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Protein

mRNA-capping enzyme

Gene

A103R

Organism
Paramecium bursaria Chlorella virus 1 (PBCV-1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

mRNA capping. Transfers a GMP cap onto the end of mRNA that terminates with a 5'-diphosphate tail.

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei82N6-GMP-lysine intermediate1

GO - Molecular functioni

GO - Biological processi

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

BRENDAi2.7.7.50. 4540.

Names & Taxonomyi

Protein namesi
Recommended name:
mRNA-capping enzyme
Alternative name(s):
GTP--RNA guanylyltransferase
mRNA guanylyltransferase (EC:2.7.7.50)
Gene namesi
Ordered Locus Names:A103R
OrganismiParamecium bursaria Chlorella virus 1 (PBCV-1)
Taxonomic identifieri10506 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePhycodnaviridaeChlorovirus
Virus hostiChlorella [TaxID: 114049]
Proteomesi
  • UP000000862 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002101071 – 330mRNA-capping enzymeAdd BLAST330

Proteomic databases

PRIDEiQ84424.

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1330
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 21Combined sources8
Beta strandi24 – 31Combined sources8
Helixi33 – 46Combined sources14
Beta strandi57 – 63Combined sources7
Helixi66 – 68Combined sources3
Helixi69 – 74Combined sources6
Beta strandi77 – 83Combined sources7
Beta strandi85 – 95Combined sources11
Beta strandi98 – 104Combined sources7
Beta strandi110 – 112Combined sources3
Helixi122 – 124Combined sources3
Beta strandi126 – 135Combined sources10
Turni136 – 139Combined sources4
Beta strandi140 – 151Combined sources12
Helixi161 – 172Combined sources12
Beta strandi181 – 187Combined sources7
Helixi196 – 209Combined sources14
Beta strandi212 – 222Combined sources11
Beta strandi227 – 235Combined sources9
Beta strandi243 – 247Combined sources5
Turni250 – 252Combined sources3
Beta strandi254 – 257Combined sources4
Turni259 – 261Combined sources3
Beta strandi264 – 266Combined sources3
Beta strandi279 – 285Combined sources7
Beta strandi288 – 294Combined sources7
Helixi304 – 316Combined sources13
Helixi320 – 323Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CKMX-ray2.50A/B1-330[»]
1CKNX-ray2.50A/B1-330[»]
1CKOX-ray3.10A1-330[»]
ProteinModelPortaliQ84424.
SMRiQ84424.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ84424.

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic GTase family.Curated

Phylogenomic databases

KOiK13917.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q84424-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVPPTINTGK NITTERAVLT LNGLQIKLHK VVGESRDDIV AKMKDLAMDD
60 70 80 90 100
HKFPRLPGPN PVSIERKDFE KLKQNKYVVS EKTDGIRFMM FFTRVFGFKV
110 120 130 140 150
CTIIDRAMTV YLLPFKNIPR VLFQGSIFDG ELCVDIVEKK FAFVLFDAVV
160 170 180 190 200
VSGVTVSQMD LASRFFAMKR SLKEFKNVPE DPAILRYKEW IPLEHPTIIK
210 220 230 240 250
DHLKKANAIY HTDGLIIMSV DEPVIYGRNF NLFKLKPGTH HTIDFIIMSE
260 270 280 290 300
DGTIGIFDPN LRKNVPVGKL DGYYNKGSIV ECGFADGTWK YIQGRSDKNQ
310 320 330
ANDRLTYEKT LLNIEENITI DELLDLFKWE
Length:330
Mass (Da):37,832
Last modified:November 1, 1996 - v1
Checksum:i6AF8A404710812D9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JF411744 Genomic DNA. Translation: AAC96471.1.
PIRiT17593.
RefSeqiNP_048451.1. NC_000852.5.

Genome annotation databases

GeneIDi918242.
KEGGivg:918242.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
JF411744 Genomic DNA. Translation: AAC96471.1.
PIRiT17593.
RefSeqiNP_048451.1. NC_000852.5.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CKMX-ray2.50A/B1-330[»]
1CKNX-ray2.50A/B1-330[»]
1CKOX-ray3.10A1-330[»]
ProteinModelPortaliQ84424.
SMRiQ84424.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ84424.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi918242.
KEGGivg:918242.

Phylogenomic databases

KOiK13917.

Enzyme and pathway databases

BRENDAi2.7.7.50. 4540.

Miscellaneous databases

EvolutionaryTraceiQ84424.

Family and domain databases

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

Entry informationi

Entry nameiMCE_PBCV1
AccessioniPrimary (citable) accession number: Q84424
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral 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

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.