Q96662 (POLG_BVDVC) 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 CP7) (BVDV) (Mucosal disease virus) [Complete proteome]
Taxonomic identifier	268305 [NCBI]
Taxonomic lineage	Viruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Pestivirus
Virus host	Bos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length	3907 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. NS2 protease seems to play a vital role in viral RNA replication control and in the pathogenicity of the virus. NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS4A is a cofactor for the NS3 protease activity By similarity. RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome.
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 Probable. Ref.7 Envelope glycoprotein E2: Host cell surface By similarity Ref.7. Cysteine protease NS2: Host membrane; Multi-pass membrane protein Potential Ref.7.
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.
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	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 Initiation of viral infection Ion transport RNA replication Transport Viral attachment to host cell Viral immunoevasion Viral penetration into host cytoplasm Virus endocytosis by host
Cellular component	Host membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Helicase Hydrolase Ionic channel Nucleotidyltransferase Protease RNA-directed RNA polymerase Serine protease Thiol protease Transferase Viral ionic channel
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	evasion by virus of host immune response Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro 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 ion channel activity Inferred from electronic annotation. Source: UniProtKB-KW 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_0000038011

Chain

169 – 270

102

Capsid protein C By similarity

PRO_0000038012

Chain

271 – 497

227

E(rns) glycoprotein By similarity

PRO_0000038013

Chain

498 – 659

162

Envelope glycoprotein E1 By similarity

PRO_0000038014

Chain

660 – 1066

407

Envelope glycoprotein E2 By similarity

PRO_0000038015

Chain

1067 – 1136

70

p7

PRO_0000038016

Chain

1137 – 2281

1145

Non-structural protein 2-3 By similarity

PRO_0000038017

Chain

1137 – 1598

462

Cysteine protease NS2 By similarity

PRO_0000038018

Chain

1599 – 2281

683

Serine protease NS3 By similarity

PRO_0000038019

Chain

2282 – 2345

64

Non-structural protein 4A

PRO_0000038020

Chain

2346 – 2692

347

Non-structural protein 4B

PRO_0000038021

Chain

2693 – 3188

496

Non-structural protein 5A

PRO_0000038022

Chain

3189 – 3907

719

RNA-directed RNA polymerase

PRO_0000038023

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

1369 – 1389

21

Helical; Potential

Transmembrane

1577 – 1597

21

Helical; Potential

Domain

1 – 168

168

Peptidase C53

Domain

1450 – 1598

149

Peptidase C74

Domain

1599 – 1772

174

Peptidase S31

Domain

1811 – 1969

159

Helicase ATP-binding

Domain

1987 – 2152

166

Helicase C-terminal

Domain

3527 – 3650

124

RdRp catalytic

Compositional bias

1432 – 1435

4

Poly-Glu

Compositional bias

3268 – 3271

4

Poly-Glu

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

1456

1

For cysteine protease NS2 activity Ref.6

Active site

1470

1

For cysteine protease NS2 activity Ref.6

Active site

1521

1

For cysteine protease NS2 activity Ref.6

Active site

1667

1

Charge relay system; for serine protease NS3 activity By similarity

Active site

1704

1

Charge relay system; for serine protease NS3 activity By similarity

Active site

1761

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

Site

1136 – 1137

2

Cleavage; by host signal peptidase By similarity

Site

1598 – 1599

2

Cleavage; by NS2; in cytopathic strains By similarity

Site

2281 – 2282

2

Cleavage; by serine protease NS3

Site

2345 – 2346

2

Cleavage; by serine protease NS3

Site

2692 – 2693

2

Cleavage; by serine protease NS3

Site

3188 – 3189

2

Cleavage; by serine protease NS3

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

1366

1

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

Glycosylation

1428

1

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

Glycosylation

1460

1

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

Glycosylation

1722

1

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

Glycosylation

2143

1

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

Glycosylation

2226

1

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

Glycosylation

2503

1

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

Glycosylation

2691

1

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

Glycosylation

2900

1

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

Glycosylation

3697

1

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

Glycosylation

3802

1

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

Experimental info

Mutagenesis

438

1

E → A: Almost no effect on membrane association of E(rns) glycoprotein. Ref.7

Mutagenesis

446

1

Q → A: Almost no effect on membrane association of E(rns) glycoprotein. Ref.7

Mutagenesis

455

1

G → A: Almost no effect on membrane association of E(rns) glycoprotein. Ref.7

Mutagenesis

460

1

L → A: Reduced membrane association of E(rns) glycoprotein. Ref.7

Mutagenesis

461

1

E → A: Greatly reduced membrane association of E(rns) glycoprotein. Ref.7

Mutagenesis

462

1

S → A: Almost no effect on membrane association of E(rns) glycoprotein. Ref.7

Mutagenesis

465

1

Q → A: Almost no effect on membrane association of E(rns) glycoprotein. Ref.7

Mutagenesis

469

1

K → A: Almost no effect on membrane association of E(rns) glycoprotein. Ref.7

Mutagenesis

471

1

T → A: Almost no effect on membrane association of E(rns) glycoprotein. Ref.7

Mutagenesis

473

1

W → A: Reduced membrane association of E(rns) glycoprotein. Ref.7

Mutagenesis

476

1

R → A: Almost no effect on membrane association of E(rns) glycoprotein. Ref.7

Mutagenesis

478

1

L → A: Reduced membrane association of E(rns) glycoprotein. Ref.7

Mutagenesis

481

1

L → A: Reduced membrane association of E(rns) glycoprotein. Ref.7

Mutagenesis

486

1

E → A: Greatly reduced membrane association of E(rns) glycoprotein. Ref.7

Mutagenesis

487

1

N → A: Almost no effect on membrane association of E(rns) glycoprotein. Ref.7

Mutagenesis

489

1

S → A: Almost no effect on membrane association of E(rns) glycoprotein. Ref.7

Mutagenesis

492

1

W → A: Reduced membrane association of E(rns) glycoprotein. Ref.7

Secondary structure

1

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3907

Helix Strand Turn

Details...

