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Protein

tRNA (guanine(26)-N(2)/guanine(27)-N(2))-dimethyltransferase

Gene

trm1

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Dimethylates the guanine residues at position 26 and 27 of one or more tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.UniRule annotation1 Publication

Catalytic activityi

4 S-adenosyl-L-methionine + guanine(26)/guanine(27) in tRNA = 4 S-adenosyl-L-homocysteine + N(2)-dimethylguanine(26)/N(2)-dimethylguanine(27) in tRNA.UniRule annotation1 Publication

GO - Molecular functioni

GO - Biological processi

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

BioCyciAAEO224324:GJBH-601-MONOMER.
MetaCyc:MONOMER-16631.
BRENDAi2.1.1.215. 396.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (guanine(26)-N(2)/guanine(27)-N(2))-dimethyltransferaseUniRule annotation (EC:2.1.1.215UniRule annotation)
Gene namesi
Name:trm1UniRule annotation
Ordered Locus Names:aq_841
OrganismiAquifex aeolicus (strain VF5)
Taxonomic identifieri224324 [NCBI]
Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
Proteomesi
  • UP000000798 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 392392tRNA (guanine(26)-N(2)/guanine(27)-N(2))-dimethyltransferasePRO_0000147678Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi224324.aq_841.

Structurei

Secondary structure

1
392
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Beta strandi9 – 135Combined sources
Helixi30 – 323Combined sources
Helixi33 – 5018Combined sources
Beta strandi54 – 607Combined sources
Helixi65 – 739Combined sources
Beta strandi77 – 837Combined sources
Helixi87 – 9913Combined sources
Helixi104 – 1063Combined sources
Beta strandi107 – 1104Combined sources
Helixi114 – 1196Combined sources
Beta strandi126 – 1316Combined sources
Helixi138 – 1403Combined sources
Helixi141 – 1477Combined sources
Beta strandi148 – 15811Combined sources
Helixi161 – 1644Combined sources
Helixi169 – 1768Combined sources
Beta strandi177 – 1793Combined sources
Helixi186 – 20318Combined sources
Turni204 – 2063Combined sources
Beta strandi207 – 21711Combined sources
Beta strandi220 – 22910Combined sources
Helixi231 – 2388Combined sources
Beta strandi241 – 2466Combined sources
Turni248 – 2503Combined sources
Beta strandi253 – 2564Combined sources
Helixi259 – 2613Combined sources
Turni267 – 2693Combined sources
Beta strandi274 – 2807Combined sources
Helixi287 – 29812Combined sources
Helixi305 – 31814Combined sources
Helixi328 – 3358Combined sources
Helixi343 – 3497Combined sources
Beta strandi356 – 3583Combined sources
Beta strandi361 – 3633Combined sources
Helixi368 – 38417Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AXSX-ray2.16A1-392[»]
3AXTX-ray2.49A1-392[»]
ProteinModelPortaliO67010.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 375374Trm1 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

eggNOGiENOG4108K3F. Bacteria.
COG1867. LUCA.
HOGENOMiHOG000229931.
InParanoidiO67010.
KOiK00555.
OMAiTEYHAEV.
OrthoDBiEOG6SNDPM.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00290. tRNA_dimethyltr_TRM1.
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.

O67010-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIVQEGIAK IIVPEIPKTV SSDMPVFYNP RMRVNRDLAV LGLEYLCKKL
60 70 80 90 100
GRPVKVADPL SASGIRAIRF LLETSCVEKA YANDISSKAI EIMKENFKLN
110 120 130 140 150
NIPEDRYEIH GMEANFFLRK EWGFGFDYVD LDPFGTPVPF IESVALSMKR
160 170 180 190 200
GGILSLTATD TAPLSGTYPK TCMRRYMARP LRNEFKHEVG IRILIKKVIE
210 220 230 240 250
LAAQYDIAMI PIFAYSHLHY FKLFFVKERG VEKVDKLIEQ FGYIQYCFNC
260 270 280 290 300
MNREVVTDLY KFKEKCPHCG SKFHIGGPLW IGKLWDEEFT NFLYEEAQKR
310 320 330 340 350
EEIEKETKRI LKLIKEESQL QTVGFYVLSK LAEKVKLPAQ PPIRIAVKFF
360 370 380 390
NGVRTHFVGD GFRTNLSFEE VMKKMEELKE KQKEFLEKKK QG
Length:392
Mass (Da):45,479
Last modified:August 1, 1998 - v1
Checksum:iD2441A3754566043
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC06976.1.
PIRiG70372.
RefSeqiNP_213571.1. NC_000918.1.
WP_010880509.1. NC_000918.1.

Genome annotation databases

EnsemblBacteriaiAAC06976; AAC06976; aq_841.
GeneIDi1193460.
KEGGiaae:aq_841.
PATRICi20959062. VBIAquAeo85532_0656.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000657 Genomic DNA. Translation: AAC06976.1.
PIRiG70372.
RefSeqiNP_213571.1. NC_000918.1.
WP_010880509.1. NC_000918.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AXSX-ray2.16A1-392[»]
3AXTX-ray2.49A1-392[»]
ProteinModelPortaliO67010.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224324.aq_841.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC06976; AAC06976; aq_841.
GeneIDi1193460.
KEGGiaae:aq_841.
PATRICi20959062. VBIAquAeo85532_0656.

Phylogenomic databases

eggNOGiENOG4108K3F. Bacteria.
COG1867. LUCA.
HOGENOMiHOG000229931.
InParanoidiO67010.
KOiK00555.
OMAiTEYHAEV.
OrthoDBiEOG6SNDPM.

Enzyme and pathway databases

BioCyciAAEO224324:GJBH-601-MONOMER.
MetaCyc:MONOMER-16631.
BRENDAi2.1.1.215. 396.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_00290. tRNA_dimethyltr_TRM1.
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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: VF5.
  2. "Aquifex aeolicus tRNA (N2,N2-guanine)-dimethyltransferase (Trm1) catalyzes transfer of methyl groups not only to guanine 26 but also to guanine 27 in tRNA."
    Awai T., Kimura S., Tomikawa C., Ochi A., Ihsanawati X., Bessho Y., Yokoyama S., Ohno S., Nishikawa K., Yokogawa T., Suzuki T., Hori H.
    J. Biol. Chem. 284:20467-20478(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiTRM1_AQUAE
AccessioniPrimary (citable) accession number: O67010
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: August 1, 1998
Last modified: February 17, 2016
This is version 90 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.