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Protein

Genome polyprotein

Gene
N/A
Organism
Bovine viral diarrhea virus (isolate NADL) (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 (Probable).Curated
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 sitei1447 – 14471For cysteine protease NS2 activityPROSITE-ProRule annotation
Active sitei1461 – 14611For cysteine protease NS2 activityPROSITE-ProRule annotation
Active sitei1512 – 15121For cysteine protease NS2 activityPROSITE-ProRule annotation
Active sitei1748 – 17481Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1785 – 17851Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1842 – 18421Charge 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

Enzyme and pathway databases

BRENDAi2.7.7.48. 925.

Protein family/group databases

MEROPSiC53.001.

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 (isolate NADL) (BVDV) (Mucosal disease virus)
Taxonomic identifieri11100 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaePestivirus
Virus hostiBos taurus (Bovine) [TaxID: 9913]
Proteomesi
  • UP000002317 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
Transmembranei1360 – 138021HelicalPROSITE-ProRule annotationAdd
BLAST
Transmembranei1658 – 167821HelicalPROSITE-ProRule annotationAdd
BLAST

GO - Cellular componenti

  • host cell cytoplasm Source: AgBase
  • host cell cytoplasmic vesicle Source: AgBase
  • host cell Golgi apparatus Source: AgBase
  • host cell mitochondrion Source: AgBase
  • host cell nucleus Source: AgBase
  • host cell surface Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • integral to membrane of host cell Source: AgBase
  • virion membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 168168N-terminal proteaseBy similarityPRO_0000038024Add
BLAST
Chaini169 – 270102Capsid protein CBy similarityPRO_0000038025Add
BLAST
Chaini271 – 497227E(rns) glycoproteinBy similarityPRO_0000038026Add
BLAST
Chaini498 – 659162Envelope glycoprotein E1By similarityPRO_0000038027Add
BLAST
Chaini660 – 1066407Envelope glycoprotein E2By similarityPRO_0000038028Add
BLAST
Chaini1067 – 113670p7By similarityPRO_0000038029Add
BLAST
Chaini1137 – 23621226Non-structural protein 2-3PRO_0000038030Add
BLAST
Chaini1137 – 1679543Cysteine protease NS2PRO_0000038031Add
BLAST
Chaini1680 – 2362683Serine protease NS3PRO_0000038032Add
BLAST
Chaini2363 – 242664Non-structural protein 4ABy similarityPRO_0000038033Add
BLAST
Chaini2427 – 2773347Non-structural protein 4BBy similarityPRO_0000038034Add
BLAST
Chaini2774 – 3269496Non-structural protein 5ABy similarityPRO_0000038035Add
BLAST
Chaini3270 – 3988719RNA-directed RNA polymeraseBy similarityPRO_0000038036Add
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
Glycosylationi1357 – 13571N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi1419 – 14191N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi1451 – 14511N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi1803 – 18031N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2224 – 22241N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2307 – 23071N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2584 – 25841N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2772 – 27721N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2981 – 29811N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi3778 – 37781N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi3867 – 38671N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi3883 – 38831N-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.By similarity
Cleavage between NS2 and NS3 is partial.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei168 – 1692Cleavage; by autolysisBy similarity
Sitei270 – 2712Cleavage; by host signal peptidaseBy similarity
Sitei497 – 4982Cleavage
Sitei659 – 6602Cleavage; by host signal peptidaseBy similarity
Sitei1066 – 10672Cleavage; by host signal peptidase; partialBy similarity
Sitei1136 – 11372Cleavage; by host signal peptidaseBy similarity
Sitei1679 – 16802Cleavage; partial; cysteine protease NS2
Sitei2362 – 23632Cleavage; by serine protease NS3By similarity
Sitei2426 – 24272Cleavage; by serine protease NS3By similarity
Sitei2773 – 27742Cleavage; by serine protease NS3By similarity
Sitei3269 – 32702Cleavage; by serine protease NS3By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

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

Binary interactionsi

WithEntry#Exp.IntActNotes
ADARF1MUM96EBI-9350731,EBI-9350738From a different organism.
DNAJC14Q95J562EBI-9612504,EBI-9612178From a different organism.
EEF1A1P681036EBI-9350549,EBI-352178From a different organism.
TRAPPC9Q32PH07EBI-9350549,EBI-9522367From a different organism.

