Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9WYV8 (PRMC_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Release factor glutamine methyltransferase

Short name=RF MTase
EC=2.1.1.297
Alternative name(s):
N5-glutamine methyltransferase PrmC
Protein-(glutamine-N5) MTase PrmC
Protein-glutamine N-methyltransferase PrmC
Gene names
Name:prmC
Ordered Locus Names:TM_0488
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif Probable. HAMAP-Rule MF_02126

Catalytic activity

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. HAMAP-Rule MF_02126

Subunit structure

Monomer and homodimer. Ref.4

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 (Ref.4).

Sequence similarities

Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 282282Release factor glutamine methyltransferase HAMAP-Rule MF_02126
PRO_0000414548

Regions

Region129 – 1335S-adenosyl-L-methionine binding HAMAP-Rule MF_02126
Region197 – 2004Substrate binding HAMAP-Rule MF_02126

Sites

Binding site1511S-adenosyl-L-methionine
Binding site1801S-adenosyl-L-methionine
Binding site1971S-adenosyl-L-methionine

Secondary structure

........................................................ 282
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9WYV8 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 68130302E620181B

FASTA28231,609
        10         20         30         40         50         60 
MDTRKNVSGA ERKIWSLIRD CSGKLEGVTE TSVLEVLLIV SRVLGIRKED LFLKDLGVSP 

        70         80         90        100        110        120 
TEEKRILELV EKRASGYPLH YILGEKEFMG LSFLVEEGVF VPRPETEELV ELALELIRKY 

       130        140        150        160        170        180 
GIKTVADIGT GSGAIGVSVA KFSDAIVFAT DVSSKAVEIA RKNAERHGVS DRFFVRKGEF 

       190        200        210        220        230        240 
LEPFKEKFAS IEMILSNPPY VKSSAHLPKD VLFEPPEALF GGEDGLDFYR EFFGRYDTSG 

       250        260        270        280 
KIVLMEIGED QVEELKKIVS DTVFLKDSAG KYRFLLLNRR SS 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD35573.1.
PIRG72369.
RefSeqNP_228298.1. NC_000853.1.
YP_008990542.1. NC_023151.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NV8X-ray2.20A/B1-282[»]
1NV9X-ray2.36A1-282[»]
1SG9X-ray2.30A/B/C1-282[»]
1VQ1X-ray2.80A/B1-282[»]
ProteinModelPortalQ9WYV8.
SMRQ9WYV8. Positions 8-281.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM0488.

Protocols and materials databases

DNASU897528.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD35573; AAD35573; TM_0488.
GeneID897528.
KEGGtma:TM0488.
tmi:THEMA_02230.
PATRIC23935881. VBITheMar51294_0495.

Phylogenomic databases

KOK02493.
OMALFEPPEA.
OrthoDBEOG68Q0SZ.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
HAMAPMF_02126. RF_methyltr_PrmC.
InterProIPR002052. DNA_methylase_N6_adenine_CS.
IPR004556. Modification_methylase_HemK.
IPR019874. Release_fac_Glu-N5_MeTfrase.
IPR029063. SAM-dependent_MTases-like.
IPR007848. Small_mtfrase_dom.
[Graphical view]
PfamPF05175. MTS. 1 hit.
[Graphical view]
SUPFAMSSF53335. SSF53335. 1 hit.
TIGRFAMsTIGR00536. hemK_fam. 1 hit.
TIGR03534. RF_mod_PrmC. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9WYV8.

Entry information

Entry namePRMC_THEMA
AccessionPrimary (citable) accession number: Q9WYV8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 14, 2011
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references