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Protein

mRNA-capping enzyme catalytic subunit

Gene

VACWR106

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

Catalytic subunit of the mRNA capping enzyme which catalyzes three enzymatic reactions: the 5' triphosphate end of the pre-mRNA is hydrolyzed to a diphosphate by RNA 5' triphosphatase; the diphosphate RNA end is capped with GMP by RNA guanylyltransferase and the GpppN cap is methylated by RNA (guanine-N7) methyltransferase. Heterodimeric mRNA capping enzyme catalyzes the linkage of a N7-methyl-guanosine moiety to the first transcribed nucleotide (cap 0 structure), whereas the polymerase associated VP39 is responsible for a second methylation at the 2'-O position of the ribose (cap 1 structure).
The heterodimeric enzyme is also involved in early viral gene transcription termination and intermediate viral gene transcription initiation. Early gene transcription termination requires the termination factor VTF, the DNA-dependent ATPase NPH-I and the Rap94 subunit of the viral RNA polymerase, as well as the presence of a specific termination motif. Binds, together with RAP94, to the termination motif 5'-UUUUUNU-3' in the nascent early mRNA.

Catalytic activityi

A 5'-phosphopolynucleotide + H2O = a polynucleotide + phosphate.
GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.
S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA.PROSITE-ProRule annotation

Cofactori

Mg2+2 Publications

Kineticsi

A-570 and A-763 mutants have 3-fold and 10-fold higher Km values for GpppA.

  1. KM=23 µM for GpppA1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi37 – 371Magnesium; Catalytic; for RNA triphosphatase activitySequence Analysis1 Publication
    Metal bindingi39 – 391Magnesium; Catalytic; for RNA triphosphatase activitySequence Analysis1 Publication
    Sitei77 – 771Essential for RNA triphosphatase activity
    Sitei107 – 1071Essential for RNA triphosphatase activity
    Sitei126 – 1261Essential for RNA triphosphatase activity
    Sitei159 – 1591Essential for RNA triphosphatase activity
    Sitei161 – 1611Essential for RNA triphosphatase activity
    Metal bindingi192 – 1921Magnesium; Catalytic; for RNA triphosphatase activitySequence Analysis1 Publication
    Metal bindingi194 – 1941Magnesium; Catalytic; for RNA triphosphatase activitySequence Analysis1 Publication
    Active sitei260 – 2601N6-GMP-lysine intermediateSequence Analysis
    Binding sitei573 – 5731S-adenosyl-L-methionine
    Binding sitei598 – 5981S-adenosyl-L-methionine; via carbonyl oxygen
    Sitei607 – 6071mRNA cap bindingPROSITE-ProRule annotation
    Binding sitei620 – 6201S-adenosyl-L-methionine
    Sitei632 – 6321mRNA cap bindingPROSITE-ProRule annotation
    Binding sitei682 – 6821mRNA capPROSITE-ProRule annotation
    Binding sitei763 – 7631mRNA capPROSITE-ProRule annotation
    Binding sitei836 – 8361mRNA capPROSITE-ProRule annotation

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Methyltransferase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    mRNA capping, mRNA processing, Transcription, Transcription regulation, Transcription termination

    Keywords - Ligandi

    GTP-binding, Metal-binding, Nucleotide-binding, RNA-binding, S-adenosyl-L-methionine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    mRNA-capping enzyme catalytic subunit
    Alternative name(s):
    Virus termination factor large subunit
    Short name:
    VTF large subunit
    mRNA-capping enzyme 97 kDa subunit
    mRNA-capping enzyme D1 subunit
    mRNA-capping enzyme large subunit
    Including the following 3 domains:
    Polynucleotide 5'-triphosphatase (EC:3.1.3.33)
    Alternative name(s):
    mRNA 5'-triphosphatase
    Short name:
    TPase
    mRNA guanylyltransferase (EC:2.7.7.50)
    Alternative name(s):
    GTP--RNA guanylyltransferase
    Short name:
    GTase
    mRNA (guanine-N(7)-)-methyltransferase (EC:2.1.1.56)
    Alternative name(s):
    mRNA cap methyltransferase
    Gene namesi
    Ordered Locus Names:VACWR106
    ORF Names:D1R
    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]
    ProteomesiUP000000344 Componenti: Genome