Helix

2697 – 2718

22

Helix

3283 – 3291

9

Beta strand

3301 – 3308

8

Helix

3325 – 3334

10

Turn

3338 – 3340

3

Turn

3350 – 3352

3

Helix

3353 – 3360

8

Helix

3372 – 3380

9

Turn

3381 – 3383

3

Helix

3386 – 3388

3

Helix

3397 – 3401

5

Helix

3418 – 3424

7

Helix

3426 – 3438

13

Beta strand

3446 – 3450

5

Beta strand

3474 – 3478

5

Helix

3480 – 3494

15

Turn

3510 – 3512

3

Helix

3513 – 3521

9

Beta strand

3524 – 3532

9

Beta strand

3534 – 3536

3

Helix

3537 – 3540

4

Helix

3543 – 3556

14

Helix

3559 – 3561

3

Helix

3562 – 3572

11

Beta strand

3574 – 3579

6

Beta strand

3582 – 3589

8

Helix

3598 – 3618

21

Beta strand

3626 – 3634

9

Beta strand

3637 – 3643

7

Helix

3644 – 3661

18

Helix

3669 – 3671

3

Beta strand

3675 – 3678

4

Helix

3679 – 3681

3

Beta strand

3687 – 3694

8

Beta strand

3699 – 3704

6

Helix

3707 – 3715

9

Helix

3727 – 3741

15

Helix

3745 – 3754

10

Beta strand

3765 – 3773

9

Helix

3775 – 3783

9

Helix

3787 – 3789

3

Beta strand

3790 – 3793

4

Helix

3795 – 3801

7

Helix

3803 – 3807

5

Helix

3815 – 3828

14

Beta strand

3829 – 3831

3

Helix

3834 – 3837

4

Helix

3839 – 3845

7

Beta strand

3854 – 3858

5

Sequences

	Sequence		Length	Mass (Da)
	Q96662 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 9E4B019FF8042410	FASTA	3,907	439,104
	10 20 30 40 50 60 MELITNELLY KTYKQKPAGV EEPVYDQAGN PLFGERGVIH PQSTLKLPHK RGEREVPTNL 70 80 90 100 110 120 ASLPKRGDCR SGNSKGPVSG IYLKPGPLFY QDYKGPVYHR APLEFFEEAS MCETTKRIGR 130 140 150 160 170 180 VTGSDSRLYH IYVCIDGCII VKSATKDRQK VLKWVHNKLN CPLWVSSCSD TKDEGVVRKK 190 200 210 220 230 240 QQKPDRLEKG RMKITPKESE KDSKTKPPDA TIVVDGVKYQ VKKKGKVKSK NTQDGLYHNK 250 260 270 280 290 300 NKPQESRKKL EKALLAWAII ALVFFQVTMG ENITQWNLQD NGTEGIQRAM FQRGVNRSLH 310 320 330 340 350 360 GIWPEKICTG VPSHLATDTE LKAIHGMMDA SEKTNYTCCR LQRHEWNKHG WCNWYNIEPW 370 380 390 400 410 420 ILLMNKTQAN LTEGQPLREC AVTCRYDRDS DLNVVTQARD SPTPLTGCKK GKNFSFAGIL 430 440 450 460 470 480 VQGPCNFEIA VSDVLFKEHD CTSVIQDTAH YLVDGMTNSL ESARQGTAKL TTWLGRQLGI 490 500 510 520 530 540 LGKKLENKSK TWFGAYAASP YCEVERKLGY IWYTKNCTPA CLPRNTKIIG PGRFDTNAED 550 560 570 580 590 600 GKILHEMGGH LSEVLLLSVV VLSDFAPETA SVIYLILHFS IPQGHTDIQD CDKNQLNLTV 610 620 630 640 650 660 ELTTAEVIPG SVWNLGKYVC VRPDWWPYET ATVLVIEEVG QVIKVVLRAL KDLTRIWTAA 670 680 690 700 710 720 TTTAFLVCLV KVVRGQVLQG ILWLMLITGA QGYPDCKPGF SYAIAKNDEI GPLGATGLTT 730 740 750 760 770 780 QWYEYSDGMR LQDSVVEVWC KNGEIKYLIR CGREARYLAV LHTRALPTSV VFEKIFDGKE 790 800 810 820 830 840 QEDIVEMDDN FEFGLCPCDA RPLIRGKFNT TLLNGPAFQM VCPIGWTGTV SCTLANKDTL 850 860 870 880 890 900 ATIVVRTYKR VRPFPYRQDC VTQKTIGEDL YDCALGGNWT CVPGDALRYV AGPVESCEWC 910 920 930 940 950 960 GYKFLKSEGL PHFPIGKCRL KNESGYRQVD ETSCNRNGVA IVPSGTVKCK IGDTVVQVIA 970 980 990 1000 1010 1020 MDDKLGPMPC KPHEIISSEG PVEKTACTFN YTRTLKNKYF EPRDNYFQQY MLKGEYQYWF 1030 1040 1050 1060 1070 1080 DLEITDHHRD YFAESLLVIV VALLGGRYVL WLLVTYMILS EQMASGVQYG AGEIVMMGNL 1090 1100 1110 1120 1130 1140 LTHDSVEVVT YFLLLYLLLR EENTKKWVIL IYHIIVMHPL KSVTVILLMV GGMAKAEPGA 1150 1160 1170 1180 1190 1200 QGYLEQVDLS FTMITIIVIG LVIARRDPTV VPLVTIVAAL KITGLGFGPG VDAAMAVLTL 1210 1220 1230 1240 1250 1260 TLLMTSYVTD YFRYKRWIQC ILSLVAGVFL IRTLKHLGEL KTPELTIPNW RPLTFILLYL 1270 1280 1290 1300 1310 1320 TSATVVTRWK IDIAGIFLQG APILLMIATL WADFLTLVLI LPTYELAKLY YLKNVKTDVE 1330 1340 1350 1360 1370 1380 KSWGVPYPDP QTLGGLDYRT IDSVYDVDES GEGVYLFPSR QKKNKNISIL LPLIRATLIS 1390 1400 1410 1420 1430 1440 CISSKWQMVY MAYLTLDFMY YMHRKVIEEI SGSTNVMSRV IAALIELNWS MEEEESKGLK 1450 1460 1470 1480 1490 1500 KFFILSGRLR NLIIKHKVRN QTVASWYGEE EVYGMPKVVT IIRACTLNKN KHCIICTVCE 1510 1520 1530 1540 1550 1560 ARKWKGGNCP KCGRHGKPII CGMTLADFEE RHYKRIFIRE GNFEGPFRQE YNGFVQYTAR 