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Protein

tRNA (guanine(26)-N(2))-dimethyltransferase

Gene

trm1

Organism
Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.UniRule annotation

Catalytic activityi

2 S-adenosyl-L-methionine + guanine(26) in tRNA = 2 S-adenosyl-L-homocysteine + N(2)-dimethylguanine(26) in tRNA.UniRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine, tRNA-binding

Enzyme and pathway databases

BioCyciMBOO456442:GH2T-1880-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (guanine(26)-N(2))-dimethyltransferaseUniRule annotation (EC:2.1.1.216UniRule annotation)
Alternative name(s):
tRNA 2,2-dimethylguanosine-26 methyltransferaseUniRule annotation
tRNA(guanine-26,N(2)-N(2)) methyltransferaseUniRule annotation
tRNA(m(2,2)G26)dimethyltransferaseUniRule annotation
Gene namesi
Name:trm1UniRule annotation
Ordered Locus Names:Mboo_1845
OrganismiMethanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8)
Taxonomic identifieri456442 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanoregulaceaeMethanoregula
Proteomesi
  • UP000002408 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 374374tRNA (guanine(26)-N(2))-dimethyltransferasePRO_1000197036Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi456442.Mboo_1845.

Structurei

3D structure databases

ProteinModelPortaliA7I9E9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 368365Trm1 methyltransferaseUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.UniRule annotation
Contains 1 Trm1 methyltransferase domain.UniRule annotation

Phylogenomic databases

eggNOGiarCOG01219. Archaea.
COG1867. LUCA.
HOGENOMiHOG000229931.
KOiK00555.
OMAiFYNPRMA.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00290. tRNA_dimethyltr_TRM1. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
IPR002905. Trm1.
IPR022923. TRM1_arc_bac.
[Graphical view]
PANTHERiPTHR10631. PTHR10631. 1 hit.
PfamiPF02005. TRM. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00308. TRM1. 1 hit.
PROSITEiPS51626. SAM_MT_TRM1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A7I9E9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVIEATEGT TTFLVPVQDS TGQFPPGTAP VFFNRRMELN RDATVLLLSV
60 70 80 90 100
LQPSDYLDAM GATGVRGLRV AHEVGIPVTI NDRDPEAIPL IRENVARLGL
110 120 130 140 150
PVTVTCRDAC SLLFEQAFDA VDIDPFGTPA PFTDAGIRGT RRFLLLTATD
160 170 180 190 200
TAPLCGAHLK AGIRRYFARP GNTGYHGEVG LRILLGFVAR ETVKYDRGIE
210 220 230 240 250
PLFCFAREHF VRLNLRLTRG PKAADRTIER LGFILQCPTC AYREELPGMF
260 270 280 290 300
PPAATCPFCG KPLRPIGPLF LGAISSDEIL GQMQARLPSC GLGTQKELEK
310 320 330 340 350
LLTTCREELP TSSHYDYHRV AQQLVVSPPK IETLLEALRS AGFDASRTHY
360 370
SGTGVKTNAP LPVLYDAIRG KNEP
Length:374
Mass (Da):40,934
Last modified:September 11, 2007 - v1
Checksum:i90693150DA475C1F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000780 Genomic DNA. Translation: ABS56360.1.
RefSeqiWP_012107411.1. NC_009712.1.

Genome annotation databases

EnsemblBacteriaiABS56360; ABS56360; Mboo_1845.
GeneIDi5410649.
KEGGimbn:Mboo_1845.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000780 Genomic DNA. Translation: ABS56360.1.
RefSeqiWP_012107411.1. NC_009712.1.

3D structure databases

ProteinModelPortaliA7I9E9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi456442.Mboo_1845.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABS56360; ABS56360; Mboo_1845.
GeneIDi5410649.
KEGGimbn:Mboo_1845.

Phylogenomic databases

eggNOGiarCOG01219. Archaea.
COG1867. LUCA.
HOGENOMiHOG000229931.
KOiK00555.
OMAiFYNPRMA.

Enzyme and pathway databases

BioCyciMBOO456442:GH2T-1880-MONOMER.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00290. tRNA_dimethyltr_TRM1. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
IPR002905. Trm1.
IPR022923. TRM1_arc_bac.
[Graphical view]
PANTHERiPTHR10631. PTHR10631. 1 hit.
PfamiPF02005. TRM. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00308. TRM1. 1 hit.
PROSITEiPS51626. SAM_MT_TRM1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRM1_METB6
AccessioniPrimary (citable) accession number: A7I9E9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: September 11, 2007
Last modified: September 7, 2016
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.