TRM2_ARATH
ID TRM2_ARATH Reviewed; 589 AA.
AC Q9SRU7; Q682B9;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable tRNA (guanine(26)-N(2))-dimethyltransferase 2;
DE EC=2.1.1.216;
DE AltName: Full=tRNA 2,2-dimethylguanosine-26 methyltransferase 2;
DE AltName: Full=tRNA(guanine-26,N(2)-N(2)) methyltransferase 2;
DE AltName: Full=tRNA(m(2,2)G26)dimethyltransferase 2;
GN OrderedLocusNames=At3g02320; ORFNames=F11A12.1, F11A12_100, F14P3.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Trm1 family. {ECO:0000255|PROSITE-ProRule:PRU00958}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF02109.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG12600.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009755; AAF02109.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC068900; AAG12600.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE73792.1; -; Genomic_DNA.
DR EMBL; AK175413; BAD43176.1; -; mRNA.
DR EMBL; AK175448; BAD43211.1; -; mRNA.
DR RefSeq; NP_186881.2; NM_111099.5.
DR AlphaFoldDB; Q9SRU7; -.
DR SMR; Q9SRU7; -.
DR STRING; 3702.AT3G02320.1; -.
DR PaxDb; Q9SRU7; -.
DR PRIDE; Q9SRU7; -.
DR ProteomicsDB; 245240; -.
DR EnsemblPlants; AT3G02320.1; AT3G02320.1; AT3G02320.
DR GeneID; 820451; -.
DR Gramene; AT3G02320.1; AT3G02320.1; AT3G02320.
DR KEGG; ath:AT3G02320; -.
DR Araport; AT3G02320; -.
DR TAIR; locus:2074552; AT3G02320.
DR eggNOG; KOG1253; Eukaryota.
DR HOGENOM; CLU_010862_4_1_1; -.
DR InParanoid; Q9SRU7; -.
DR OMA; YRVSYSH; -.
DR OrthoDB; 1414511at2759; -.
DR PhylomeDB; Q9SRU7; -.
DR PRO; PR:Q9SRU7; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SRU7; baseline and differential.
DR Genevisible; Q9SRU7; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006400; P:tRNA modification; IDA:TAIR.
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 2: Evidence at transcript level;
KW Methyltransferase; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT CHAIN 1..589
FT /note="Probable tRNA (guanine(26)-N(2))-dimethyltransferase
FT 2"
FT /id="PRO_0000147676"
FT DOMAIN 9..465
FT /note="Trm1 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00958"
FT REGION 51..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 75
FT /note="E -> G (in Ref. 3; BAD43211/BAD43176)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 65604 MW; BAB293DC27D3A704 CRC64;
METDLNDYTV IKEGEAEILM HKKNQVFFNK AQVNNRDMSI AVLREFLSKR KQEHEAKSSK
RTRPASKVIE KDASEASKEE TPSENGMNNG DHEVASEDGP SSVSKDPAKT TERFAPREPK
PPKVLEALSA SGLRALRYAR EIEGIGQVVA LDNDLASVEA CQRNIKFNGS VAISKVESHH
TDARVHMLTH PKEFDVVDLD PYGSPSIFLD SAIQSVTDGG LLMCTATDMA VLCGGNGEVC
YSKYGSYPLR AKYCHEMALR ILLASIESHA NRYKRYIVPV LSVQMDFYVR VFVRVYTSAS
AMKNTPLKLS YVYQCIGCDS FHLQPVGRSL PKNNSVRYLP AIGPVVKQDC NHCGKKYNMG
GPIWSAPMHD PEWVTSILNS VKSMKDRYPA YDRISAVLTT VSEELLDVPL FLSLHNLCAT
LKCISPSAAM FRSAVINANY RISGTHVNPL GMKTDAPMEV IWDIMRCWVK NHPIKAQSPE
QPGSVILSKE PSHEVDFSRH IGSLSKAQAK KVARFLPNPE KHWGPKLRAG RQITSKHVSL
IGHEAVNGHL SQHHEELKEE DEEAEPEDNV QDKVDPKRQK TATDNITST
