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Protein

mRNA-capping enzyme subunit alpha

Gene

CEG1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Second step of mRNA capping. Transfer of the GMP moiety of GTP to the 5'-end of RNA via an enzyme-GMP covalent reaction intermediate.

Miscellaneous

Present with 279 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.

Cofactori

a divalent metal cationNote: Divalent metal ions.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei70N6-GMP-lysine intermediate1 Publication1

GO - Molecular functioni

  • GTP binding Source: UniProtKB-KW
  • mRNA guanylyltransferase activity Source: SGD

GO - Biological processi

Keywordsi

Molecular functionNucleotidyltransferase, Transferase
Biological processmRNA capping, mRNA processing
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:G3O-30626-MONOMER
YEAST:G3O-30626-MONOMER
ReactomeiR-SCE-72086 mRNA Capping
R-SCE-77075 RNA Pol II CTD phosphorylation and interaction with CE

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA-capping enzyme subunit alpha
Alternative name(s):
GTP--RNA guanylyltransferase
Short name:
GTase
mRNA guanylyltransferase (EC:2.7.7.50)
Gene namesi
Name:CEG1
Ordered Locus Names:YGL130W
ORF Names:G2853
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL130W
SGDiS000003098 CEG1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi57E → A: No effect. 1 Publication1
Mutagenesisi58E → A: No effect. 1 Publication1
Mutagenesisi59K → A, T, S or R: No effect. 1 Publication1
Mutagenesisi66Y → A: Temperature-sensitive. 1 Publication1
Mutagenesisi70K → A, R, M, I or T: Lethal. 1 Publication1
Mutagenesisi71T → A: No effect. 1 Publication1
Mutagenesisi72D → A: No effect. 1 Publication1
Mutagenesisi73G → A: Lethal. 1 Publication1
Mutagenesisi95D → A: Temperature-sensitive. 1 Publication1
Mutagenesisi96R → A: Temperature-sensitive. 1 Publication1
Mutagenesisi97E → A: Temperature-sensitive. 1 Publication1
Mutagenesisi107 – 109RFP → AAA: Reduced growth at 25 degrees and lethal at 37 degrees. 1 Publication3
Mutagenesisi114K → A: No effect. 1 Publication1
Mutagenesisi115K → A: No effect. 1 Publication1
Mutagenesisi116K → A: No effect. 1 Publication1
Mutagenesisi117E → A: No effect. 1 Publication1
Mutagenesisi118E → A: No effect. 1 Publication1
Mutagenesisi129L → A: No effect. 1 Publication1
Mutagenesisi130D → A: Lethal. 1 Publication1
Mutagenesisi131G → A: Temperature-sensitive. 1 Publication1
Mutagenesisi132E → A: Lethal. 1 Publication1
Mutagenesisi134V → A: No effect. 1 Publication1
Mutagenesisi218D → A: No effect. 1 Publication1
Mutagenesisi219K → A: No effect. 1 Publication1
Mutagenesisi225D → A: Lethal. 1 Publication1
Mutagenesisi226G → A: Lethal. 1 Publication1
Mutagenesisi241K → A: No effect. 1 Publication1
Mutagenesisi242D → A: No effect. 1 Publication1
Mutagenesisi249K → A: Lethal. 1 Publication1
Mutagenesisi253E → A: No effect. 1 Publication1
Mutagenesisi254N → A: No effect. 1 Publication1
Mutagenesisi255T → A: Temperature-sensitive. 1 Publication1
Mutagenesisi257D → A: Lethal. 1 Publication1
Mutagenesisi274K → A: No effect. 1 Publication1
Mutagenesisi275D → A: No effect. 1 Publication1
Mutagenesisi276D → A: No effect. 1 Publication1
Mutagenesisi395E → A: No effect. 1 Publication1
Mutagenesisi396D → A: No effect. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002101061 – 459mRNA-capping enzyme subunit alphaAdd BLAST459

Proteomic databases

MaxQBiQ01159
PaxDbiQ01159
PRIDEiQ01159

PTM databases

iPTMnetiQ01159

Interactioni

Subunit structurei

The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an RNA 5'-triphosphatase.

Binary interactionsi

WithEntry#Exp.IntActNotes
CET1O132979EBI-10503,EBI-4473

Protein-protein interaction databases

BioGridi33121, 590 interactors
ComplexPortaliCPX-580 mRNA cap methyltransferase complex
DIPiDIP-2298N
IntActiQ01159, 27 interactors
MINTiQ01159
STRINGi4932.YGL130W

Structurei

Secondary structure

1459
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ01159
SMRiQ01159
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ01159

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic GTase family.Curated

Phylogenomic databases

GeneTreeiENSGT00530000063473
HOGENOMiHOG000162728
InParanoidiQ01159
KOiK00987
OMAiYYVCEKS
OrthoDBiEOG092C2LUY

Family and domain databases

InterProiView protein in InterPro
IPR001339 mRNA_cap_enzyme
IPR017075 mRNA_cap_enzyme_alpha
IPR013846 mRNA_cap_enzyme_C
IPR012340 NA-bd_OB-fold
PfamiView protein in Pfam
PF03919 mRNA_cap_C, 1 hit
PF01331 mRNA_cap_enzyme, 1 hit
PIRSFiPIRSF036959 mRNA_cap_alpha, 1 hit
SUPFAMiSSF50249 SSF50249, 1 hit

Sequencei

Sequence statusi: Complete.

