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Q01499

- POLG_BVDVS

UniProt

Q01499 - POLG_BVDVS

Protein

Genome polyprotein

Gene
N/A
Organism
Bovine viral diarrhea virus (strain SD-1) (BVDV) (Mucosal disease virus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    Initial binding to target cell probably involves interaction of E(rns) with glycosaminoglycans. E1 and/or E2 are responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis By similarity.By similarity
    P7 forms a leader sequence to properly orient NS2 in the membrane.By similarity
    Uncleaved NS2-3 is required for production of infectious virus.By similarity
    NS2 protease seems to play a vital role in viral RNA replication control and in the pathogenicity of the virus.PROSITE-ProRule annotation
    NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase.By similarity
    NS4A is a cofactor for the NS3 protease activity.By similarity
    RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome.PROSITE-ProRule annotation

    Catalytic activityi

    Leu is conserved at position P1 for all four cleavage sites. Alanine is found at position P1' of the NS4A-NS4B cleavage site, whereas serine is found at position P1' of the NS3-NS4A, NS4B-NS5A and NS5A-NS5B cleavage sites.
    Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
    NTP + H2O = NDP + phosphate.
    ATP + H2O = ADP + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei22 – 221For N-terminal protease activityPROSITE-ProRule annotation
    Active sitei49 – 491For N-terminal protease activityPROSITE-ProRule annotation
    Active sitei69 – 691For N-terminal protease activityPROSITE-ProRule annotation
    Sitei168 – 1692Cleavage; by autolysisBy similarity
    Sitei270 – 2712Cleavage; by host signal peptidaseBy similarity
    Sitei497 – 4982CleavageBy similarity
    Sitei659 – 6602Cleavage; by host signal peptidaseBy similarity
    Sitei1066 – 10672Cleavage; by host signal peptidase; partialBy similarity
    Sitei1136 – 11372Cleavage; by host signal peptidaseBy similarity
    Active sitei1447 – 14471For cysteine protease NS2 activityPROSITE-ProRule annotation
    Active sitei1461 – 14611For cysteine protease NS2 activityPROSITE-ProRule annotation
    Active sitei1512 – 15121For cysteine protease NS2 activityPROSITE-ProRule annotation
    Sitei1589 – 15902Cleavage; partial; cysteine protease NS2PROSITE-ProRule annotation
    Active sitei1658 – 16581Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
    Active sitei1695 – 16951Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
    Active sitei1752 – 17521Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
    Sitei2272 – 22732Cleavage; by serine protease NS3By similarity
    Sitei2336 – 23372Cleavage; by serine protease NS3By similarity
    Sitei2683 – 26842Cleavage; by serine protease NS3By similarity
    Sitei3179 – 31802Cleavage; by serine protease NS3By similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent helicase activity Source: InterPro
    3. cysteine-type endopeptidase activity Source: InterPro
    4. ion channel activity Source: UniProtKB-KW
    5. ribonuclease T2 activity Source: InterPro
    6. RNA binding Source: InterPro
    7. RNA-directed RNA polymerase activity Source: UniProtKB-KW
    8. serine-type endopeptidase activity Source: InterPro
    9. serine-type exopeptidase activity Source: InterPro

    GO - Biological processi

    1. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
    2. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
    3. induction by virus of host autophagy Source: UniProtKB-KW
    4. pore formation by virus in membrane of host cell Source: UniProtKB-KW
    5. protein oligomerization Source: UniProtKB-KW
    6. suppression by virus of host IRF3 activity Source: UniProtKB-KW
    7. viral protein processing Source: InterPro
    8. viral RNA genome replication Source: InterPro
    9. virion attachment to host cell Source: UniProtKB-KW

    Keywords - Molecular functioni

    Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Serine protease, Thiol protease, Transferase, Viral ion channel

    Keywords - Biological processi

    Activation of host autophagy by virus, Clathrin-mediated endocytosis of virus by host, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host IRF3 by virus, Inhibition of host RLR pathway by virus, Ion transport, Transport, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi3.4.21.113. 925.

