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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)DescriptionActionsGraphical viewLength
Active sitei22For N-terminal protease activityPROSITE-ProRule annotation1
Active sitei49For N-terminal protease activityPROSITE-ProRule annotation1
Active sitei69For N-terminal protease activityPROSITE-ProRule annotation1
Active sitei1456For cysteine protease NS2 activityPROSITE-ProRule annotation1 Publication1
Active sitei1470For cysteine protease NS2 activityPROSITE-ProRule annotation1 Publication1
Active sitei1521For cysteine protease NS2 activityPROSITE-ProRule annotation1 Publication1
Active sitei1667Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1704Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1761Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1

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)DescriptionActionsGraphical viewLength
Transmembranei1144 – 1164HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei1189 – 1209HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei1217 – 1237HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei1247 – 1267HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei1281 – 1301HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei1369 – 1389HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei1577 – 1597HelicalPROSITE-ProRule annotationAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host membrane, Membrane, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi438E → A: Almost no effect on membrane association of E(rns) glycoprotein. 1 Publication1
Mutagenesisi446Q → A: Almost no effect on membrane association of E(rns) glycoprotein. 1 Publication1
Mutagenesisi455G → A: Almost no effect on membrane association of E(rns) glycoprotein. 1 Publication1
Mutagenesisi460L → A: Reduced membrane association of E(rns) glycoprotein. 1 Publication1
Mutagenesisi461E → A: Greatly reduced membrane association of E(rns) glycoprotein. 1 Publication1
Mutagenesisi462S → A: Almost no effect on membrane association of E(rns) glycoprotein. 1 Publication1
Mutagenesisi465Q → A: Almost no effect on membrane association of E(rns) glycoprotein. 1 Publication1
Mutagenesisi469K → A: Almost no effect on membrane association of E(rns) glycoprotein. 1 Publication1
Mutagenesisi471T → A: Almost no effect on membrane association of E(rns) glycoprotein. 1 Publication1
Mutagenesisi473W → A: Reduced membrane association of E(rns) glycoprotein. 1 Publication1
Mutagenesisi476R → A: Almost no effect on membrane association of E(rns) glycoprotein. 1 Publication1
Mutagenesisi478L → A: Reduced membrane association of E(rns) glycoprotein. 1 Publication1
Mutagenesisi481L → A: Reduced membrane association of E(rns) glycoprotein. 1 Publication1
Mutagenesisi486E → A: Greatly reduced membrane association of E(rns) glycoprotein. 1 Publication1
Mutagenesisi487N → A: Almost no effect on membrane association of E(rns) glycoprotein. 1 Publication1
Mutagenesisi489S → A: Almost no effect on membrane association of E(rns) glycoprotein. 1 Publication1
Mutagenesisi492W → A: Reduced membrane association of E(rns) glycoprotein. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3937.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000380111 – 168N-terminal proteaseBy similarityAdd BLAST168
ChainiPRO_0000038012169 – 270Capsid protein CBy similarityAdd BLAST102
ChainiPRO_0000038013271 – 497E(rns) glycoproteinBy similarityAdd BLAST227
ChainiPRO_0000038014498 – 659Envelope glycoprotein E1By similarityAdd BLAST162
ChainiPRO_0000038015660 – 1066Envelope glycoprotein E2By similarityAdd BLAST407
ChainiPRO_00000380161067 – 1136p7Add BLAST70
ChainiPRO_00000380171137 – 2281Non-structural protein 2-3By similarityAdd BLAST1145
ChainiPRO_00000380181137 – 1598Cysteine protease NS2PROSITE-ProRule annotationAdd BLAST462
ChainiPRO_00000380191599 – 2281Serine protease NS3By similarityAdd BLAST683
ChainiPRO_00000380202282 – 2345Non-structural protein 4AAdd BLAST64
ChainiPRO_00000380212346 – 2692Non-structural protein 4BAdd BLAST347
ChainiPRO_00000380222693 – 3188Non-structural protein 5AAdd BLAST496
ChainiPRO_00000380233189 – 3907RNA-directed RNA polymeraseAdd BLAST719

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi272N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi281N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi296N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi335N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi365N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi370N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi413N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi487N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi597N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi809N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi878N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi922N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi990N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1366N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1428N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1460N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1722N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2143N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2226N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2503N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2691N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2900N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi3697N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi3802N-linked (GlcNAc...); by hostSequence analysis1

