Q01499 (POLG_BVDVS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Genome polyprotein Cleaved into the following 13 chains: N-terminal protease Short name=N-pro EC=3.4.22.- Alternative name(s): Autoprotease p20 Capsid protein C E(rns) glycoprotein Alternative name(s): gp44/48 Envelope glycoprotein E1 Alternative name(s): gp33 Envelope glycoprotein E2 Alternative name(s): gp55 p7 Non-structural protein 2-3 Cysteine protease NS2 EC=3.4.22.- Alternative name(s): Non-structural protein 2 Serine protease NS3 EC=3.4.21.113 EC=3.6.1.15 EC=3.6.4.13 Alternative name(s): Non-structural protein 3 Non-structural protein 4A Short name=NS4A Non-structural protein 4B Short name=NS4B Non-structural protein 5A Short name=NS5A RNA-directed RNA polymerase EC=2.7.7.48 Alternative name(s): NS5B
Organism	Bovine viral diarrhea virus (strain SD-1) (BVDV) (Mucosal disease virus) [Complete proteome]
Taxonomic identifier	31656 [NCBI]
Taxonomic lineage	Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Pestivirus › Bovine viral diarrhea virus
Virus host	Bos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length	3898 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. 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 By similarity. 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 By similarity.
Catalytic activity	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). NTP + H2O = NDP + phosphate. ATP + H2O = ADP + phosphate.
Subunit structure	The E(rns) glycoprotein is found as a homodimer; disulfide-linked By similarity. The E1 and E2 envelope glycoproteins form disulfide-linked homodimers as well as heterodimers By similarity.
Subcellular location	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. Envelope glycoprotein E2: Host cell surface By similarity. Cysteine protease NS2: Host membrane; Multi-pass membrane protein Potential.
Post-translational modification	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. Cleavage between E2 and p7 is partial By similarity.
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.
Sequence similarities	Belongs to the pestivirus polyprotein family. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 1 peptidase C53 domain. Contains 1 peptidase C74 domain. Contains 1 peptidase S31 domain. Contains 1 RdRp catalytic domain.

Ontologies

Keywords
Biological process	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 IFN-mediated response initiation by virus Inhibition of host IRF3 by virus Inhibition of host innate immune response by virus Ion transport Transport Viral RNA replication Viral attachment to host cell Viral immunoevasion Viral penetration into host cytoplasm Virus endocytosis by host Virus entry into host cell
Cellular component	Host membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Helicase Hydrolase Ion channel Nucleotidyltransferase Protease RNA-directed RNA polymerase Serine protease Thiol protease Transferase Viral ion channel
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	induction by virus of host autophagy Inferred from electronic annotation. Source: UniProtKB-KW ion transport Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host IRF3 activity Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host type I interferon production Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro viral attachment to host cell Inferred from electronic annotation. Source: UniProtKB-KW viral entry into host cell via clathrin-mediated endocytosis Inferred from electronic annotation. Source: UniProtKB-KW viral genome replication Inferred from electronic annotation. Source: InterPro viral protein processing Inferred from electronic annotation. Source: InterPro
Cellular_component	host cell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell host cell surface Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent helicase activity Inferred from electronic annotation. Source: InterPro RNA binding Inferred from electronic annotation. Source: InterPro RNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro ribonuclease T2 activity Inferred from electronic annotation. Source: InterPro serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro serine-type exopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 168

