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Protein

Genome polyprotein

Gene
N/A
Organism
Bovine viral diarrhea virus (strain SD-1) (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.By similarity
NS2 protease seems to play a vital role in viral RNA replication control and in the pathogenicity of the virus.PROSITE-ProRule annotation
NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase.By similarity
NS4A is a cofactor for the NS3 protease activity.By similarity
RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome.PROSITE-ProRule annotation

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 sitei1447For cysteine protease NS2 activityPROSITE-ProRule annotation1
Active sitei1461For cysteine protease NS2 activityPROSITE-ProRule annotation1
Active sitei1512For cysteine protease NS2 activityPROSITE-ProRule annotation1
Active sitei1658Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1695Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1752Charge 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

Enzyme and pathway databases

BRENDAi3.4.21.113. 925.

Protein family/group databases

MEROPSiS31.001.

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 (strain SD-1) (BVDV) (Mucosal disease virus)
Taxonomic identifieri31656 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaePestivirus
Virus hostiBos taurus (Bovine) [TaxID: 9913]
Proteomesi
  • UP000007619 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
Transmembranei1360 – 1380HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei1568 – 1588HelicalPROSITE-ProRule annotationAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000380371 – 168N-terminal proteaseBy similarityAdd BLAST168
ChainiPRO_0000038038169 – 270Capsid protein CBy similarityAdd BLAST102
ChainiPRO_0000038039271 – 497E(rns) glycoproteinBy similarityAdd BLAST227
ChainiPRO_0000038040498 – 659Envelope glycoprotein E1By similarityAdd BLAST162
ChainiPRO_0000038041660 – 1066Envelope glycoprotein E2By similarityAdd BLAST407
ChainiPRO_00000380421067 – 1136p7By similarityAdd BLAST70
ChainiPRO_00000380431137 – 2272Non-structural protein 2-3By similarityAdd BLAST1136
ChainiPRO_00000380441137 – 1589Cysteine protease NS2PROSITE-ProRule annotationAdd BLAST453
ChainiPRO_00000380451590 – 2272Serine protease NS3By similarityAdd BLAST683
ChainiPRO_00000380462273 – 2336Non-structural protein 4ABy similarityAdd BLAST64
ChainiPRO_00000380472337 – 2683Non-structural protein 4BBy similarityAdd BLAST347
ChainiPRO_00000380482684 – 3179Non-structural protein 5ABy similarityAdd BLAST496
ChainiPRO_00000380493180 – 3898RNA-directed RNA polymeraseBy similarityAdd 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
Glycosylationi1357N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1419N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1451N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1713N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2134N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2217N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2494N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2682N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2751N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2891N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2988N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi3688N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi3777N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi3793N-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.By similarity

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; partialBy similarity2
Sitei1136 – 1137Cleavage; by host signal peptidaseBy similarity2
Sitei1589 – 1590Cleavage; partial; cysteine protease NS2PROSITE-ProRule annotation2
Sitei2272 – 2273Cleavage; by serine protease NS3By similarity2
Sitei2336 – 2337Cleavage; by serine protease NS3By similarity2
Sitei2683 – 2684Cleavage; by serine protease NS3By similarity2
Sitei3179 – 3180Cleavage; by serine protease NS3By similarity2

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

Structurei

Secondary structure

13898
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi700 – 706Combined sources7
Beta strandi714 – 716Combined sources3
Beta strandi718 – 720Combined sources3
Beta strandi730 – 732Combined sources3
Beta strandi734 – 750Combined sources17
Beta strandi756 – 765Combined sources10
Helixi767 – 769Combined sources3
Beta strandi771 – 776Combined sources6
Beta strandi783 – 786Combined sources4
Beta strandi793 – 795Combined sources3
Helixi797 – 799Combined sources3
Beta strandi801 – 808Combined sources8
Beta strandi811 – 814Combined sources4
Beta strandi817 – 820Combined sources4
Beta strandi828 – 835Combined sources8
Turni837 – 839Combined sources3
Beta strandi842 – 852Combined sources11
Beta strandi863 – 866Combined sources4
Beta strandi869 – 875Combined sources7
Helixi878 – 880Combined sources3
Beta strandi882 – 886Combined sources5
Beta strandi894 – 899Combined sources6
Beta strandi902 – 906Combined sources5
Beta strandi910 – 914Combined sources5
Beta strandi916 – 920Combined sources5
Beta strandi924 – 928Combined sources5
Beta strandi934 – 936Combined sources3
Beta strandi939 – 941Combined sources3
Beta strandi946 – 951Combined sources6
Beta strandi954 – 961Combined sources8
Beta strandi964 – 967Combined sources4
Beta strandi969 – 973Combined sources5
Beta strandi976 – 982Combined sources7
Beta strandi985 – 993Combined sources9
Turni1005 – 1007Combined sources3
Beta strandi1011 – 1013Combined sources3
Beta strandi1016 – 1024Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YQ2X-ray2.58A/B696-1026[»]
2YQ3X-ray3.29A/B696-1026[»]
ProteinModelPortaliQ01499.
SMRiQ01499.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 168Peptidase C53Add BLAST168
Domaini1441 – 1589Peptidase C74PROSITE-ProRule annotationAdd BLAST149
Domaini1590 – 1763Peptidase S31PROSITE-ProRule annotationAdd BLAST174
Domaini1802 – 1960Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST159
Domaini1978 – 2143Helicase C-terminalPROSITE-ProRule annotationAdd BLAST166
Domaini3518 – 3641RdRp catalyticPROSITE-ProRule annotationAdd BLAST124

