Release factor glutamine methyltransferase

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Q9WYV8 (PRMC_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 73. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Release factor glutamine methyltransferase
Short name=RF MTase
EC=2.1.1.n16

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

Organism

Thermotoga maritima

Taxonomic identifier

2336 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga

Protein attributes

Sequence length	282 AA.
Sequence status	Complete.
Protein existence	Evidence 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 MF_02126
Catalytic activity	S-adenosyl-L-methionine + glutamine in release factor = S-adenosyl-L-homocysteine + N5-methylglutamine in release factor. HAMAP 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). HAMAP MF_02126
Sequence similarities	Belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily.

Ontologies

Keywords
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	nucleic acid binding Inferred from electronic annotation. Source: InterPro protein methyltransferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 282

282

Release factor glutamine methyltransferase HAMAP MF_02126

PRO_0000414548

Regions

Region

129 – 133

S-adenosyl-L-methionine binding HAMAP MF_02126

Region

197 – 200

Substrate binding HAMAP MF_02126

Sites

Binding site

151

S-adenosyl-L-methionine

Binding site

180

S-adenosyl-L-methionine

Binding site

197

S-adenosyl-L-methionine

Sequences

Sequence

Length

Mass (Da)

Tools

Q9WYV8 [UniParc].

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

282

31,609

        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' referencesShow '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. Fraser C.M. Nature 399:323-329(1999) [PubMed: 10360571] [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: 14651272] [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: 12741815] [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: 18247349] [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.

PIR

G72369.

RefSeq

NP_228298.1. NC_000853.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9WYV8.

SMR

Q9WYV8. Positions 8-281.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

897528.

GenomeReviews

Gene locus TM_0488 in contig AE000512_GR.

KEGG

tma:TM0488.

NMPDR

fig|243274.1.peg.482.

PATRIC

23935881. VBITheMar51294_0495.

TIGR

TM_0488.

Phylogenomic databases

HOGENOM

HBG732041.

OMA

FFLENHA.

PhylomeDB

Q9WYV8.

ProtClustDB

PRK09328.

Enzyme and pathway databases

BioCyc

TMAR243274:TM_0488-MONOMER.

Family and domain databases

HAMAP

MF_02126. RF_methyltr_PrmC.
[Tree]

InterPro

IPR002052. DNA_methylase_N6_adenine_CS.
IPR004556. Modification_methylase_HemK.
IPR019874. Release_fac_Glu-N5_MeTfrase.
IPR007848. Small_mtfrase.
[Graphical view]

K02493.

Pfam

PF05175. MTS. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00536. HemK_fam. 1 hit.
TIGR03534. RF_mod_PrmC. 1 hit.

ProtoNet

Search...

Entry information

Entry name

PRMC_THEMA

Accession

Primary (citable) accession number: Q9WYV8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 14, 2011
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents