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Protein

Genome polyprotein

Gene
N/A
Organism
Bovine viral diarrhea virus (strain CP7) (BVDV) (Mucosal disease virus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.
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 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
Active sitei1456 – 14561For cysteine protease NS2 activityPROSITE-ProRule annotation1 Publication
Active sitei1470 – 14701For cysteine protease NS2 activityPROSITE-ProRule annotation1 Publication
Active sitei1521 – 15211For cysteine protease NS2 activityPROSITE-ProRule annotation1 Publication
Active sitei1667 – 16671Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1704 – 17041Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1761 – 17611Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

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

Protein family/group databases

TCDBi1.A.53.1.5. the hepatitis c virus p7 viroporin cation-selective channel (hcv-p7) family.

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 CP7) (BVDV) (Mucosal disease virus)
Taxonomic identifieri268305 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaePestivirus
Virus hostiBos taurus (Bovine) [TaxID: 9913]
Proteomesi
  • UP000007618 Componenti: Genome

Subcellular locationi

E(rns) glycoprotein :
Cysteine protease NS2 :
  • Host membrane PROSITE-ProRule annotation; Multi-pass membrane protein PROSITE-ProRule annotation

Topology

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
Transmembranei1369 – 138921HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei1577 – 159721HelicalPROSITE-ProRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host membrane, Membrane, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi438 – 4381E → A: Almost no effect on membrane association of E(rns) glycoprotein. 1 Publication
Mutagenesisi446 – 4461Q → A: Almost no effect on membrane association of E(rns) glycoprotein. 1 Publication
Mutagenesisi455 – 4551G → A: Almost no effect on membrane association of E(rns) glycoprotein. 1 Publication
Mutagenesisi460 – 4601L → A: Reduced membrane association of E(rns) glycoprotein. 1 Publication
Mutagenesisi461 – 4611E → A: Greatly reduced membrane association of E(rns) glycoprotein. 1 Publication
Mutagenesisi462 – 4621S → A: Almost no effect on membrane association of E(rns) glycoprotein. 1 Publication
Mutagenesisi465 – 4651Q → A: Almost no effect on membrane association of E(rns) glycoprotein. 1 Publication
Mutagenesisi469 – 4691K → A: Almost no effect on membrane association of E(rns) glycoprotein. 1 Publication
Mutagenesisi471 – 4711T → A: Almost no effect on membrane association of E(rns) glycoprotein. 1 Publication
Mutagenesisi473 – 4731W → A: Reduced membrane association of E(rns) glycoprotein. 1 Publication
Mutagenesisi476 – 4761R → A: Almost no effect on membrane association of E(rns) glycoprotein. 1 Publication
Mutagenesisi478 – 4781L → A: Reduced membrane association of E(rns) glycoprotein. 1 Publication
Mutagenesisi481 – 4811L → A: Reduced membrane association of E(rns) glycoprotein. 1 Publication
Mutagenesisi486 – 4861E → A: Greatly reduced membrane association of E(rns) glycoprotein. 1 Publication
Mutagenesisi487 – 4871N → A: Almost no effect on membrane association of E(rns) glycoprotein. 1 Publication
Mutagenesisi489 – 4891S → A: Almost no effect on membrane association of E(rns) glycoprotein. 1 Publication
Mutagenesisi492 – 4921W → A: Reduced membrane association of E(rns) glycoprotein. 1 Publication

Chemistry

ChEMBLiCHEMBL3937.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 168168N-terminal proteaseBy similarityPRO_0000038011Add
BLAST
Chaini169 – 270102Capsid protein CBy similarityPRO_0000038012Add
BLAST
Chaini271 – 497227E(rns) glycoproteinBy similarityPRO_0000038013Add
BLAST
Chaini498 – 659162Envelope glycoprotein E1By similarityPRO_0000038014Add
BLAST
Chaini660 – 1066407Envelope glycoprotein E2By similarityPRO_0000038015Add
BLAST
Chaini1067 – 113670p7PRO_0000038016Add
BLAST
Chaini1137 – 22811145Non-structural protein 2-3By similarityPRO_0000038017Add
BLAST
Chaini1137 – 1598462Cysteine protease NS2PROSITE-ProRule annotationPRO_0000038018Add
BLAST
Chaini1599 – 2281683Serine protease NS3By similarityPRO_0000038019Add
BLAST
Chaini2282 – 234564Non-structural protein 4APRO_0000038020Add
BLAST
Chaini2346 – 2692347Non-structural protein 4BPRO_0000038021Add
BLAST
Chaini2693 – 3188496Non-structural protein 5APRO_0000038022Add
BLAST
Chaini3189 – 3907719RNA-directed RNA polymerasePRO_0000038023Add
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
Glycosylationi1366 – 13661N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi1428 – 14281N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi1460 – 14601N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi1722 – 17221N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2143 – 21431N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2226 – 22261N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2503 – 25031N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2691 – 26911N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2900 – 29001N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi3697 – 36971N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi3802 – 38021N-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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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; partial
Sitei1136 – 11372Cleavage; by host signal peptidaseBy similarity
Sitei1598 – 15992Cleavage; by NS2; in cytopathic strainsBy similarity
Sitei2281 – 22822Cleavage; by serine protease NS3
Sitei2345 – 23462Cleavage; by serine protease NS3
Sitei2692 – 26932Cleavage; by serine protease NS3
Sitei3188 – 31892Cleavage; by serine protease NS3

Keywords - PTMi

Disulfide bond, Glycoprotein

Miscellaneous databases

PMAP-CutDBQ96662.

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

Protein-protein interaction databases

IntActiQ96662. 1 interaction.

Chemistry

BindingDBiQ96662.

Structurei

Secondary structure

1
3907
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi273 – 2786Combined sources
Helixi286 – 2938Combined sources
Beta strandi297 – 3037Combined sources
Helixi318 – 3225Combined sources
Helixi332 – 3343Combined sources
Helixi340 – 34910Combined sources
Helixi351 – 3544Combined sources
Helixi357 – 37317Combined sources
Beta strandi377 – 38711Combined sources
Turni388 – 3914Combined sources
Beta strandi392 – 40110Combined sources
Beta strandi413 – 4164Combined sources
Beta strandi419 – 4268Combined sources
Helixi2697 – 271822Combined sources
Helixi3283 – 32919Combined sources
Beta strandi3301 – 33088Combined sources
Helixi3325 – 333410Combined sources
Turni3338 – 33403Combined sources
Turni3350 – 33523Combined sources
Helixi3353 – 33608Combined sources
Helixi3372 – 33809Combined sources
Turni3381 – 33833Combined sources
Helixi3386 – 33883Combined sources
Helixi3397 – 34015Combined sources
Helixi3418 – 34247Combined sources
Helixi3426 – 343813Combined sources
Beta strandi3446 – 34505Combined sources
Beta strandi3474 – 34785Combined sources
Helixi3480 – 349415Combined sources
Turni3510 – 35123Combined sources
Helixi3513 – 35219Combined sources
Beta strandi3524 – 35329Combined sources
Beta strandi3534 – 35363Combined sources
Helixi3537 – 35404Combined sources
Helixi3543 – 355614Combined sources
Helixi3559 – 35613Combined sources
Helixi3562 – 357211Combined sources
Beta strandi3574 – 35796Combined sources
Beta strandi3582 – 35898Combined sources
Helixi3598 – 361821Combined sources
Beta strandi3627 – 36348Combined sources
Beta strandi3637 – 36437Combined sources
Helixi3644 – 366118Combined sources
Helixi3669 – 36713Combined sources
Beta strandi3675 – 36784Combined sources
Helixi3679 – 36813Combined sources
Beta strandi3687 – 36948Combined sources
Beta strandi3699 – 37046Combined sources
Helixi3707 – 37159Combined sources
Helixi3727 – 374115Combined sources
Helixi3745 – 375410Combined sources
Beta strandi3765 – 37739Combined sources
Helixi3775 – 37839Combined sources
Helixi3787 – 37893Combined sources
Beta strandi3790 – 37934Combined sources
Helixi3795 – 38017Combined sources
Helixi3803 – 38075Combined sources
Helixi3815 – 382814Combined sources
Beta strandi3829 – 38313Combined sources
Helixi3834 – 38374Combined sources
Helixi3839 – 38457Combined sources
Beta strandi3854 – 38585Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AJJNMR-A2693-2720[»]
2AJMNMR-A2693-2720[»]
2AJNNMR-A2693-2720[»]
2AJONMR-A2693-2720[»]
2CJQX-ray2.60A3189-3907[»]
4DVKX-ray2.21A/B271-435[»]
4DVLX-ray2.75A/B271-435[»]
4DVNX-ray2.38A/B271-435[»]
4DW3X-ray2.35A/B271-435[»]
4DW4X-ray2.23A/B271-435[»]
4DW5X-ray2.21A/B271-435[»]
4DW7X-ray3.08A/B271-435[»]
4DWAX-ray3.01A/B271-435[»]
4DWCX-ray2.89A/B271-435[»]
ProteinModelPortaliQ96662.
SMRiQ96662. Positions 2693-2720, 3280-3860.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96662.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 168168Peptidase C53Add
BLAST
Domaini1450 – 1598149Peptidase C74PROSITE-ProRule annotationAdd
BLAST
Domaini1599 – 1772174Peptidase S31PROSITE-ProRule annotationAdd
BLAST
Domaini1811 – 1969159Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1987 – 2152166Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini3527 – 3650124RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1432 – 14354Poly-Glu
Compositional biasi3268 – 32714Poly-Glu

