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Protein

Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase

Gene

PAPS

Organism
Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Displays methyltransferase, positive regulation of the poly(A) polymerase and transcription elongation activities. Involved in the modification of both mRNA ends and in intermediate and late gene positive transcription elongation. At the mRNAs 5' end, methylates the ribose 2' OH group of the first transcribed nucleotide, thereby producing a 2'-O-methylpurine cap. At the 3' end, functions as a processivity factor which stimulates the activity of the viral poly(A) polymerase VP55 that creates mRNA's poly(A) tail. In the presence of VP39, VP55 does not dissociate from the RNA allowing tail elongation to around 250 adenylates.3 Publications

Catalytic activityi

S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(purine-ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-[mRNA].

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei22mRNA cap1
Binding sitei39S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication1
Binding sitei66S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication1
Binding sitei68S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1 Publication1
Binding sitei72S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation1 Publication1
Binding sitei95S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication1
Binding sitei97S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication1
Binding sitei116S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygenPROSITE-ProRule annotation1 Publication1
Binding sitei138S-adenosyl-L-methioninePROSITE-ProRule annotation1 Publication1
Active sitei175For methyltransferase activity1 Publication1
Binding sitei182mRNA cap1
Binding sitei233mRNA cap1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Elongation factor, Methyltransferase, Transferase

Keywords - Biological processi

mRNA capping, mRNA processing, Protein biosynthesis, Transcription

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.57. 6591.

Names & Taxonomyi

Protein namesi
Recommended name:
Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase (EC:2.1.1.57)
Alternative name(s):
Poly(A) polymerase regulatory subunit
Poly(A) polymerase small subunit
Short name:
PAP-S
VP39
Gene namesi
Name:PAPS
Ordered Locus Names:VACWR095
ORF Names:J3R
OrganismiVaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Taxonomic identifieri10254 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stagePoxviridaeChordopoxvirinaeOrthopoxvirusVaccinia virus
Virus hostiBos taurus (Bovine) [TaxID: 9913]
Proteomesi
  • UP000000344 Componenti: Genome

Subcellular locationi

  • Virion Curated

  • Note: Localizes to the virion core.Curated

GO - Cellular componenti

  • virion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi56H → R: Complete loss of poly(A) polymerase stimulatory activity; when associated with S-58. 1 Publication1
Mutagenesisi58I → S: Complete loss of poly(A) polymerase stimulatory activity; when associated with R-56. 1 Publication1
Mutagenesisi96G → D: Complete loss of elongation factor activity. 1 Publication1
Mutagenesisi175K → R: Complete loss of methyltransferase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000991121 – 333Cap-specific mRNA (nucleoside-2'-O-)-methyltransferaseAdd BLAST333

Interactioni

Subunit structurei

Methyltransferase activity: Monomer, poly(A) polymerase activity: Heterodimer composed of a catalytic component, VP55, and a processivity factor, VP39. Interacts with Rap94 and NPH-I; these interactions might help linking transcription to capping and polyadenylation.6 Publications

Protein-protein interaction databases

DIPiDIP-48310N.

Structurei

Secondary structure

1333
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 15Combined sources3
Helixi24 – 28Combined sources5
Helixi37 – 55Combined sources19
Turni58 – 61Combined sources4
Beta strandi63 – 68Combined sources6
Helixi73 – 84Combined sources12
Beta strandi90 – 97Combined sources8
Helixi101 – 103Combined sources3
Beta strandi109 – 113Combined sources5
Helixi118 – 128Combined sources11
Beta strandi133 – 137Combined sources5
Helixi150 – 167Combined sources18
Beta strandi170 – 176Combined sources7
Helixi181 – 183Combined sources3
Beta strandi188 – 191Combined sources4
Beta strandi194 – 196Combined sources3
Beta strandi208 – 213Combined sources6
Beta strandi215 – 217Combined sources3
Beta strandi221 – 224Combined sources4
Helixi226 – 241Combined sources16
Helixi243 – 245Combined sources3
Beta strandi246 – 248Combined sources3
Beta strandi253 – 255Combined sources3
Helixi258 – 267Combined sources10
Helixi279 – 294Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AV6X-ray2.80A3-297[»]
1B42X-ray2.20A1-297[»]
1BKYX-ray2.00A1-307[»]
1EAMX-ray2.00A1-307[»]
1EQAX-ray2.20A1-297[»]
1JSZX-ray1.93A1-307[»]
1JTEX-ray2.00A1-307[»]
1JTFX-ray2.60A1-307[»]
1P39X-ray2.00A1-307[»]
1V39X-ray1.80A1-307[»]
1VP3X-ray1.90A1-333[»]
1VP9X-ray1.95A1-307[»]
1VPTX-ray1.80A1-333[»]
2GA9X-ray2.30A1-297[»]
2GAFX-ray2.40A1-297[»]
2VP3X-ray1.95A1-307[»]
3ER8X-ray3.18A/B1-297[»]
3ER9X-ray2.06A1-297[»]
3ERCX-ray3.21A/B1-297[»]
3MAGX-ray1.80A1-307[»]
3MCTX-ray2.00A1-297[»]
4DCGX-ray1.80A1-307[»]
ProteinModelPortaliP07617.
SMRiP07617.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07617.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni169 – 333Binding to Rap94Add BLAST165
Regioni169 – 249Binding to NPH-IAdd BLAST81
Regioni177 – 180mRNA cap binding4
Regioni205 – 207mRNA cap binding3

