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Protein

tRNA (adenine(57)-N(1)/adenine(58)-N(1))-methyltransferase TrmI

Gene

trmI

Organism
Pyrococcus abyssi (strain GE5 / Orsay)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenosine at position(s) 57 (m1A57) and 58 (m1A58) in the T-loop of some tRNAs. Methylates the first adenine of an AA sequence.2 Publications

Catalytic activityi

2 S-adenosyl-L-methionine + adenine(57)/adenine(58) in tRNA = 2 S-adenosyl-L-homocysteine + N(1)-methyladenine(57)/N(1)-methyladenine(58) in tRNA.PROSITE-ProRule annotation2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei125S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication1
Binding sitei153S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication1
Binding sitei169S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16690.
BRENDAi2.1.1.219. 5242.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA (adenine(57)-N(1)/adenine(58)-N(1))-methyltransferase TrmI (EC:2.1.1.219)
Alternative name(s):
tRNA(m1A57/58)-methyltransferase
Gene namesi
Name:trmI
Synonyms:pimT-like
Ordered Locus Names:PYRAB04300
ORF Names:PAB0283
OrganismiPyrococcus abyssi (strain GE5 / Orsay)
Taxonomic identifieri272844 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000810 Componenti: Chromosome
  • UP000009139 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi78H → Y: Decreases efficiency of the dimethylation reaction. 1 Publication1
Mutagenesisi196C → S: Decreases stability of TrmI at extreme temperatures; when associated with S-233. 1 Publication1
Mutagenesisi233C → S: Decreases stability of TrmI at extreme temperatures; when associated with S-196. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004073101 – 253tRNA (adenine(57)-N(1)/adenine(58)-N(1))-methyltransferase TrmIAdd BLAST253

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi196Interchain (with C-233)
Disulfide bondi233Interchain (with C-196)

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homotetramer composed of a dimer of dimers; disulfide-linked. Disulfide bonds are important for the stability of TrmI at extreme temperatures.2 Publications

Protein-protein interaction databases

STRINGi272844.PAB0283.

Structurei

Secondary structure

1253
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 11Combined sources5
Beta strandi17 – 21Combined sources5
Beta strandi24 – 29Combined sources6
Beta strandi32 – 35Combined sources4
Helixi36 – 39Combined sources4
Beta strandi47 – 49Combined sources3
Beta strandi55 – 59Combined sources5
Helixi63 – 69Combined sources7
Helixi79 – 88Combined sources10
Beta strandi96 – 100Combined sources5
Helixi106 – 115Combined sources10
Beta strandi119 – 124Combined sources6
Helixi128 – 141Combined sources14
Turni144 – 146Combined sources3
Beta strandi147 – 150Combined sources4
Helixi154 – 156Combined sources3
Beta strandi162 – 168Combined sources7
Helixi173 – 176Combined sources4
Helixi177 – 183Combined sources7
Beta strandi184 – 196Combined sources13
Helixi197 – 209Combined sources13
Helixi211 – 213Combined sources3
Beta strandi218 – 220Combined sources3
Beta strandi227 – 230Combined sources4
Beta strandi233 – 236Combined sources4
Beta strandi238 – 241Combined sources4
Beta strandi246 – 252Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LGAX-ray2.05A/B/C/D1-253[»]
3LHDX-ray2.59A/B/C/D1-253[»]
3MB5X-ray1.60A1-253[»]
ProteinModelPortaliQ9V1J7.
SMRiQ9V1J7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9V1J7.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni104 – 107S-adenosyl-L-methionine binding4

Domaini

Contains a large catalytic C-terminal domain that binds S-adenosyl-L-methionine and a smaller N-terminal domain that may play a role in tRNA recognition. Domains are connected by a linker region.1 Publication

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. TRM61 family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiarCOG00978. Archaea.
COG2519. LUCA.
HOGENOMiHOG000245274.
KOiK07442.
OMAiRPDHRMI.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
IPR014816. tRNA_MeTrfase_Gcd14.
[Graphical view]
PfamiPF08704. GCD14. 1 hit.
[Graphical view]
PIRSFiPIRSF017269. GCD14. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51620. SAM_TRM61. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9V1J7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIREGDKVVL VDPRGKRYLI TVSKRDFHTD LGILKLEEII GRNFGEAIKS
60 70 80 90 100
HKGHEFKILR PRIVDYLDKM KRGPQIVHPK DAALIVAYAG ISPGDFIVEA
110 120 130 140 150
GVGSGALTLF LANIVGPEGR VVSYEIREDF AKLAWENIKW AGFDDRVTIK
160 170 180 190 200
LKDIYEGIEE ENVDHVILDL PQPERVVEHA AKALKPGGFF VAYTPCSNQV
210 220 230 240 250
MRLHEKLREF KDYFMKPRTI NVLVFDQEVK KECMRPRTTA LVHTGYITFA

RRI
Length:253
Mass (Da):28,873
Last modified:May 1, 2000 - v1
Checksum:iAFE9CB4FA59470C1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ248284 Genomic DNA. Translation: CAB49352.1.
HE613800 Genomic DNA. Translation: CCE69811.1.
PIRiA75159.
RefSeqiWP_010867553.1. NC_000868.1.

Genome annotation databases

EnsemblBacteriaiCAB49352; CAB49352; PAB0283.
GeneIDi1495324.
KEGGipab:PAB0283.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ248284 Genomic DNA. Translation: CAB49352.1.
HE613800 Genomic DNA. Translation: CCE69811.1.
PIRiA75159.
RefSeqiWP_010867553.1. NC_000868.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3LGAX-ray2.05A/B/C/D1-253[»]
3LHDX-ray2.59A/B/C/D1-253[»]
3MB5X-ray1.60A1-253[»]
ProteinModelPortaliQ9V1J7.
SMRiQ9V1J7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272844.PAB0283.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB49352; CAB49352; PAB0283.
GeneIDi1495324.
KEGGipab:PAB0283.

Phylogenomic databases

eggNOGiarCOG00978. Archaea.
COG2519. LUCA.
HOGENOMiHOG000245274.
KOiK07442.
OMAiRPDHRMI.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16690.
BRENDAi2.1.1.219. 5242.

Miscellaneous databases

EvolutionaryTraceiQ9V1J7.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR029063. SAM-dependent_MTases.
IPR014816. tRNA_MeTrfase_Gcd14.
[Graphical view]
PfamiPF08704. GCD14. 1 hit.
[Graphical view]
PIRSFiPIRSF017269. GCD14. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51620. SAM_TRM61. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTRMI_PYRAB
AccessioniPrimary (citable) accession number: Q9V1J7
Secondary accession number(s): G8ZGD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 89 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

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.