Protein-protein interaction databases

IntActiP19711. 59 interactions.

Structurei

Secondary structure

1
3988
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi784 – 7863Combined sources
Beta strandi793 – 7953Combined sources
Beta strandi797 – 7993Combined sources
Beta strandi803 – 8053Combined sources
Beta strandi807 – 8093Combined sources
Beta strandi811 – 8144Combined sources
Beta strandi817 – 8204Combined sources
Beta strandi828 – 8358Combined sources
Beta strandi837 – 8393Combined sources
Beta strandi842 – 8509Combined sources
Beta strandi863 – 8664Combined sources
Beta strandi869 – 8757Combined sources
Turni878 – 8803Combined sources
Beta strandi882 – 8865Combined sources
Beta strandi894 – 8996Combined sources
Beta strandi902 – 9065Combined sources
Beta strandi910 – 9145Combined sources
Beta strandi916 – 9227Combined sources
Beta strandi925 – 9284Combined sources
Beta strandi934 – 9363Combined sources
Beta strandi939 – 9413Combined sources
Beta strandi946 – 9516Combined sources
Beta strandi954 – 9607Combined sources
Beta strandi969 – 9713Combined sources
Beta strandi987 – 9937Combined sources
Turni1005 – 10073Combined sources
Beta strandi1014 – 10229Combined sources
Helixi3364 – 33729Combined sources
Beta strandi3373 – 33764Combined sources
Beta strandi3382 – 33843Combined sources
Beta strandi3388 – 33925Combined sources
Beta strandi3402 – 34043Combined sources
Helixi3406 – 34149Combined sources
Helixi3419 – 34213Combined sources
Beta strandi3422 – 34276Combined sources
Helixi3431 – 344010Combined sources
Helixi3453 – 346210Combined sources
Helixi3467 – 34693Combined sources
Turni3470 – 34723Combined sources
Helixi3478 – 34814Combined sources
Turni3482 – 34843Combined sources
Helixi3501 – 35044Combined sources
Helixi3507 – 351812Combined sources
Beta strandi3527 – 35315Combined sources
Beta strandi3535 – 35373Combined sources
Helixi3539 – 35435Combined sources
Beta strandi3549 – 35513Combined sources
Beta strandi3555 – 35584Combined sources
Helixi3563 – 35708Combined sources
Helixi3572 – 35754Combined sources
Helixi3586 – 35883Combined sources
Helixi3591 – 35933Combined sources
Helixi3594 – 360310Combined sources
Beta strandi3605 – 36128Combined sources
Beta strandi3615 – 36173Combined sources
Helixi3618 – 36214Combined sources
Helixi3624 – 363714Combined sources
Helixi3640 – 36423Combined sources
Helixi3643 – 365210Combined sources
Beta strandi3655 – 36606Combined sources
Beta strandi3665 – 36684Combined sources
Helixi3679 – 369921Combined sources
Helixi3703 – 37053Combined sources
Helixi3706 – 37094Combined sources
Beta strandi3710 – 37156Combined sources
Beta strandi3718 – 37247Combined sources
Helixi3725 – 374117Combined sources
Beta strandi3750 – 37534Combined sources
Beta strandi3756 – 37594Combined sources
Helixi3760 – 37623Combined sources
Beta strandi3768 – 37758Combined sources
Beta strandi3780 – 37856Combined sources
Helixi3788 – 379710Combined sources
Beta strandi3802 – 38043Combined sources
Beta strandi3808 – 38103Combined sources
Helixi3811 – 382212Combined sources
Helixi3826 – 383712Combined sources
Beta strandi3846 – 38549Combined sources
Helixi3856 – 38649Combined sources
Helixi3868 – 38703Combined sources
Beta strandi3871 – 38744Combined sources
Helixi3876 – 38827Combined sources
Helixi3885 – 38884Combined sources
Helixi3896 – 390813Combined sources
Beta strandi3910 – 39123Combined sources
Turni3915 – 39184Combined sources
Helixi3920 – 39267Combined sources
Beta strandi3935 – 39395Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S48X-ray3.00A3340-3948[»]
1S49X-ray3.00A3340-3948[»]
1S4FX-ray3.00A/B/C/D3348-3948[»]
4ILDX-ray3.27A/B781-1030[»]
4JNTX-ray4.09A/B693-1030[»]
DisProtiDP00675.
ProteinModelPortaliP19711.
SMRiP19711. Positions 2774-2801, 3361-3948.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19711.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 168168Peptidase C53Add
BLAST
Domaini1441 – 1679239Peptidase C74PROSITE-ProRule annotationAdd
BLAST
Domaini1680 – 1853174Peptidase S31PROSITE-ProRule annotationAdd
BLAST
Domaini1892 – 2050159Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2068 – 2233166Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini3608 – 3731124RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

