ID   CAPSD_AQRVC             Reviewed;        1214 AA.
AC   Q8JU60;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   23-FEB-2022, entry version 76.
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 C (isolate Golden shiner/USA/GSRV/1977) (AQRV-C).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Spinareovirinae; Aquareovirus.
OX   NCBI_TaxID=185783;
OH   NCBI_TaxID=28800; Notemigonus crysoleucas (Golden shiner) (Cyprinus crysoleucas).
OH   NCBI_TaxID=90988; Pimephales promelas (Fathead minnow).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=12124458; DOI=10.1099/0022-1317-83-8-1941;
RA   Attoui H., Fang Q., Mohd Jaafar F., Cantaloube J.F., Biagini P.,
RA   de Micco P., de Lamballerie X.;
RT   "Common evolutionary origin of aquareoviruses and orthoreoviruses revealed
RT   by genome characterization of Golden shiner reovirus, Grass carp reovirus,
RT   Striped bass reovirus and golden ide reovirus (genus Aquareovirus, family
RT   Reoviridae).";
RL   J. Gen. Virol. 83:1941-1951(2002).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF403400; AAM92746.1; -; Genomic_RNA.
DR   RefSeq; NP_938062.1; NC_005168.1.
DR   SMR; Q8JU60; -.
DR   GeneID; 2648331; -.
DR   KEGG; vg:2648331; -.
DR   Proteomes; UP000006713; Genome.
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   Reference proteome; T=2 icosahedral capsid protein; Virion; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1214
FT                   /note="Major inner capsid protein VP3"
FT                   /id="PRO_0000404169"
FT   ZN_FING         117..140
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1214 AA;  132053 MW;  CAE57A8B548185DB CRC64;
     MPRRSARKAQ SATASPADTN VVPAKDAPTT NSPPSTTSPN QAAADANQQQ AGIVSSQSGP
     NAVGDSAPST SVNNDGDIIT RPTSDSIAAV ANATKPAAVV SDPQSMKVTP IVNPSSYVCN
     VCNARFSTMS ALSEHLRSDH RDDASTLLAT PMINNAIRSF LTAWDGIRIL SPDVSSKHLS
     AYLDSAVANG PELIVEDTGL CTSFMLLDNI PSAHLTKELI GFTWFMQMYQ MTPPLPEGAV
     NRIVCMTNWA SLGDEGRGLE VRLPPPTDSS VHAYKTVLSR GYIDNAQFNP LALRSNVLLM
     LLQFTLSNLK INKSSTFTSD VTTITSGRMI RAFEGRPELL ALAYPGRAVL PTQTKNAQFL
     STAIADRIGR LDRANLIGGE VSAMVECMEL CDALTLHIRE TYVMLLRSMH QDPTQIVQIV
     NECANNLLNS TIPISLRPTI LCPWFASSED LRLQQVMHLV NISSNTAAAL PLVEALSTLL
     RSVTPLVLDP TVLTNAITTI SESTTQTISP ISEILRLLQP MGNDYAAFWK CIASWAYNGL
     VTTVLSEDAF PDSSQSITHL PSMWKCLFLT LAGPMTSDPH SPVKVFMALA NLLAQPEPIA
     IGVPGMHQTT PASQFSHPGV WPPGFLNPQL INPQQAPLLR AFAEHIRANW PQPSEFGYGS
     TLQGSANLFI PPNRMVYPWP NQPLPRLTVA PTYDSAMSNW ISTTIAFFIR VVNSVNMTAT
     VNDLTRRTMT GVMTAMRQVK TMTPFYIQHM CPTELSVLAS VTVTPPFQVP FTRLVQNDVI
     TNVLVARVDP AQRGDAAVDI RATHATFAAA LPVDPAAIVV AMLCGQTETN LIPSHHYGKA
     FAPLFASNAM FTRNQRAVIT REAFVCARSA VAQCQDAGFL VPRPLDALRQ FDVTSAAAAE
     IMHAVNDAFK TAFDLDGALL DGLALYGDPR IADLSAAYLQ YGGNVVREHV PPGPSHIHRT
     LQQVESTFMA EMNLFNVARG NLYLVQTATN GNWSPMAPVA APPFVRGGPN VRVVGRFGTI
     VPRPDGLEPQ LIDDGNVPRD IAGDWVYPSD VLQVSVAVFC DYVWPMVKAG RTRVLVELGH
     YVYTLHYYDP QISLDEAPIL EEWLSKINPA GIPPVPFCIP IPQVYPCITA RRVHYAFTSE
     NNNDSLFSTN AASIDTAFGE NAAVSPLRWP GLVDPNYRVG TNDLPNRITL YNSLYRYNFT
     YPTLDGIMYV RSAT