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.

Q01499-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELITNELLY KTYKQKPVGV EEPVYDQAGN PLFGERGAIH PQSTLKLPHK
60 70 80 90 100
RGERNVPTSL ASLPKRGDCR SGNSKGPVSG IYLKPGPLFY QDYKGPVYHR
110 120 130 140 150
APLELFEEGS MCETTKRIGR VTGSDGKLYH IYICIDGCIT VKSATRSHQR
160 170 180 190 200
VLRWVHNRLD CPLWVTSCSD TKEEGATKKK QQKPDRLEKG RMKIVPKESE
210 220 230 240 250
KDSKTKPPDA TIVVDGVKYQ VKKKGKVKSK NTQDGLYHNK NKPPESRKKL
260 270 280 290 300
EKALLAWAIL AVVLIEVTMG ENITQWNLQD NGTEGIQRAM FQRGVNRSLH
310 320 330 340 350
GIWPEKICTG VPSHLATDVE LKTIHGMMDA SEKTNYTCCR LQRHEWNKHG
360 370 380 390 400
WCNWYNIEPW ILIMNRTQAN LTEGQPPREC AVTCRYDRDS DLNVVTQARD
410 420 430 440 450
SPTPLTGCKK GKNFSFAGVL TRGPCNFEIA ASDVLFKEHE CTGVFQDTAH
460 470 480 490 500
YLVDGVTNSL ESARQGTAKL TTWLGKQLGI LGKKLENKSK TWFGAYAASP
510 520 530 540 550
YCDVDRKIGY IWFTKNCTPA CLPKNTKIIG PGKFDTNAED GKILHEMGGH
560 570 580 590 600
LSEVLLLSLV VLSDFAPETA SAMYLILHFS IPQSHVDITD CDKTQLNLTI
610 620 630 640 650
ELTTADVIPG SVWNLGKYVC IRPDWWPYET AAVLAFEEVG QVVKIVLRAL
660 670 680 690 700
RDLTRIWNAA TTTAFLVCLI KMVRGQVVQG ILWLLLITGV QGHLDCKPEY
710 720 730 740 750
SYAIAKNDRV GPLGAEGLTT VWKDYSHEMK LEDTMVIAWC KGGKFTYLSR
760 770 780 790 800
CTRETRYLAI LHSRALPTSV VFKKLFEGQK QEDTVEMDDD FEFGLCPCDA
810 820 830 840 850
KPIVRGKFNT TLLNGPAFQM VCPIGWTGTV SCMLANRDTL DTAVVRTYRR
860 870 880 890 900
SVPFPYRQGC ITQKTLGEDL YDCALGGNWT CVTGDQSRYT GGLIESCKWC
910 920 930 940 950
GYKFQKSEGL PHYPIGKCRL NNETGYRLVD DTSCDREGVA IVPHGLVKCK
960 970 980 990 1000
IGDTTVQVIA TDTKLGPMPC KPHEIISSEG PIEKTACTFN YTRTLKNKYF
1010 1020 1030 1040 1050
EPRDSYFQQY MLKGDYQYWF DLEVTDHHRD YFAESILVVV VALLGGRYVL
1060 1070 1080 1090 1100
WLLVTYMVLS EQKASGAQYG AGEVVMMGNL LTHDNVEVVT YFFLLYLLLR
1110 1120 1130 1140 1150
EESVKKWVLL LYHILVAHPL KSVIVILLMI GDVVKADPGG QGYLGQIDVC
1160 1170 1180 1190 1200
FTMVVIIIIG LIIARRDPTI VPLITIVASL RVTGLTYSPG VDAAMAVITI
1210 1220 1230 1240 1250
TLLMVSYVTD YFRYKRWLQC ILSLVSGVFL IRCLIHLGRI ETPEVTIPNW
1260 1270 1280 1290 1300
RPLTLILFYL ISTTVVTMWK IDLAGLLLQG VPILLLITTL WADFLTLILI
1310 1320 1330 1340 1350
LPTYELVKLY YLKTIKTDIE KSWLGGLDYK RVDSIYDVDE SGEGVYLFPS
1360 1370 1380 1390 1400
RQKAQKNFSM LLPLVRATLI SCVSSKWQLI YMAYLSVDFM YYMHRKVIEE
1410 1420 1430 1440 1450
ISGGTNMISR IVAALIELNW SMEEEESKGL KKFYLLSGRL RNLIIKHKVR
1460 1470 1480 1490 1500
