P19711 (POLG_BVDVN) 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 (isolate NADL) (BVDV) (Mucosal disease virus) [Reference proteome]
Taxonomic identifier	11100 [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	3988 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 Probable. Ref.7 Ref.9 P7 forms a leader sequence to properly orient NS2 in the membrane By similarity. Ref.7 Ref.9 Uncleaved NS2-3 is required for production of infectious virus. Ref.7 Ref.9 NS2 protease seems to play a vital role in viral RNA replication control and in the pathogenicity of the virus. Ref.7 Ref.9 NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. Ref.7 Ref.9 NS4A is a cofactor for the NS3 protease activity By similarity. Ref.7 Ref.9 RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome. Ref.7 Ref.9
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. Ref.4 Envelope glycoprotein E2: Host cell surface Ref.4. Cysteine protease NS2: Host membrane; Multi-pass membrane protein Potential Ref.4.
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. Cleavage between NS2 and NS3 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. The cytopathic NADL strain contains an insertion (Jiv 90) that potentiate the partial cleavage of NS2-3. Removal of this insertion in the NADL Jiv 90- strain results in a non-cytopathic strain in which NS2-3 remains uncleaved.
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 Direct protein sequencing Reference 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_0000038024

Chain

169 – 270

102

Capsid protein C By similarity

PRO_0000038025

Chain

271 – 497

227

E(rns) glycoprotein By similarity

PRO_0000038026

Chain

498 – 659

162

Envelope glycoprotein E1 By similarity

PRO_0000038027

Chain

660 – 1066

407

Envelope glycoprotein E2 By similarity

PRO_0000038028

Chain

1067 – 1136

70

p7 By similarity

PRO_0000038029

Chain

1137 – 2362

1226

Non-structural protein 2-3

PRO_0000038030

Chain

1137 – 1679

543

Cysteine protease NS2

PRO_0000038031

Chain

1680 – 2362

683

Serine protease NS3

PRO_0000038032

Chain

2363 – 2426

64

Non-structural protein 4A By similarity

PRO_0000038033

Chain

2427 – 2773

347

Non-structural protein 4B By similarity

PRO_0000038034

Chain

2774 – 3269

496

Non-structural protein 5A By similarity

PRO_0000038035

Chain

3270 – 3988

719

RNA-directed RNA polymerase By similarity

PRO_0000038036

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

1658 – 1678

21

Helical; Potential

Domain

1 – 168

168

Peptidase C53

Domain

1441 – 1679

239

Peptidase C74

Domain

1680 – 1853

174

Peptidase S31

Domain

1892 – 2050

159

Helicase ATP-binding

Domain

2068 – 2233

166

Helicase C-terminal

Domain

3608 – 3731

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

1748

1

Charge relay system; for serine protease NS3 activity By similarity

Active site

1785

1

Charge relay system; for serine protease NS3 activity By similarity

Active site

1842

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

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

1679 – 1680

2

Cleavage; partial; cysteine protease NS2

Site

2362 – 2363

2

Cleavage; by serine protease NS3 By similarity

Site

2426 – 2427

2

Cleavage; by serine protease NS3 By similarity

Site

2773 – 2774

2

Cleavage; by serine protease NS3 By similarity

Site

3269 – 3270

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

1803

1

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

Glycosylation

2224

1

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

Glycosylation

2307

1

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

Glycosylation

2584

1

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

Glycosylation

2772

1

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

Glycosylation

2981

1

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

Glycosylation

3778

1

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

Glycosylation

3867

1

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

Glycosylation

3883

1

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

Secondary structure

1

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3988

Helix Strand Turn

Details...

