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Q9WYV8

- PRMC_THEMA

UniProt

Q9WYV8 - PRMC_THEMA

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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: 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 – 2411
Turni25 – 284
Helixi32 – 4413
Helixi48 – 514
Beta strandi53 – 553
Helixi60 – 7415
Helixi79 – 835
Beta strandi85 – 884
Beta strandi91 – 944
Helixi106 – 12015
Beta strandi124 – 1296
Helixi134 – 1429
Beta strandi146 – 1527
Helixi154 – 16613
Beta strandi172 – 1798
Helixi182 – 1876
Turni188 – 1903
Beta strandi193 – 1964
Helixi203 – 2053
Helixi211 – 2133
Helixi216 – 2194
Turni222 – 2243
Helixi227 – 2359
Beta strandi242 – 2465
Helixi249 – 2513
Helixi252 – 2554
Turni256 – 2583
Beta strandi259 – 2613
Beta strandi263 – 2664
Beta strandi270 – 2789

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiLFEPPEA.
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-like.
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:
EMBL
GenBank
DDBJ
Links Updated
AE000512 Genomic DNA. Translation: AAD35573.1.
PIRiG72369.
RefSeqiNP_228298.1. NC_000853.1.
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:
EMBL
GenBank
DDBJ
Links Updated
AE000512 Genomic DNA. Translation: AAD35573.1 .
PIRi G72369.
RefSeqi NP_228298.1. NC_000853.1.
YP_008990542.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NV8 X-ray 2.20 A/B 1-282 [» ]
1NV9 X-ray 2.36 A 1-282 [» ]
1SG9 X-ray 2.30 A/B/C 1-282 [» ]
1VQ1 X-ray 2.80 A/B 1-282 [» ]
ProteinModelPortali Q9WYV8.
SMRi Q9WYV8. Positions 8-281.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243274.TM0488.

Protocols and materials databases

DNASUi 897528.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD35573 ; AAD35573 ; TM_0488 .
GeneIDi 18092302.
897528.
KEGGi tma:TM0488.
tmi:THEMA_02230.
PATRICi 23935881. VBITheMar51294_0495.

Phylogenomic databases

InParanoidi Q9WYV8.
KOi K02493.
OMAi LFEPPEA.
OrthoDBi EOG68Q0SZ.

Miscellaneous databases

EvolutionaryTracei Q9WYV8.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
HAMAPi MF_02126. RF_methyltr_PrmC.
InterProi IPR002052. 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 ]
Pfami PF05175. MTS. 1 hit.
[Graphical view ]
SUPFAMi SSF53335. SSF53335. 1 hit.
TIGRFAMsi TIGR00536. hemK_fam. 1 hit.
TIGR03534. RF_mod_PrmC. 1 hit.
ProtoNeti Search...

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: October 29, 2014
This is version 94 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