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.
IPR032843. Jiv.
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.
PF14901. Jiv90. 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.

P19711-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELITNELLY KTYKQKPVGV EEPVYDQAGD PLFGERGAVH PQSTLKLPHK
60 70 80 90 100
RGERDVPTNL ASLPKRGDCR SGNSRGPVSG IYLKPGPLFY QDYKGPVYHR
110 120 130 140 150
APLELFEEGS MCETTKRIGR VTGSDGKLYH IYVCIDGCII IKSATRSYQR
160 170 180 190 200
VFRWVHNRLD CPLWVTTCSD TKEEGATKKK TQKPDRLERG KMKIVPKESE
210 220 230 240 250
KDSKTKPPDA TIVVEGVKYQ VRKKGKTKSK NTQDGLYHNK NKPQESRKKL
260 270 280 290 300
EKALLAWAII AIVLFQVTMG ENITQWNLQD NGTEGIQRAM FQRGVNRSLH
310 320 330 340 350
GIWPEKICTG VPSHLATDIE LKTIHGMMDA SEKTNYTCCR LQRHEWNKHG
360 370 380 390 400
WCNWYNIEPW ILVMNRTQAN LTEGQPPREC AVTCRYDRAS DLNVVTQARD
410 420 430 440 450
SPTPLTGCKK GKNFSFAGIL MRGPCNFEIA ASDVLFKEHE RISMFQDTTL
460 470 480 490 500
YLVDGLTNSL EGARQGTAKL TTWLGKQLGI LGKKLENKSK TWFGAYAASP
510 520 530 540 550
YCDVDRKIGY IWYTKNCTPA CLPKNTKIVG PGKFGTNAED GKILHEMGGH
560 570 580 590 600
LSEVLLLSLV VLSDFAPETA SVMYLILHFS IPQSHVDVMD CDKTQLNLTV
610 620 630 640 650
ELTTAEVIPG SVWNLGKYVC IRPNWWPYET TVVLAFEEVS QVVKLVLRAL
660 670 680 690 700
RDLTRIWNAA TTTAFLVCLV KIVRGQMVQG ILWLLLITGV QGHLDCKPEF
710 720 730 740 750
SYAIAKDERI GQLGAEGLTT TWKEYSPGMK LEDTMVIAWC EDGKLMYLQR
760 770 780 790 800
CTRETRYLAI LHTRALPTSV VFKKLFDGRK QEDVVEMNDN FEFGLCPCDA
810 820 830 840 850
KPIVRGKFNT TLLNGPAFQM VCPIGWTGTV SCTSFNMDTL ATTVVRTYRR
860 870 880 890 900
SKPFPHRQGC ITQKNLGEDL HNCILGGNWT CVPGDQLLYK GGSIESCKWC
910 920 930 940 950
GYQFKESEGL PHYPIGKCKL ENETGYRLVD STSCNREGVA IVPQGTLKCK
960 970 980 990 1000
IGKTTVQVIA MDTKLGPMPC RPYEIISSEG PVEKTACTFN YTKTLKNKYF
1010 1020 1030 1040 1050
EPRDSYFQQY MLKGEYQYWF DLEVTDHHRD YFAESILVVV VALLGGRYVL
1060 1070 1080 1090 1100
WLLVTYMVLS EQKALGIQYG SGEVVMMGNL LTHNNIEVVT YFLLLYLLLR
1110 1120 1130 1140 1150
EESVKKWVLL LYHILVVHPI KSVIVILLMI GDVVKADSGG QEYLGKIDLC
1160 1170 1180 1190 1200
FTTVVLIVIG LIIARRDPTI VPLVTIMAAL RVTELTHQPG VDIAVAVMTI
1210 1220 1230 1240 1250