1570 1580 1590 1600 1610 1620 GQLFLRNLPI LATKVKMIMV GNLGEEIGDL EHLGWILRGP AVCKKITEHE KCHVNILDKL 1630 1640 1650 1660 1670 1680 TAFFGVMPRG TTPRAPVRFP TALLKVRRGL ETGWAYTHQG GISSVDHVTA GKDLLVCDSM 1690 1700 1710 1720 1730 1740 GRTRVVCQSN NKLTDETEYG VKTDSGCPDG ARCYVLNPEA VNISGSKGAV VHLQKTGGEF 1750 1760 1770 1780 1790 1800 TCVTASGTPA FFDLKNLKGW SGLPIFEASS GRVVGRVKVG KNEESKPTKL MSGIQTVSKN 1810 1820 1830 1840 1850 1860 TADLTEMVKK ITSMNRGDFR QITLATGAGK TTELPKAVIE EIGRHKRVLV LIPLRAAAES 1870 1880 1890 1900 1910 1920 VYQYMRLKHP SISFNLRIGD MKEGDMATGI TYASYGYFCQ MPQPKLRAAM IEYSYIFLDE 1930 1940 1950 1960 1970 1980 YHCATPEQLA VIGKIHRFSE SIRVVAMTAT PAGSVTTTGQ KHPIEEFIAP EVMKGEDLGS 1990 2000 2010 2020 2030 2040 QFLDIAGLKI PVEEMKGNML VFVPTRNMAV EVAKKLKAKG YNSGYYYSGE DPANLRVVTS 2050 2060 2070 2080 2090 2100 QSPYVVVATN AIESGVTLPD LDTVVDTGLK CEKRVRVSSK IPFIVTGLKR MAVTVGEQAQ 2110 2120 2130 2140 2150 2160 RRGRVGRVKP GRYYRSQETA TGSKDYHYDL LQAQRYGIED GINVTKSFRE MNYDWSLYEE 2170 2180 2190 2200 2210 2220 DSLLITQLEI LNNLLISEDL PAAVKNIMAR TDHPEPIQLA YNSYEVQVPV LFPKIRNGEV 2230 2240 2250 2260 2270 2280 TDTYENYSFL NARKLGEDVP VYVYATEDED LAVDLLGLDW PDPGNQQVVE TGKALKQVVG 2290 2300 2310 2320 2330 2340 LSSAENALLI ALFGYVGYQA LSKRHVPMIT DIYTIEDQRL EDTTHLQYAP NAIRTEGKET 2350 2360 2370 2380 2390 2400 ELKELAVGDL DKIMGSISDY ASEGLNFVRS QAEKMRSAPA FKENVEAAKG YVQKFIDSLI 2410 2420 2430 2440 2450 2460 ENKETIIRYG LWGTHTALYK SIAARLGHET AFATLVIKWL AFGGESVSDH MRQAAVDLVV 2470 2480 2490 2500 2510 2520 YYVINKPSFP GDSETQQEGR RFVASLFISA LATYTYKTWN YNNLSKVVEP ALAYLPYATN 2530 2540 2550 2560 2570 2580 ALKMFTPTRL ESVVILSTTI YKTYLSIRKG KSDGLLGTGI SAAMEILSQN PVSVGISVML 2590 2600 2610 2620 2630 2640 GVGAIAAHNA IESSEQKRTL LMKVFVKNFL DQAATDELVK ENPEKIIMAL FEAVQTIGNP 2650 2660 2670 2680 2690 2700 LRLIYHLYGV YYKGWEAKEL SERTAGRNLF TLIMFEAFEL LGMDSEGKIR NLSGNYVLDL 2710 2720 2730 2740 2750 2760 IYSLHKQINR GLKKIVLGWA