168

N-terminal protease By similarity

PRO_0000038037

Chain

169 – 270

102

Capsid protein C By similarity

PRO_0000038038

Chain

271 – 497

227

E(rns) glycoprotein By similarity

PRO_0000038039

Chain

498 – 659

162

Envelope glycoprotein E1 By similarity

PRO_0000038040

Chain

660 – 1066

407

Envelope glycoprotein E2 By similarity

PRO_0000038041

Chain

1067 – 1136

70

p7 By similarity

PRO_0000038042

Chain

1137 – 2272

1136

Non-structural protein 2-3 By similarity

PRO_0000038043

Chain

1137 – 1589

453

Cysteine protease NS2 By similarity

PRO_0000038044

Chain

1590 – 2272

683

Serine protease NS3 By similarity

PRO_0000038045

Chain

2273 – 2336

64

Non-structural protein 4A By similarity

PRO_0000038046

Chain

2337 – 2683

347

Non-structural protein 4B By similarity

PRO_0000038047

Chain

2684 – 3179

496

Non-structural protein 5A By similarity

PRO_0000038048

Chain

3180 – 3898

719

RNA-directed RNA polymerase By similarity

PRO_0000038049

Regions

Transmembrane

1144 – 1164

21

Helical; Potential

Transmembrane

1189 – 1209

21

Helical; Potential

Transmembrane

1217 – 1237

21

Helical; Potential

Transmembrane

1247 – 1267

21

Helical; Potential

Transmembrane

1281 – 1301

21

Helical; Potential

Transmembrane

1360 – 1380

21

Helical; Potential

Transmembrane

1568 – 1588

21

Helical; Potential

Domain

1 – 168

168

Peptidase C53

Domain

1441 – 1589

149

Peptidase C74

Domain

1590 – 1763

174

Peptidase S31

Domain

1802 – 1960

159

Helicase ATP-binding

Domain

1978 – 2143

166

Helicase C-terminal

Domain

3518 – 3641

124

RdRp catalytic

Sites

Active site

22

1

For N-terminal protease activity By similarity

Active site

49

1

For N-terminal protease activity By similarity

Active site

69

1

For N-terminal protease activity By similarity

Active site

1447

1

For cysteine protease NS2 activity By similarity

Active site

1461

1

For cysteine protease NS2 activity By similarity

Active site

1512

1

For cysteine protease NS2 activity By similarity

Active site

1658

1

Charge relay system; for serine protease NS3 activity By similarity

Active site

1695

1

Charge relay system; for serine protease NS3 activity By similarity

Active site

1752

1

Charge relay system; for serine protease NS3 activity By similarity

Site

168 – 169

2

Cleavage; by autolysis By similarity

Site

270 – 271

2

Cleavage; by host signal peptidase By similarity

Site

497 – 498

2

Cleavage By similarity

Site

659 – 660

2

Cleavage; by host signal peptidase By similarity

Site

1066 – 1067

2

Cleavage; by host signal peptidase; partial By similarity

Site

1136 – 1137

2

Cleavage; by host signal peptidase By similarity

Site

1589 – 1590

2

Cleavage; partial; cysteine protease NS2 By similarity

Site

2272 – 2273

2

Cleavage; by serine protease NS3 By similarity

Site

2336 – 2337

2

Cleavage; by serine protease NS3 By similarity

Site

2683 – 2684

2

Cleavage; by serine protease NS3 By similarity

Site

3179 – 3180

2

Cleavage; by serine protease NS3 By similarity

Amino acid modifications

Glycosylation

272

1

N-linked (GlcNAc...); by host Potential

Glycosylation

281

1

N-linked (GlcNAc...); by host Potential

Glycosylation

296

1

N-linked (GlcNAc...); by host Potential

Glycosylation

335

1

N-linked (GlcNAc...); by host Potential

Glycosylation

365

1

N-linked (GlcNAc...); by host Potential

Glycosylation

370

1

N-linked (GlcNAc...); by host Potential

Glycosylation

413

1

N-linked (GlcNAc...); by host Potential

Glycosylation

487

1

N-linked (GlcNAc...); by host Potential

Glycosylation

597

1

N-linked (GlcNAc...); by host Potential

Glycosylation

809

1

N-linked (GlcNAc...); by host Potential

Glycosylation

878

1

N-linked (GlcNAc...); by host Potential

Glycosylation

922

1

N-linked (GlcNAc...); by host Potential

Glycosylation

990

1

N-linked (GlcNAc...); by host Potential

Glycosylation

1357

1

N-linked (GlcNAc...); by host Potential

Glycosylation

1419

1

N-linked (GlcNAc...); by host Potential

Glycosylation

1451

1

N-linked (GlcNAc...); by host Potential

Glycosylation

1713

1

N-linked (GlcNAc...); by host Potential

Glycosylation

2134

1

N-linked (GlcNAc...); by host Potential

Glycosylation

2217

1

N-linked (GlcNAc...); by host Potential

Glycosylation

2494

1

N-linked (GlcNAc...); by host Potential

Glycosylation

2682

1

N-linked (GlcNAc...); by host Potential

Glycosylation

2751

1

N-linked (GlcNAc...); by host Potential

Glycosylation

2891

1

N-linked (GlcNAc...); by host Potential

Glycosylation

2988

1

N-linked (GlcNAc...); by host Potential

Glycosylation

3688

1

N-linked (GlcNAc...); by host Potential

Glycosylation

3777

1

N-linked (GlcNAc...); by host Potential

Glycosylation

3793

1

N-linked (GlcNAc...); by host Potential

Secondary structure

1

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3898

Helix Strand Turn

Details...

Beta strand

700 – 706

7

Beta strand

714 – 716

3

Beta strand

718 – 720

3

Beta strand

730 – 732

3

Beta strand

734 – 750

17

Beta strand

756 – 765

10

Helix

767 – 769

3

Beta strand

771 – 776

6

Beta strand

783 – 786

4

Beta strand

793 – 795

3

Helix

797 – 799

3

Beta strand

801 – 808

8

Beta strand

811 – 814

4

Beta strand

817 – 820

4

Beta strand

828 – 835

8

Turn

837 – 839

3

Beta strand

842 – 852

11

Beta strand

863 – 866

4

Beta strand

869 – 875

7

Helix

878 – 880

3

Beta strand

882 – 886

5

Beta strand

894 – 899

6

Beta strand

902 – 906

5

Beta strand

910 – 914

5

Beta strand

916 – 920

5

Beta strand

924 – 928

5

Beta strand

934 – 936

3

Beta strand

939 – 941

3

Beta strand

946 – 951

6

Beta strand

954 – 961

8

Beta strand

964 – 967

4

Beta strand

969 – 973

5

Beta strand

976 – 982

7

Beta strand

985 – 993

9

Turn

1005 – 1007

3

Beta strand

1011 – 1013

3

Beta strand

1016 – 1024

9

Sequences

	Sequence		Length	Mass (Da)
	Q01499 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 31ACEE140D407ED3	FASTA	3,898	437,808
	10 20 30 40 50 60 MELITNELLY KTYKQKPVGV EEPVYDQAGN PLFGERGAIH PQSTLKLPHK RGERNVPTSL 70 80 90 100 110 120 ASLPKRGDCR SGNSKGPVSG IYLKPGPLFY QDYKGPVYHR APLELFEEGS MCETTKRIGR 130 140 150 160 170 180 VTGSDGKLYH IYICIDGCIT VKSATRSHQR VLRWVHNRLD CPLWVTSCSD TKEEGATKKK 190 200 210 220 230 240 QQKPDRLEKG RMKIVPKESE KDSKTKPPDA TIVVDGVKYQ VKKKGKVKSK NTQDGLYHNK 250 260 270 280 290 300 NKPPESRKKL EKALLAWAIL AVVLIEVTMG ENITQWNLQD NGTEGIQRAM FQRGVNRSLH 310 320 330 340 350 360 GIWPEKICTG VPSHLATDVE LKTIHGMMDA SEKTNYTCCR LQRHEWNKHG WCNWYNIEPW 370 380 390 400 410 420 ILIMNRTQAN LTEGQPPREC AVTCRYDRDS DLNVVTQARD SPTPLTGCKK GKNFSFAGVL 430 440 450 460 470 480 TRGPCNFEIA ASDVLFKEHE CTGVFQDTAH YLVDGVTNSL ESARQGTAKL TTWLGKQLGI 490 500 510 520 530 540 LGKKLENKSK TWFGAYAASP YCDVDRKIGY IWFTKNCTPA CLPKNTKIIG PGKFDTNAED 550 560 570 580 590 600 GKILHEMGGH LSEVLLLSLV VLSDFAPETA SAMYLILHFS IPQSHVDITD CDKTQLNLTI 610 620 630 640 650 660 ELTTADVIPG SVWNLGKYVC IRPDWWPYET AAVLAFEEVG QVVKIVLRAL RDLTRIWNAA 670 680 690 700 710 720 TTTAFLVCLI KMVRGQVVQG ILWLLLITGV