Helix

3364 – 3372

9

Beta strand

3373 – 3376

4

Beta strand

3382 – 3384

3

Beta strand

3388 – 3392

5

Beta strand

3402 – 3404

3

Helix

3406 – 3414

9

Helix

3419 – 3421

3

Beta strand

3422 – 3427

6

Helix

3431 – 3440

10

Helix

3453 – 3462

10

Helix

3467 – 3469

3

Turn

3470 – 3472

3

Helix

3478 – 3481

4

Turn

3482 – 3484

3

Helix

3501 – 3504

4

Helix

3507 – 3518

12

Beta strand

3527 – 3531

5

Beta strand

3535 – 3537

3

Helix

3539 – 3543

5

Beta strand

3549 – 3551

3

Beta strand

3555 – 3558

4

Helix

3563 – 3570

8

Helix

3572 – 3575

4

Helix

3586 – 3588

3

Helix

3591 – 3593

3

Helix

3594 – 3603

10

Beta strand

3605 – 3612

8

Beta strand

3615 – 3617

3

Helix

3618 – 3621

4

Helix

3624 – 3637

14

Helix

3640 – 3642

3

Helix

3643 – 3652

10

Beta strand

3655 – 3660

6

Beta strand

3665 – 3668

4

Helix

3679 – 3699

21

Helix

3703 – 3705

3

Helix

3706 – 3709

4

Beta strand

3710 – 3715

6

Beta strand

3718 – 3724

7

Helix

3725 – 3741

17

Beta strand

3750 – 3753

4

Beta strand

3756 – 3759

4

Helix

3760 – 3762

3

Beta strand

3768 – 3775

8

Beta strand

3780 – 3785

6

Helix

3788 – 3797

10

Beta strand

3802 – 3804

3

Beta strand

3808 – 3810

3

Helix

3811 – 3822

12

Helix

3826 – 3837

12

Beta strand

3846 – 3854

9

Helix

3856 – 3864

9

Helix

3868 – 3870

3

Beta strand

3871 – 3874

4

Helix

3876 – 3882

7

Helix

3885 – 3888

4

Helix

3896 – 3908

13

Beta strand

3910 – 3912

3

Turn

3915 – 3918

4

Helix

3920 – 3926

7

Beta strand

3935 – 3939

5

Sequences

	Sequence		Length	Mass (Da)
	P19711 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 4474212F338661B8	FASTA	3,988	449,163
	10 20 30 40 50 60 MELITNELLY KTYKQKPVGV EEPVYDQAGD PLFGERGAVH PQSTLKLPHK RGERDVPTNL 70 80 90 100 110 120 ASLPKRGDCR SGNSRGPVSG IYLKPGPLFY QDYKGPVYHR APLELFEEGS MCETTKRIGR 130 140 150 160 170 180 VTGSDGKLYH IYVCIDGCII IKSATRSYQR VFRWVHNRLD CPLWVTTCSD TKEEGATKKK 190 200 210 220 230 240 TQKPDRLERG KMKIVPKESE KDSKTKPPDA TIVVEGVKYQ VRKKGKTKSK NTQDGLYHNK 250 260 270 280 290 300 NKPQESRKKL EKALLAWAII AIVLFQVTMG ENITQWNLQD NGTEGIQRAM FQRGVNRSLH 310 320 330 340 350 360 GIWPEKICTG VPSHLATDIE LKTIHGMMDA SEKTNYTCCR LQRHEWNKHG WCNWYNIEPW 370 380 390 400 410 420 ILVMNRTQAN LTEGQPPREC AVTCRYDRAS DLNVVTQARD SPTPLTGCKK GKNFSFAGIL 430 440 450 460 470 480 MRGPCNFEIA ASDVLFKEHE RISMFQDTTL YLVDGLTNSL EGARQGTAKL TTWLGKQLGI 490 500 510 520 530 540 LGKKLENKSK TWFGAYAASP YCDVDRKIGY IWYTKNCTPA CLPKNTKIVG PGKFGTNAED 550 560 570 580 590 600 GKILHEMGGH LSEVLLLSLV VLSDFAPETA SVMYLILHFS IPQSHVDVMD CDKTQLNLTV 610 620 630 640 650 660 ELTTAEVIPG SVWNLGKYVC IRPNWWPYET TVVLAFEEVS