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Q9CWQ0 (DPH5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Diphthine synthase

EC=2.1.1.98
Alternative name(s):
Diphthamide biosynthesis methyltransferase
Gene names
Name:Dph5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length281 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the trimethylation of the amino group of the modified target histidine residue in translation elongation factor 2 (EFE2), to form an intermediate called diphthine. The three successive methylation reactions represent the second step of diphthamide biosynthesis. Ref.5

Catalytic activity

3 S-adenosyl-L-methionine + 2-(3-carboxy-3-aminopropyl)-L-histidine-[translation elongation factor 2] = 3 S-adenosyl-L-homocysteine + 2-(3-carboxy-3-(trimethylammonio)propyl)-L-histidine-[translation elongation factor 2]. HAMAP-Rule MF_01084

Pathway

Protein modification; peptidyl-diphthamide biosynthesis. HAMAP-Rule MF_01084

Sequence similarities

Belongs to the diphthine synthase family.

Ontologies

Keywords
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpeptidyl-diphthamide biosynthetic process from peptidyl-histidine

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functiondiphthine synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 281281Diphthine synthase HAMAP-Rule MF_01084
PRO_0000156134

Regions

Region112 – 1132S-adenosyl-L-methionine binding By similarity

Sites

Binding site91S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site841S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity
Binding site871S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site1631S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity
Binding site2251S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity
Binding site2501S-adenosyl-L-methionine; via carbonyl oxygen By similarity

Experimental info

Sequence conflict161T → K in BAB26968. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9CWQ0 [UniParc].

Last modified October 3, 2012. Version 2.
Checksum: 28AEC5E6ABBC3C1F

FASTA28131,218
        10         20         30         40         50         60 
MLYLIGLGLG DAKDITVKGL EVVRRCSRVY LEAYTSVLTV GKEALEEFYG RKLILADREE 

        70         80         90        100        110        120 
VEQEADNIFK DADVSDVAFL VVGDPFGATT HSDLILRATK LGIPYQVIHN ASIMNAVGCC 

       130        140        150        160        170        180 
GLQLYRFGET VSIVFWTDTW RPESFFDKVK RNRANGMHTL CLLDIKVKEQ SLENLIRGRK 

       190        200        210        220        230        240 
IYEPPRYMSV NQAAQQLLEI VQNHRARGEE PAITEETLCV GLARVGAEDQ KIAAGTLQQM 

       250        260        270        280 
CTVSLGEPLH SLVITGGNLH PLEMEMLSLF SIPESQSTDG L 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryonic stem cell.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Olfactory epithelium.
[5]"Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2."
Liu S., Milne G.T., Kuremsky J.G., Fink G.R., Leppla S.H.
Mol. Cell. Biol. 24:9487-9497(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK010475 mRNA. Translation: BAB26968.1.
AC131113 Genomic DNA. No translation available.
CH466532 Genomic DNA. Translation: EDL12395.1.
BC060372 mRNA. Translation: AAH60372.1.
CCDSCCDS17782.1.
RefSeqNP_081469.2. NM_027193.2.
UniGeneMm.5915.

3D structure databases

ProteinModelPortalQ9CWQ0.
SMRQ9CWQ0. Positions 1-270.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9CWQ0.

Proteomic databases

PaxDbQ9CWQ0.
PRIDEQ9CWQ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000043342; ENSMUSP00000043730; ENSMUSG00000033554.
GeneID69740.
KEGGmmu:69740.
UCSCuc008rbs.1. mouse.

Organism-specific databases

CTD51611.
MGIMGI:1916990. Dph5.

Phylogenomic databases

eggNOGCOG1798.
GeneTreeENSGT00390000010568.
HOGENOMHOG000205302.
HOVERGENHBG044879.
InParanoidQ9CWQ0.
KOK00586.
OMAANCPAVA.
TreeFamTF105603.

Enzyme and pathway databases

UniPathwayUPA00559.

Gene expression databases

ArrayExpressQ9CWQ0.
CleanExMM_DPH5.
GenevestigatorQ9CWQ0.

Family and domain databases

Gene3D3.30.950.10. 1 hit.
3.40.1010.10. 1 hit.
HAMAPMF_01084. Diphthine_synth.
InterProIPR000878. 4pyrrol_Mease.
IPR014777. 4pyrrole_Mease_sub1.
IPR014776. 4pyrrole_Mease_sub2.
IPR004551. Dphthn_synthase.
[Graphical view]
PfamPF00590. TP_methylase. 1 hit.
[Graphical view]
PIRSFPIRSF036432. Diphthine_synth. 1 hit.
SUPFAMSSF53790. SSF53790. 1 hit.
TIGRFAMsTIGR00522. dph5. 1 hit.
ProtoNetSearch...

Other

NextBio330226.
PROQ9CWQ0.
SOURCESearch...

Entry information

Entry nameDPH5_MOUSE
AccessionPrimary (citable) accession number: Q9CWQ0
Secondary accession number(s): Q6PAC5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: October 3, 2012
Last modified: July 9, 2014
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot