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CAPSD_AQRVG
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   23-FEB-2022, entry version 47.
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; Reoviridae; Spinareovirinae; Aquareovirus.
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; -; 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   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
 
 
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