    Protein family/group databases

    MEROPSiS31.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Genome polyprotein
    Cleaved into the following 13 chains:
    N-terminal protease (EC:3.4.22.-)
    Short name:
    N-pro
    Alternative name(s):
    Autoprotease p20
    Alternative name(s):
    gp44/48
    Alternative name(s):
    gp33
    Alternative name(s):
    gp55
    Alternative name(s):
    Non-structural protein 2
    Alternative name(s):
    Non-structural protein 3
    Alternative name(s):
    NS5B
    OrganismiBovine viral diarrhea virus (strain SD-1) (BVDV) (Mucosal disease virus)
    Taxonomic identifieri31656 [NCBI]
    Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stageFlaviviridaePestivirus
    Virus hostiBos taurus (Bovine) [TaxID: 9913]
    ProteomesiUP000007619: Genome

    Subcellular locationi

    Chain E(rns) glycoprotein : Host membrane; Peripheral membrane protein
    Note: The C-terminus membrane anchor of Erns represents an amphipathic helix embedded in plane into the membrane.By similarity
    Chain Cysteine protease NS2 : Host membrane PROSITE-ProRule annotation; Multi-pass membrane protein PROSITE-ProRule annotation

    GO - Cellular componenti

    1. host cell surface Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. integral to membrane of host cell Source: UniProtKB-KW

    Keywords - Cellular componenti

    Host membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 168168N-terminal proteaseBy similarityPRO_0000038037Add
    BLAST
    Chaini169 – 270102Capsid protein CBy similarityPRO_0000038038Add
    BLAST
    Chaini271 – 497227E(rns) glycoproteinBy similarityPRO_0000038039Add
    BLAST
    Chaini498 – 659162Envelope glycoprotein E1By similarityPRO_0000038040Add
    BLAST
    Chaini660 – 1066407Envelope glycoprotein E2By similarityPRO_0000038041Add
    BLAST
    Chaini1067 – 113670p7By similarityPRO_0000038042Add
    BLAST
    Chaini1137 – 22721136Non-structural protein 2-3By similarityPRO_0000038043Add
    BLAST
    Chaini1137 – 1589453Cysteine protease NS2PROSITE-ProRule annotationPRO_0000038044Add
    BLAST
    Chaini1590 – 2272683Serine protease NS3By similarityPRO_0000038045Add
    BLAST
    Chaini2273 – 233664Non-structural protein 4ABy similarityPRO_0000038046Add
    BLAST
    Chaini2337 – 2683347Non-structural protein 4BBy similarityPRO_0000038047Add
    BLAST
    Chaini2684 – 3179496Non-structural protein 5ABy similarityPRO_0000038048Add
    BLAST
    Chaini3180 – 3898719RNA-directed RNA polymeraseBy similarityPRO_0000038049Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi272 – 2721N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi281 – 2811N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi296 – 2961N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi335 – 3351N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi365 – 3651N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi370 – 3701N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi413 – 4131N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi487 – 4871N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi597 – 5971N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi809 – 8091N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi878 – 8781N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi922 – 9221N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi990 – 9901N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi1357 – 13571N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi1419 – 14191N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi1451 – 14511N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi1713 – 17131N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi2134 – 21341N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi2217 – 22171N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi2494 – 24941N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi2682 – 26821N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi2751 – 27511N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi2891 – 28911N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi2988 – 29881N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi3688 – 36881N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi3777 – 37771N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi3793 – 37931N-linked (GlcNAc...); by hostSequence Analysis

    Post-translational modificationi

    The E(rns) glycoprotein is heavily glycosylated.By similarity
    The viral RNA of pestiviruses is expressed as a single polyprotein which undergoes post-translational proteolytic processing resulting in the production of at least eleven individual proteins. The N-terminal protease cleaves itself from the nascent polyprotein autocatalytically and thereby generates the N-terminus of the adjacent viral capsid protein C By similarity.By similarity
    Cleavage between E2 and p7 is partial.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    The E(rns) glycoprotein is found as a homodimer; disulfide-linked. The E1 and E2 envelope glycoproteins form disulfide-linked homodimers as well as heterodimers.By similarity

    Structurei

    Secondary structure

    1
    3898
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi700 – 7067
    Beta strandi714 – 7163
    Beta strandi718 – 7203
    Beta strandi730 – 7323
    Beta strandi734 – 75017
    Beta strandi756 – 76510
    Helixi767 – 7693
    Beta strandi771 – 7766
    Beta strandi783 – 7864
    Beta strandi793 – 7953
    Helixi797 – 7993
    Beta strandi801 – 8088
    Beta strandi811 – 8144
    Beta strandi817 – 8204
    Beta strandi828 – 8358
    Turni837 – 8393
    Beta strandi842 – 85211
    Beta strandi863 – 8664
    Beta strandi869 – 8757
    Helixi878 – 8803
    Beta strandi882 – 8865
    Beta strandi894 – 8996
    Beta strandi902 – 9065
    Beta strandi910 – 9145
    Beta strandi916 – 9205
    Beta strandi924 – 9285
    Beta strandi934 – 9363
    Beta strandi939 – 9413
    Beta strandi946 – 9516
    Beta strandi954 – 9618
    Beta strandi964 – 9674
    Beta strandi969 – 9735
    Beta strandi976 – 9827
    Beta strandi985 – 9939
    Turni1005 – 10073
    Beta strandi1011 – 10133
    Beta strandi1016 – 10249

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YQ2X-ray2.58A/B696-1026[»]
    2YQ3X-ray3.29A/B696-1026[»]
    ProteinModelPortaliQ01499.
    SMRiQ01499. Positions 2684-2711, 3271-3858.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1144 – 116421HelicalPROSITE-ProRule annotationAdd
    BLAST
    Transmembranei1189 – 120921HelicalPROSITE-ProRule annotationAdd
    BLAST
    Transmembranei1217 – 123721HelicalPROSITE-ProRule annotationAdd
    BLAST
    Transmembranei1247 – 126721HelicalPROSITE-ProRule annotationAdd
    BLAST
    Transmembranei1281 – 130121HelicalPROSITE-ProRule annotationAdd
    BLAST
    Transmembranei1360 – 138021HelicalPROSITE-ProRule annotationAdd
    BLAST
    Transmembranei1568 – 158821HelicalPROSITE-ProRule annotationAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 168168Peptidase C53Add
    BLAST
    Domaini1441 – 1589149Peptidase C74PROSITE-ProRule annotationAdd
    BLAST
    Domaini1590 – 1763174Peptidase S31PROSITE-ProRule annotationAdd
    BLAST
    Domaini1802 – 1960159Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1978 – 2143166Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini3518 – 3641124RdRp catalyticPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the pestivirus polyprotein family.Curated
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
    Contains 1 peptidase C53 domain.Curated
    Contains 1 peptidase C74 domain.PROSITE-ProRule annotation
    Contains 1 peptidase S31 domain.PROSITE-ProRule annotation
    Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    3.90.730.10. 1 hit.
    InterProiIPR021824. Capsid-C_pestivirus.
    IPR011492. DEAD_Flavivir.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR022120. Pept_C74_NS2-pestiV.
    IPR008751. Peptidase_C53.
    IPR000280. Pestivirus_NS3_S31.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR002166. RNA_pol_HCV.
    IPR001568. RNase_T2-like.
    IPR018188. RNase_T2_AS.
    [Graphical view]
    PfamiPF11889. DUF3409. 1 hit.
    PF07652. Flavi_DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF05550. Peptidase_C53. 1 hit.
    PF12387. Peptidase_C74. 1 hit.
    PF05578. Peptidase_S31. 1 hit.
    PF00998. RdRP_3. 1 hit.
    [Graphical view]
    PRINTSiPR00729. CDVENDOPTASE.
    ProDomiPD003091. Peptidase_C53. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    SSF55895. SSF55895. 1 hit.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51692. PESTIVIRUS_NS2_PRO. 1 hit.
    PS51535. PESTIVIRUS_NS3PRO. 1 hit.
    PS50507. RDRP_SSRNA_POS. 1 hit.
    PS00531. RNASE_T2_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q01499-1 [UniParc]FASTAAdd to Basket

