ID Q6T1V3_9FLAV Unreviewed; 3448 AA.
AC Q6T1V3;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 131.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
OS Bovine viral diarrhea virus 2.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Pestivirus; Pestivirus tauri.
OX NCBI_TaxID=54315 {ECO:0000313|EMBL:AAR24084.1};
RN [1] {ECO:0000313|EMBL:AAR24084.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=890/256 {ECO:0000313|EMBL:AAR24084.1};
RX PubMed=16005739; DOI=10.1016/j.vaccine.2005.03.026;
RA Dehan P., Couvreur B., Hamers C., Lewalle P., Thiry E., Kerkhofs P.,
RA Pastoret P.P.;
RT "Point mutations in an infectious bovine viral diarrhoea virus type 2 cDNA
RT transcript that yields an attenuated and protective viral progeny.";
RL Vaccine 23:4236-4246(2005).
CC -!- FUNCTION: Acts as a cofactor for the NS3 protease activity.
CC {ECO:0000256|ARBA:ARBA00023576}.
CC -!- FUNCTION: Packages viral RNA to form a viral nucleocapsid and thereby
CC protects viral RNA. Also plays a role in transcription regulation.
CC Protects the incoming virus against IFN-induced effectors.
CC {ECO:0000256|ARBA:ARBA00034097}.
CC -!- FUNCTION: Plays a role in the regulation of viral RNA replication.
CC {ECO:0000256|ARBA:ARBA00023574}.
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=Leu is conserved at position P1 for all four cleavage sites.
CC Alanine is found at position P1' of the NS4A-NS4B cleavage site,
CC whereas serine is found at position P1' of the NS3-NS4A, NS4B-NS5A
CC and NS5A-NS5B cleavage sites.; EC=3.4.21.113;
CC Evidence={ECO:0000256|ARBA:ARBA00001160};
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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host
CC cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Virion membrane
CC {ECO:0000256|ARBA:ARBA00004650}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004650}.
CC -!- SIMILARITY: Belongs to the pestivirus polyprotein family.
CC {ECO:0000256|ARBA:ARBA00010133}.
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DR EMBL; AY442521; AAR24084.1; -; Genomic_RNA.
DR MEROPS; S31.001; -.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0039707; P:virus-mediated pore formation in host cell membrane; IEA:UniProtKB-KW.
DR CDD; cd23201; Pestivirus_RdRp; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.60.40.4200; Pestivirus envelope glycoprotein E2, C-terminal domain; 1.
DR Gene3D; 2.60.320.20; Pestivirus envelope glycoprotein E2, domain A; 1.
DR Gene3D; 2.60.40.3000; Pestivirus envelope glycoprotein E2, domain B; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR011492; Flavi_DEAD.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR022120; NS2.
DR InterPro; IPR030399; NS2_C74.
DR InterPro; IPR049486; NS3-hel_C_flaviviridae.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032521; Pestivirus_E2.
DR InterPro; IPR042309; Pestivirus_E2_A.
DR InterPro; IPR042310; Pestivirus_E2_B.
DR InterPro; IPR042311; Pestivirus_E2_D.
DR InterPro; IPR000280; Pestivirus_NS3_S31.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR002166; RNA_pol_HCV.
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; PF12387; Peptidase_C74; 1.
DR Pfam; PF05578; Peptidase_S31; 1.
DR Pfam; PF16329; Pestivirus_E2; 1.
DR Pfam; PF00998; RdRP_3; 1.
DR PRINTS; PR00729; CDVENDOPTASE.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 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; PS51692; PESTIVIRUS_NS2_PRO; 1.