QVVKLVLRAL RDLTRIWNAA 670 680 690 700 710 720 TTTAFLVCLV KIVRGQMVQG ILWLLLITGV QGHLDCKPEF SYAIAKDERI GQLGAEGLTT 730 740 750 760 770 780 TWKEYSPGMK LEDTMVIAWC EDGKLMYLQR CTRETRYLAI LHTRALPTSV VFKKLFDGRK 790 800 810 820 830 840 QEDVVEMNDN FEFGLCPCDA KPIVRGKFNT TLLNGPAFQM VCPIGWTGTV SCTSFNMDTL 850 860 870 880 890 900 ATTVVRTYRR SKPFPHRQGC ITQKNLGEDL HNCILGGNWT CVPGDQLLYK GGSIESCKWC 910 920 930 940 950 960 GYQFKESEGL PHYPIGKCKL ENETGYRLVD STSCNREGVA IVPQGTLKCK IGKTTVQVIA 970 980 990 1000 1010 1020 MDTKLGPMPC RPYEIISSEG PVEKTACTFN YTKTLKNKYF EPRDSYFQQY MLKGEYQYWF 1030 1040 1050 1060 1070 1080 DLEVTDHHRD YFAESILVVV VALLGGRYVL WLLVTYMVLS EQKALGIQYG SGEVVMMGNL 1090 1100 1110 1120 1130 1140 LTHNNIEVVT YFLLLYLLLR EESVKKWVLL LYHILVVHPI KSVIVILLMI GDVVKADSGG 1150 1160 1170 1180 1190 1200 QEYLGKIDLC FTTVVLIVIG LIIARRDPTI VPLVTIMAAL RVTELTHQPG VDIAVAVMTI 1210 1220 1230 1240 1250 1260 TLLMVSYVTD YFRYKKWLQC ILSLVSAVFL IRSLIYLGRI EMPEVTIPNW RPLTLILLYL 1270 1280 1290 1300 1310 1320 ISTTIVTRWK VDVAGLLLQC VPILLLVTTL WADFLTLILI LPTYELVKLY YLKTVRTDTE 1330 1340 1350 1360 1370 1380 RSWLGGIDYT RVDSIYDVDE SGEGVYLFPS RQKAQGNFSI LLPLIKATLI SCVSSKWQLI 1390 1400 1410 1420 1430 1440 YMSYLTLDFM YYMHRKVIEE ISGGTNIISR LVAALIELNW SMEEEESKGL KKFYLLSGRL 1450 1460 1470 1480 1490 1500 RNLIIKHKVR NETVASWYGE EEVYGMPKIM TIIKASTLSK SRHCIICTVC EGREWKGGTC 1510 1520 1530 1540 1550 1560 PKCGRHGKPI TCGMSLADFE ERHYKRIFIR EGNFEGMCSR CQGKHRRFEM DREPKSARYC 1570 1580 1590 1600 1610 1620 AECNRLHPAE EGDFWAESSM LGLKITYFAL MDGKVYDITE WAGCQRVGIS PDTHRVPCHI 1630 1640 1650 1660 1670 1680 SFGSRMPFRQ EYNGFVQYTA RGQLFLRNLP VLATKVKMLM VGNLGEEIGN LEHLGWILRG 1690 1700 1710 1720 1730 1740 PAVCKKITEH EKCHINILDK LTAFFGIMPR GTTPRAPVRF PTSLLKVRRG LETAWAYTHQ 1750 1760 1770 1780 1790 1800 GGISSVDHVT AGKDLLVCDS MGRTRVVCQS NNRLTDETEY GVKTDSGCPD GARCYVLNPE 1810 1820 1830 1840 1850 1860 AVNISGSKGA VVHLQKTGGE FTCVTASGTP AFFDLKNLKG WSGLPIFEAS SGRVVGRVKV 1870 1880 1890 1900 1910 1920 GKNEESKPTK IMSGIQTVSK NRADLTEMVK KITSMNRGDF KQITLATGAG KTTELPKAVI 1930 1940 1950 1960 1970 1980 EEIGRHKRVL VLIPLRAAAE SVYQYMRLKH PSISFNLRIG DMKEGDMATG ITYASYGYFC 1990 2000 2010 2020 2030 2040 QMPQPKLRAA MVEYSYIFLD EYHCATPEQL AIIGKIHRFS ESIRVVAMTA TPAGSVTTTG 2050 2060 2070 2080 2090 2100 QKHPIEEFIA PEVMKGEDLG SQFLDIAGLK IPVDEMKGNM LVFVPTRNMA VEVAKKLKAK 2110 2120 2130 2140 2150 2160 GYNSGYYYSG EDPANLRVVT SQSPYVIVAT NAIESGVTLP DLDTVIDTGL KCEKRVRVSS 2170 2180 2190 2200 2210 2220 KIPFIVTGLK RMAVTVGEQA QRRGRVGRVK PGRYYRSQET ATGSKDYHYD LLQAQRYGIE 2230 2240 2250 2260 2270 2280 DGINVTKSFR EMNYDWSLYE EDSLLITQLE ILNNLLISED LPAAVKNIMA RTDHPEPIQL 2290 2300 2310 2320 2330 2340 AYNSYEVQVP VLFPKIRNGE VTDTYENYSF LNARKLGEDV