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:

MVA098R, ACAM3000_MVA_098

From

Vaccinia virus (strain Ankara) (VACV)

[TaxID: 126794]

Taxonomy

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

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein existence

3: Inferred from homology;

References

[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1006/viro.1998.9123; PubMed=9601507 [NCBI, ExPASy, EBI, Israel, Japan] Antoine G., Scheiflinger F., Dorner F., Falkner F.G.; "The complete genomic sequence of the modified vaccinia Ankara strain: comparison with other orthopoxviruses."; Virology 244:365-396(1998).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=Isolate Acambis 3000; Esposito J.J., Frace M., Sammons S.A., Olsen-Rasmussen M.S., Osborne J., Khristova M., Wohlhueter R.M.; Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.

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

U94848; AAB96511.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY603355; AAT10496.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T37374; T37374.

3D structure databases

ModBase

O57209.

Ontologies

GO:0004484;	Molecular function: mRNA guanylyltransferase activity (inferred from electronic annotation from EC).
GO:0004651;	Molecular function: polynucleotide 5'-phosphatase activity (inferred from electronic annotation from EC).
GO:0006370;	Biological process: mRNA capping (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR004971; Pox_MCEL.
Graphical view of domain structure.

Pfam

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

ProtoNet

O57209.

Other

UniRef

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

Keywords

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_0000210121`
`ACT_SITE`	`260 260`		`N6-GMP-lysine intermediate (Potential).`

Sequence information

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

Molecular weight: 96761 Da [This is the MW of the unprocessed precursor]

CRC64: BC7052355070FE2C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDANIVSSST 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 EKVPYDELIK ELTTLSRHIF MASPENVILS PPINAPIKTF 

       250        260        270        280        290        300 
MLPKQDIVGL DLENLYAVTK TDGIPITIRV TSKGLYCYFT 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 TKNFFELNRG AIKCEGLDVE DLLSYYVVYV 


FSKR

O57209 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