Q01159-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVLAMESRVA PEIPGLIQPG NVTQDLKMMV CKLLNSPKPT KTFPGSQPVS
60 70 80 90 100
FQHSDVEEKL LAHDYYVCEK TDGLRVLMFI VINPVTGEQG CFMIDRENNY
110 120 130 140 150
YLVNGFRFPR LPQKKKEELL ETLQDGTLLD GELVIQTNPM TKLQELRYLM
160 170 180 190 200
FDCLAINGRC LTQSPTSSRL AHLGKEFFKP YFDLRAAYPN RCTTFPFKIS
210 220 230 240 250
MKHMDFSYQL VKVAKSLDKL PHLSDGLIFT PVKAPYTAGG KDSLLLKWKP
260 270 280 290 300
EQENTVDFKL ILDIPMVEDP SLPKDDRNRW YYNYDVKPVF SLYVWQGGAD
310 320 330 340 350
VNSRLKHFDQ PFDRKEFEIL ERTYRKFAEL SVSDEEWQNL KNLEQPLNGR
360 370 380 390 400
IVECAKNQET GAWEMLRFRD DKLNGNHTSV VQKVLESIND SVSLEDLEEI
410 420 430 440 450
VGDIKRCWDE RRANMAGGSG RPLPSQSQNA TLSTSKPVHS QPPSNDKEPK

YVDEDDWSD
Length:459
Mass (Da):52,764
Last modified:February 1, 1995 - v2
Checksum:iF7F5A3E59EEFA15F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti45G → S (PubMed:7500935).Curated1
Sequence conflicti300D → N (PubMed:7500935).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10263 Genomic DNA Translation: BAA01103.1
X87252 Genomic DNA Translation: CAA60705.1
Z72652 Genomic DNA Translation: CAA96839.1
BK006941 Genomic DNA Translation: DAA07979.1
PIRiS59731
RefSeqiNP_011385.3, NM_001180995.3

Genome annotation databases

EnsemblFungiiYGL130W; YGL130W; YGL130W
GeneIDi852747
KEGGisce:YGL130W

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10263 Genomic DNA Translation: BAA01103.1
X87252 Genomic DNA Translation: CAA60705.1
Z72652 Genomic DNA Translation: CAA96839.1
BK006941 Genomic DNA Translation: DAA07979.1
PIRiS59731
RefSeqiNP_011385.3, NM_001180995.3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KYHX-ray3.00C/D1-459[»]
ProteinModelPortaliQ01159
SMRiQ01159
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33121, 590 interactors
ComplexPortaliCPX-580 mRNA cap methyltransferase complex
DIPiDIP-2298N
IntActiQ01159, 27 interactors
MINTiQ01159
STRINGi4932.YGL130W

PTM databases

iPTMnetiQ01159

Proteomic databases

MaxQBiQ01159
PaxDbiQ01159
PRIDEiQ01159

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL130W; YGL130W; YGL130W
GeneIDi852747
KEGGisce:YGL130W

Organism-specific databases

EuPathDBiFungiDB:YGL130W
SGDiS000003098 CEG1

Phylogenomic databases

GeneTreeiENSGT00530000063473
HOGENOMiHOG000162728
InParanoidiQ01159
KOiK00987
OMAiYYVCEKS
OrthoDBiEOG092C2LUY

Enzyme and pathway databases

BioCyciMetaCyc:G3O-30626-MONOMER
YEAST:G3O-30626-MONOMER
ReactomeiR-SCE-72086 mRNA Capping
R-SCE-77075 RNA Pol II CTD phosphorylation and interaction with CE

Miscellaneous databases

EvolutionaryTraceiQ01159
PROiPR:Q01159

Family and domain databases

InterProiView protein in InterPro
IPR001339 mRNA_cap_enzyme
IPR017075 mRNA_cap_enzyme_alpha
IPR013846 mRNA_cap_enzyme_C
IPR012340 NA-bd_OB-fold
PfamiView protein in Pfam
PF03919 mRNA_cap_C, 1 hit
PF01331 mRNA_cap_enzyme, 1 hit
PIRSFiPIRSF036959 mRNA_cap_alpha, 1 hit
SUPFAMiSSF50249 SSF50249, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiMCE1_YEAST
AccessioniPrimary (citable) accession number: Q01159
Secondary accession number(s): D6VU18, Q9URD1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 1995
Last modified: September 12, 2018
This is version 174 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names
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Main funding by: National Institutes of Health

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