ID Q5QCY7_9FLAV Unreviewed; 683 AA.
AC Q5QCY7;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
OS Pestivirus strain D32/00_HoBi.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Pestivirus; Pestivirus brazilense.
OX NCBI_TaxID=266829 {ECO:0000313|EMBL:AAV70883.1};
RN [1] {ECO:0000313|EMBL:AAV70883.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=D32/00_HoBi {ECO:0000313|EMBL:AAV70883.1};
RX PubMed=15557237; DOI=10.1099/vir.0.80238-0;
RA Schirrmeier H., Strebelow G., Depner K., Hoffmann B., Beer M.;
RT "Genetic and antigenic characterization of an atypical pestivirus isolate,
RT a putative member of a novel pestivirus species.";
RL J. Gen. Virol. 85:3647-3652(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; AY713481; AAV70883.1; -; Genomic_RNA.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0044423; C:virion component; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 CDD; cd17931; DEXHc_viral_Ns3; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011492; Flavi_DEAD.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR049486; NS3-hel_C_flaviviridae.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000280; Pestivirus_NS3_S31.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF234; ATP-DEPENDENT RNA HELICASE DHX40-RELATED; 1.
DR Pfam; PF20907; Flav_NS3-hel_C; 1.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF05578; Peptidase_S31; 1.
DR PRINTS; PR00729; CDVENDOPTASE.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51535; PESTIVIRUS_NS3PRO; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Fusion of virus membrane with host endosomal membrane
KW {ECO:0000256|ARBA:ARBA00022510};
KW Fusion of virus membrane with host membrane
KW {ECO:0000256|ARBA:ARBA00022506};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00868};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU00868};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU00868}; Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595};
KW Virion {ECO:0000256|ARBA:ARBA00022844};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT DOMAIN 1..174
FT /note="Peptidase S31"
FT /evidence="ECO:0000259|PROSITE:PS51535"
FT DOMAIN 213..371
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 384..554
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 664..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 69
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00868"
FT ACT_SITE 106
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00868"
FT ACT_SITE 163
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00868"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAV70883.1"
FT NON_TER 683
FT /evidence="ECO:0000313|EMBL:AAV70883.1"
SQ SEQUENCE 683 AA; 75301 MW; 3DED8F439DCE41A2 CRC64;
GPAVCKKIVS HEKCHTGIAD KLTAFFGIMP RGTTPRAPVR FPTSLIKIRR GLETGWAYTH
QGGISSVDHV TAGKDLLVCD SMGRTRVVCQ SNNKMTDETE YGIKTDSGCP EGARCYVLNP
EAQNIAGTRG AMVHLQKTGG EFTCVTASGT PAFFDLKNLK GWSGLPIFEA SSGRVVGRVK
VGKNEESKPT KLMSGIQTVS KSTTDLTEMV KKIVAMNRGE FKQITLATGA GKTTELPRSV
IEEIGRHKRV LVLIPLRAAA ESVYQYMKQK HPSIAFNLRI GEMKEGDMAT GITYASYGYF
CQMPQPKLRA AMVEYSYIFL DEYHCATPEQ LAIIGKIHRF SENLRVVAMT ATPAGSVTTT
GQKHPIEEFI APEVMKGEDL GSNFLDIAGL KIPTEEMKGN MLVFVPTRNM AVEVAKKLKA
KGYNSGYYYS GEDPANLRVV TSQSPYVVVA TNAIESGVTL PDLDVVVDTG LKCEKRVRIS
SKMPFIVTGL KRMAVTVGEQ AQRRGRVGRV KPGRFYRSQE TASGSKDYHY DLLQAQRYGI
EDGINITKSF REMNYDWSLY EEDSLLITQL EVLNNLLISD DLPAAVKNIM ARTDHPEPIQ
LAYNSYEVQV PVLFPKIRNG EVTNEYEAYS FLNARKLGED VPAYIYATEN EDLAVDLLGL
DWPDPGSQQT NETGKALKQV SGL
//
