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Protein

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

Gene

trm1

Organism
Methanococcus maripaludis (strain S2 / LL)
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

BioCyciMMAR267377:GJ77-250-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
Synonyms:trmI
Ordered Locus Names:MMP0228
OrganismiMethanococcus maripaludis (strain S2 / LL)
Taxonomic identifieri267377 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
Proteomesi
  • UP000000590 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 373373tRNA (guanine(26)-N(2))-dimethyltransferasePRO_0000408227Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi267377.MMP0228.

Structurei

3D structure databases

ProteinModelPortaliP0CW65.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 365364Trm1 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.
OMAiTPMPFAD.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
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.

P0CW65-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIISEGETK LMVPEESTLS KKDTVFYNPV METNRDISVS VVQSFLDDFK
60 70 80 90 100
RDEFLMCDPL GGSGARGIRY AKELKFNGDL KVSIGDINPS AVKMIKENLK
110 120 130 140 150
LNELENVEVF HEDANVLLSK NFKVFNVVDL DPFGSPVPYL DSGIRASLTK
160 170 180 190 200
GGLLCMTATD TAVLCGAYRK TCIRKYNAVP LKGDKELAVR LMIGYAVKMA
210 220 230 240 250
SKYDIGLKPI FSHVTDHYAR TFMVTERGAG KADSAIENLG YIRQDSEQKS
260 270 280 290 300
FKTFEEGSEK GYAGPFYLGE ISDKNIVQNA LNTAKTRNYS KRAVNILEMI
310 320 330 340 350
SRESEINQVG CFDIHELCSF IKKLVPPVND IMENLKENGF KVTRVHYNPY
360 370
GLKTDAELSD LVVLISEYHS KKY
Length:373
Mass (Da):41,820
Last modified:May 3, 2011 - v1
Checksum:i5CF5D79F5A905058
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX950229 Genomic DNA. Translation: CAF29784.1.
RefSeqiWP_011170172.1. NC_005791.1.

Genome annotation databases

EnsemblBacteriaiCAF29784; CAF29784; MMP0228.
GeneIDi2762025.
KEGGimmp:MMP0228.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX950229 Genomic DNA. Translation: CAF29784.1.
RefSeqiWP_011170172.1. NC_005791.1.

3D structure databases

ProteinModelPortaliP0CW65.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi267377.MMP0228.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAF29784; CAF29784; MMP0228.
GeneIDi2762025.
KEGGimmp:MMP0228.

Phylogenomic databases

eggNOGiarCOG01219. Archaea.
COG1867. LUCA.
HOGENOMiHOG000229931.
KOiK00555.
OMAiTPMPFAD.

Enzyme and pathway databases

BioCyciMMAR267377:GJ77-250-MONOMER.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
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_METMP
AccessioniPrimary (citable) accession number: P0CW65
Secondary accession number(s): Q9HH73
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 3, 2011
Last modified: September 7, 2016
This is version 36 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.