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.
IPR022120. NS2.
IPR030399. NS2_C74.
IPR027417. P-loop_NTPase.
IPR008751. Peptidase_C53.
IPR032521. Pestivirus_E2.
IPR000280. Pestivirus_NS3_S31.
IPR007094. RNA-dir_pol_PSvirus.
IPR002166. RNA_pol_HCV.
IPR001568. RNase_T2-like.
IPR033130. RNase_T2_His_AS_2.
[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.
PF16329. Pestivirus_E2. 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.

Q96662-1 [UniParc]FASTAAdd to basket

« Hide

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

AAVGASS
Length:3,907
Mass (Da):439,104
Last modified:February 1, 1997 - v1
Checksum:i9E4B019FF8042410
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63479 Genomic RNA. Translation: AAC55984.1.
AF220247 Genomic RNA. Translation: AAG00378.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U63479 Genomic RNA. Translation: AAC55984.1.
AF220247 Genomic RNA. Translation: AAG00378.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AJJNMR-A2693-2720[»]
2AJMNMR-A2693-2720[»]
2AJNNMR-A2693-2720[»]
2AJONMR-A2693-2720[»]
2CJQX-ray2.60A3189-3907[»]
4DVKX-ray2.21A/B271-435[»]
4DVLX-ray2.75A/B271-435[»]
4DVNX-ray2.38A/B271-435[»]
4DW3X-ray2.35A/B271-435[»]
4DW4X-ray2.23A/B271-435[»]
4DW5X-ray2.21A/B271-435[»]
4DW7X-ray3.08A/B271-435[»]
4DWAX-ray3.01A/B271-435[»]
4DWCX-ray2.89A/B271-435[»]
ProteinModelPortaliQ96662.
SMRiQ96662. Positions 2693-2720, 3280-3860.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ96662. 1 interaction.

Chemistry

BindingDBiQ96662.
ChEMBLiCHEMBL3937.

Protein family/group databases

TCDBi1.A.53.1.5. the hepatitis c virus p7 viroporin cation-selective channel (hcv-p7) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ96662.
PMAP-CutDBQ96662.

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.
IPR022120. NS2.
IPR030399. NS2_C74.
IPR027417. P-loop_NTPase.
IPR008751. Peptidase_C53.
IPR032521. Pestivirus_E2.
IPR000280. Pestivirus_NS3_S31.
IPR007094. RNA-dir_pol_PSvirus.
IPR002166. RNA_pol_HCV.
IPR001568. RNase_T2-like.
IPR033130. RNase_T2_His_AS_2.
[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.
PF16329. Pestivirus_E2. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_BVDVC
AccessioniPrimary (citable) accession number: Q96662
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: February 1, 1997
Last modified: March 16, 2016
This is version 133 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, Direct protein sequencing

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.