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Protein

Release factor glutamine methyltransferase

Gene

prmC

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.Curated

Catalytic activityi

S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine = S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N(5)-methyl-L-glutamine.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei151S-adenosyl-L-methionine2 Publications1
Binding sitei180S-adenosyl-L-methionine2 Publications1
Binding sitei197S-adenosyl-L-methionine2 Publications1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.297. 6331.

Names & Taxonomyi

Protein namesi
Recommended name:
Release factor glutamine methyltransferase (EC:2.1.1.297)
Short name:
RF MTase
Alternative name(s):
N5-glutamine methyltransferase PrmC
Protein-(glutamine-N5) MTase PrmC
Protein-glutamine N-methyltransferase PrmC
Gene namesi
Name:prmC
Ordered Locus Names:TM_0488
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004145481 – 282Release factor glutamine methyltransferaseAdd BLAST282

Interactioni

Subunit structurei

Monomer and homodimer.2 Publications

Protein-protein interaction databases

STRINGi243274.TM0488.

Structurei

Secondary structure

1282
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 24Combined sources11
Turni25 – 28Combined sources4
Helixi32 – 44Combined sources13
Helixi48 – 51Combined sources4
Beta strandi53 – 55Combined sources3
Helixi60 – 74Combined sources15
Helixi79 – 83Combined sources5
Beta strandi85 – 88Combined sources4
Beta strandi91 – 94Combined sources4
Helixi106 – 120Combined sources15
Beta strandi124 – 129Combined sources6
Helixi134 – 142Combined sources9
Beta strandi146 – 152Combined sources7
Helixi154 – 166Combined sources13
Beta strandi172 – 179Combined sources8
Helixi182 – 187Combined sources6
Turni188 – 190Combined sources3
Beta strandi193 – 196Combined sources4
Helixi203 – 205Combined sources3
Helixi211 – 213Combined sources3
Helixi216 – 219Combined sources4
Turni222 – 224Combined sources3
Helixi227 – 235Combined sources9
Beta strandi242 – 246Combined sources5
Helixi249 – 251Combined sources3
Helixi252 – 255Combined sources4
Turni256 – 258Combined sources3
Beta strandi259 – 261Combined sources3
Beta strandi263 – 266Combined sources4
Beta strandi270 – 278Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NV8X-ray2.20A/B1-282[»]
1NV9X-ray2.36A1-282[»]
1SG9X-ray2.30A/B/C1-282[»]
1VQ1X-ray2.80A/B1-282[»]
ProteinModelPortaliQ9WYV8.
SMRiQ9WYV8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WYV8.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni129 – 133S-adenosyl-L-methionine binding5
Regioni197 – 200Substrate binding4

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105EQY. Bacteria.
COG2890. LUCA.
InParanoidiQ9WYV8.
KOiK02493.
OMAiMDTRKNV.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_02126. RF_methyltr_PrmC. 1 hit.
InterProiIPR002052. DNA_methylase_N6_adenine_CS.
IPR004556. Modification_methylase_HemK.
IPR019874. Release_fac_Glu-N5_MeTfrase.
IPR029063. SAM-dependent_MTases.
IPR007848. Small_mtfrase_dom.
[Graphical view]
PfamiPF05175. MTS. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00536. hemK_fam. 1 hit.
TIGR03534. RF_mod_PrmC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9WYV8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTRKNVSGA ERKIWSLIRD CSGKLEGVTE TSVLEVLLIV SRVLGIRKED
60 70 80 90 100
LFLKDLGVSP TEEKRILELV EKRASGYPLH YILGEKEFMG LSFLVEEGVF
110 120 130 140 150
VPRPETEELV ELALELIRKY GIKTVADIGT GSGAIGVSVA KFSDAIVFAT
160 170 180 190 200
DVSSKAVEIA RKNAERHGVS DRFFVRKGEF LEPFKEKFAS IEMILSNPPY
210 220 230 240 250
VKSSAHLPKD VLFEPPEALF GGEDGLDFYR EFFGRYDTSG KIVLMEIGED
260 270 280
QVEELKKIVS DTVFLKDSAG KYRFLLLNRR SS
Length:282
Mass (Da):31,609
Last modified:November 1, 1999 - v1
Checksum:i68130302E620181B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35573.1.
PIRiG72369.
RefSeqiNP_228298.1. NC_000853.1.
WP_004081478.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD35573; AAD35573; TM_0488.
GeneIDi897528.
KEGGitma:TM0488.
tmi:THEMA_02230.
tmw:THMA_0501.
PATRICi23935881. VBITheMar51294_0495.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35573.1.
PIRiG72369.
RefSeqiNP_228298.1. NC_000853.1.
WP_004081478.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NV8X-ray2.20A/B1-282[»]
1NV9X-ray2.36A1-282[»]
1SG9X-ray2.30A/B/C1-282[»]
1VQ1X-ray2.80A/B1-282[»]
ProteinModelPortaliQ9WYV8.
SMRiQ9WYV8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM0488.

Protocols and materials databases

DNASUi897528.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35573; AAD35573; TM_0488.
GeneIDi897528.
KEGGitma:TM0488.
tmi:THEMA_02230.
tmw:THMA_0501.
PATRICi23935881. VBITheMar51294_0495.

Phylogenomic databases

eggNOGiENOG4105EQY. Bacteria.
COG2890. LUCA.
InParanoidiQ9WYV8.
KOiK02493.
OMAiMDTRKNV.

Enzyme and pathway databases

BRENDAi2.1.1.297. 6331.

Miscellaneous databases

EvolutionaryTraceiQ9WYV8.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_02126. RF_methyltr_PrmC. 1 hit.
InterProiIPR002052. DNA_methylase_N6_adenine_CS.
IPR004556. Modification_methylase_HemK.
IPR019874. Release_fac_Glu-N5_MeTfrase.
IPR029063. SAM-dependent_MTases.
IPR007848. Small_mtfrase_dom.
[Graphical view]
PfamiPF05175. MTS. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00536. hemK_fam. 1 hit.
TIGR03534. RF_mod_PrmC. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPRMC_THEMA
AccessioniPrimary (citable) accession number: Q9WYV8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 14, 2011
Last sequence update: November 1, 1999
Last modified: November 2, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The crystal structure corresponding to PDB 1SG9 shows a glutamate anhydride cross-link formed between the Glu-97 side chains from two molecules, but this has not been observed in other PrmC structures from T.maritima. This cross-link is suggested being an artifact of concentration during crystallization (PubMed:18247349).1 Publication

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.