TLLMVSYVTD YFRYKKWLQC ILSLVSAVFL IRSLIYLGRI EMPEVTIPNW
1260 1270 1280 1290 1300
RPLTLILLYL ISTTIVTRWK VDVAGLLLQC VPILLLVTTL WADFLTLILI
1310 1320 1330 1340 1350
LPTYELVKLY YLKTVRTDTE RSWLGGIDYT RVDSIYDVDE SGEGVYLFPS
1360 1370 1380 1390 1400
RQKAQGNFSI LLPLIKATLI SCVSSKWQLI YMSYLTLDFM YYMHRKVIEE
1410 1420 1430 1440 1450
ISGGTNIISR LVAALIELNW SMEEEESKGL KKFYLLSGRL RNLIIKHKVR
1460 1470 1480 1490 1500
NETVASWYGE EEVYGMPKIM TIIKASTLSK SRHCIICTVC EGREWKGGTC
1510 1520 1530 1540 1550
PKCGRHGKPI TCGMSLADFE ERHYKRIFIR EGNFEGMCSR CQGKHRRFEM
1560 1570 1580 1590 1600
DREPKSARYC AECNRLHPAE EGDFWAESSM LGLKITYFAL MDGKVYDITE
1610 1620 1630 1640 1650
WAGCQRVGIS PDTHRVPCHI SFGSRMPFRQ EYNGFVQYTA RGQLFLRNLP
1660 1670 1680 1690 1700
VLATKVKMLM VGNLGEEIGN LEHLGWILRG PAVCKKITEH EKCHINILDK
1710 1720 1730 1740 1750
LTAFFGIMPR GTTPRAPVRF PTSLLKVRRG LETAWAYTHQ GGISSVDHVT
1760 1770 1780 1790 1800
AGKDLLVCDS MGRTRVVCQS NNRLTDETEY GVKTDSGCPD GARCYVLNPE
1810 1820 1830 1840 1850
AVNISGSKGA VVHLQKTGGE FTCVTASGTP AFFDLKNLKG WSGLPIFEAS
1860 1870 1880 1890 1900
SGRVVGRVKV GKNEESKPTK IMSGIQTVSK NRADLTEMVK KITSMNRGDF
1910 1920 1930 1940 1950
KQITLATGAG KTTELPKAVI EEIGRHKRVL VLIPLRAAAE SVYQYMRLKH
1960 1970 1980 1990 2000
PSISFNLRIG DMKEGDMATG ITYASYGYFC QMPQPKLRAA MVEYSYIFLD
2010 2020 2030 2040 2050
EYHCATPEQL AIIGKIHRFS ESIRVVAMTA TPAGSVTTTG QKHPIEEFIA
2060 2070 2080 2090 2100
PEVMKGEDLG SQFLDIAGLK IPVDEMKGNM LVFVPTRNMA VEVAKKLKAK
2110 2120 2130 2140 2150
GYNSGYYYSG EDPANLRVVT SQSPYVIVAT NAIESGVTLP DLDTVIDTGL
2160 2170 2180 2190 2200
KCEKRVRVSS KIPFIVTGLK RMAVTVGEQA QRRGRVGRVK PGRYYRSQET
2210 2220 2230 2240 2250
ATGSKDYHYD LLQAQRYGIE DGINVTKSFR EMNYDWSLYE EDSLLITQLE
2260 2270 2280 2290 2300
ILNNLLISED LPAAVKNIMA RTDHPEPIQL AYNSYEVQVP VLFPKIRNGE
2310 2320 2330 2340 2350
VTDTYENYSF LNARKLGEDV PVYIYATEDE DLAVDLLGLD WPDPGNQQVV
2360 2370 2380 2390 2400
ETGKALKQVT GLSSAENALL VALFGYVGYQ ALSKRHVPMI TDIYTIEDQR
2410 2420 2430 2440 2450
LEDTTHLQYA PNAIKTDGTE TELKELASGD VEKIMGAISD YAAGGLEFVK
2460 2470 2480 2490 2500
SQAEKIKTAP LFKENAEAAK GYVQKFIDSL IENKEEIIRY GLWGTHTALY
