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Protein

mRNA-capping enzyme subunit alpha

Gene

CGT1

Organism
Candida albicans (Yeast)
Status
Reviewed-Annotation score: Annotation score: 3 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei67 – 671N6-GMP-lysine intermediateSequence analysis

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

mRNA capping, mRNA processing

Keywords - Ligandi

GTP-binding, Nucleotide-binding

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:CGT1
OrganismiCandida albicans (Yeast)
Taxonomic identifieri5476 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida

Organism-specific databases

CGDiCAL0000174743. CGT1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 449449mRNA-capping enzyme subunit alphaPRO_0000210099Add
BLAST

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.

Structurei

Secondary structure

1
449
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 164Combined sources
Helixi19 – 3315Combined sources
Beta strandi43 – 475Combined sources
Helixi50 – 545Combined sources
Helixi56 – 594Combined sources
Beta strandi62 – 687Combined sources
Beta strandi70 – 8011Combined sources
Turni81 – 833Combined sources
Beta strandi84 – 918Combined sources
Beta strandi96 – 983Combined sources
Beta strandi112 – 1143Combined sources
Beta strandi119 – 13012Combined sources
Beta strandi133 – 1353Combined sources
Beta strandi138 – 14912Combined sources
Helixi159 – 16911Combined sources
Helixi171 – 18010Combined sources
Helixi182 – 1854Combined sources
Beta strandi193 – 1964Combined sources
Helixi202 – 2054Combined sources
Helixi206 – 2094Combined sources
Helixi212 – 2143Combined sources
Beta strandi219 – 22911Combined sources
Beta strandi233 – 24210Combined sources
Helixi245 – 2473Combined sources
Beta strandi250 – 2578Combined sources
Beta strandi259 – 2624Combined sources
Beta strandi274 – 2774Combined sources
Beta strandi283 – 2908Combined sources
Beta strandi296 – 3027Combined sources
Helixi306 – 3149Combined sources
Beta strandi315 – 3173Combined sources
Beta strandi323 – 3286Combined sources
Beta strandi330 – 3323Combined sources
Beta strandi335 – 3417Combined sources
Helixi351 – 36313Combined sources
Helixi367 – 38923Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P16X-ray2.70A/B2-395[»]
ProteinModelPortaliP78587.
SMRiP78587. Positions 1-390.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP78587.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi427 – 4359Poly-Gln

Sequence similaritiesi

Belongs to the eukaryotic GTase family.Curated

Phylogenomic databases

PhylomeDBiP78587.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
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.

P78587-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIQLEEREIP VIPGNKLDEE ETKELRLMVA ELLGRRNTGF PGSQPVSFER
60 70 80 90 100
RHLEETLMQK DYFVCEKTDG LRCLLFLIND PDKGEGVFLV TRENDYYFIP
110 120 130 140 150
NIHFPLSVNE TREKPTYHHG TLLDGELVLE NRNVSEPVLR YVIFDALAIH
160 170 180 190 200
GKCIIDRPLP KRLGYITENV MKPFDNFKKH NPDIVNSPEF PFKVGFKTML
210 220 230 240 250
TSYHADDVLS KMDKLFHASD GLIYTCAETP YVFGTDQTLL KWKPAEENTV
260 270 280 290 300
DFQLEFVFNE VQDPDLDERD PTSTYLDYDA KPNLIKLRVW QGSNVHTDFA
310 320 330 340 350
KLDLSDDDWE RLKALEQPLQ GRIAECRQST TKKGYWEMLR FRNDKSNGNH
360 370 380 390 400
ISVVEKILVS IKDGVKEKEV IEWCPKISRA WKKRENDRRQ KHFNGVARPA
410 420 430 440
SVSHEEPLRK KIKTESNGNG HQTPPRQEQQ QQSQQILNDI PTYEDSDDE
Length:449
Mass (Da):52,253
Last modified:May 1, 1997 - v1
Checksum:iD93F44BF112305BB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83180 Genomic DNA. Translation: BAA11833.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83180 Genomic DNA. Translation: BAA11833.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P16X-ray2.70A/B2-395[»]
ProteinModelPortaliP78587.
SMRiP78587. Positions 1-390.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

CGDiCAL0000174743. CGT1.

Phylogenomic databases

PhylomeDBiP78587.

Miscellaneous databases

EvolutionaryTraceiP78587.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
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_CANAX
AccessioniPrimary (citable) accession number: P78587
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: September 7, 2016
This is version 94 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.