Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

mRNA-capping enzyme subunit alpha

Gene

ceg1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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 (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei67N6-GMP-lysine intermediateBy similarity1

GO - Molecular functioni

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

GO - Biological processi

  • 7-methylguanosine mRNA capping Source: PomBase
  • 7-methylguanosine RNA capping Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

mRNA capping, mRNA processing

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-72086. mRNA Capping.
R-SPO-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
Synonyms:pce1
ORF Names:SPBC2F12.08c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC2F12.08c.
PomBaseiSPBC2F12.08c. ceg1.

Subcellular locationi

GO - Cellular componenti

  • mRNA cap methyltransferase complex Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi67K → A: Loss of function. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002101041 – 402mRNA-capping enzyme subunit alphaAdd BLAST402

Proteomic databases

MaxQBiP40997.
PRIDEiP40997.

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.By similarity

Protein-protein interaction databases

BioGridi276891. 3 interactors.
MINTiMINT-4689944.

Structurei

Secondary structure

1402
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 7Combined sources3
Beta strandi14 – 17Combined sources4
Helixi20 – 34Combined sources15
Beta strandi38 – 40Combined sources3
Beta strandi43 – 48Combined sources6
Helixi53 – 59Combined sources7
Beta strandi62 – 79Combined sources18
Beta strandi81 – 85Combined sources5
Beta strandi86 – 92Combined sources7
Beta strandi98 – 101Combined sources4
Beta strandi112 – 114Combined sources3
Beta strandi120 – 131Combined sources12
Helixi133 – 135Combined sources3
Beta strandi137 – 149Combined sources13
Helixi154 – 156Combined sources3
Helixi159 – 169Combined sources11
Helixi171 – 179Combined sources9
Helixi182 – 185Combined sources4
Beta strandi189 – 194Combined sources6
Beta strandi197 – 199Combined sources3
Helixi203 – 208Combined sources6
Helixi211 – 213Combined sources3
Beta strandi218 – 228Combined sources11
Beta strandi232 – 241Combined sources10
Helixi244 – 246Combined sources3
Beta strandi249 – 256Combined sources8
Beta strandi261 – 263Combined sources3
Beta strandi272 – 280Combined sources9
Beta strandi283 – 290Combined sources8
Helixi294 – 303Combined sources10
Beta strandi308 – 316Combined sources9
Beta strandi322 – 327Combined sources6
Helixi337 – 348Combined sources12
Helixi353 – 358Combined sources6
Helixi360 – 370Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4PZ6X-ray2.41A/B1-402[»]
4PZ7X-ray2.11A/B1-402[»]
4PZ8X-ray3.10A1-402[»]
ProteinModelPortaliP40997.
SMRiP40997.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic GTase family.Curated

Phylogenomic databases

HOGENOMiHOG000162728.
InParanoidiP40997.
KOiK00987.
OMAiYLIDRHN.
OrthoDBiEOG092C2LUY.
PhylomeDBiP40997.

Family and domain databases

InterProiIPR001339. mRNA_cap_enzyme.
IPR013846. mRNA_cap_enzyme_C.
IPR017075. mRNA_capping_enz_asu.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamiPF03919. mRNA_cap_C. 1 hit.
PF01331. mRNA_cap_enzyme. 1 hit.
[Graphical view]
PIRSFiPIRSF036959. mRNA_cap_alpha. 1 hit.
SUPFAMiSSF50249. SSF50249. 1 hit.

Sequencei

Sequence statusi: Complete.

P40997-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPSEKDIEE VSVPGVLAPR DDVRVLKTRI AKLLGTSPDT FPGSQPVSFS
60 70 80 90 100
KKHLQALKEK NYFVCEKSDG IRCLLYMTEH PRYENRPSVY LFDRKMNFYH
110 120 130 140 150
VEKIFYPVEN DKSGKKYHVD TLLDGELVLD IYPGGKKQLR YLVFDCLACD
160 170 180 190 200
GIVYMSRLLD KRLGIFAKSI QKPLDEYTKT HMRETAIFPF LTSLKKMELG
210 220 230 240 250
HGILKLFNEV IPRLRHGNDG LIFTCTETPY VSGTDQSLLK WKPKEMNTID
260 270 280 290 300
FMLKLEFAQP EEGDIDYSAM PEFQLGVWEG RNMYSFFAFM YVDEKEWEKL
310 320 330 340 350
KSFNVPLSER IVECYLDDEN RWRFLRFRDD KRDANHISTV KSVLQSIEDG
360 370 380 390 400
VSKEDLLKEM PIIREAYYNR KKPSVTKRKL DETSNDDAPA IKKVAKESEK

EI
Length:402
Mass (Da):46,875
Last modified:February 1, 1995 - v1
Checksum:i76B1E2052DABB974
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16143 Genomic DNA. Translation: AAA64996.1.
U18811 Genomic DNA. Translation: AAA58715.1.
CU329671 Genomic DNA. Translation: CAB10156.1.
PIRiT40133.
RefSeqiNP_595708.1. NM_001021605.2.

Genome annotation databases

EnsemblFungiiSPBC2F12.08c.1; SPBC2F12.08c.1:pep; SPBC2F12.08c.
GeneIDi2540362.
KEGGispo:SPBC2F12.08c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16143 Genomic DNA. Translation: AAA64996.1.
U18811 Genomic DNA. Translation: AAA58715.1.
CU329671 Genomic DNA. Translation: CAB10156.1.
PIRiT40133.
RefSeqiNP_595708.1. NM_001021605.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4PZ6X-ray2.41A/B1-402[»]
4PZ7X-ray2.11A/B1-402[»]
4PZ8X-ray3.10A1-402[»]
ProteinModelPortaliP40997.
SMRiP40997.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276891. 3 interactors.
MINTiMINT-4689944.

Proteomic databases

MaxQBiP40997.
PRIDEiP40997.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC2F12.08c.1; SPBC2F12.08c.1:pep; SPBC2F12.08c.
GeneIDi2540362.
KEGGispo:SPBC2F12.08c.

Organism-specific databases

EuPathDBiFungiDB:SPBC2F12.08c.
PomBaseiSPBC2F12.08c. ceg1.

Phylogenomic databases

HOGENOMiHOG000162728.
InParanoidiP40997.
KOiK00987.
OMAiYLIDRHN.
OrthoDBiEOG092C2LUY.
PhylomeDBiP40997.

Enzyme and pathway databases

ReactomeiR-SPO-72086. mRNA Capping.
R-SPO-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Miscellaneous databases

PROiP40997.

Family and domain databases

InterProiIPR001339. mRNA_cap_enzyme.
IPR013846. mRNA_cap_enzyme_C.
IPR017075. mRNA_capping_enz_asu.
IPR012340. NA-bd_OB-fold.
[Graphical view]
PfamiPF03919. mRNA_cap_C. 1 hit.
PF01331. mRNA_cap_enzyme. 1 hit.
[Graphical view]
PIRSFiPIRSF036959. mRNA_cap_alpha. 1 hit.
SUPFAMiSSF50249. SSF50249. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMCE1_SCHPO
AccessioniPrimary (citable) accession number: P40997
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 30, 2016
This is version 122 of the entry and version 1 of the sequence. [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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.