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    MELITNELLY KTYKQKPVGV EEPVYDQAGN PLFGERGAIH PQSTLKLPHK     50
    RGERNVPTSL ASLPKRGDCR SGNSKGPVSG IYLKPGPLFY QDYKGPVYHR 100
    APLELFEEGS MCETTKRIGR VTGSDGKLYH IYICIDGCIT VKSATRSHQR 150
    VLRWVHNRLD CPLWVTSCSD TKEEGATKKK QQKPDRLEKG RMKIVPKESE 200
    KDSKTKPPDA TIVVDGVKYQ VKKKGKVKSK NTQDGLYHNK NKPPESRKKL 250
    EKALLAWAIL AVVLIEVTMG ENITQWNLQD NGTEGIQRAM FQRGVNRSLH 300
    GIWPEKICTG VPSHLATDVE LKTIHGMMDA SEKTNYTCCR LQRHEWNKHG 350
    WCNWYNIEPW ILIMNRTQAN LTEGQPPREC AVTCRYDRDS DLNVVTQARD 400
    SPTPLTGCKK GKNFSFAGVL TRGPCNFEIA ASDVLFKEHE CTGVFQDTAH 450
    YLVDGVTNSL ESARQGTAKL TTWLGKQLGI LGKKLENKSK TWFGAYAASP 500
    YCDVDRKIGY IWFTKNCTPA CLPKNTKIIG PGKFDTNAED GKILHEMGGH 550
    LSEVLLLSLV VLSDFAPETA SAMYLILHFS IPQSHVDITD CDKTQLNLTI 600
    ELTTADVIPG SVWNLGKYVC IRPDWWPYET AAVLAFEEVG QVVKIVLRAL 650
    RDLTRIWNAA TTTAFLVCLI KMVRGQVVQG ILWLLLITGV QGHLDCKPEY 700
    SYAIAKNDRV GPLGAEGLTT VWKDYSHEMK LEDTMVIAWC KGGKFTYLSR 750
    CTRETRYLAI LHSRALPTSV VFKKLFEGQK QEDTVEMDDD FEFGLCPCDA 800
    KPIVRGKFNT TLLNGPAFQM VCPIGWTGTV SCMLANRDTL DTAVVRTYRR 850
    SVPFPYRQGC ITQKTLGEDL YDCALGGNWT CVTGDQSRYT GGLIESCKWC 900
    GYKFQKSEGL PHYPIGKCRL NNETGYRLVD DTSCDREGVA IVPHGLVKCK 950
    IGDTTVQVIA TDTKLGPMPC KPHEIISSEG PIEKTACTFN YTRTLKNKYF 1000
    EPRDSYFQQY MLKGDYQYWF DLEVTDHHRD YFAESILVVV VALLGGRYVL 1050
    WLLVTYMVLS EQKASGAQYG AGEVVMMGNL LTHDNVEVVT YFFLLYLLLR 1100
    EESVKKWVLL LYHILVAHPL KSVIVILLMI GDVVKADPGG QGYLGQIDVC 1150
    FTMVVIIIIG LIIARRDPTI VPLITIVASL RVTGLTYSPG VDAAMAVITI 1200
    TLLMVSYVTD YFRYKRWLQC ILSLVSGVFL IRCLIHLGRI ETPEVTIPNW 1250
    RPLTLILFYL ISTTVVTMWK IDLAGLLLQG VPILLLITTL WADFLTLILI 1300
    LPTYELVKLY YLKTIKTDIE KSWLGGLDYK RVDSIYDVDE SGEGVYLFPS 1350
    RQKAQKNFSM LLPLVRATLI SCVSSKWQLI YMAYLSVDFM YYMHRKVIEE 1400
    ISGGTNMISR IVAALIELNW SMEEEESKGL KKFYLLSGRL RNLIIKHKVR 1450
    NETVAGWYGE EEVYGMPKIM TIIKASTLNK NKHCIICTVC EGRKWKGGTC 1500
    PKCGRHGKPI TCGMSLADFE ERHYKRIFIR EGNFEGPFRQ EYNGFIQYTA 1550
    RGQLFLRNLP ILATKVKMLM VGNLGEEVGD LEHLGWILRG PAVCKKITEH 1600
    ERCHINILDK LTAFFGIMPR GTTPRAPVRF PTSLLKVRRG LETGWAYTHQ 1650
    GGISSVDHVT AGKDLLVCDS MGRTRVVCQS NNKLTDETEY GVKTDSGCPD 1700
    GARCYVLNPE AVNISGSKGA VVHLQKTGGE FTCVTASGTP AFFDLKNLKG 1750
    WSGLPIFEAS SGRVVGRVKV GKNEESKPTK IMSGIQTVSK NTADLTEMVK 1800
    KITSMNRGDF KQITLATGAG KTTELPKAVI EEIGRHKRVL VLIPLRAAAE 1850
    SVYQYMRLKH PSISFNLRIG DMKEGDMATG ITYASYGYFC QMPQPKLRAA 1900
    MVEYSYIFLD EYHCATPEQL AIIGKIHRFS ESIRVVAMTA TPAGSVTTTG 1950