PAPFSCDWTP SDERIRLPTN NYLRVETKCP CGYEMKALRN 2770 2780 2790 2800 2810 2820 VGGSLTKVEE KGPFLCRNRL GRGPVNYRVT KYYDDNLKEI KPVAKLEGFV DHYYKGVTAR 2830 2840 2850 2860 2870 2880 IDYGRGKMLL ATDKWEVEHG VVTRLAKRYT GVGFKGAYLG DEPNHRDLVE RDCATITKNT 2890 2900 2910 2920 2930 2940 VQFLKMKKGC AFTYDLTLSN LTRLIELVHK NNLEEKDIPA ATVTTWLAYT FVNEDIGTIK 2950 2960 2970 2980 2990 3000 PVLGERVVTD PVVDVNLQPE VQVDTSEVGI TLVGRAALMT TGTTPVVEKT EPNADGGPSS 3010 3020 3030 3040 3050 3060 IKIGLDEGRY PGPGLQDRTL TDEIHSRDER PFVLVLGSKN SMSNRAKTAR NINLYKGNNP 3070 3080 3090 3100 3110 3120 REIRDLMAQG RMLVVALKDF NPELSELVDF KGTFLDREAL EALSLGRPKS KQVTTATVRE 3130 3140 3150 3160 3170 3180 LLEQEVQVEI PSWFGAGDPV FLEVTLKGDR YHLVGDVDRV KDQAKELGAT DQTRIVKEVG 3190 3200 3210 3220 3230 3240 ARTYTMKLSS WFLQATNKQM SLTPLFEELL LRCPPKIKSN KGHMASAYQL AQGNWEPLDC 3250 3260 3270 3280 3290 3300 GVHLGTIPAR RVKIHPYEAY LKLKDLLEEE EKKPKCRDTV IREHNKWILK KVRHQGNLNT 3310 3320 3330 3340 3350 3360 KKILNPGKLS EQLDREGHKR NIYNNQIGTI MTEAGSRLEK LPVVRAQTDT KSFHEAIRDK 3370 3380 3390 3400 3410 3420 IDKNENQQSP GLHDKLLEIF HTIAQPSLRH TYSDVTWEQL EAGVNRKGAA GFLEKKNVGE 3430 3440 3450 3460 3470 3480 VLDSEKHLVE QLIRDLKTGR KIRYYETAIP KNEKRDVSDD WQSGDLVDEK KPRVIQYPEA 3490 3500 3510 3520 3530 3540 KTRLAITKVM YNWVKQQPVV IPGYEGKTPL FNIFNKVRKE WDLFNEPVAV SFDTKAWDTQ 3550 3560 3570 3580 3590 3600 VTSRDLRLIG EIQKYYYRKE WHKFIDTITD HMVEVPVITA DGEVYIRNGQ RGSGQPDTSA 3610 3620 3630 3640 3650 3660 GNSMLNVLTM MYAFCESTGV PYKSFNRVAR IHVCGDDGFL ITEKGLGLKF ANNGMQILHE 3670 3680 3690 3700 3710 3720 AGKPQKITEG ERMKVAYRFE DIEFCSHTPV PVRWSDNTSS YMAGRDTAVI LSKMATRLDS 3730 3740 3750 3760 3770 3780 SGERGTIAYE KAVAFSFLLM YSWNPLVRRI CLLVLSQQPE TTPSTQTTYY YKGDPIGAYK 3790 3800 3810 3820 3830 3840 DVIGKNLCEL KRTGFEKLAN LNLSLSTLGI WSKHTSKRII QDCVTIGKEE GNWLVNADRL 3850 3860 3870 3880 3890 3900 ISSKTGHLYI PDKGYTLQGK HYEQLQLQAR TSPVTGVGTE RYKLGPIVNL LLRRLRVLLM AAVGASS

References

[1]	"Recovery of cytopathogenic and noncytopathogenic bovine viral diarrhea viruses from cDNA constructs." Meyers G., Tautz N., Becher P., Thiel H., Kuemmerer B.M. J. Virol. 70:8606-8613(1996) [PubMed: 8970985] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Mutations in the 5' nontranslated region of bovine viral diarrhea virus result in altered growth characteristics." Becher P., Orlich M., Thiel H.-J. J. Virol. 74:7884-7894(2000) [PubMed: 10933696] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: Isolate CP7-5A.
[3]	"Processing in the pestivirus E2-NS2 region: identification of proteins p7 and E2p7." Elbers K., Tautz N., Becher P., Stoll D., Ruemenapf T., Thiel H.-J. J. Virol. 70:4131-4135(1996) [PubMed: 8648755] [Abstract] Cited for: PROTEIN SEQUENCE OF 1067-1083, PROTEOLYTIC PROCESSING OF POLYPROTEIN.
[4]	"Serine protease of pestiviruses: determination of cleavage sites." Tautz N., Elbers K., Stoll D., Meyers G., Thiel H.-J. J. Virol. 71:5415-5422(1997) [PubMed: 9188613] [Abstract] Cited for: PROTEIN SEQUENCE OF 2282-2289; 2693-2705 AND 3189-3202, PROTEOLYTIC PROCESSING OF POLYPROTEIN.
[5]	"E2-p7 region of the bovine viral diarrhea virus polyprotein: processing and functional studies." Harada T., Tautz N., Thiel H.-J. J. Virol. 74:9498-9506(2000) [PubMed: 11000219] [Abstract] Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
[6]	"Temporal modulation of an autoprotease is crucial for replication and pathogenicity of an RNA virus." Lackner T., Mueller A., Pankraz A., Becher P., Thiel H.-J., Gorbalenya A.E., Tautz N. J. Virol. 78:10765-10775(2004) [PubMed: 15367643] [Abstract] Cited for: CLEAVAGE BETWEEN NS2 AND NS3, ACTIVE SITES OF NS2 PROTEASE. Strain: CP7 and NCP7.
[7]	"The pestivirus glycoprotein Erns is anchored in plane in the membrane via an amphipathic helix." Tews B.A., Meyers G. J. Biol. Chem. 282:32730-32741(2007) [PubMed: 17848558] [Abstract] Cited for: SUBCELLULAR LOCATION OF E(RNS) GLYCOPROTEIN, MUTAGENESIS OF GLU-438; GLN-446; GLY-455; LEU-460; GLU-461; SER-462; GLN-465; LYS-469; THR-471; TRP-473; ARG-476; LEU-478; LEU-481; GLU-486; ASN-487; SER-489 AND TRP-492.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U63479 Genomic RNA. Translation: AAC55984.1.
AF220247 Genomic RNA. Translation: AAG00378.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AJJ	NMR	-	A	2693-2720	[»]
2AJM	NMR	-	A	2693-2720	[»]
2AJN	NMR	-	A	2693-2720	[»]
2AJO	NMR	-	A	2693-2720	[»]
2CJQ	X-ray	2.60	A	3189-3907	[»]

ProteinModelPortal

Q96662.

SMR

Q96662. Positions 2693-2720, 3280-3860.

ModBase

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Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR021824. Capsid-C_pestivirus.
IPR014001. DEAD-like_helicase.
IPR011492. DEAD_Flavivir.
IPR001650. Helicase_C.
IPR022120. Pept_C74_NS2-pestiV.
IPR008751. Peptidase_C53.
IPR000280. Peptidase_S31.
IPR007094. RNA-dir_pol_PSvirus.
IPR002166. RNA_pol_HCV.
IPR001568. RNase_T2.
IPR018188. RNase_T2_AS.
[Graphical view]

Gene3D

G3DSA:3.90.730.10. RNase_T2. 1 hit.

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

Search...

Other

PMAP-CutDB

Q96662.

Entry information

Entry name

POLG_BVDVC

Accession

Primary (citable) accession number: Q96662

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	February 1, 1997
Last modified:	November 16, 2011
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program