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Reviewed, UniProtKB/Swiss-Prot Q9VJQ4 (MCES_DROME)

Last modified January 19, 2010. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    mRNA cap guanine-N7 methyltransferase
    EC=2.1.1.56
Alternative name(s):
    mRNA (guanine-N(7)-)-methyltransferase
Gene names
Name: l(2)35Bd
ORF Names: CG3688
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

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Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC By similarity.

Catalytic activity

S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the methyltransferase superfamily. mRNA cap methyltransferase family.

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Ontologies

Keywords
   Biological processmRNA capping
mRNA processing
   Cellular componentNucleus
   LigandRNA-binding
S-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processmRNA capping

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentnucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionRNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA (guanine-N7-)-methyltransferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

CG1427-RCQ9VNE31EBI-88322,EBI-149620
Gint3Q9V8K81EBI-88322,EBI-93425

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427mRNA cap guanine-N7 methyltransferase
PRO_0000248330

Regions

Region112 – 1132mRNA cap binding By similarity

Sites

Binding site1161S-adenosyl-L-methionine By similarity
Binding site1431S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site1461mRNA cap By similarity
Binding site1521mRNA cap By similarity
Binding site1651S-adenosyl-L-methionine By similarity
Binding site1771mRNA cap By similarity
Binding site2021S-adenosyl-L-methionine By similarity
Binding site2251S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site2291mRNA cap By similarity
Binding site3141mRNA cap By similarity
Binding site4031mRNA cap By similarity

Amino acid modifications

Modified residue221Phosphoserine Ref.4
Modified residue241Phosphoserine Ref.4
Modified residue291Phosphoserine Ref.4
Modified residue461Phosphoserine Ref.4
Modified residue481Phosphoserine Ref.4

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Sequences

Sequence LengthMass (Da)Tools
Q9VJQ4-1 [UniParc].

Last modified October 1, 2002. Version 2.
Checksum: E585788C8868F2FB

FASTA42748,679
        10         20         30         40         50         60 
MSLNYEQNAA DEQFARAHKA VSLSDDEESE GQAETTSAPN QEPHVSKSPR EYYDEPGGKG 

        70         80         90        100        110        120 
NGSGADDQDE PETEAASGAA NTHVVAHHYN ELKEAGRKDR QKSKIFFMRN FNNWIKSQLI 

       130        140        150        160        170        180 
NEYMSQIKQN KRMGDALRVL DMCCGKGGDL LKWEKAAISH LICTDIAEVS VEQCQRRYQD 

       190        200        210        220        230        240 
ILQRSEKSKF ANKFTAEFFA CDSTLVRLRE RYKDPSLQLN LVSCQFAFHY CFESMAQADC 

       250        260        270        280        290        300 
MMRNAAECLK PGGFFIATMP DAYEIIRRLR AAGPDARRFG NDVYSIEFDC ETDPLPLFGA 

       310        320        330        340        350        360 
KYQFHLEGVV DCPEFLVHFP TLVKLGRKYG LQLLKRSTFA DYYKENLHHG RHLLQRMSGL 

       370        380        390        400        410        420 
ESVQPQRCEN DEEFAHVSNF QGAQRSRSVG TLSKSEWEAA TLYLVCAFKK CKNTWDTNGK 


PLFEFDD

« Hide

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References

« Hide 'large scale' references
[1]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract]
Cited for: GENOME REANNOTATION.
[3]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[4]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-24; SER-29; SER-46 AND SER-48, MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014134 Genomic DNA. Translation: AAF53430.2.
AY071407 mRNA. Translation: AAL49029.1.
RefSeqNP_523568.2.
UniGeneDm.6528

3D structure databases

HSSPHSSP built from PDB template 1RI5 based on UniProtKB Q8SR66.
SMRQ9VJQ4. Positions 104-412.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9VJQ4. 2 interactions.
STRINGQ9VJQ4.

Genome annotation databases

EnsemblFBtr0080696; FBpp0080257; FBgn0001974; Drosophila melanogaster. [Genome view]
GeneID34877.
KEGGdme:Dmel_CG3688.
NMPDRfig|7227.3.peg.2464.

Organism-specific databases

FlyBaseFBgn0001974. l(2)35Bd.

Phylogenomic databases

eggNOGinNOG08094.
InParanoidQ9VJQ4.
OMAKWRKGRI.
OrthoDBEOG9R241F.
PhylomeDBQ9VJQ4.

Enzyme and pathway databases

BRENDA2.1.1.56. 48.

Gene expression databases

BgeeQ9VJQ4.
GermOnlineCG3688. Drosophila melanogaster.

Family and domain databases

InterProIPR016899. mRNA_G-N7_MeTrfase.
IPR004971. Pox_MCEL.
[Graphical view]
PfamPF03291. Pox_MCEL. 1 hit.
[Graphical view]
PIRSFPIRSF028762. ABD1. 1 hit.
ProtoNetSearch...

Other Resources

NextBio790657.

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Entry information

Entry nameMCES_DROME
AccessionPrimary (citable) accession number: Q9VJQ4
Secondary accession number(s): Q9N6X4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: October 1, 2002
Last modified: January 19, 2010
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

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Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents