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Q9ZCB3 (RFTRM_RICPR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional methyltransferase

Including the following 2 domains:

  1. Release factor glutamine methyltransferase
    Short name=RF MTase
    EC=2.1.1.n16
    Alternative name(s):
    M.RprHemKP
    N5-glutamine methyltransferase PrmC
    Protein-(glutamine-N5) MTase PrmC
    Protein-glutamine N-methyltransferase PrmC
  2. tRNA (guanine-N(7)-)-methyltransferase
    EC=2.1.1.33
    Alternative name(s):
    tRNA (guanine(46)-N(7))-methyltransferase
    tRNA(m7G46)-methyltransferase
Gene names
Name:prmC/trmB
Synonyms:hemK
Ordered Locus Names:RP847
OrganismRickettsia prowazekii (strain Madrid E) [Reference proteome] [HAMAP]
Taxonomic identifier272947 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group ›

Protein attributes

Sequence length518 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_01057

Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA By similarity. HAMAP-Rule MF_01057

Catalytic activity

S-adenosyl-L-methionine + glutamine in release factor = S-adenosyl-L-homocysteine + N5-methylglutamine in release factor. HAMAP-Rule MF_01057

S-adenosyl-L-methionine + guanine46 in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine46 in tRNA. HAMAP-Rule MF_01057

Sequence similarities

In the N-terminal section; belongs to the protein N5-glutamine methyltransferase family. PrmC subfamily.

In the C-terminal section; belongs to the methyltransferase superfamily. TrmB family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 518518Bifunctional methyltransferase HAMAP-Rule MF_01057
PRO_0000157174

Regions

Region1 – 302302RF MTase HAMAP-Rule MF_01057
Region1 – 300300HemK HAMAP-Rule MF_01057
Region140 – 1445S-adenosyl-L-methionine binding By similarity
Region207 – 2104Substrate binding By similarity
Region301 – 518218tRNA (guanine-N(7)-)-methyltransferase HAMAP-Rule MF_01057
Region305 – 518214tRNA MTase HAMAP-Rule MF_01057

Sites

Binding site1631S-adenosyl-L-methionine By similarity
Binding site1921S-adenosyl-L-methionine By similarity
Binding site2071S-adenosyl-L-methionine By similarity
Binding site3471S-adenosyl-L-methionine By similarity
Binding site3721S-adenosyl-L-methionine By similarity
Binding site3991S-adenosyl-L-methionine By similarity
Binding site4211S-adenosyl-L-methionine By similarity
Binding site4251Substrate By similarity
Binding site4571Substrate Potential

Sequences

Sequence LengthMass (Da)Tools
Q9ZCB3 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: C66BB8DB273704A1

FASTA51859,564
        10         20         30         40         50         60 
MQYSIKQILS NANDKLNKIG INLPGLEARI LLQHVTNKPI EHLLIKLNEQ LSEAEIEAFE 

        70         80         90        100        110        120 
KLLERRLAHE PIAYIIGVKE FYSREFIVNK HVLIPRIDTE VLVDVVIGLV VSRNNLHMFS 

       130        140        150        160        170        180 
KLKSLDSVLT TQSYNILELG TGSGCIAISL LCELPNTNII ATDISVDAIK VAKSNSIKYN 

       190        200        210        220        230        240 
VTDRIQIIHS NWFEKLDKQK FDFIVSNPPY ISHTEKLKMA IETINYEPSI ALFAEEDGLE 

       250        260        270        280        290        300 
AYSIIAKNAK QFLKPNGKII LEIGFSQAAK VSKIFLNYGY NIDYIYRDLQ SHNRVIEISP 

       310        320        330        340        350        360 
INLNRSYARR IGKSLSKMQQ KLLDNELPKY LFSKEKFKSE KRKVFLEIGF GMGEHLINQA 

       370        380        390        400        410        420 
KINPDTLFIG VEVYLNGVAN VLKHSAQHNI TNFLLFPNNL DLILNDLPNN SLDGIYILFP 

       430        440        450        460        470        480 
DPWIKNKKKK KRIFNKERLK ILQNKLKNNG NLVFASDIEN YFYEAMALIR QNGNFEIIHN 

       490        500        510 
DDYLQPHDNY IITKYHQKAI NANRTAKFMI LQHALTDH

« Hide

References

[1]"The genome sequence of Rickettsia prowazekii and the origin of mitochondria."
Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G.
Nature 396:133-140(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Madrid E.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ235273 Genomic DNA. Translation: CAA15271.1.
PIRG71646.
RefSeqNP_221195.1. NC_000963.1.

3D structure databases

ProteinModelPortalQ9ZCB3.
ModBaseSearch...

Protein-protein interaction databases

STRING272947.RP847.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAA15271; CAA15271; CAA15271.
GeneID883464.
KEGGrpr:RP847.
PATRIC17902570. VBIRicPro72556_0885.

Phylogenomic databases

eggNOGCOG0220.
HOGENOMHOG000010896.
KOK02493.
OMAIGVEVYL.
ProtClustDBPRK01544.

Family and domain databases

HAMAPMF_01057. tRNA_methyltr_TrmB. Fused.
MF_02126. RF_methyltr_PrmC. Fused.
InterProIPR002052. DNA_methylase_N6_adenine_CS.
IPR004556. Modification_methylase_HemK.
IPR019874. Release_fac_Glu-N5_MeTfrase.
IPR007848. Small_mtfrase_dom.
IPR003358. tRNA_(Gua-N-7)_MeTrfase.
[Graphical view]
PfamPF02390. Methyltransf_4. 1 hit.
PF05175. MTS. 1 hit.
[Graphical view]
TIGRFAMsTIGR00536. hemK_fam. 1 hit.
TIGR03534. RF_mod_PrmC. 1 hit.
TIGR00091. TIGR00091. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRFTRM_RICPR
AccessionPrimary (citable) accession number: Q9ZCB3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: May 1, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Rickettsia prowazekii

Rickettsia prowazekii (strain Madrid E): entries and gene names

SIMILARITY comments

Index of protein domains and families

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