TRM1_YEAST
ID TRM1_YEAST Reviewed; 570 AA.
AC P15565; D6VSA6; Q9URQ7; Q9URQ8;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase, mitochondrial;
DE EC=2.1.1.216;
DE AltName: Full=tRNA 2,2-dimethylguanosine-26 methyltransferase;
DE AltName: Full=tRNA(guanine-26,N(2)-N(2)) methyltransferase;
DE AltName: Full=tRNA(m(2,2)G26)dimethyltransferase;
DE Flags: Precursor;
GN Name=TRM1; OrderedLocusNames=YDR120C; ORFNames=YD9727.15C;
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], AND ALTERNATIVE INITIATION.
RX PubMed=3299379; DOI=10.1073/pnas.84.15.5172;
RA Ellis S.R., Hopper A.K., Martin N.C.;
RT "Amino-terminal extension generated from an upstream AUG codon is not
RT required for mitochondrial import of yeast N2,N2-dimethylguanosine-specific
RT tRNA methyltransferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5172-5176(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC STRAIN=D4, and YF+;
RX PubMed=9801306; DOI=10.1093/nar/26.22.5102;
RA Liu J., Liu J., Straby K.B.;
RT "Point and deletion mutations eliminate one or both methyl group transfers
RT catalysed by the yeast TRM1 encoded tRNA (m22G26)dimethyltransferase.";
RL Nucleic Acids Res. 26:5102-5108(1998).
RN [3]
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 [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 SUBCELLULAR LOCATION.
RX PubMed=7599275; DOI=10.1016/0300-9084(96)88103-x;
RA Rose A.M., Belford H.G., Shen W.C., Greer C.L., Hopper A.K., Martin N.C.;
RT "Location of N2,N2-dimethylguanosine-specific tRNA methyltransferase.";
RL Biochimie 77:45-53(1995).
RN [6]
RP MUTAGENESIS OF LYS-290.
RX PubMed=10048958; DOI=10.1016/s0378-1119(98)00550-2;
RA Liu J.M., Zhou G.Q., Straby K.B.;
RT "Caenorhabditis elegans ZC376.5 encodes a tRNA
RT (m2/2G(26))dimethyltransferance in which (246)arginine is important for the
RT enzyme activity.";
RL Gene 226:73-81(1999).
RN [7]
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 [8]
RP ACETYLATION AT MET-1 (ISOFORM 2), AND SUBCELLULAR LOCATION.
RX PubMed=15911569; DOI=10.1534/genetics.105.043620;
RA Murthi A., Hopper A.K.;
RT "Genome-wide screen for inner nuclear membrane protein targeting in
RT Saccharomyces cerevisiae: roles for N-acetylation and an integral membrane
RT protein.";
RL Genetics 170:1553-1560(2005).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=19602197; DOI=10.1111/j.1600-0854.2009.00956.x;
RA Lai T.P., Stauffer K.A., Murthi A., Shaheen H.H., Peng G., Martin N.C.,
RA Hopper A.K.;
RT "Mechanism and a peptide motif for targeting peripheral proteins to the
RT yeast inner nuclear membrane.";
RL Traffic 10:1243-1256(2009).
CC -!- FUNCTION: Dimethylates a single guanine residue at position 26 of most
CC tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.
CC Required for the modification of both mitochondrial and cytoplasmic
CC tRNAs.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43140, Rhea:RHEA-COMP:10359, Rhea:RHEA-COMP:10360,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=2.1.1.216;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00958,
CC ECO:0000269|PubMed:9801306};
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion. Nucleus inner
CC membrane; Peripheral membrane protein; Nucleoplasmic side.
CC Note=Predominantly targeted to the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=P15565-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P15565-2; Sequence=VSP_018902;
CC -!- PTM: Isoform 2 is N-acetylated by NatC at position 1. N-acetylation is
CC necessary for targeting of the protein to the inner nuclear membrane.
CC -!- MISCELLANEOUS: Present with 15500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Trm1 family. {ECO:0000255|PROSITE-ProRule:PRU00958}.
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DR EMBL; M17193; AAA35150.1; -; Genomic_DNA.
DR EMBL; AF086825; AAD29858.1; -; Genomic_DNA.
DR EMBL; AF086826; AAD29859.1; -; Genomic_DNA.
DR EMBL; Z48758; CAA88673.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11966.1; -; Genomic_DNA.
DR PIR; A28323; A28323.
DR RefSeq; NP_010405.3; NM_001180428.3. [P15565-1]
DR AlphaFoldDB; P15565; -.
DR SMR; P15565; -.
DR BioGRID; 32176; 207.
DR DIP; DIP-5202N; -.
DR IntAct; P15565; 12.
DR MINT; P15565; -.
DR STRING; 4932.YDR120C; -.
DR iPTMnet; P15565; -.
DR MaxQB; P15565; -.
DR PaxDb; P15565; -.
DR PRIDE; P15565; -.
DR EnsemblFungi; YDR120C_mRNA; YDR120C; YDR120C. [P15565-1]
DR GeneID; 851698; -.
DR KEGG; sce:YDR120C; -.
DR SGD; S000002527; TRM1.
DR VEuPathDB; FungiDB:YDR120C; -.
DR eggNOG; KOG1253; Eukaryota.
DR GeneTree; ENSGT00530000063646; -.
DR HOGENOM; CLU_010862_4_1_1; -.
DR InParanoid; P15565; -.
DR OMA; YRVSYSH; -.
DR BioCyc; MetaCyc:G3O-29720-MON; -.
DR BioCyc; YEAST:G3O-29720-MON; -.
DR BRENDA; 2.1.1.216; 5243.
DR PRO; PR:P15565; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P15565; protein.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:SGD.
DR GO; GO:0005634; C:nucleus; 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; IMP:SGD.
DR GO; GO:0002940; P:tRNA N2-guanine methylation; IBA:GO_Central.
DR Gene3D; 3.30.56.70; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002905; Trm1.
DR InterPro; IPR042296; tRNA_met_Trm1_C.
DR PANTHER; PTHR10631; PTHR10631; 1.
DR Pfam; PF02005; TRM; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00308; TRM1; 1.
DR PROSITE; PS51626; SAM_MT_TRM1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative initiation; Membrane; Methyltransferase;
KW Mitochondrion; Nucleus; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; Transit peptide; tRNA processing;
KW tRNA-binding.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT CHAIN ?..570
FT /note="tRNA (guanine(26)-N(2))-dimethyltransferase,
FT mitochondrial"
FT /id="PRO_0000035779"
FT DOMAIN 43..489
FT /note="Trm1 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00958"
FT REGION 91..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..155
FT /note="Required and sufficient for inner nuclear membrane
FT localization"
FT MOTIF 95..101
FT /note="Nuclear localization signal"
FT COMPBIAS 100..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..16
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018902"
FT VARIANT 203
FT /note="T -> S (in strain: D4 and YF+)"
FT VARIANT 467
FT /note="S -> L (in strain: D4; loss of activity)"
FT VARIANT 517
FT /note="G -> R (in strain: D4 and YF+)"
FT MUTAGEN 290
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10048958"
FT MOD_RES P15565-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:15911569"
SQ SEQUENCE 570 AA; 64052 MW; 0AD935838BD90673 CRC64;
MEGFFRIPLK RANLHGMLKA AISKIKANFT AYGAPRINIE DFNIVKEGKA EILFPKKETV
FYNPIQQFNR DLSVTCIKAW DNLYGEECGQ KRNNKKSKKK RCAETNDDSS KRQKMGNGSP
KEAVGNSNRN EPYINILEAL SATGLRAIRY AHEIPHVREV IANDLLPEAV ESIKRNVEYN
SVENIVKPNL DDANVLMYRN KATNNKFHVI DLDPYGTVTP FVDAAIQSIE EGGLMLVTCT
DLSVLAGNGY PEKCFALYGG ANMVSHESTH ESALRLVLNL LKQTAAKYKK TVEPLLSLSI
DFYVRVFVKV KTSPIEVKNV MSSTMTTYHC SRCGSYHNQP LGRISQREGR NNKTFTKYSV
AQGPPVDTKC KFCEGTYHLA GPMYAGPLHN KEFIEEVLRI NKEEHRDQDD TYGTRKRIEG
MLSLAKNELS DSPFYFSPNH IASVIKLQVP PLKKVVAGLG SLGFECSLTH AQPSSLKTNA
PWDAIWYVMQ KCDDEKKDLS KMNPNTTGYK ILSAMPGWLS GTVKSEYDSK LSFAPNEQSG
NIEKLRKLKI VRYQENPTKN WGPKARPNTS