    Subcellular locationi

    • Virion Curated

    • Note: All the enzymes and other proteins required to synthesize early mRNAs are packaged within the virion core along with the DNA genome.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Virion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi77 – 793RTK → ATA: Almost complete loss of RNA triphosphatase activity, 70% loss of guanylyltransferase activity. 1 Publication
    Mutagenesisi107 – 1071K → A: Complete loss of triphosphatase activity, no effect on guanylyltransferase activity. 1 Publication
    Mutagenesisi126 – 1261E → A: Complete loss of triphosphatase activity, no effect on guanylyltransferase activity. 1 Publication
    Mutagenesisi135 – 1362KK → AA: 70% loss of RNA triphosphatase activity, 40% loss of guanylyltransferase activity. 1 Publication
    Mutagenesisi159 – 1591D → A: Complete loss of triphosphatase activity, no effect on guanylyltransferase activity. 1 Publication
    Mutagenesisi161 – 1611K → A: Complete loss of triphosphatase activity, no effect on guanylyltransferase activity. 1 Publication
    Mutagenesisi192 – 1943EIE → AIA: Complete loss of RNA triphosphatase activity, 50% loss of guanylyltransferase activity. 1 Publication
    Mutagenesisi260 – 2601K → A: Complete loss of guanylyltransferase activity, no effect on RNA triphosphatase activity. 1 Publication
    Mutagenesisi524 – 5263KIG → AIA: 50% loss of RNA triphosphatase activity and 40% loss of guanylyltransferase activity. 1 Publication
    Mutagenesisi570 – 5701N → A: Retains substantial methyltransferase activity in vitro; lethal in vivo. 1 Publication
    Mutagenesisi573 – 5731K → A: Complete loss of methyltransferase activity; lethal in vivo. 1 Publication
    Mutagenesisi607 – 6071K → A: Retains substantial methyltransferase activity in vitro; lethal in vivo. 1 Publication
    Mutagenesisi608 – 6081Y → A: Almost complete loss of methyltransferase activity; lethal in vivo. 1 Publication
    Mutagenesisi676 – 6761D → A: Complete loss of methyltransferase activity; lethal in vivo. 1 Publication
    Mutagenesisi679 – 6791F → A: Almost complete loss of methyltransferase activity; lethal in vivo. 1 Publication
    Mutagenesisi682 – 6821H → A: Complete loss of methyltransferase activity; lethal in vivo. 1 Publication
    Mutagenesisi763 – 7631E → A: Retains substantial methyltransferase activity in vitro; lethal in vivo. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 844844mRNA-capping enzyme catalytic subunitPRO_0000210124Add
    BLAST

    Interactioni

    Subunit structurei

    Heterodimer of a catalytic and a regulatory subunit. Intrinsic methyltransferase activity of the catalytic subunit is weak and needs to be stimulated 30- to 50-fold by the regulatory subunit, which is itself catalytically inert.1 Publication

    Protein-protein interaction databases

    DIPiDIP-60664N.

