TRM1_ARATH
ID TRM1_ARATH Reviewed; 593 AA.
AC Q9LFU5; F4KB92; Q8RXS4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Probable tRNA (guanine(26)-N(2))-dimethyltransferase 1;
DE EC=2.1.1.216;
DE AltName: Full=tRNA 2,2-dimethylguanosine-26 methyltransferase 1;
DE AltName: Full=tRNA(guanine-26,N(2)-N(2)) methyltransferase 1;
DE AltName: Full=tRNA(m(2,2)G26)dimethyltransferase 1;
GN OrderedLocusNames=At5g15810; ORFNames=F14F8_190;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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=AAL86317.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAC01780.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL391144; CAC01780.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92210.2; -; Genomic_DNA.
DR EMBL; AY080697; AAL86317.1; ALT_INIT; mRNA.
DR PIR; T51410; T51410.
DR RefSeq; NP_197085.3; NM_121586.3.
DR AlphaFoldDB; Q9LFU5; -.
DR SMR; Q9LFU5; -.
DR STRING; 3702.AT5G15810.1; -.
DR iPTMnet; Q9LFU5; -.
DR PaxDb; Q9LFU5; -.
DR PRIDE; Q9LFU5; -.
DR ProteomicsDB; 245239; -.
DR EnsemblPlants; AT5G15810.1; AT5G15810.1; AT5G15810.
DR GeneID; 831438; -.
DR Gramene; AT5G15810.1; AT5G15810.1; AT5G15810.
DR KEGG; ath:AT5G15810; -.
DR Araport; AT5G15810; -.
DR eggNOG; KOG1253; Eukaryota.
DR HOGENOM; CLU_010862_4_1_1; -.
DR InParanoid; Q9LFU5; -.
DR OMA; CCYSRSP; -.
DR OrthoDB; 1414511at2759; -.
DR PhylomeDB; Q9LFU5; -.
DR PRO; PR:Q9LFU5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFU5; baseline and differential.
DR Genevisible; Q9LFU5; 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: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..593
FT /note="Probable tRNA (guanine(26)-N(2))-dimethyltransferase
FT 1"
FT /id="PRO_0000147675"
FT DOMAIN 9..465
FT /note="Trm1 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00958"
FT REGION 56..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..574
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 593 AA; 65845 MW; CA1BD30312B88B40 CRC64;
METDLNDYTV IKEGEAEVLM HKKNQVFFNK AQVNNRDMSI AVLRAFIIKR KQEHEAMLSK
RARSSGKVVE KDVSETSKEE TPTENGDDNG KTNGEHEVTT QDGPKEAAKT AYESARRELK
PPRVLEALSA SGLRALRYAR EVEGIGQVVA LDNDPASVEA CQRNIKFNGL MSTSKVESHL
TDARVHMLSH PKDFDVVDLD PYGAPSIFLD SAVQSVADGG LLMCTATDMA VLCGANGEVC
YSKYGSYPLK GKYCHEMALR ILLASIESHA NRYKRYIVPV LSVQMDFYVR VFVRVYTSAS
AMKNTPLKLS YVYQCIGCDS FHLQSVGRSL PKNNSVRYLP GVGPVVPQDC THCGKKYNMG
GPIWSAPIHD QEWVNSILNG VKSMKDRYPA YDRICAVLTT ISEELPDVPL FLSLHSLSAT
LKCTSPSAAL FRSAVINAKY RVSGSHVNPL GIKTDAPMEI IWDIMRCWVK NHPIKPQSPE
HPGSVILSKE PSHQADFSRH VGSLSKAQAK KVARFLPNPE KHWGPKIRAG RTITSKHVSL
LGHEAVNGHL NNNHKEAGDE EEEEEEEEPE EDIIEGEPEL KRQKTTEDFA STS