PVYIYATEDE DLAVDLLGLD 2350 2360 2370 2380 2390 2400 WPDPGNQQVV ETGKALKQVT GLSSAENALL VALFGYVGYQ ALSKRHVPMI TDIYTIEDQR 2410 2420 2430 2440 2450 2460 LEDTTHLQYA PNAIKTDGTE TELKELASGD VEKIMGAISD YAAGGLEFVK SQAEKIKTAP 2470 2480 2490 2500 2510 2520 LFKENAEAAK GYVQKFIDSL IENKEEIIRY GLWGTHTALY KSIAARLGHE TAFATLVLKW 2530 2540 2550 2560 2570 2580 LAFGGESVSD HVKQAAVDLV VYYVMNKPSF PGDSETQQEG RRFVASLFIS ALATYTYKTW 2590 2600 2610 2620 2630 2640 NYHNLSKVVE PALAYLPYAT SALKMFTPTR LESVVILSTT IYKTYLSIRK GKSDGLLGTG 2650 2660 2670 2680 2690 2700 ISAAMEILSQ NPVSVGISVM LGVGAIAAHN AIESSEQKRT LLMKVFVKNF LDQAATDELV 2710 2720 2730 2740 2750 2760 KENPEKIIMA LFEAVQTIGN PLRLIYHLYG VYYKGWEAKE LSERTAGRNL FTLIMFEAFE 2770 2780 2790 2800 2810 2820 LLGMDSQGKI RNLSGNYILD LIYGLHKQIN RGLKKMVLGW APAPFSCDWT PSDERIRLPT 2830 2840 2850 2860 2870 2880 DNYLRVETRC PCGYEMKAFK NVGGKLTKVE ESGPFLCRNR PGRGPVNYRV TKYYDDNLRE 2890 2900 2910 2920 2930 2940 IKPVAKLEGQ VEHYYKGVTA KIDYSKGKML LATDKWEVEH GVITRLAKRY TGVGFNGAYL 2950 2960 2970 2980 2990 3000 GDEPNHRALV ERDCATITKN TVQFLKMKKG CAFTYDLTIS NLTRLIELVH RNNLEEKEIP 3010 3020 3030 3040 3050 3060 TATVTTWLAY TFVNEDVGTI KPVLGERVIP DPVVDINLQP EVQVDTSEVG ITIIGRETLM 3070 3080 3090 3100 3110 3120 TTGVTPVLEK VEPDASDNQN SVKIGLDEGN YPGPGIQTHT LTEEIHNRDA RPFIMILGSR 3130 3140 3150 3160 3170 3180 NSISNRAKTA RNINLYTGND PREIRDLMAA GRMLVVALRD VDPELSEMVD FKGTFLDREA 3190 3200 3210 3220 3230 3240 LEALSLGQPK PKQVTKEAVR NLIEQKKDVE IPNWFASDDP VFLEVALKND KYYLVGDVGE 3250 3260 3270 3280 3290 3300 LKDQAKALGA TDQTRIIKEV GSRTYAMKLS SWFLKASNKQ MSLTPLFEEL LLRCPPATKS 3310 3320 3330 3340 3350 3360 NKGHMASAYQ LAQGNWEPLG CGVHLGTIPA RRVKIHPYEA YLKLKDFIEE EEKKPRVKDT 3370 3380 3390 3400 3410 3420 VIREHNKWIL KKIRFQGNLN TKKMLNPGKL SEQLDREGRK RNIYNHQIGT IMSSAGIRLE 3430 3440 3450 3460 3470 3480 KLPIVRAQTD TKTFHEAIRD KIDKSENRQN PELHNKLLEI FHTIAQPTLK HTYGEVTWEQ 3490 3500 3510 3520 3530 3540 LEAGVNRKGA AGFLEKKNIG EVLDSEKHLV EQLVRDLKAG RKIKYYETAI PKNEKRDVSD 3550 3560 3570 3580 3590 3600 DWQAGDLVVE KRPRVIQYPE AKTRLAITKV MYNWVKQQPV VIPGYEGKTP LFNIFDKVRK 3610 3620 3630 3640 3650 3660 EWDSFNEPVA VSFDTKAWDT QVTSKDLQLI GEIQKYYYKK EWHKFIDTIT DHMTEVPVIT 3670 3680 3690 3700 3710 3720 ADGEVYIRNG QRGSGQPDTS AGNSMLNVLT MMYGFCESTG VPYKSFNRVA RIHVCGDDGF 3730 3740 3750 3760 3770 3780 LITEKGLGLK FANKGMQILH EAGKPQKITE GEKMKVAYRF EDIEFCSHTP VPVRWSDNTS 3790 3800 3810 3820 3830 3840 SHMAGRDTAV ILSKMATRLD SSGERGTTAY EKAVAFSFLL MYSWNPLVRR ICLLVLSQQP 3850 3860 3870 3880 3890 3900 ETDPSKHATY YYKGDPIGAY KDVIGRNLSE LKRTGFEKLA NLNLSLSTLG VWTKHTSKRI 3910 3920 3930 3940 3950 3960 IQDCVAIGKE EGNWLVKPDR LISSKTGHLY IPDKGFTLQG KHYEQLQLRT ETNPVMGVGT 3970 3980 ERYKLGPIVN LLLRRLKILL MTAVGVSS