NETVAGWYGE EEVYGMPKIM TIIKASTLNK NKHCIICTVC EGRKWKGGTC
1510 1520 1530 1540 1550
PKCGRHGKPI TCGMSLADFE ERHYKRIFIR EGNFEGPFRQ EYNGFIQYTA
1560 1570 1580 1590 1600
RGQLFLRNLP ILATKVKMLM VGNLGEEVGD LEHLGWILRG PAVCKKITEH
1610 1620 1630 1640 1650
ERCHINILDK LTAFFGIMPR GTTPRAPVRF PTSLLKVRRG LETGWAYTHQ
1660 1670 1680 1690 1700
GGISSVDHVT AGKDLLVCDS MGRTRVVCQS NNKLTDETEY GVKTDSGCPD
1710 1720 1730 1740 1750
GARCYVLNPE AVNISGSKGA VVHLQKTGGE FTCVTASGTP AFFDLKNLKG
1760 1770 1780 1790 1800
WSGLPIFEAS SGRVVGRVKV GKNEESKPTK IMSGIQTVSK NTADLTEMVK
1810 1820 1830 1840 1850
KITSMNRGDF KQITLATGAG KTTELPKAVI EEIGRHKRVL VLIPLRAAAE
1860 1870 1880 1890 1900
SVYQYMRLKH PSISFNLRIG DMKEGDMATG ITYASYGYFC QMPQPKLRAA
1910 1920 1930 1940 1950
MVEYSYIFLD EYHCATPEQL AIIGKIHRFS ESIRVVAMTA TPAGSVTTTG
1960 1970 1980 1990 2000
QKHPIEEFIA PEVMEGEDLG SQFLDIAGLK IPVDEMKGNM LVFVPTRNMA
2010 2020 2030 2040 2050
VEVAKKLKAK GYNSGYYYSG EDPANLRVVT SQSPYVIVAT NAIESGVTLP
2060 2070 2080 2090 2100
DLDTVVDTGL KCEKRVRVSS KIPFIVTGLK RMAVTVGEQA QRRGRVGRVK
2110 2120 2130 2140 2150
PGRYYRSQET ATGSKDYHYD LLQAQRYGIE DGINVTKSFR EMNYDWSLYE
2160 2170 2180 2190 2200
EDSLLITQLE ILNNLLISED LPAAVKNIMA RTDHPEPIQL AYNSYEVQVP
2210 2220 2230 2240 2250
VLFPKIRNGE VTDTYENYSF LNARKLGEDV PVYIYATEDE DLAVDLLGLD
2260 2270 2280 2290 2300
WPDPGNQQVV ETGKALKQVA GLSSAENALL VALFGYVGYQ ALSKRHVPMI
2310 2320 2330 2340 2350
TDIYTIEDQR LEDTTHLQYA PNAIKTEGTE TELKELASGD VEKIMGAISD
2360 2370 2380 2390 2400
YAAGGLDFVK SQAEKIKTAP LFKENVEAAR GYVQKLIDSL IEDKDVIIRY
2410 2420 2430 2440 2450
GLWGTHTALY KSIAARLGHE TAFATLVLKW LAFGGETVSD HIRQAAVDLV
2460 2470 2480 2490 2500
VYYVMNKPSF PGDTETQQEG RRFVASLFIS ALATYTYKTW NYNNLSKVVE
2510 2520 2530 2540 2550
PALAYLPYAT SALKMFTPTR LESVVILSTT IYKTYLSIRK GKSDGLLGTG
2560 2570 2580 2590 2600
ISAAMEILSQ NPVSVGISVM LGVGAIAAHN AIESSEQKRT LLMKVFVKNF
2610 2620 2630 2640 2650
LDQAATDELV KENPEKIIMA LFEAVQTIGN PLRLIYHLYG VYYKGWEAKE
2660 2670 2680 2690 2700
LSERTAGRNL FTLIMFEAFE LLGMDSEGKI RNLSGNYILD LIHGLHKQIN
2710 2720 2730 2740 2750
RGLKKIVLGW APAPFSCDWT PSDERIRLPT DSYLRVETKC PCGYEMKALK
2760 2770 2780 2790 2800
NVSGKLTKVE ESGPFLCRNR PGRGPVNYRV TKYYDDNLRE IRPVAKLEGQ
2810 2820 2830 2840 2850
VEHYYKGVTA RIDYSKGKTL LATDKWEVEH GTLTRLTKRY TGVGFRGAYL
2860 2870 2880 2890 2900
GDEPNHRDLV ERDCATITKN TVQFLKMKKG CAFTYDLTIS NLTRLIELVH
2910 2920 2930 2940 2950
RNNLEEKEIP TATVTTWLAY TFVNEDVGTI KPVLGERVIP DPVVDINLQP