DR PROSITE; PS51535; PESTIVIRUS_NS3PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 3: Inferred from homology;
KW Activation of host autophagy by virus {ECO:0000256|ARBA:ARBA00023050};
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 GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00868};
KW Inhibition of host innate immune response by virus
KW {ECO:0000256|ARBA:ARBA00022632};
KW Inhibition of host IRF3 by virus {ECO:0000256|ARBA:ARBA00022931};
KW Inhibition of host RLR pathway by virus {ECO:0000256|ARBA:ARBA00022482};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU00868};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU00868}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023065};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280};
KW Viral ion channel {ECO:0000256|ARBA:ARBA00023039};
KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022844};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT TRANSMEM 508..527
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 547..571
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 583..604
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 624..647
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 659..683
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 695..713
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 734..757
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 763..780
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 801..820
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 826..850
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 909..936
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 990..1138
FT /note="Peptidase C74"
FT /evidence="ECO:0000259|PROSITE:PS51692"
FT DOMAIN 1139..1312
FT /note="Peptidase S31"
FT /evidence="ECO:0000259|PROSITE:PS51535"
FT DOMAIN 1351..1491
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1522..1692
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 3068..3191
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT ACT_SITE 1207
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00868"
FT ACT_SITE 1244
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00868"
FT ACT_SITE 1301
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:AAR24084.1"
SQ SEQUENCE 3448 AA; 386999 MW; F0116815E780DB54 CRC64;
TKIIGPGKFD TNAEDGKILH EMGGHLSEFA LLSLVVLSDF APETASVIYL VLHFAIPQSH
VDVDTCDKNQ LNLTVATTVA EVIPGTVWNL GKYVCIRPDW WPYETTTVFV LEEAGQVIKL
GLRAIRDLTR IWNAATTTAF LIFLVKALRG QLIQGLLWLM LITGAQGFPE CKEGFQYAIS
KDRKMGLLGP ESLTTTWHLP TKKLVDSMVQ VWCEGKDLKI LKTCTKEERY LVAVHERALS
TSAEFMPISD GTIGPDVIDM PDDFEFGLCP CDAKPVIKGK FNASLLNGPA FQMVCPQGWT
GTIECTLANQ DTLDTTVVRT YRRTTPFQRR KWCSYEKIIG EDIHECILGG NWTCITGDHS
KLKDGPIKKC KWCGYDFVNS EGLPHYPIGK CMLINESGYR YVDDTSCDRG GVAIVPTGTV
KCRIGDVTVQ VVATNNDLGP MPCSPAEVIA SEGPVEKTAC TFNYSRTLPN KYYEPRDRYF
QQYMLKGEWQ YWFDLDHVDH HKDYFSEFII IAVVALLGGK YVLWLLITYT ILSEQMAMGA
GVNTEEIVMI GNLLTHSDIE VVVYFLLLYL IVKEELVRKW VILVYHILVA NPMKTIGVIL
LMLGGAVKAS RIDADDQSAT DPCFLLVTGI VAVLMTAMVY FLLLYLIVKE ELVRKWVILV