References

[1]	"Molecular cloning and nucleotide sequence of the pestivirus bovine viral diarrhea virus." Collett M.S., Larson R., Gold C., Strick D., Anderson D.K., Purchio A.F. Virology 165:191-199(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Proteins encoded by bovine viral diarrhea virus: the genomic organization of a pestivirus." Collett M.S., Larson R., Belzer S.K., Retzel E. Virology 165:200-208(1988) [PubMed] [Europe PMC] [Abstract] Cited for: GENOMIC ORGANIZATION.
[3]	"Bovine viral diarrhea virus NS3 serine proteinase: polyprotein cleavage sites, cofactor requirements, and molecular model of an enzyme essential for pestivirus replication." Xu J., Mendez E., Caron P.R., Lin C., Murcko M.A., Collett M.S., Rice C.M. J. Virol. 71:5312-5322(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2363-2376; 2427-2441; 2774-2788 AND 3270-3284, PROTEOLYTIC PROCESSING OF POLYPROTEIN.
[4]	"Localization of pestiviral envelope proteins E(rns) and E2 at the cell surface and on isolated particles." Weiland F., Weiland E., Unger G., Saalmuller A., Thiel H.-J. J. Gen. Virol. 80:1157-1165(1999) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[5]	"Hepatitis C virus and other flaviviridae viruses enter cells via low density lipoprotein receptor." Agnello V., Abel G., Elfahal M., Knight G.B., Zhang Q.X. Proc. Natl. Acad. Sci. U.S.A. 96:12766-12771(1999) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE OF BOVINE LOW-DENSITY-LIPOPROTEIN RECEPTOR IN VIRUS ATTACHMENT TO HOST CELL.
[6]	"Interactions of bovine viral diarrhoea virus glycoprotein E(rns) with cell surface glycosaminoglycans." Iqbal M., Flick-Smith H., McCauley J.W. J. Gen. Virol. 81:451-459(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION OF E(RNS) WITH CELL SURFACE GLYCOSAMINOGLYCANS.
[7]	"Uncleaved NS2-3 is required for production of infectious bovine viral diarrhea virus." Agapov E.V., Murray C.L., Frolov I., Qu L., Myers T.M., Rice C.M. J. Virol. 78:2414-2425(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF NS2-3. Strain: Isolate NADL Jiv 90(-).
[8]	"CD46 is a cellular receptor for bovine viral diarrhea virus." Maurer K., Krey T., Moennig V., Thiel H.-J., Ruemenapf T. J. Virol. 78:1792-1799(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION OF VIRUS WITH BOVINE CD46.
[9]	"Bovine viral diarrhea virus entry is dependent on clathrin-mediated endocytosis." Lecot S., Belouzard S., Dubuisson J., Rouille Y. J. Virol. 79:10826-10829(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF E1/E2 HETERODIMER.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M31182 Genomic RNA. Translation: AAA42854.1.

PIR

GNWVBV. A29198.

RefSeq

NP_040937.1. NC_001461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1S48	X-ray	3.00	A	3340-3948	[»]
1S49	X-ray	3.00	A	3340-3948	[»]
1S4F	X-ray	3.00	A/B/C/D	3348-3948	[»]

ProteinModelPortal

P19711.

SMR

P19711. Positions 2774-2801, 3361-3948.

ModBase

Search...

Protein family/group databases

MEROPS

C74.001.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

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

Search...

Other

EvolutionaryTrace

P19711.

Entry information

Entry name

POLG_BVDVN

Accession

Primary (citable) accession number: P19711

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program