.H., Ismail S.I., Emam B.A., Phizicky E.M., Alkuraya F.S.;
RT "Mutation in WDR4 impairs tRNA m(7)G46 methylation and causes a distinct
RT form of microcephalic primordial dwarfism.";
RL Genome Biol. 16:RESEARCH210.1-RESEARCH210.11(2015).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH TRM8, FUNCTION,
RP SUBUNIT, AND DOMAINS WD REPEATS.
RX PubMed=18184583; DOI=10.1016/j.str.2007.10.025;
RA Leulliot N., Chaillet M., Durand D., Ulryck N., Blondeau K.,
RA van Tilbeurgh H.;
RT "Structure of the yeast tRNA m7G methylation complex.";
RL Structure 16:52-61(2008).
CC -!- FUNCTION: Required for the formation of N(7)-methylguanine at position
CC 46 (m7G46) in tRNA, a modification required to maintain stability of
CC tRNAs; its absence resulting in tRNA decay. In the complex, it is
CC required to stabilize and induce conformational changes of the
CC catalytic subunit. {ECO:0000255|HAMAP-Rule:MF_03056,
CC ECO:0000269|PubMed:15811913, ECO:0000269|PubMed:16387656,
CC ECO:0000269|PubMed:17382321, ECO:0000269|PubMed:18184583,
CC ECO:0000269|PubMed:26416026}.
CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC {ECO:0000269|PubMed:26416026}.
CC -!- SUBUNIT: Forms a heterodimer with the catalytic subunit TRM8.
CC {ECO:0000255|HAMAP-Rule:MF_03056, ECO:0000269|PubMed:18184583}.
CC -!- INTERACTION:
CC Q03774; Q12009: TRM8; NbExp=8; IntAct=EBI-19486, EBI-19552;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03056,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 5910 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the WD repeat TRM82 family. {ECO:0000255|HAMAP-
CC Rule:MF_03056}.
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DR EMBL; Z50046; CAA90385.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12005.1; -; Genomic_DNA.
DR PIR; S57989; S57989.
DR RefSeq; NP_010449.1; NM_001180472.1.
DR PDB; 2VDU; X-ray; 2.40 A; B/D=1-444.
DR PDBsum; 2VDU; -.
DR AlphaFoldDB; Q03774; -.
DR SMR; Q03774; -.
DR BioGRID; 32216; 64.
DR ComplexPortal; CPX-1632; tRNA (guanine-N(7)-)-methyltransferase.
DR DIP; DIP-8795N; -.
DR IntAct; Q03774; 7.
DR MINT; Q03774; -.
DR STRING; 4932.YDR165W; -.
DR iPTMnet; Q03774; -.
DR MaxQB; Q03774; -.
DR PaxDb; Q03774; -.
DR PRIDE; Q03774; -.
DR EnsemblFungi; YDR165W_mRNA; YDR165W; YDR165W.
DR GeneID; 851743; -.
DR KEGG; sce:YDR165W; -.
DR SGD; S000002572; TRM82.
DR VEuPathDB; FungiDB:YDR165W; -.
DR eggNOG; KOG3914; Eukaryota.
DR GeneTree; ENSGT00390000012174; -.
DR HOGENOM; CLU_022082_0_0_1; -.
DR InParanoid; Q03774; -.
DR OMA; PPIYNYI; -.
DR BioCyc; YEAST:YDR165W-MON; -.
DR BRENDA; 2.1.1.33; 984.
DR UniPathway; UPA00989; -.
DR EvolutionaryTrace; Q03774; -.
DR PRO; PR:Q03774; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03774; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0106143; C:tRNA (m7G46) methyltransferase complex; IDA:SGD.
DR GO; GO:0043527; C:tRNA methyltransferase complex; IPI:ComplexPortal.
DR GO; GO:0106004; P:tRNA (guanine-N7)-methylation; IDA:SGD.
DR GO; GO:0030488; P:tRNA methylation; IDA:ComplexPortal.
DR Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03056; TRM82; 1.
DR InterPro; IPR028884; Trm82.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR16288; PTHR16288; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW tRNA processing; WD repeat.
FT CHAIN 1..444
FT /note="tRNA (guanine-N(7)-)-methyltransferase non-catalytic
FT subunit TRM82"
FT /id="PRO_0000051295"
FT REPEAT 1..47
FT /note="WD 1"
FT REPEAT 48..99
FT /note="WD 2"
FT REPEAT 100..147
FT /note="WD 3"
FT REPEAT 148..192
FT /note="WD 4"
FT REPEAT 193..237
FT /note="WD 5"
FT REPEAT 238..279
FT /note="WD 6"
FT REPEAT 308..354
FT /note="WD 7"
FT REGION 55..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 223
FT /note="K->L: Decreased tRNA methylation."
FT /evidence="ECO:0000269|PubMed:26416026"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 14..23
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:2VDU"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:2VDU"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 254..268
FT /evidence="ECO:0007829|PDB:2VDU"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:2VDU"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:2VDU"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 317..326
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 330..337
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 345..352
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 357..363
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 366..371
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 383..390
FT /evidence="ECO:0007829|PDB:2VDU"
FT TURN 391..394
FT /evidence="ECO:0007829|PDB:2VDU"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:2VDU"
FT HELIX 400..414
FT /evidence="ECO:0007829|PDB:2VDU"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:2VDU"
FT HELIX 424..426
FT /evidence="ECO:0007829|PDB:2VDU"
SQ SEQUENCE 444 AA; 50488 MW; F1E0847F44376969 CRC64;
MSVIHPLQNL LTSRDGSLVF AIIKNCILSF KYQSPNHWEF AGKWSDDFDK IQESRNTTAK
EQQGQSSENE NENKKLKSNK GDSIKRTAAK VPSPGLGAPP IYSYIRNLRL TSDESRLIAC
ADSDKSLLVF DVDKTSKNVL KLRKRFCFSK RPNAISIAED DTTVIIADKF GDVYSIDINS
IPEEKFTQEP ILGHVSMLTD VHLIKDSDGH QFIITSDRDE HIKISHYPQC FIVDKWLFGH
KHFVSSICCG KDYLLLSAGG DDKIFAWDWK TGKNLSTFDY NSLIKPYLND QHLAPPRFQN
ENNDIIEFAV SKIIKSKNLP FVAFFVEATK CIIILEMSEK QKGDLALKQI ITFPYNVISL
SAHNDEFQVT LDNKESSGVQ KNFAKFIEYN LNENSFVVNN EKSNEFDSAI IQSVQGDSNL
VTKKEEIYPL YNVSSLRKHG EHYS
