ID   MCE_RDVF                Reviewed;         801 AA.
AC   Q85437;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   29-SEP-2021, entry version 63.
DE   RecName: Full=Putative mRNA-capping enzyme P5;
DE   AltName: Full=Structural protein 5;
DE   AltName: Full=mRNA guanylyltransferase;
DE            EC=2.7.7.50;
OS   Rice dwarf virus (isolate Fujian) (RDV).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Phytoreovirus.
OX   NCBI_TaxID=142804;
OH   NCBI_TaxID=114194; Alopecurus aequalis.
OH   NCBI_TaxID=90397; Echinochloa crus-galli (Barnyard grass) (Panicum crus-galli).
OH   NCBI_TaxID=94400; Nephotettix cincticeps (Green rice leafhopper) (Selenocephalus cincticeps).
OH   NCBI_TaxID=4530; Oryza sativa (Rice).
OH   NCBI_TaxID=147271; Paspalum.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Liu Y., Li Y., Pan N., Chen Z.;
RT   "cDNA synthesis, molecular cloning and sequence analysis of rice dwarf
RT   virus segment S5.";
RL   J. Basic Sci. Eng. 2:109-116(1994).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16432031; DOI=10.1099/vir.0.81425-0;
RA   Wei T., Shimizu T., Hagiwara K., Kikuchi A., Moriyasu Y., Suzuki N.,
RA   Chen H., Omura T.;
RT   "Pns12 protein of Rice dwarf virus is essential for formation of viroplasms
RT   and nucleation of viral-assembly complexes.";
RL   J. Gen. Virol. 87:429-438(2006).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=20190042; DOI=10.1093/jb/mvq017;
RA   Miyazaki N., Wu B., Hagiwara K., Wang C.Y., Xing L., Hammar L.,
RA   Higashiura A., Tsukihara T., Nakagawa A., Omura T., Cheng R.H.;
RT   "The functional organization of the internal components of Rice dwarf
RT   virus.";
RL   J. Biochem. 147:843-850(2010).
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 (Probable). {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:0000269|PubMed:20190042}. Host
CC       cytoplasm {ECO:0000269|PubMed:16432031}. Note=Located inside the inner
CC       capsid (PubMed:20190042). Found in the interior of spherical
CC       cytoplasmic structures, called virus factories, that appear early after
CC       infection and are the site of viral replication and packaging.
CC       {ECO:0000269|PubMed:20190042, ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the phytoreovirus protein P5 family.
CC       {ECO:0000305}.
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DR   EMBL; U36563; AAA88762.1; -; mRNA.
DR   RefSeq; NP_620532.1; NC_003762.1.
DR   SMR; Q85437; -.
DR   GeneID; 956497; -.
DR   KEGG; vg:956497; -.
DR   UniPathway; UPA00922; -.
DR   Proteomes; UP000002239; 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   2: Evidence at transcript level;
KW   GTP-binding; Host cytoplasm; mRNA capping; mRNA processing;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   RNA-binding; Transferase; Virion.
FT   CHAIN           1..801
FT                   /note="Putative mRNA-capping enzyme P5"
FT                   /id="PRO_0000222787"
SQ   SEQUENCE   801 AA;  90708 MW;  BA7549701337A093 CRC64;
     MSNPDYCIPN FSQTVNERTI IDIFTICRYR SPLVVFCLSH TELAKKYAQD VSMSSGTHVH
     IIDGSVEITT SLYRTFRTIA TQLLGRMQIV VFVTVDKSVV STQVMKSTAW ASRGSFVELR
     NQSVDSSTLV NKLENLVSFA PLYNVPKCGP DYYGPTVYSE LLSLATNART HWYATIDYSM
     FTRSVLTGFI AKYFNEEAVP IDKRIVSIVG YNPPYVWTCL RHGIRPTYIQ KSLPNPGGKG
     PFGLILPVIN ELVLKSKVKY VMHNPQIKLL CLDTFMLSTS MNILYIGAYP ATHLLSLQLN
     GWTILAFDPK ITSDWTDAMA KATGAKVIGV NKEFDFKSFS VQANQLNMFQ NSKLSVIDDT
     WVETDYEKFQ AEKQAYFEWL IDRTSIDVRL ISMKWNRSKD TSVSHLLALL PQPYGASIRE
     MRAFFHKKGA SDIKILAAET EKYMDDFTAM SVSDQINTQK FMHCMITTVG DALKMDLDGG
     RAVIASYSLS NSSNPKERVL KFLSDANNGK AMVVFGAPNT YRLAYAKKVG LVLDSAIKMS
     KDLITFSNPT GRRWRDYGYS QSELYDAGYV EITIDQMVDY SSDVYNGVGY FANSTYNDLF
     SWYIPKWYVH KRMLMQDIRL SPAALVKCFT TLIRNICYVP HETYYRFRGI LVDKYLRSKN
     VDSISLFHYW SGSKTFTVLS HFEVPHECGP LVFEASTDVN VSGHLLSLAI AAHFVASPMI
     LWAEQMKYMA VDRMLPPNLD KSLFFDNKVT PSGALQRWHS REEVLLAAEI CESYAAMMLN
     NKHSPDIIGT LKSAINLVFK I