2510 2520 2530 2540 2550
KSIAARLGHE TAFATLVLKW LAFGGESVSD HVKQAAVDLV VYYVMNKPSF
2560 2570 2580 2590 2600
PGDSETQQEG RRFVASLFIS ALATYTYKTW NYHNLSKVVE PALAYLPYAT
2610 2620 2630 2640 2650
SALKMFTPTR LESVVILSTT IYKTYLSIRK GKSDGLLGTG ISAAMEILSQ
2660 2670 2680 2690 2700
NPVSVGISVM LGVGAIAAHN AIESSEQKRT LLMKVFVKNF LDQAATDELV
2710 2720 2730 2740 2750
KENPEKIIMA LFEAVQTIGN PLRLIYHLYG VYYKGWEAKE LSERTAGRNL
2760 2770 2780 2790 2800
FTLIMFEAFE LLGMDSQGKI RNLSGNYILD LIYGLHKQIN RGLKKMVLGW
2810 2820 2830 2840 2850
APAPFSCDWT PSDERIRLPT DNYLRVETRC PCGYEMKAFK NVGGKLTKVE
2860 2870 2880 2890 2900
ESGPFLCRNR PGRGPVNYRV TKYYDDNLRE IKPVAKLEGQ VEHYYKGVTA
2910 2920 2930 2940 2950
KIDYSKGKML LATDKWEVEH GVITRLAKRY TGVGFNGAYL GDEPNHRALV
2960 2970 2980 2990 3000
ERDCATITKN TVQFLKMKKG CAFTYDLTIS NLTRLIELVH RNNLEEKEIP
3010 3020 3030 3040 3050
TATVTTWLAY TFVNEDVGTI KPVLGERVIP DPVVDINLQP EVQVDTSEVG
3060 3070 3080 3090 3100
ITIIGRETLM TTGVTPVLEK VEPDASDNQN SVKIGLDEGN YPGPGIQTHT
3110 3120 3130 3140 3150
LTEEIHNRDA RPFIMILGSR NSISNRAKTA RNINLYTGND PREIRDLMAA
3160 3170 3180 3190 3200
GRMLVVALRD VDPELSEMVD FKGTFLDREA LEALSLGQPK PKQVTKEAVR
3210 3220 3230 3240 3250
NLIEQKKDVE IPNWFASDDP VFLEVALKND KYYLVGDVGE LKDQAKALGA
3260 3270 3280 3290 3300
TDQTRIIKEV GSRTYAMKLS SWFLKASNKQ MSLTPLFEEL LLRCPPATKS
3310 3320 3330 3340 3350
NKGHMASAYQ LAQGNWEPLG CGVHLGTIPA RRVKIHPYEA YLKLKDFIEE
3360 3370 3380 3390 3400
EEKKPRVKDT VIREHNKWIL KKIRFQGNLN TKKMLNPGKL SEQLDREGRK
3410 3420 3430 3440 3450
RNIYNHQIGT IMSSAGIRLE KLPIVRAQTD TKTFHEAIRD KIDKSENRQN
3460 3470 3480 3490 3500
PELHNKLLEI FHTIAQPTLK HTYGEVTWEQ LEAGVNRKGA AGFLEKKNIG
3510 3520 3530 3540 3550
EVLDSEKHLV EQLVRDLKAG RKIKYYETAI PKNEKRDVSD DWQAGDLVVE
3560 3570 3580 3590 3600
KRPRVIQYPE AKTRLAITKV MYNWVKQQPV VIPGYEGKTP LFNIFDKVRK
3610 3620 3630 3640 3650
EWDSFNEPVA VSFDTKAWDT QVTSKDLQLI GEIQKYYYKK EWHKFIDTIT
3660 3670 3680 3690 3700
DHMTEVPVIT ADGEVYIRNG QRGSGQPDTS AGNSMLNVLT MMYGFCESTG
3710 3720 3730 3740 3750
VPYKSFNRVA RIHVCGDDGF LITEKGLGLK FANKGMQILH EAGKPQKITE
3760 3770 3780 3790 3800
GEKMKVAYRF EDIEFCSHTP VPVRWSDNTS SHMAGRDTAV ILSKMATRLD
3810 3820 3830 3840 3850
SSGERGTTAY EKAVAFSFLL MYSWNPLVRR ICLLVLSQQP ETDPSKHATY
3860 3870 3880 3890 3900
YYKGDPIGAY KDVIGRNLSE LKRTGFEKLA NLNLSLSTLG VWTKHTSKRI
3910 3920 3930 3940 3950
IQDCVAIGKE EGNWLVKPDR LISSKTGHLY IPDKGFTLQG KHYEQLQLRT
3960 3970 3980
ETNPVMGVGT ERYKLGPIVN LLLRRLKILL MTAVGVSS
Length:3,988
Mass (Da):449,163
Last modified:February 1, 1996 - v2
Checksum:i4474212F338661B8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31182 Genomic RNA. Translation: AAA42854.1.
PIRiA29198. GNWVBV.
RefSeqiNP_040937.1. NC_001461.1.

Genome annotation databases

GeneIDi1489735.
KEGGivg:1489735.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31182 Genomic RNA. Translation: AAA42854.1.
PIRiA29198. GNWVBV.
RefSeqiNP_040937.1. NC_001461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S48X-ray3.00A3340-3948[»]
1S49X-ray3.00A3340-3948[»]
1S4FX-ray3.00A/B/C/D3348-3948[»]
4ILDX-ray3.27A/B781-1030[»]
4JNTX-ray4.09A/B693-1030[»]
DisProtiDP00675.
ProteinModelPortaliP19711.
SMRiP19711. Positions 2774-2801, 3361-3948.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP19711. 59 interactions.

Protein family/group databases

MEROPSiC53.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1489735.
KEGGivg:1489735.

Enzyme and pathway databases

BRENDAi2.7.7.48. 925.

Miscellaneous databases

EvolutionaryTraceiP19711.

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.
IPR032843. Jiv.
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.
PF14901. Jiv90. 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...

Publicationsi

  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.

Entry informationi

Entry nameiPOLG_BVDVN
AccessioniPrimary (citable) accession number: P19711
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1996
Last modified: March 16, 2016
This is version 147 of the entry and version 2 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. 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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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.