    QKHPIEEFIA PEVMEGEDLG SQFLDIAGLK IPVDEMKGNM LVFVPTRNMA 2000
    VEVAKKLKAK GYNSGYYYSG EDPANLRVVT SQSPYVIVAT NAIESGVTLP 2050
    DLDTVVDTGL KCEKRVRVSS KIPFIVTGLK RMAVTVGEQA QRRGRVGRVK 2100
    PGRYYRSQET ATGSKDYHYD LLQAQRYGIE DGINVTKSFR EMNYDWSLYE 2150
    EDSLLITQLE ILNNLLISED LPAAVKNIMA RTDHPEPIQL AYNSYEVQVP 2200
    VLFPKIRNGE VTDTYENYSF LNARKLGEDV PVYIYATEDE DLAVDLLGLD 2250
    WPDPGNQQVV ETGKALKQVA GLSSAENALL VALFGYVGYQ ALSKRHVPMI 2300
    TDIYTIEDQR LEDTTHLQYA PNAIKTEGTE TELKELASGD VEKIMGAISD 2350
    YAAGGLDFVK SQAEKIKTAP LFKENVEAAR GYVQKLIDSL IEDKDVIIRY 2400
    GLWGTHTALY KSIAARLGHE TAFATLVLKW LAFGGETVSD HIRQAAVDLV 2450
    VYYVMNKPSF PGDTETQQEG RRFVASLFIS ALATYTYKTW NYNNLSKVVE 2500
    PALAYLPYAT SALKMFTPTR LESVVILSTT IYKTYLSIRK GKSDGLLGTG 2550
    ISAAMEILSQ NPVSVGISVM LGVGAIAAHN AIESSEQKRT LLMKVFVKNF 2600
    LDQAATDELV KENPEKIIMA LFEAVQTIGN PLRLIYHLYG VYYKGWEAKE 2650
    LSERTAGRNL FTLIMFEAFE LLGMDSEGKI RNLSGNYILD LIHGLHKQIN 2700
    RGLKKIVLGW APAPFSCDWT PSDERIRLPT DSYLRVETKC PCGYEMKALK 2750
    NVSGKLTKVE ESGPFLCRNR PGRGPVNYRV TKYYDDNLRE IRPVAKLEGQ 2800
    VEHYYKGVTA RIDYSKGKTL LATDKWEVEH GTLTRLTKRY TGVGFRGAYL 2850
    GDEPNHRDLV ERDCATITKN TVQFLKMKKG CAFTYDLTIS NLTRLIELVH 2900
    RNNLEEKEIP TATVTTWLAY TFVNEDVGTI KPVLGERVIP DPVVDINLQP 2950
    EVQVDTSEVG ITIIGKEAVM TTGVTPVMEK VEPDTDNNQS SVKIGLDEGN 3000
    YPGPGVQTHT LVEEIHNKDA RPFIMVLGSK SSMSNRAKTA RNINLYTGND 3050
    PREIRDLMAE GRILVVALRD IDPDLSELVD FKGTFLDREA LEALSLGQPK 3100
    PKQVTKAAIR DLLKEERQVE IPDWFTSDDP VFLDIAMKKD KYHLIGDVVE 3150
    VKDQAKALGA TDQTRIVKEV GSRTYTMKLS SWFLQASSKQ MSLTPLFEEL 3200
    LLRCPPATKS NKGHMASAYQ LAQGNWEPLG CGVHLGTVPA RRVKMHPYEA 3250
    YLKLKDLVEE EEKKPRIRDT VIREHNKWIL KKIKFQGNLN TKKMLNPGKL 3300
    SEQLDREGHK RNIYNNQIST VMSSAGIRLE KLPIVRAQTD TKSFHEAIRD 3350
    KIDKNENRQN PELHNKLLEI FHTIADPSLK HTYGEVTWEQ LEAGINRKGA 3400
    AGFLEKKNIG EVLDSEKHLV EQLVRDLKAG RKIRYYETAI PKNEKRDVSD 3450
    DWQAGDLVDE KKPRVIQYPE AKTRLAITKV MYNWVKQQPV VIPGYEGKTP 3500
    LFNIFNKVRK EWDLFNEPVA VSFDTKAWDT QVTSRDLHLI GEIQKYYYRK 3550
    EWHKFIDTIT DHMVEVPVIT ADGEVYIRNG QRGSGQPDTS AGNSMLNVLT 3600
    MIYAFCESTG VPYKSFNRVA KIHVCGDDGF LITEKGLGLK FSNKGMQILH 3650
    EAGKPQKLTE GEKMKVAYKF EDIEFCSHTP VPVRWSDNTS SYMAGRDTAV 3700
    ILSKMATRLD SSGERGTTAY EKAVAFSFLL MYSWNPLVRR ICLLVLSQRP 3750
    ETAPSTQTTY YYKGDPIGAY KDVIGRNLSE LKRTGFEKLA NLNLSLSTLG 3800
    IWTKHTSKRI IQDCVAIGKE EGNWLVNADR LISSKTGHLY IPDKGFTLQG 3850
    KHYEQLQLGA ETNPVMGVGT ERYKLGPIVN LLLRRLKVLL MAAVGASS 3898
    Length:3,898
    Mass (Da):437,808
