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Database: UniProt
Entry: Q6F5N9_BVDV
LinkDB: Q6F5N9_BVDV
Original site: Q6F5N9_BVDV 
ID   Q6F5N9_BVDV             Unreviewed;       147 AA.
AC   Q6F5N9;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE   Flags: Fragment;
GN   Name=NS3 {ECO:0000313|EMBL:BAD27053.1};
OS   Bovine viral diarrhea virus (BVDV) (Mucosal disease virus).
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC   Amarillovirales; Flaviviridae; Pestivirus; Pestivirus bovis.
OX   NCBI_TaxID=11099 {ECO:0000313|EMBL:BAD27053.1};
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1] {ECO:0000313|EMBL:BAD27053.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IS10 NCP/98 {ECO:0000313|EMBL:BAD27053.1};
RX   PubMed=14749175; DOI=10.1016/j.virusres.2003.10.006;
RA   Nagai M., Hayashi M., Sugita S., Sakoda Y., Mori M., Murakami T., Ozawa T.,
RA   Yamada N., Akashi H.;
RT   "Phylogenetic analysis of bovine viral diarrhea viruses using five
RT   different genetic regions.";
RL   Virus Res. 99:103-113(2004).
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         Evidence={ECO:0000256|ARBA:ARBA00001556};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00001491};
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DR   EMBL; AB105724; BAD27053.1; -; Genomic_RNA.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR011492; Flavi_DEAD.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF07652; Flavi_DEAD; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW   Virion {ECO:0000256|ARBA:ARBA00022804};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT   DOMAIN          1..134
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAD27053.1"
FT   NON_TER         147
FT                   /evidence="ECO:0000313|EMBL:BAD27053.1"
SQ   SEQUENCE   147 AA;  16487 MW;  E596B8DFBC4C4659 CRC64;
     KAVIEEIGRH KRVLVLIPLR AAAESVYQYM RLKHPSISFN LRIGDMKEGD MATGITYASY
     GYFCQMPQPK LRAAMVEYSY IFLDEYHCAT PEQLAVIGKI HRFSESIRVV AMTATPAGSV
     TTTGQKHPIE EFIAPEVMKG EDLGSQF
//
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