ID   CAPSD_AQRVA             Reviewed;        1210 AA.
AC   Q8VA41;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   23-FEB-2022, entry version 74.
DE   RecName: Full=Major inner capsid protein VP3;
DE            EC=3.6.4.13;
DE   AltName: Full=ATP-dependent DNA helicase VP3;
GN   Name=S3;
OS   Aquareovirus A (isolate Chum salmon/Japan/CSRV/1981) (AQRV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Spinareovirinae; Aquareovirus.
OX   NCBI_TaxID=928295;
OH   NCBI_TaxID=8018; Oncorhynchus keta (Chum salmon) (Salmo keta).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3819694; DOI=10.1099/0022-1317-68-2-353;
RA   Winton J.R., Lannan C.N., Fryer J.L., Hedrick R.P., Meyers T.R.,
RA   Plumb J.A., Yamamoto T.;
RT   "Morphological and biochemical properties of four members of a novel group
RT   of reoviruses isolated from aquatic animals.";
RL   J. Gen. Virol. 68:353-364(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Rao S., Carner G.R., Chen W., Winton J.R.;
RT   "Complete genome sequence of the chum salmon virus.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Self-assembles to form an icosahedral capsid with a pseudo
CC       T=2 symmetry, about 60 nm in diameter, and consisting of 120 VP3
CC       subunits. Displays NTPase, RNA 5'-triphosphatase (RTPase) and RNA
CC       helicase activities and probably participates in transcription of the
CC       viral genome. Helicase activity might be involved in unwinding or
CC       reannealing dsRNA during RNA synthesis. RTPase enzymatic activity
CC       represents the first step in RNA capping, which yields a 5'-
CC       diphosphorylated plus-strand RNA (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Interacts with VP6. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the reoviridae major inner capsid protein
CC       family. {ECO:0000305}.
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DR   EMBL; AF418296; AAL31498.1; -; Genomic_RNA.
DR   RefSeq; YP_398631.1; NC_007584.1.
DR   SMR; Q8VA41; -.
DR   GeneID; 3773157; -.
DR   KEGG; vg:3773157; -.
DR   GO; GO:0039616; C:T=2 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0039625; C:viral inner capsid; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006370; P:7-methylguanosine mRNA capping; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1830.10; -; 1.
DR   InterPro; IPR044949; Lambda-1/VP3.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Capsid protein; Helicase; Hydrolase; Inner capsid protein;
KW   Metal-binding; mRNA capping; mRNA processing; Nucleotide-binding;
KW   T=2 icosahedral capsid protein; Virion; Zinc; Zinc-finger.
FT   CHAIN           1..1210
FT                   /note="Major inner capsid protein VP3"
FT                   /id="PRO_0000404168"
FT   ZN_FING         113..136
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1210 AA;  131944 MW;  B499741E0C2BBB09 CRC64;
     MPRTSRNVRA TEVATTAIPP SNAATDTTVD TTVAPTIASA DAAQHASNIS SSQLGPAGVS
     DKVPSSVVTN DGDISVTPIS ENAAQLASSN QPASVIRNPV AAATISIVNP SSLRCQQCGA
     KFSSMTQLAE HVRTEHRTGA GSLVTSPAIN QAIESWLLTW EDLRLLAPTI ATDALNKYMG
     EAVAKAPLLI VEDEGLCTSF LASDTISIAG LQREIVGFTW FMETLQMIPA LPEGAVNHPI
     CHTGWASKDS VSRHLDVRLS PPTHGGCFSI HYRTVEGIRQ GHAIQPSYFP CQRPHAGPQV
     RSVQSQDQQV YSVDSGPDPR SRGRYVRFFD NKELFAVAYP GREVLMEANR NALFLDESLP
     DRVGCIGRAQ NVSGDVSAHI DTYELCDDLT LAIREMYHNM LFSMHLDPAS VMEIVQDVSQ
     QLVAASIPFA QTDTILCPWA ASTPTLQLSQ VLNLLNVANN TSAALPLIEA AATLIMGITP
     LRMEPRILSE AIKRVPETTT IVPSPTGELT RLLKPLGNDY SAIYRCIAGC LYSGLVQMFI
     SADAYPDPTQ SITSIPAIWK SLIVMLAAPM TTDPHAAVKA FMSMANLLAQ PEPIIIPAPG
     MTQSTPAVQF SHPEVWPPGF VDPTTLDRNR TPLLHALATM IHAHWPQPGV IQYGRSRLGS
     ANLFLPANQL TYPWPTQPLP RITVGPTYDS AMFRWIDSVF GFYINVVNSR YVATIVGDTT
     RRTLTGLMAA LMQVKTMTPF YIERMCPTEV AVVGGVTVFP PFQVPITRLD PTQVITNVMV
     SPRGPPAPCR RSRRSHRYYA YAAPIPCQSI PLRLSLLCCV RQTEATLGPS YHYGSAITPM
     FLSEELFTRN QRAVIASEAF VCARSIIAQC VPDGFQVPRP LQDFNQYNAS GSTAADLLKA
     VDDMFKTAFD IDGSLIEGIG LYGDPRVADL SVAYLRQNGA VERVHTAPDS SFLHEAMQVT
     SQVMVNEPNL WAIARGDIIL AQNATHNNWD PLNPVGLPIF ARGGPNVHVV GSRGMIIPQP
     GGLAPMIRDD AGNPQQIEGD WIYPISVLQV SVANFRDHVW PMIQAGRTRV RIEMGHFLYS
     IHYHEPFGQI TEAPAIDTWL AGISPTGIPP FPLSAPIPQI TIPITARRVY FGYCTMNNTG
     ATFSTLGAAI QSAWGTDVTI QRNRWPALID PNYIPGQSQL PARVQLYNPL RRYNYRYPSL
     KGMLYIPGVE