    Last modified:July 1, 1993 - v1
    Checksum:i31ACEE140D407ED3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M96751 Genomic RNA. Translation: AAA42860.1.
    PIRiA44217.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M96751 Genomic RNA. Translation: AAA42860.1 .
    PIRi A44217.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YQ2 X-ray 2.58 A/B 696-1026 [» ]
    2YQ3 X-ray 3.29 A/B 696-1026 [» ]
    ProteinModelPortali Q01499.
    SMRi Q01499. Positions 2684-2711, 3271-3858.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S31.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 3.4.21.113. 925.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    3.90.730.10. 1 hit.
    InterProi IPR021824. Capsid-C_pestivirus.
    IPR011492. DEAD_Flavivir.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR022120. Pept_C74_NS2-pestiV.
    IPR008751. Peptidase_C53.
    IPR000280. Pestivirus_NS3_S31.
    IPR007094. RNA-dir_pol_PSvirus.
    IPR002166. RNA_pol_HCV.
    IPR001568. RNase_T2-like.
    IPR018188. RNase_T2_AS.
    [Graphical view ]
    Pfami PF11889. DUF3409. 1 hit.
    PF07652. Flavi_DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF05550. Peptidase_C53. 1 hit.
    PF12387. Peptidase_C74. 1 hit.
    PF05578. Peptidase_S31. 1 hit.
    PF00998. RdRP_3. 1 hit.
    [Graphical view ]
    PRINTSi PR00729. CDVENDOPTASE.
    ProDomi PD003091. Peptidase_C53. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    SSF55895. SSF55895. 1 hit.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51692. PESTIVIRUS_NS2_PRO. 1 hit.
    PS51535. PESTIVIRUS_NS3PRO. 1 hit.
    PS50507. RDRP_SSRNA_POS. 1 hit.
    PS00531. RNASE_T2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and nucleotide sequence of a pestivirus genome, noncytopathic bovine viral diarrhea virus strain SD-1."
      Deng R., Brock K.V.
      Virology 191:867-869(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

    Entry informationi

    Entry nameiPOLG_BVDVS
    AccessioniPrimary (citable) accession number: Q01499
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    BVDV is divided in two types: cytopathic and non-cytopathic. Both types of viruses can be found in animals suffering from mucosal disease, as a cytopathic BVDV can develop from a non-cytopathic virus within the infected animal by deletions, mutations or insertions. Both types express uncleaved NS2-3, but cytopathic strains also express NS3.

    Keywords - Technical termi

    3D-structure, Complete proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3