ID   MCE_WTV                 Reviewed;         804 AA.
AC   P12366;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   29-SEP-2021, entry version 61.
DE   RecName: Full=Putative mRNA-capping enzyme P5;
DE   AltName: Full=Structural protein 5;
DE   AltName: Full=mRNA guanylyltransferase P5;
DE            EC=2.7.7.50;
OS   Wound tumor virus (WTV).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Phytoreovirus.
OX   NCBI_TaxID=10987;
OH   NCBI_TaxID=4058; Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OH   NCBI_TaxID=47083; Melilotus officinalis (Yellow sweet clover) (Trifolium officinale).
OH   NCBI_TaxID=60916; Trifolium incarnatum (Crimson clover).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3479793; DOI=10.1073/pnas.84.23.8301;
RA   Anzola J.V., Xu Z., Asamizu T., Nuss D.L.;
RT   "Segment-specific inverted repeats found adjacent to conserved terminal
RT   sequences in wound tumor virus genome and defective interfering RNAs.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:8301-8305(1987).
CC   -!- FUNCTION: Enzyme involved in mRNA capping (Potential). Binds to GTP and
CC       might have guanylyltransferase activity. Together with the RNA-directed
CC       RNA polymerase P1 and protein P7, forms an transcriptional complex
CC       positioned near the channels situated at each of the five-fold vertices
CC       of the core (By similarity). {ECO:0000250, ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-
CC         end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + diphosphate;
CC         Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50;
CC   -!- PATHWAY: mRNA processing; mRNA capping.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Host cytoplasm
CC       {ECO:0000250}. Note=Located inside the inner capsid. Found in the
CC       interior of spherical cytoplasmic structures, called virus factories,
CC       that appear early after infection and are the site of viral replication
CC       and packaging. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the phytoreovirus protein P5 family.
CC       {ECO:0000305}.
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DR   EMBL; J03020; AAA48499.1; -; Genomic_RNA.
DR   PIR; A39972; A39972.
DR   SMR; P12366; -.
DR   UniPathway; UPA00922; -.
DR   Proteomes; UP000242823; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004484; F:mRNA guanylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-UniPathway.
DR   CDD; cd20759; capping_2-OMTase_Phytoreovirus; 1.
DR   InterPro; IPR044310; P5_Phytoreov.
PE   3: Inferred from homology;
KW   GTP-binding; Host cytoplasm; mRNA capping; mRNA processing;
KW   Nucleotide-binding; Nucleotidyltransferase; RNA-binding; Transferase;
KW   Virion.
FT   CHAIN           1..804
FT                   /note="Putative mRNA-capping enzyme P5"
FT                   /id="PRO_0000222763"
SQ   SEQUENCE   804 AA;  91063 MW;  D22D918BB56492C6 CRC64;
     MAIDSYCIPN FSQTIDNRTI VNIFQSCKYR SQLSVCFLND KSAADKFSNS MRQGSGTITF
     IIHAEDGEIS EQLHSTFRSV STMLLCGMQL FVFIVAPRNV ISSETGKAIT WAFRGSFIEL
     RDHGRGEQAL HDILEQFYRL SPLVNVPKMG MAYYGPTSFA ELLSLSSKNK TSWRYVIDYS
     MFTRSALVGF ASHMMDECSF ANKQINVIGY NPPYVWAGLR HGVTTRFTEM STPDPEGYGP
     IKLILPRLTG NVLLKKVKYV QHDPQKKLLC DDSVMFALSR NILYIGVYPA THLLDYNLKG
     WRMVAVDPKI NAAWAETLKQ RTSIDLVPIS AKFEFNAQST RDIVLKYFSG VPFSIIDDSW
     VEGTEDYEKF QELKQSYFEQ LVMNGSTSKL RVSMISMKWN RTKDVKCRRL LALLPQPYGG
     SLRELRAYFH VNGAAEVNIK KSEVNSYMDK FTSLSISEQI GSQKFMHMLI TNYGDALKLK
     TGRDKAIIAS YSLSNAINKK ERVLKFLSDA AKSETLIIFG APNLNRVKFM IKSGIVLGSD
     VTISNDLITF KNASGKVWKD YGYTQSELIK SSMIEITIEQ MLCISSSSYN GVGYFANSIY
     NDMFSWYVPE WLFEKYFSIQ DIRLSPVALV KCFTTSIRNL CYVPHLTYYA LRGSFVEKVL
     ITNNVLNSSY LITGTSHSTF KVLSNFEVPS PAGVLKFKAG DDVNISGHLL SLVIAAHFVA
     SPTLLWATHM KRMTTPVNLP KNLDKLLFFD NKIKNGMLEK WHSREEVVLA AMIVENYVAH
     ILNGRHSIEI IQEITQVIYE KFNA