YHILVANPMK TIGVILLMPG GVVIASRIDA GDQSATDPCF LLVTGIVAVL MIARREPATL
PLIIALLAIR TSGFLLPASI DITVAVVLIA LLLASYVTDY FRYKKWLQFS FSLIAGIFII
RSLKHINQME VPETSMPNWR PLVLVIFYIT STAITTNWNI DLAGFLLQWA PAVIMMATMW
ADFWTLIIVL PSYELSKLYF LKNVRTDVEK NWLGKVKYKQ ISSVYDICDS EEAVYLFPSR
HKSGSRPDFI LPFLKAVLIS CISSQWQVVY ISYLILEITY YMHRKIIDEV SGGANFLSRL
IAAIIELNWA IDDEECKGLK KLYLLSGGVK NLIVKHKVRN EAVHRWFGEE EIYGAPKVIT
IIKASTLSKN RHCIICTICE GKDWNGANCP KCGRQGKPIT CGMTLADFEE KHYKKIFIRE
GCHDGPSREE YKGYVQYIAR GQLFLRNLPI LATKMKLLMV GNLGAEIGDL EHLGWVLRGP
AVCKKITNHE KCHVNIMDKL TAFFGIMPRG TTPRAPVRFP TALLKVRRGL ETGWAYTHQG
GISSVDHVTA GKDLLVCDSM GRTRVVCHSN NKMTDETEYG IKTDSGCPEG ARCYVLNPEA
VNISGTKGAM VHLQKTGGEF TCVTASGTPA FFDLKNLKGW SGLPIFEASS GRVVGRVKVG
KNEDSKPTKL MSGIQTVSKN QTDLADIVKK LTSMNRGEFK QITLATGAGK TTELPRSVIE
EIGRHKRVLV LIPLRAAAES VYQYMRVKYP SISFNLRIGD MKEGDMATGI TYASYGYFCQ
LPQPKLRAAM VEYSYIFLDE YHCATPEQLA IIGKIHRFSE NLRVVAMTAT PAGTGTTTGQ
KHPIEEFIAP EVMKGEDLGS EYLDIAGLKI PPEEMKGNML VFVPTRNMAV ETAKKLKAKG
YNSGYYYSGG NPENLRVVTS QSPYVVVTTN AIESGVTLPD LDTVVDTGLK CEKRVRISSK
MPFIVTGLKR MAVTIGEQAQ RRGRVGRVKP GRYYRSQETA SGSKDYHYDL LQAQRYGIED
GINVTKSFRE MNYDWSLYEE DSLMITQLEV LNNLLISEDL PAAVKNIMAR TDHPEPIQLA
YNSHENQIPV LLPKIKNGEV TDSYENYTYL NARKLGEDVP AYVYATEDED LAVDLLGMDW
PDPGNQQVVE TGRALKQVTG LSTAENALLI ALFGYVGYQT LSKRHIPMVT DIYTLEDHRL
EDTTHLQFAP NAIRTDGKDS ELKELAVGDL DKYLDALVDY SKQGMKFIKV QAEKVKDSQS
TKEGLQTIKE YVDKFIQSLT ENKEEIIRYG LWGAHTALYK SLAARLGHET AFATLVVKWL
AFGGETVSAH IKQAAVDLVV YYIMNKPSFP GDTETQQEGR RFVASLFISA LATYTYETWN
YNNLARVVEP TLAYLPYATS ALKLFTPTRL ESVVILSSTI YKTYLSIRKG KSDGLLGTGI
SAAMEILNQN PISVGISVML GVGAIAAHNA IESSEQKRTL LMKVFVKNFL DQAATDELVK
ENPEKIIMAL FEAVQTIGNP LRLIYHLYGV YYKGWEAKEL AEKTAGRNLF TLIMFEAFEL
LGMDSEGKIR NLSGNYILDL IFNLHNKLNK GLKKLVLGWA PAPFSCDWTP SDERISLPHN
NYLRVETRCP CGYEMKAIKN VAGKLTKVEE KGPFLCRNRL GRGPPNFRVT KFYDDNLAEV
KPVAKLEGQV DLYYKGVTAK LDYNNGKVLL ATNKWEVDHA FLTRLVKKHT GIGFKGAYLG
DRPDHQDLVD RDCATITKNS VQFLKMKKGC AFTYDLTISN LVRLIELVHK NNLQEREIPT
VTVTTWLAYS FVNEDLGSIK PVLGEKVIPE PPTELSLQPT VGLVTTETAI TITGEAEVMT
TGITPVVEMK EEPQLDHQST TLKVGLKEGE YPGPGVNPNH LVEVIDEKDD RPFVLIIGNK
SSTSNRARTA KNIRLYKGNN PREIRDLMSQ GRILTVALKE LDPELKELVD YKGTFLNREA
LEALSLGKPI KRKTTTAMIR RLIEPEVEEE LPDWFQAEEP LFLEAKIQAD LYHLIGSVDS
IKSKAKELGA TDNTKIVKEV GARTYTMKLS SWSTQVTKKQ MSLAPLFEEL LIKCPPCSKI
SKGHMVSAYQ LAQGYWEPLG CGVYMGTIPA RRLKIHPYEA YLKLKELVEV ELSRVTAKES
IIREHNTWIL RKVRHEGNLR TKSMINPGKI SDQLCRDGHK RNIYNKIIGS TMGSAGIRLE
KLPVVRAQTD TTSFHQAIRE KIDKPENKQT PELHEELMKV FDCLKIPELK ESYDEVSWEQ
LEAGINRKGA AGYLESKNIG EVLDTEKHIV EQLIKDLRKG KKIRYYETAI PKNEKRDVSD
DWEAGEFVDE KKPRVIQYPD AKVRLAIAKV MYKWVKQKPV VIPGYEGKTP LFDIFNKVKK
EWDSFQDPVA VSFDTKAWDT QVTSKDLMLI KDIQKYYFKR STHKFLDTIT EHMVEVPVIT
ADGEVYIRNG QRGSGQPDTS AGNSMLNVLT MIYAFCKSTG IPYRGFSRVA RIHVCGDDGF
LITERGLGLK FSEKGMQILH EAGKPQKITE GEKMKVAYRF EDIEFCSHTP VPVRWADNTS
SYMAGRSTAT ILAKMPTRLD SSGERGSTAY EKPVAFSFLL MYSWNPVVRR ICLLVLSQFP
EISPSKNTIY YYQGDPIAAY REVIGKQLCE LKRTGFEKLA SLNLNMTTLG IWTKHTSKRL
IQDCVEIGKR EGNWLVNADR LIAGKTGKFY IPSTGVTLLG KHYEEINLKQ KAAQSPIEGV
DRYKLGPIVN VILRRLRVML TTVASGSW
//