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Poxvirus/kinetoplastid 2'-O-MTase family.PROSITE-ProRule annotation

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR000176. mRNA_MeTrfase-like.
IPR025804. Pox/kineto_cap_MeTfrase.
IPR030375. Poxvir_cap_MeTfrase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01358. PARP_regulatory. 1 hit.
[Graphical view]
PIRSFiPIRSF003726. PolA_polym_reg_poxV. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51612. SAM_MT_2O_PK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07617-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVVSLDKPF MYFEEIDNEL DYEPESANEV AKKLPYQGQL KLLLGELFFL
60 70 80 90 100
SKLQRHGILD GATVVYIGSA PGTHIRYLRD HFYNLGVIIK WMLIDGRHHD
110 120 130 140 150
PILNGLRDVT LVTRFVDEEY LRSIKKQLHP SKIILISDVR SKRGGNEPST
160 170 180 190 200
ADLLSNYALQ NVMISILNPV ASSLKWRCPF PDQWIKDFYI PHGNKMLQPF
210 220 230 240 250
APSYSAEMRL LSIYTGENMR LTRVTKSDAV NYEKKMYYLN KIVRNKVVVN
260 270 280 290 300
FDYPNQEYDY FHMYFMLRTV YCNKTFPTTK AKVLFLQQSI FRFLNIPTTS
310 320 330
TEKVSHEPIQ RKISSKNSMS KNRNSKRSVR SNK
Length:333
Mass (Da):38,888
Last modified:April 1, 1988 - v1
Checksum:i55A299DA4AAE1AD4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01978 Genomic DNA. Translation: CAA26017.1.
AY243312 Genomic DNA. Translation: AAO89374.1.
PIRiH23092. QQVZF9.
RefSeqiYP_232977.1. NC_006998.1.

Genome annotation databases

GeneIDi3707551.
KEGGivg:3707551.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01978 Genomic DNA. Translation: CAA26017.1.
AY243312 Genomic DNA. Translation: AAO89374.1.
PIRiH23092. QQVZF9.
RefSeqiYP_232977.1. NC_006998.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AV6X-ray2.80A3-297[»]
1B42X-ray2.20A1-297[»]
1BKYX-ray2.00A1-307[»]
1EAMX-ray2.00A1-307[»]
1EQAX-ray2.20A1-297[»]
1JSZX-ray1.93A1-307[»]
1JTEX-ray2.00A1-307[»]
1JTFX-ray2.60A1-307[»]
1P39X-ray2.00A1-307[»]
1V39X-ray1.80A1-307[»]
1VP3X-ray1.90A1-333[»]
1VP9X-ray1.95A1-307[»]
1VPTX-ray1.80A1-333[»]
2GA9X-ray2.30A1-297[»]
2GAFX-ray2.40A1-297[»]
2VP3X-ray1.95A1-307[»]
3ER8X-ray3.18A/B1-297[»]
3ER9X-ray2.06A1-297[»]
3ERCX-ray3.21A/B1-297[»]
3MAGX-ray1.80A1-307[»]
3MCTX-ray2.00A1-297[»]
4DCGX-ray1.80A1-307[»]
ProteinModelPortaliP07617.
SMRiP07617.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48310N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3707551.
KEGGivg:3707551.

Enzyme and pathway databases

BRENDAi2.1.1.57. 6591.

Miscellaneous databases

EvolutionaryTraceiP07617.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR000176. mRNA_MeTrfase-like.
IPR025804. Pox/kineto_cap_MeTfrase.
IPR030375. Poxvir_cap_MeTfrase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF01358. PARP_regulatory. 1 hit.
[Graphical view]
PIRSFiPIRSF003726. PolA_polym_reg_poxV. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51612. SAM_MT_2O_PK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMCE_VACCW
AccessioniPrimary (citable) accession number: P07617
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: November 2, 2016
This is version 111 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, Direct protein sequencing, 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.