Polynucleotide 5'-triphosphatase
     (EC 3.1.3.33)
     (mRNA 5'-triphosphatase)
     (TPase)
mRNA guanylyltransferase
     (EC 2.7.7.50)
     (GTP--RNA guanylyltransferase)
     (GTase)

Gene name

	OrderedLocusNames:	VACWR106
	ORFNames:	D1R

From

Vaccinia virus (strain Western Reserve / WR) (VACV)

[TaxID: 10254]

Taxonomy

Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae; Orthopoxvirus.

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0042-6822(86)90011-5; PubMed=3739227 [NCBI, ExPASy, EBI, Israel, Japan] Niles E.G., Condit R.C., Caro P., Davidson K., Matusick L., Seto J.; "Nucleotide sequence and genetic map of the 16-kb vaccinia virus HindIII D fragment."; Virology 153:96-112(1986).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J., Wohlhueter R.; "Sequencing of the coding region of Vaccinia-WR to an average 9-fold redundancy and an error rate of 0.16/10kb."; Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[3]	INTERACTION WITH SMALL SUBUNIT, AND PROTEIN SEQUENCE OF 1-20 AND 498-517. PubMed=2161527 [NCBI, ExPASy, EBI, Israel, Japan] Guo P., Moss B.; "Interaction and mutual stabilization of the two subunits of vaccinia virus mRNA capping enzyme coexpressed in Escherichia coli."; Proc. Natl. Acad. Sci. U.S.A. 87:4023-4027(1990).

Comments

FUNCTION: Catalyzes the first two reactions in the mRNA cap formation pathway.
CATALYTIC ACTIVITY: A 5'-phosphopolynucleotide + H₂O = a polynucleotide + phosphate.
CATALYTIC ACTIVITY: GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.
SUBUNIT: Heterodimer of a large and a small subunit.
SIMILARITY: Belongs to the viral GTase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M15058; AAA48253.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY243312; AAO89385.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A03872; QQVZ1.

RefSeq

YP_232988.1; -.

3D structure databases

PDB

2VDW; X-ray; 2.70 A; A/C/E/G=545-844.

[ExPASy / RCSB / EBI]

PDBsum

2VDW; -.

ModBase

P04298.

Family and domain databases

InterPro

IPR004971; Pox_MCEL.
Graphical view of domain structure.

Pfam

PF03291; Pox_MCEL; 1.
Pfam graphical view of domain structure.

BLOCKS

P04298.

Genome annotation databases

GeneID

3707562; -.

Other

ProtoNet

P04298.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Direct protein sequencing; Hydrolase; mRNA capping; mRNA processing; Multifunctional enzyme; Nucleotidyltransferase; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 844`	`844`	`mRNA-capping enzyme large subunit.`	`PRO_0000210124`
`ACT_SITE`	`260 260`		`N6-GMP-lysine intermediate (Potential).`

Sequence information

Length: 844 AA [This is the length of the unprocessed precursor]

Molecular weight: 96734 Da [This is the MW of the unprocessed precursor]

CRC64: 8B9FD3DE836FA6E7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDANVVSSST IATYIDALAK NASELEQRST AYEINNELEL VFIKPPLITL TNVVNISTIQ 

        70         80         90        100        110        120 
ESFIRFTVTN KEGVKIRTKI PLSKVHGLDV KNVQLVDAID NIVWEKKSLV TENRLHKECL 

       130        140        150        160        170        180 
LRLSTEERHI FLDYKKYGSS IRLELVNLIQ AKTKNFTIDF KLKYFLGSGA QSKSSLLHAI 

       190        200        210        220        230        240 
NHPKSRPNTS LEIEFTPRDN ETVPYDELIK ELTTLSRHIF MASPENVILS PPINAPIKTF 

       250        260        270        280        290        300 
MLPKQDIVGL DLENLYAVTK TDGIPITIRV TSNGLYCYFT HLGYIIRYPV KRIIDSEVVV 

       310        320        330        340        350        360 
FGEAVKDKNW TVYLIKLIEP VNAINDRLEE SKYVESKLVD ICDRIVFKSK KYEGPFTTTS 

       370        380        390        400        410        420 
EVVDMLSTYL PKQPEGVILF YSKGPKSNID FKIKKENTID QTANVVFRYM SSEPIIFGES 

       430        440        450        460        470        480 
SIFVEYKKFS NDKGFPKEYG SGKIVLYNGV NYLNNIYCLE YINTHNEVGI KSVVVPIKFI 

       490        500        510        520        530        540 
AEFLVNGEIL KPRIDKTMKY INSEDYYGNQ HNIIVEHLRD QSIKIGDIFN EDKLSDVGHQ 

       550        560        570        580        590        600 
YANNDKFRLN PEVSYFTNKR TRGPLGILSN YVKTLLISMY CSKTFLDDSN KRKVLAIDFG 

       610        620        630        640        650        660 
NGADLEKYFY GEIALLVATD PDADAIARGN ERYNKLNSGI KTKYYKFDYI QETIRSDTFV 

       670        680        690        700        710        720 
SSVREVFYFG KFNIIDWQFA IHYSFHPRHY ATVMNNLSEL TASGGKVLIT TMDGDKLSKL 

       730        740        750        760        770        780 
TDKKTFIIHK NLPSSENYMS VEKIADDRIV VYNPSTMSTP MTEYIIKKND IVRVFNEYGF 

       790        800        810        820        830        840 
VLVDNVDFAT IIERSKKFIN GASTMEDRPS TRNFFELNRG AIKCEGLDVE DLLSYYVVYV 


FSKR

P04298 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools