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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)DescriptionActionsGraphical viewLength
Active sitei67N6-GMP-lysine intermediateSequence analysis1

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)DescriptionActionsGraphical viewLength
ChainiPRO_00002100991 – 449mRNA-capping enzyme subunit alphaAdd BLAST449

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

1449
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi13 – 16Combined sources4
Helixi19 – 33Combined sources15
Beta strandi43 – 47Combined sources5
Helixi50 – 54Combined sources5
Helixi56 – 59Combined sources4
Beta strandi62 – 68Combined sources7
Beta strandi70 – 80Combined sources11
Turni81 – 83Combined sources3
Beta strandi84 – 91Combined sources8
Beta strandi96 – 98Combined sources3
Beta strandi112 – 114Combined sources3
Beta strandi119 – 130Combined sources12
Beta strandi133 – 135Combined sources3
Beta strandi138 – 149Combined sources12
Helixi159 – 169Combined sources11
Helixi171 – 180Combined sources10
Helixi182 – 185Combined sources4
Beta strandi193 – 196Combined sources4
Helixi202 – 205Combined sources4
Helixi206 – 209Combined sources4
Helixi212 – 214Combined sources3
Beta strandi219 – 229Combined sources11
Beta strandi233 – 242Combined sources10
Helixi245 – 247Combined sources3
Beta strandi250 – 257Combined sources8
Beta strandi259 – 262Combined sources4
Beta strandi274 – 277Combined sources4
Beta strandi283 – 290Combined sources8
Beta strandi296 – 302Combined sources7
Helixi306 – 314Combined sources9
Beta strandi315 – 317Combined sources3
Beta strandi323 – 328Combined sources6
Beta strandi330 – 332Combined sources3
Beta strandi335 – 341Combined sources7
Helixi351 – 363Combined sources13
Helixi367 – 389Combined sources23

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP78587.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi427 – 435Poly-Gln9

Sequence similaritiesi

Belongs to the eukaryotic GTase family.Curated

Phylogenomic databases

PhylomeDBiP78587.

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.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1P16X-ray2.70A/B2-395[»]
ProteinModelPortaliP78587.
SMRiP78587.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

CGDiCAL0000174743. CGT1.

Phylogenomic databases

PhylomeDBiP78587.

Miscellaneous databases

EvolutionaryTraceiP78587.

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_CANAX
AccessioniPrimary (citable) accession number: P78587
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: November 2, 2016
This is version 96 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.