ID   MCE_RGDV                Reviewed;         799 AA.
AC   Q1WNZ7;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   29-SEP-2021, entry version 40.
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   Rice gall dwarf virus (RGDV).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Phytoreovirus.
OX   NCBI_TaxID=10986;
OH   NCBI_TaxID=94400; Nephotettix cincticeps (Green rice leafhopper) (Selenocephalus cincticeps).
OH   NCBI_TaxID=4530; Oryza sativa (Rice).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND FUNCTION.
RA   Ichimi K., Kikuchi A., Moriyasu Y., Zhong X.B., Hagiwara K., Kamiunten H.,
RA   Omura T.;
RT   "Sequence analysis and GTP-binding ability of the minor core protein P5 of
RT   Rice gall dwarf virus.";
RL   Jpn. Agric. Res. Q. 36:83-87(2002).
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:0000269|Ref.1,
CC       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; D76429; BAE92557.1; -; Genomic_RNA.
DR   RefSeq; YP_001111372.1; NC_009247.1.
DR   SMR; Q1WNZ7; -.
DR   GeneID; 5075723; -.
DR   KEGG; vg:5075723; -.
DR   UniPathway; UPA00922; -.
DR   Proteomes; UP000006720; 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; Reference proteome;
KW   RNA-binding; Transferase; Virion.
FT   CHAIN           1..799
FT                   /note="Putative mRNA-capping enzyme P5"
FT                   /id="PRO_0000402404"
SQ   SEQUENCE   799 AA;  90875 MW;  26AFA6280AFC58BE CRC64;
     MQAKTTSEEY VIPNFAQTIN NRTIVNIFES CKYRSPLIIC ALNDAVLAKE YSNSMAMGSG
     TITFMIDNDV DIMSSLYTTF RTVSTLLLMG NQLCVFIVVP MSVISTDALT AIAYAYRGAM
     IELRHYGRGD DYVQERLESL FKLSPLCGTP HMGPKYYGPT VFSELLDLSH HNKTSWYSVI
     DYSMFTRTAL VGFASYMMKT LSLNSSIVNI VGYNPPYVWA AMMHGVTIRY IEKEIPNPKG
     KGPMGLIMPE LNGRVLTNKV KYVLHNPQIK LLCLDSMMFM SSRNIVYIGA YPATHLLDMN
     LRGWNIYAVD PEITQQWISD MKAKTGANIC ASSRKFMFDV SENIKINEFF GNQPYSIIDD
     SWVPDNYEQF QDKKRNYFQE LVKSDQKVTL ITMKWNTRKN VTCEKLLALL PQPYGGKLYE
     MRAFFHRNGI GSITIDANSV EKYIQKFQEL PLGAQVGTQK FMHTMISRVQ DVMSIQPKKG
     DVIIASYSLS NASNPKKKVL EYLTKASKSE AMIIFGAPNL ERVKYMRERG VLPGNNITIN
     GEKITFNNPS GKKWTDFGYT NSELLACDMI EVTIEQMVSF MSTSFRGTGY YSNSIYNDLF
     SWFIPIWVWN QTMQIQDIRL SPVALVKCFT TKIRNLCYVP HSTYYALRGH LVAKMFSENN
     IENNCYSISG KSNETFTVLK DFKFPTSIGV LEFKAGEKVN ISGHLLSLAV AAHFVAVPVT
     MWARHIKYMT VDRQKPPDVD RILFFDNKIK RNTLEKWHTK SEVILAALIA GEYVGLMLNN
     FHSKAIVDDL CNTVLATFR