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)DescriptionActionsGraphical viewLength
Sitei168 – 169Cleavage; by autolysisBy similarity2
Sitei270 – 271Cleavage; by host signal peptidaseBy similarity2
Sitei497 – 498CleavageBy similarity2
Sitei659 – 660Cleavage; by host signal peptidaseBy similarity2
Sitei1066 – 1067Cleavage; by host signal peptidase; partial2
Sitei1136 – 1137Cleavage; by host signal peptidaseBy similarity2
Sitei1598 – 1599Cleavage; by NS2; in cytopathic strainsBy similarity2
Sitei2281 – 2282Cleavage; by serine protease NS32
Sitei2345 – 2346Cleavage; by serine protease NS32
Sitei2692 – 2693Cleavage; by serine protease NS32
Sitei3188 – 3189Cleavage; by serine protease NS32

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 interactor.

Chemistry databases

BindingDBiQ96662.

Structurei

Secondary structure

13907
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi273 – 278Combined sources6
Helixi286 – 293Combined sources8
Beta strandi297 – 303Combined sources7
Helixi318 – 322Combined sources5
Helixi332 – 334Combined sources3
Helixi340 – 349Combined sources10
Helixi351 – 354Combined sources4
Helixi357 – 373Combined sources17
Beta strandi377 – 387Combined sources11
Turni388 – 391Combined sources4
Beta strandi392 – 401Combined sources10
Beta strandi413 – 416Combined sources4
Beta strandi419 – 426Combined sources8
Helixi2697 – 2718Combined sources22
Helixi3283 – 3291Combined sources9
Beta strandi3301 – 3308Combined sources8
Helixi3325 – 3334Combined sources10
Turni3338 – 3340Combined sources3
Turni3350 – 3352Combined sources3
Helixi3353 – 3360Combined sources8
Helixi3372 – 3380Combined sources9
Turni3381 – 3383Combined sources3
Helixi3386 – 3388Combined sources3
Helixi3397 – 3401Combined sources5
Helixi3418 – 3424Combined sources7
Helixi3426 – 3438Combined sources13
Beta strandi3446 – 3450Combined sources5
Beta strandi3474 – 3478Combined sources5
Helixi3480 – 3494Combined sources15
Turni3510 – 3512Combined sources3
Helixi3513 – 3521Combined sources9
Beta strandi3524 – 3532Combined sources9
Beta strandi3534 – 3536Combined sources3
Helixi3537 – 3540Combined sources4
Helixi3543 – 3556Combined sources14
Helixi3559 – 3561Combined sources3
Helixi3562 – 3572Combined sources11
Beta strandi3574 – 3579Combined sources6
Beta strandi3582 – 3589Combined sources8
Helixi3598 – 3618Combined sources21
Beta strandi3627 – 3634Combined sources8
Beta strandi3637 – 3643Combined sources7
Helixi3644 – 3661Combined sources18
Helixi3669 – 3671Combined sources3
Beta strandi3675 – 3678Combined sources4
Helixi3679 – 3681Combined sources3
Beta strandi3687 – 3694Combined sources8
Beta strandi3699 – 3704Combined sources6
Helixi3707 – 3715Combined sources9
Helixi3727 – 3741Combined sources15
Helixi3745 – 3754Combined sources10
Beta strandi3765 – 3773Combined sources9
Helixi3775 – 3783Combined sources9
Helixi3787 – 3789Combined sources3
Beta strandi3790 – 3793Combined sources4
Helixi3795 – 3801Combined sources7
Helixi3803 – 3807Combined sources5
Helixi3815 – 3828Combined sources14
Beta strandi3829 – 3831Combined sources3
Helixi3834 – 3837Combined sources4
Helixi3839 – 3845Combined sources7
Beta strandi3854 – 3858Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96662.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 168Peptidase C53Add BLAST168
Domaini1450 – 1598Peptidase C74PROSITE-ProRule annotationAdd BLAST149
Domaini1599 – 1772Peptidase S31PROSITE-ProRule annotationAdd BLAST174
Domaini1811 – 1969Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST159
Domaini1987 – 2152Helicase C-terminalPROSITE-ProRule annotationAdd BLAST166
Domaini3527 – 3650RdRp catalyticPROSITE-ProRule annotationAdd BLAST124

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1432 – 1435Poly-Glu4
Compositional biasi3268 – 3271Poly-Glu4

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ96662. 1 interactor.

Chemistry databases

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: November 2, 2016
This is version 135 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.