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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei151 – 1511S-adenosyl-L-methionine2 Publications
Binding sitei180 – 1801S-adenosyl-L-methionine2 Publications
Binding sitei197 – 1971S-adenosyl-L-methionine2 Publications

GO - Molecular functioni

  1. nucleic acid binding Source: InterPro
  2. protein-glutamine N-methyltransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. peptidyl-glutamine methylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

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
ProteomesiUP000008183: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 282282Release factor glutamine methyltransferasePRO_0000414548Add
BLAST

Interactioni

Subunit structurei

Monomer and homodimer.2 Publications

Protein-protein interaction databases

STRINGi243274.TM0488.

Structurei

Secondary structure

1
282
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 2411Combined sources
Turni25 – 284Combined sources
Helixi32 – 4413Combined sources
Helixi48 – 514Combined sources
Beta strandi53 – 553Combined sources
Helixi60 – 7415Combined sources
Helixi79 – 835Combined sources
Beta strandi85 – 884Combined sources
Beta strandi91 – 944Combined sources
Helixi106 – 12015Combined sources
Beta strandi124 – 1296Combined sources
Helixi134 – 1429Combined sources
Beta strandi146 – 1527Combined sources
Helixi154 – 16613Combined sources
Beta strandi172 – 1798Combined sources
Helixi182 – 1876Combined sources
Turni188 – 1903Combined sources
Beta strandi193 – 1964Combined sources
Helixi203 – 2053Combined sources
Helixi211 – 2133Combined sources
Helixi216 – 2194Combined sources
Turni222 – 2243Combined sources
Helixi227 – 2359Combined sources
Beta strandi242 – 2465Combined sources
Helixi249 – 2513Combined sources
Helixi252 – 2554Combined sources
Turni256 – 2583Combined sources
Beta strandi259 – 2613Combined sources
Beta strandi263 – 2664Combined sources
Beta strandi270 – 2789Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 8-281.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WYV8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni129 – 1335S-adenosyl-L-methionine binding
Regioni197 – 2004Substrate binding

Sequence similaritiesi

Phylogenomic databases

InParanoidiQ9WYV8.
KOiK02493.
OMAiEIGEDQV.
OrthoDBiEOG68Q0SZ.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_02126. RF_methyltr_PrmC.
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. NC_023151.1.
YP_008990542.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD35573; AAD35573; TM_0488.
GeneIDi18092302.
897528.
KEGGitma:TM0488.
tmi:THEMA_02230.
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. NC_023151.1.
YP_008990542.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 8-281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM0488.

Protocols and materials databases

DNASUi897528.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35573; AAD35573; TM_0488.
GeneIDi18092302.
897528.
KEGGitma:TM0488.
tmi:THEMA_02230.
PATRICi23935881. VBITheMar51294_0495.

Phylogenomic databases

InParanoidiQ9WYV8.
KOiK02493.
OMAiEIGEDQV.
OrthoDBiEOG68Q0SZ.

Miscellaneous databases

EvolutionaryTraceiQ9WYV8.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_02126. RF_methyltr_PrmC.
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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  2. "X-ray crystallographic studies of HemK from Thermotoga maritima, an N5-glutamine methyltransferase."
    Yoon H.J., Kang K.Y., Ahn H.J., Shim S.M., Ha J.Y., Lee S.K., Mikami B., Suh S.W.
    Mol. Cells 16:266-269(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  3. "Structures along the catalytic pathway of PrmC/HemK, an N5-glutamine AdoMet-dependent methyltransferase."
    Schubert H.L., Phillips J.D., Hill C.P.
    Biochemistry 42:5592-5599(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEXES WITH S-ADENOSYL-L-HOMOCYSTEINE; S-ADENOSYL-L-METHIONINE AND GLUTAMINE.
  4. "A novel mode of dimerization via formation of a glutamate anhydride crosslink in a protein crystal structure."
    Agarwal R., Burley S.K., Swaminathan S.
    Proteins 71:1038-1041(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-METHIONINE AND GLUTAMINE, SUBUNIT, GLUTAMATE ANHYDRIDE CROSS-LINK.
  5. "Crystal structure of N5-glutamine methyltransferase, HemK(EC 2.1.1.-) (TM0488) from Thermotoga maritima at 2.80 A resolution."
    Joint Center for Structural Genomics (JCSG)
    Submitted (JUL-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH S-ADENOSYL-L-METHIONINE.

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: February 4, 2015
This is version 97 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

External Data

Dasty 3

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 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.