2960 2970 2980 2990 3000
EVQVDTSEVG ITIIGKEAVM TTGVTPVMEK VEPDTDNNQS SVKIGLDEGN
3010 3020 3030 3040 3050
YPGPGVQTHT LVEEIHNKDA RPFIMVLGSK SSMSNRAKTA RNINLYTGND
3060 3070 3080 3090 3100
PREIRDLMAE GRILVVALRD IDPDLSELVD FKGTFLDREA LEALSLGQPK
3110 3120 3130 3140 3150
PKQVTKAAIR DLLKEERQVE IPDWFTSDDP VFLDIAMKKD KYHLIGDVVE
3160 3170 3180 3190 3200
VKDQAKALGA TDQTRIVKEV GSRTYTMKLS SWFLQASSKQ MSLTPLFEEL
3210 3220 3230 3240 3250
LLRCPPATKS NKGHMASAYQ LAQGNWEPLG CGVHLGTVPA RRVKMHPYEA
3260 3270 3280 3290 3300
YLKLKDLVEE EEKKPRIRDT VIREHNKWIL KKIKFQGNLN TKKMLNPGKL
3310 3320 3330 3340 3350
SEQLDREGHK RNIYNNQIST VMSSAGIRLE KLPIVRAQTD TKSFHEAIRD
3360 3370 3380 3390 3400
KIDKNENRQN PELHNKLLEI FHTIADPSLK HTYGEVTWEQ LEAGINRKGA
3410 3420 3430 3440 3450
AGFLEKKNIG EVLDSEKHLV EQLVRDLKAG RKIRYYETAI PKNEKRDVSD
3460 3470 3480 3490 3500
DWQAGDLVDE KKPRVIQYPE AKTRLAITKV MYNWVKQQPV VIPGYEGKTP
3510 3520 3530 3540 3550
LFNIFNKVRK EWDLFNEPVA VSFDTKAWDT QVTSRDLHLI GEIQKYYYRK
3560 3570 3580 3590 3600
EWHKFIDTIT DHMVEVPVIT ADGEVYIRNG QRGSGQPDTS AGNSMLNVLT
3610 3620 3630 3640 3650
MIYAFCESTG VPYKSFNRVA KIHVCGDDGF LITEKGLGLK FSNKGMQILH
3660 3670 3680 3690 3700
EAGKPQKLTE GEKMKVAYKF EDIEFCSHTP VPVRWSDNTS SYMAGRDTAV
3710 3720 3730 3740 3750
ILSKMATRLD SSGERGTTAY EKAVAFSFLL MYSWNPLVRR ICLLVLSQRP
3760 3770 3780 3790 3800
ETAPSTQTTY YYKGDPIGAY KDVIGRNLSE LKRTGFEKLA NLNLSLSTLG
3810 3820 3830 3840 3850
IWTKHTSKRI IQDCVAIGKE EGNWLVNADR LISSKTGHLY IPDKGFTLQG
3860 3870 3880 3890
KHYEQLQLGA ETNPVMGVGT ERYKLGPIVN LLLRRLKVLL MAAVGASS
Length:3,898
Mass (Da):437,808
Last modified:July 1, 1993 - v1
Checksum:i31ACEE140D407ED3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96751 Genomic RNA. Translation: AAA42860.1.
PIRiA44217.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96751 Genomic RNA. Translation: AAA42860.1.
PIRiA44217.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YQ2X-ray2.58A/B696-1026[»]
2YQ3X-ray3.29A/B696-1026[»]
ProteinModelPortaliQ01499.
SMRiQ01499.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS31.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.21.113. 925.

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_BVDVS
AccessioniPrimary (citable) accession number: Q01499
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 2, 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

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.