    Structurei

    Secondary structure

    1
    844
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 53Combined sources
    Helixi11 – 2414Combined sources
    Beta strandi36 – 449Combined sources
    Helixi48 – 547Combined sources
    Beta strandi58 – 6912Combined sources
    Beta strandi71 – 788Combined sources
    Helixi82 – 843Combined sources
    Beta strandi87 – 893Combined sources
    Helixi92 – 976Combined sources
    Beta strandi103 – 11614Combined sources
    Beta strandi119 – 13012Combined sources
    Helixi134 – 1407Combined sources
    Beta strandi142 – 15211Combined sources
    Beta strandi154 – 17017Combined sources
    Helixi175 – 1817Combined sources
    Beta strandi182 – 1854Combined sources
    Beta strandi188 – 1958Combined sources
    Beta strandi198 – 2003Combined sources
    Helixi205 – 22016Combined sources
    Beta strandi226 – 2294Combined sources
    Beta strandi236 – 2416Combined sources
    Helixi244 – 2474Combined sources
    Beta strandi255 – 2595Combined sources
    Beta strandi262 – 27110Combined sources
    Beta strandi274 – 2796Combined sources
    Turni280 – 2823Combined sources
    Beta strandi283 – 2886Combined sources
    Beta strandi298 – 31821Combined sources
    Helixi327 – 33711Combined sources
    Turni338 – 3403Combined sources
    Beta strandi343 – 3497Combined sources
    Helixi359 – 36911Combined sources
    Turni370 – 3723Combined sources
    Beta strandi377 – 3848Combined sources
    Helixi385 – 3884Combined sources
    Beta strandi389 – 3935Combined sources
    Beta strandi398 – 4058Combined sources
    Beta strandi422 – 43211Combined sources
    Beta strandi435 – 44511Combined sources
    Beta strandi447 – 4537Combined sources
    Turni454 – 4574Combined sources
    Beta strandi458 – 4658Combined sources
    Helixi466 – 4683Combined sources
    Beta strandi470 – 48415Combined sources
    Beta strandi489 – 4924Combined sources
    Helixi494 – 5029Combined sources
    Beta strandi508 – 5103Combined sources
    Helixi511 – 52212Combined sources
    Helixi525 – 5273Combined sources
    Helixi563 – 58018Combined sources
    Turni583 – 5853Combined sources
    Beta strandi593 – 5964Combined sources
    Turni600 – 6045Combined sources
    Helixi605 – 6106Combined sources
    Beta strandi614 – 6218Combined sources
    Helixi623 – 63614Combined sources
    Beta strandi646 – 6516Combined sources
    Beta strandi656 – 6583Combined sources
    Helixi659 – 6646Combined sources
    Beta strandi672 – 6798Combined sources
    Helixi681 – 6833Combined sources
    Turni687 – 6893Combined sources
    Helixi690 – 70011Combined sources
    Beta strandi701 – 71212Combined sources
    Helixi714 – 7174Combined sources
    Beta strandi724 – 7274Combined sources
    Beta strandi730 – 7323Combined sources
    Turni734 – 7363Combined sources
    Beta strandi737 – 7415Combined sources
    Beta strandi743 – 7453Combined sources
    Beta strandi748 – 7525Combined sources
    Turni754 – 7563Combined sources
    Beta strandi757 – 7593Combined sources
    Beta strandi761 – 7644Combined sources
    Helixi768 – 77710Combined sources
    Beta strandi780 – 7878Combined sources
    Helixi788 – 7936Combined sources
    Helixi796 – 8005Combined sources
    Helixi802 – 8054Combined sources
    Helixi809 – 82315Combined sources
    Beta strandi826 – 8283Combined sources
    Helixi829 – 8335Combined sources
    Beta strandi836 – 8438Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VDWX-ray2.70A/C/E/G545-844[»]
    4CKBX-ray2.80A/D1-844[»]
    4CKCX-ray2.90A/D1-844[»]
    4CKEX-ray2.90A/D1-844[»]
    ProteinModelPortaliP04298.
    SMRiP04298. Positions 545-844.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04298.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini516 – 844329mRNA cap 0 methyltransferasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 539539Triphosphatase-guanylyltransferaseAdd
    BLAST
    Regioni549 – 5502S-adenosyl-L-methionine binding
    Regioni569 – 5702mRNA cap bindingPROSITE-ProRule annotation
    Regioni678 – 6803S-adenosyl-L-methionine binding

    Domaini

    The N-terminus contains the triphosphatase and guanylyltransferase domains, whereas the C-terminus contains the methyltransferase domain. The N-terminus is involved in binding to the temination motif 5'-UUUUUNU-3' in the nascent mRNA.1 Publication

