ID CAPSD_AQRVG Reviewed; 1215 AA.
AC B2BNE1;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 08-NOV-2023, entry version 50.
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 G (isolate American grass carp/USA/PB01-155/-) (AQRV-G).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Spinareoviridae; Aquareovirus; Aquareovirus G.
OX NCBI_TaxID=648234;
OH NCBI_TaxID=7959; Ctenopharyngodon idella (Grass carp) (Leuciscus idella).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=18191982; DOI=10.1016/j.virol.2007.12.006;
RA Mohd Jaafar F., Goodwin A.E., Belhouchet M., Merry G., Fang Q.,
RA Cantaloube J.F., Biagini P., de Micco P., Mertens P.P., Attoui H.;
RT "Complete characterisation of the American grass carp reovirus genome
RT (genus Aquareovirus: family Reoviridae) reveals an evolutionary link
RT between aquareoviruses and coltiviruses.";
RL Virology 373:310-321(2008).
RN [2]
RP FUNCTION, AND INTERACTION WITH VP6.
RC STRAIN=GCRV;
RX PubMed=18625243; DOI=10.1016/j.jmb.2008.06.075;
RA Cheng L., Fang Q., Shah S., Atanasov I.C., Zhou Z.H.;
RT "Subnanometer-resolution structures of the grass carp reovirus core and
RT virion.";
RL J. Mol. Biol. 382:213-222(2008).
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. Inner capsid (core) component. Displays NTPase, RNA 5'-
CC triphosphatase (RTPase) and RNA helicase activities and probably
CC participates in transcription of the viral genome. Helicase activity
CC might be involved in unwinding or reannealing dsRNA during RNA
CC synthesis. RTPase enzymatic activity represents the first step in RNA
CC capping, which yields a 5'-diphosphorylated plus-strand RNA (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:18625243}.
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:0000269|PubMed:18625243}.
CC -!- SUBCELLULAR LOCATION: Virion.
CC -!- SIMILARITY: Belongs to the reoviridae major inner capsid protein
CC family. {ECO:0000305}.
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DR EMBL; EF589100; ABV01041.1; -; Genomic_RNA.
DR RefSeq; YP_001837096.1; NC_010586.1.
DR SMR; B2BNE1; -.
DR GeneID; 6218801; -.
DR KEGG; vg:6218801; -.
DR Proteomes; UP000001674; 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; Inner capsid protein lambda-1; 1.
DR InterPro; IPR044949; Lambda-1/VP3.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF13912; zf-C2H2_6; 1.
DR SMART; SM00355; ZnF_C2H2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
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..1215
FT /note="Major inner capsid protein VP3"
FT /id="PRO_0000404170"
FT ZN_FING 118..141
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1215 AA; 131922 MW; 782A78C06255EBF7 CRC64;
MPRRPRRNAK TSDKAEDAQT LVAPAANASV SSTVNTTTSP TLAAGNESQQ RAGIDPNQAG
SAGVGDAAPS SRVDNDGDVI TRPTSDSIAA IANATKPAAV INNAQATALV PTSNPHAYRC
NVCNAEFPSM SAMTEHLRTS HRDEPSTLLA TPVINAAIQA FLQAWDGLRL LAPDVSSEAL
SKYLDSTVDS SPDLIVEDQG LCTSFMLIDN VPASHLSPEL IGFTWFMQMY QMTPPLPEGA
VNRIVCMTNW ASLGDPSRGI EVRLPPPTDN TVHAYKTVLS QGYVASSQFS PLTFRANTLL
MLTQFVLSNL KINKSSTFTS DVTTLTVGRM ICSFEARPEL LALAYPGRAV LPVNTKNAQF
LATAIPDRIG RIDRANLIGG EVSASVECME LCDSLTLYIR ENYLMLLRSM HQDPTRIVQI
VNECARNLLN SSIPVNLRPS ILCPWFASTA DLRLQQAIHL VNISSNTAAA LPQVEALSSL
LRSVTPLVLN PTILTNAITT ISESTTQTIS PISEILRLLS PTGNDYAAFW KCIASWAYNG
LVQTVLSEDA FPDSSQSITH LPSMWKCMLL TLAAPMTSDP HSPVKVFMSL ANLLAQPEPI
VINVDGMHQT TPASQFSHPG VWPPGFINPA QIPVAQAPLL RAFADHIHAN WPQPSDFEYG
SAAQGSGNLF IPPNRMVYPW PNAPLPRMTV AATFDSAMSQ WISTTIAFFI RVVNAPIMAP
TVNDLTRRTI TGVLTAMRQV KTMTPFYIQH MCPTELAVLG SITLVPPFQV PFTRLVQNDA
ITNVLVARVD PTQRGDAAVD IRATHATFSA ALPVDPASIV VAMLCGQTPT NLIPSHHYGK
AFAPLFTSNA MFTRNQRAVI TREALVCARS IVAQCQDDGF NVPRPLAGLR QFDITSAAAA
EIWHAVNDAF KTAFDIDGAL LDGMGLYGDP RIADISVAYL QYDGRVTREH VPPDQSFIHR
ALLTTENTFL AEMNLFNVGA GDIFLIQTPT NGNWAPMVPV AHPPFARGGP NVNVVGNHGT
LAMRPNGLEP QLIDNAGVPR DIAGDWIYPI DVLQVSVSTF RDYVWPLVVA GRVRVRIEIP
HYVYTTHYHQ PQTTFTDAQL VETWLAGIDP TGIPPIPFSI PIPQVGACIT SRRVYHVFAA
QNNNNSLFST NSSSIATVFG EDAGVSPARW PALVDPNYQF GTNELPNRIT LYGSLFRYNF
TYPSLSGVMF MRSAE
//