QGHLDCKPEY SYAIAKNDRV GPLGAEGLTT 730 740 750 760 770 780 VWKDYSHEMK LEDTMVIAWC KGGKFTYLSR CTRETRYLAI LHSRALPTSV VFKKLFEGQK 790 800 810 820 830 840 QEDTVEMDDD FEFGLCPCDA KPIVRGKFNT TLLNGPAFQM VCPIGWTGTV SCMLANRDTL 850 860 870 880 890 900 DTAVVRTYRR SVPFPYRQGC ITQKTLGEDL YDCALGGNWT CVTGDQSRYT GGLIESCKWC 910 920 930 940 950 960 GYKFQKSEGL PHYPIGKCRL NNETGYRLVD DTSCDREGVA IVPHGLVKCK IGDTTVQVIA 970 980 990 1000 1010 1020 TDTKLGPMPC KPHEIISSEG PIEKTACTFN YTRTLKNKYF EPRDSYFQQY MLKGDYQYWF 1030 1040 1050 1060 1070 1080 DLEVTDHHRD YFAESILVVV VALLGGRYVL WLLVTYMVLS EQKASGAQYG AGEVVMMGNL 1090 1100 1110 1120 1130 1140 LTHDNVEVVT YFFLLYLLLR EESVKKWVLL LYHILVAHPL KSVIVILLMI GDVVKADPGG 1150 1160 1170 1180 1190 1200 QGYLGQIDVC FTMVVIIIIG LIIARRDPTI VPLITIVASL RVTGLTYSPG VDAAMAVITI 1210 1220 1230 1240 1250 1260 TLLMVSYVTD YFRYKRWLQC ILSLVSGVFL IRCLIHLGRI ETPEVTIPNW RPLTLILFYL 1270 1280 1290 1300 1310 1320 ISTTVVTMWK IDLAGLLLQG VPILLLITTL WADFLTLILI LPTYELVKLY YLKTIKTDIE 1330 1340 1350 1360 1370 1380 KSWLGGLDYK RVDSIYDVDE SGEGVYLFPS RQKAQKNFSM LLPLVRATLI SCVSSKWQLI 1390 1400 1410 1420 1430 1440 YMAYLSVDFM YYMHRKVIEE ISGGTNMISR IVAALIELNW SMEEEESKGL KKFYLLSGRL 1450 1460 1470 1480 1490 1500 RNLIIKHKVR NETVAGWYGE EEVYGMPKIM TIIKASTLNK NKHCIICTVC EGRKWKGGTC 1510 1520 1530 1540 1550 1560 PKCGRHGKPI TCGMSLADFE ERHYKRIFIR EGNFEGPFRQ EYNGFIQYTA RGQLFLRNLP 1570 1580 1590 1600 1610 1620 ILATKVKMLM VGNLGEEVGD LEHLGWILRG PAVCKKITEH ERCHINILDK LTAFFGIMPR 1630 1640 1650 1660 1670 1680 GTTPRAPVRF PTSLLKVRRG LETGWAYTHQ GGISSVDHVT AGKDLLVCDS MGRTRVVCQS 1690 1700 1710 1720 1730 1740 NNKLTDETEY GVKTDSGCPD GARCYVLNPE AVNISGSKGA VVHLQKTGGE FTCVTASGTP 1750 1760 1770 1780 1790 1800 AFFDLKNLKG WSGLPIFEAS SGRVVGRVKV GKNEESKPTK IMSGIQTVSK NTADLTEMVK 1810 1820 1830 1840 1850 1860 KITSMNRGDF KQITLATGAG KTTELPKAVI EEIGRHKRVL VLIPLRAAAE SVYQYMRLKH 1870 1880 1890 1900 1910 1920 PSISFNLRIG DMKEGDMATG ITYASYGYFC QMPQPKLRAA MVEYSYIFLD EYHCATPEQL 1930 1940 1950 1960 1970 1980 AIIGKIHRFS ESIRVVAMTA TPAGSVTTTG QKHPIEEFIA PEVMEGEDLG SQFLDIAGLK 1990 2000 2010 2020 2030 2040 IPVDEMKGNM LVFVPTRNMA VEVAKKLKAK GYNSGYYYSG EDPANLRVVT SQSPYVIVAT 2050 2060 2070 2080 2090 2100 NAIESGVTLP DLDTVVDTGL KCEKRVRVSS KIPFIVTGLK RMAVTVGEQA QRRGRVGRVK 2110 2120 2130 2140 2150 2160 PGRYYRSQET ATGSKDYHYD LLQAQRYGIE DGINVTKSFR EMNYDWSLYE EDSLLITQLE 2170 2180 2190 2200 2210 2220 ILNNLLISED LPAAVKNIMA RTDHPEPIQL AYNSYEVQVP VLFPKIRNGE VTDTYENYSF 2230 2240 2250 2260 2270 2280 LNARKLGEDV PVYIYATEDE DLAVDLLGLD WPDPGNQQVV ETGKALKQVA GLSSAENALL 2290 2300 2310 2320 2330 2340 VALFGYVGYQ ALSKRHVPMI TDIYTIEDQR LEDTTHLQYA PNAIKTEGTE TELKELASGD 2350 2360 2370 2380 2390 2400 VEKIMGAISD YAAGGLDFVK SQAEKIKTAP LFKENVEAAR GYVQKLIDSL IEDKDVIIRY 2410 2420 2430 2440 2450 2460 GLWGTHTALY KSIAARLGHE TAFATLVLKW LAFGGETVSD HIRQAAVDLV VYYVMNKPSF 2470 2480 2490 2500 2510 2520 PGDTETQQEG RRFVASLFIS ALATYTYKTW NYNNLSKVVE PALAYLPYAT SALKMFTPTR 2530 2540 2550 2560 2570 2580 LESVVILSTT IYKTYLSIRK GKSDGLLGTG ISAAMEILSQ NPVSVGISVM LGVGAIAAHN 2590 2600 2610 2620 2630 2640 AIESSEQKRT LLMKVFVKNF LDQAATDELV KENPEKIIMA LFEAVQTIGN PLRLIYHLYG 2650 2660 2670 2680 2690 2700 VYYKGWEAKE LSERTAGRNL FTLIMFEAFE LLGMDSEGKI RNLSGNYILD LIHGLHKQIN 2710 2720 2730 2740 2750 2760 RGLKKIVLGW APAPFSCDWT PSDERIRLPT DSYLRVETKC PCGYEMKALK NVSGKLTKVE 2770 2780 2790 2800 2810 2820 ESGPFLCRNR PGRGPVNYRV TKYYDDNLRE IRPVAKLEGQ VEHYYKGVTA RIDYSKGKTL 2830 2840 2850 2860 2870 2880 LATDKWEVEH GTLTRLTKRY TGVGFRGAYL GDEPNHRDLV ERDCATITKN TVQFLKMKKG 2890 2900 2910 2920 2930 2940 CAFTYDLTIS NLTRLIELVH RNNLEEKEIP TATVTTWLAY TFVNEDVGTI KPVLGERVIP 2950 2960 2970 2980 2990 3000 DPVVDINLQP EVQVDTSEVG ITIIGKEAVM TTGVTPVMEK VEPDTDNNQS SVKIGLDEGN 3010 3020 3030 3040 3050 3060 YPGPGVQTHT LVEEIHNKDA RPFIMVLGSK SSMSNRAKTA RNINLYTGND PREIRDLMAE 3070 3080 3090 3100 3110 3120 GRILVVALRD IDPDLSELVD FKGTFLDREA LEALSLGQPK PKQVTKAAIR DLLKEERQVE 3130 3140 3150 3160 3170 3180 IPDWFTSDDP VFLDIAMKKD KYHLIGDVVE VKDQAKALGA TDQTRIVKEV GSRTYTMKLS 3190 3200 3210 3220 3230 3240 SWFLQASSKQ MSLTPLFEEL LLRCPPATKS NKGHMASAYQ LAQGNWEPLG CGVHLGTVPA 3250 3260 3270 3280 3290 3300 RRVKMHPYEA YLKLKDLVEE EEKKPRIRDT VIREHNKWIL KKIKFQGNLN TKKMLNPGKL 3310 3320 3330 3340 3350 3360 SEQLDREGHK RNIYNNQIST VMSSAGIRLE KLPIVRAQTD TKSFHEAIRD KIDKNENRQN 3370 3380 3390 3400 3410 3420 PELHNKLLEI FHTIADPSLK HTYGEVTWEQ LEAGINRKGA AGFLEKKNIG EVLDSEKHLV 3430 3440 3450 3460 3470 3480 EQLVRDLKAG RKIRYYETAI PKNEKRDVSD DWQAGDLVDE KKPRVIQYPE AKTRLAITKV 3490 3500 3510 3520 3530 3540 MYNWVKQQPV VIPGYEGKTP LFNIFNKVRK EWDLFNEPVA VSFDTKAWDT QVTSRDLHLI 3550 3560 3570 3580 3590 3600 GEIQKYYYRK EWHKFIDTIT DHMVEVPVIT ADGEVYIRNG QRGSGQPDTS AGNSMLNVLT 3610 3620 3630 3640 3650 3660 MIYAFCESTG VPYKSFNRVA KIHVCGDDGF LITEKGLGLK FSNKGMQILH EAGKPQKLTE 3670 3680 3690 3700 3710 3720 GEKMKVAYKF EDIEFCSHTP VPVRWSDNTS SYMAGRDTAV ILSKMATRLD SSGERGTTAY 3730 3740 3750 3760 3770 3780 EKAVAFSFLL MYSWNPLVRR ICLLVLSQRP ETAPSTQTTY YYKGDPIGAY KDVIGRNLSE 3790 3800 3810 3820 3830 3840 LKRTGFEKLA NLNLSLSTLG IWTKHTSKRI IQDCVAIGKE EGNWLVNADR LISSKTGHLY 3850 3860 3870 3880 3890 IPDKGFTLQG KHYEQLQLGA ETNPVMGVGT ERYKLGPIVN LLLRRLKVLL MAAVGASS

References

[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].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M96751 Genomic RNA. Translation: AAA42860.1.

PIR

A44217.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q01499.

SMR

Q01499. Positions 2684-2711, 3271-3858.

ModBase

Search...

Protein family/group databases

MEROPS

S31.001.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

3.4.21.113. 925.

Family and domain databases

Gene3D

3.90.730.10. 1 hit.

InterPro

IPR021824. Capsid-C_pestivirus.
IPR011492. DEAD_Flavivir.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
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]

Pfam

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]

PRINTS

PR00729. CDVENDOPTASE.

ProDom

PD003091. Peptidase_C53. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]

SUPFAM

SSF55895. RNase_T2. 1 hit.

PROSITE

PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51535. PESTIVIRUS_NS3PRO. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
PS00531. RNASE_T2_2. 1 hit.
[Graphical view]

ProtoNet

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Entry information

Entry name

POLG_BVDVS

Accession

Primary (citable) accession number: Q01499

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	May 1, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program