    Sequence similaritiesi

    In the N-terminal section; belongs to the dsDNA virus mRNA guanylyltransferase family.Curated
    In the C-terminal section; belongs to the class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family.PROSITE-ProRule annotation
    Contains 1 mRNA cap 0 methyltransferase domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR019602. mRNA_cap_ATPase/GuylTrfase_vir.
    IPR004971. mRNA_G-N7_MeTrfase_dom.
    IPR029063. SAM-dependent_MTases.
    [Graphical view]
    PfamiPF10640. Pox_ATPase-GT. 1 hit.
    PF03291. Pox_MCEL. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51562. RNA_CAP0_MT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P04298-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDANVVSSST IATYIDALAK NASELEQRST AYEINNELEL VFIKPPLITL
    60 70 80 90 100
    TNVVNISTIQ ESFIRFTVTN KEGVKIRTKI PLSKVHGLDV KNVQLVDAID
    110 120 130 140 150
    NIVWEKKSLV TENRLHKECL LRLSTEERHI FLDYKKYGSS IRLELVNLIQ
    160 170 180 190 200
    AKTKNFTIDF KLKYFLGSGA QSKSSLLHAI NHPKSRPNTS LEIEFTPRDN
    210 220 230 240 250
    ETVPYDELIK ELTTLSRHIF MASPENVILS PPINAPIKTF MLPKQDIVGL
    260 270 280 290 300
    DLENLYAVTK TDGIPITIRV TSNGLYCYFT HLGYIIRYPV KRIIDSEVVV
    310 320 330 340 350
    FGEAVKDKNW TVYLIKLIEP VNAINDRLEE SKYVESKLVD ICDRIVFKSK
    360 370 380 390 400
    KYEGPFTTTS EVVDMLSTYL PKQPEGVILF YSKGPKSNID FKIKKENTID
    410 420 430 440 450
    QTANVVFRYM SSEPIIFGES SIFVEYKKFS NDKGFPKEYG SGKIVLYNGV
    460 470 480 490 500
    NYLNNIYCLE YINTHNEVGI KSVVVPIKFI AEFLVNGEIL KPRIDKTMKY
    510 520 530 540 550
    INSEDYYGNQ HNIIVEHLRD QSIKIGDIFN EDKLSDVGHQ YANNDKFRLN
    560 570 580 590 600
    PEVSYFTNKR TRGPLGILSN YVKTLLISMY CSKTFLDDSN KRKVLAIDFG
    610 620 630 640 650
    NGADLEKYFY GEIALLVATD PDADAIARGN ERYNKLNSGI KTKYYKFDYI
    660 670 680 690 700
    QETIRSDTFV SSVREVFYFG KFNIIDWQFA IHYSFHPRHY ATVMNNLSEL
    710 720 730 740 750
    TASGGKVLIT TMDGDKLSKL TDKKTFIIHK NLPSSENYMS VEKIADDRIV
    760 770 780 790 800
    VYNPSTMSTP MTEYIIKKND IVRVFNEYGF VLVDNVDFAT IIERSKKFIN
    810 820 830 840
    GASTMEDRPS TRNFFELNRG AIKCEGLDVE DLLSYYVVYV FSKR
    Length:844
    Mass (Da):96,734
    Last modified:March 20, 1987 - v1
    Checksum:i8B9FD3DE836FA6E7
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti705 – 7051G → D in strain: mutant Dts36.

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M15058 Genomic DNA. Translation: AAA48253.1.
    AY243312 Genomic DNA. Translation: AAO89385.1.
    PIRiA03872. QQVZ1.
    RefSeqiYP_232988.1. NC_006998.1.

    Genome annotation databases

    GeneIDi3707562.
    KEGGivg:3707562.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M15058 Genomic DNA. Translation: AAA48253.1.
    AY243312 Genomic DNA. Translation: AAO89385.1.
    PIRiA03872. QQVZ1.
    RefSeqiYP_232988.1. NC_006998.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VDWX-ray2.70A/C/E/G545-844[»]
    4CKBX-ray2.80A/D1-844[»]
    4CKCX-ray2.90A/D1-844[»]
    4CKEX-ray2.90A/D1-844[»]
    ProteinModelPortaliP04298.
    SMRiP04298. Positions 545-844.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-60664N.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    GeneIDi3707562.
    KEGGivg:3707562.

