ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P25950


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name MCEL_RFVKA
Primary accession number P25950
Secondary accession numbers None
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on May 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 46)
Name and origin of the protein
Protein name mRNA-capping enzyme large subunit
Synonyms None
Includes 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
ORFNames: D3R
From
Rabbit fibroma virus (strain Kasza) (RFV) (Shope fibroma virus (strain Kasza)) [TaxID: 10272] 
Taxonomy Viruses; dsDNA viruses, no RNA stage; Poxviridae; Chordopoxvirinae; Leporipoxvirus.
Virus host Oryctolagus cuniculus (Rabbit) [TaxID: 9986]
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0042-6822(91)91009-6; PubMed=1649507 [NCBI, ExPASy, EBI, Israel, Japan]
Upton C., Stuart D., McFadden G.;
"Identification and DNA sequence of the large subunit of the capping enzyme from Shope fibroma virus.";
Virology 183:773-777(1991).
Comments
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
M63902; AAA47224.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A40478; QQVZRA.
3D structure databases
ModBase P25950.
Ontologies
GO
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.
IPR002035; VWF_A.
Graphical view of domain structure.
Pfam PF03291; Pox_MCEL; 1.
Pfam graphical view of domain structure.
PRINTS PR00453; VWFADOMAIN.
ProtoNet P25950.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Hydrolase; mRNA capping; mRNA processing; Multifunctional enzyme; Nucleotidyltransferase; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   836  836     mRNA-capping enzyme large subunit. PRO_0000210131
ACT_SITE   256   256        N6-GMP-lysine intermediate (Potential). 
Sequence information
Length: 836 AA [This is the length of the unprocessed precursor] Molecular weight: 97018 Da [This is the MW of the unprocessed precursor] CRC64: 7375FDA548AE1730 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDDSKKKRGT DYIEELILLY EDVPNPVQTD DMNHEVELTF IQPPVITLST LLPFATSQES 

        70         80         90        100        110        120 
YILFTVTNKG VKIRNRINLS KIHGLDLKNI QLVDSIDNII WEKKTLVKEH KIDSVALVKY 

       130        140        150        160        170        180 
STEEKYIFLD YKKYLSAIKL ELVNVVQVKV KHVTVDFKFK YFLGSGAQAK SSLLHVLNHP 

       190        200        210        220        230        240 
KSKPNPSLEF EIITTDEKID SASLRKELIA LFKLVFMASP SNIILDVVFK NPVQTILLKK 

       250        260        270        280        290        300 
NELPGIDLTN LYVTTKTDGV GVLITVTNKG IYCFFTHLQY TIRYDTTFES NESVTLYGEA 

       310        320        330        340        350        360 
VKQNNVWQIY LIKLITPKVS DRFKEKEYVE ERLQNICDRM TFKVKKYEGP FESHSEIIDL 

       370        380        390        400        410        420 
LTTYLPSQPE GVVLFYSDQR NQPDYKIKLD NTTDHMINII YRYMSSEPVI FGENSTFLEY 

       430        440        450        460        470        480 
KKFSDDKGFP KDYGTGKLML TDNVRYLNNI YCIAFTNVYE DVGIKNVVVP IKFISEFSAT 

       490        500        510        520        530        540 
GELIKPRIDK TFKYLYKEYY GNQYQIVVAH IRDQNIKIGD VLDEDKLSDV GQHYANDKYR 

       550        560        570        580        590        600 
LNPDVSYFTN KRTRGPLGIL SNYVKTLLIS LYCSKTFLDN SNKRKVLAID FGNGADLEKY 

       610        620        630        640        650        660 
FYGEISSLVA TDPDKEAIGR CIERYNSLNS GIKSKYYKFD YIQETIRSVT YVSSVREVFF 

       670        680        690        700        710        720 
FGKFDLVDWQ FAIHYSFHPK HYATVMNNLT ELTASGGKVL ITTMDGDLLS QLTDKKTFVI 

       730        740        750        760        770        780 
HKNLPSSENY MSVEKIHEDQ ILVYNPSSMS RPMQEYIVKR VNLTKIFSEY GFELIDCVHF 

       790        800        810        820        830 
DTIIERSKRF INSVSKMEER KSTKNFFELN REALKHEGTD IDDLLRYYIV YVFSKR 

P25950 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!