    Miscellaneous databases

    EvolutionaryTraceiP04298.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    InterProiIPR019602. mRNA_cap_ATPase/GuylTrfase_vir.
    IPR004971. mRNA_G-N7_MeTrfase_dom.
    IPR029063. SAM-dependent_MTases.
    [Graphical view]
    PfamiPF10640. Pox_ATPase-GT. 1 hit.
    PF03291. Pox_MCEL. 1 hit.
    [Graphical view]
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS51562. RNA_CAP0_MT. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Nucleotide sequence and genetic map of the 16-kb vaccinia virus HindIII D fragment."
      Niles E.G., Condit R.C., Caro P., Davidson K., Matusick L., Seto J.
      Virology 153:96-112(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Sequencing of the coding region of Vaccinia-WR to an average 9-fold redundancy and an error rate of 0.16/10kb."
      Esposito J.J., Frace A.M., Sammons S.A., Olsen-Rasmussen M., Osborne J., Wohlhueter R.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Catalytic activity of vaccinia mRNA capping enzyme subunits coexpressed in Escherichia coli."
      Shuman S.
      J. Biol. Chem. 265:11960-11966(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR.
    4. "Interaction and mutual stabilization of the two subunits of vaccinia virus mRNA capping enzyme coexpressed in Escherichia coli."
      Guo P., Moss B.
      Proc. Natl. Acad. Sci. U.S.A. 87:4023-4027(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMALL SUBUNIT, PROTEIN SEQUENCE OF 1-20 AND 498-517.
    5. "Intrinsic RNA (guanine-7) methyltransferase activity of the vaccinia virus capping enzyme D1 subunit is stimulated by the D12 subunit. Identification of amino acid residues in the D1 protein required for subunit association and methyl group transfer."
      Mao X., Shuman S.
      J. Biol. Chem. 269:24472-24479(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN METHYLTRANSFERASE.
    6. "Mutational analysis of the RNA triphosphatase component of vaccinia virus mRNA capping enzyme."
      Yu L., Shuman S.
      J. Virol. 70:6162-6168(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE OF TRIPHOSPHATASE ACTIVITY, MUTAGENESIS OF 77-ARG--LYS-79; 135-LYS-LYS-136; 160-PHE-LYS-161; 192-GLU--GLU-194; LYS-260 AND 524-LYS--GLY-526.
    7. "Mapping the active site of vaccinia virus RNA triphosphatase."
      Gong C., Shuman S.
      Virology 309:125-134(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF TRIPHOSPHATASE ACTIVITY, MUTAGENESIS OF LYS-107; GLU-126; ASP-159 AND LYS-161.
    8. "Phenotypic analysis of a temperature sensitive mutant in the large subunit of the vaccinia virus mRNA capping enzyme."
      Shatzer A.N., Kato S.E., Condit R.C.
      Virology 375:236-252(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: IHDW and mutant Dts36.
    9. "Vaccinia virus early gene transcription termination factors VTF and Rap94 interact with the U9 termination motif in the nascent RNA in a transcription ternary complex."
      Christen L.A., Piacente S., Mohamed M.R., Niles E.G.
      Virology 376:225-235(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Structure-function analysis of vaccinia virus mRNA cap (guanine-N7) methyltransferase."
      Zheng S., Shuman S.
      RNA 14:696-705(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-570; LYS-573; LYS-607; TYR-608; ASP-676; PHE-679; HIS-682 AND GLU-763.
    11. "Structural insights into the mechanism and evolution of the vaccinia virus mRNA cap N7 methyl-transferase."
      De la Pena M., Kyrieleis O.J., Cusack S.
      EMBO J. 26:4913-4925(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 545-844 IN COMPLEX WITH ADOHCY AND THE REGULATORY SUBUNIT.
    12. "Crystal structure of vaccinia virus mRNA capping enzyme provides insights into the mechanism and evolution of the capping apparatus."
      Kyrieleis O.J., Chang J., de la Pena M., Shuman S., Cusack S.
      Structure 22:452-465(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH GTP AND S-ADENOSYL-L-HOMOCYSTEINE, COFACTOR.

    Entry informationi

    Entry nameiMCEL_VACCW
    AccessioniPrimary (citable) accession number: P04298
    Secondary accession number(s): Q76ZS6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 1987
    Last sequence update: March 20, 1987
    Last modified: July 22, 2015
    This is version 86 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, Multifunctional enzyme, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.