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Q01499

- POLG_BVDVS

UniProt

Q01499 - POLG_BVDVS

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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: 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)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
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; partialBy similarity
Sitei1136 – 11372Cleavage; by host signal peptidaseBy similarity
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
Sitei1589 – 15902Cleavage; partial; cysteine protease NS2PROSITE-ProRule annotation
Active sitei1658 – 16581Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1695 – 16951Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Active sitei1752 – 17521Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation
Sitei2272 – 22732Cleavage; by serine protease NS3By similarity
Sitei2336 – 23372Cleavage; by serine protease NS3By similarity
Sitei2683 – 26842Cleavage; by serine protease NS3By similarity
Sitei3179 – 31802Cleavage; by serine protease NS3By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent helicase activity Source: InterPro
  3. cysteine-type endopeptidase activity Source: InterPro
  4. ion channel activity Source: UniProtKB-KW
  5. ribonuclease T2 activity Source: InterPro
  6. RNA binding Source: InterPro
  7. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  8. serine-type endopeptidase activity Source: InterPro
  9. serine-type exopeptidase activity Source: InterPro

GO - Biological processi

  1. clathrin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
  2. fusion of virus membrane with host endosome membrane Source: UniProtKB-KW
  3. induction by virus of host autophagy Source: UniProtKB-KW
  4. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  5. protein oligomerization Source: UniProtKB-KW
  6. suppression by virus of host IRF3 activity Source: UniProtKB-KW
  7. viral protein processing Source: InterPro
  8. viral RNA genome replication Source: InterPro
  9. virion attachment to host cell Source: UniProtKB-KW
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 positive-strand viruses, no DNA stageFlaviviridaePestivirus
Virus hostiBos taurus (Bovine) [TaxID: 9913]
ProteomesiUP000007619: Genome

Subcellular locationi

Chain E(rns) glycoprotein : Host membrane; Peripheral membrane protein
Note: The C-terminus membrane anchor of Erns represents an amphipathic helix embedded in plane into the membrane.By similarity
Chain 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
Transmembranei1568 – 158821HelicalPROSITE-ProRule annotationAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. integral to membrane of host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 168168N-terminal proteaseBy similarityPRO_0000038037Add
BLAST
Chaini169 – 270102Capsid protein CBy similarityPRO_0000038038Add
BLAST
Chaini271 – 497227E(rns) glycoproteinBy similarityPRO_0000038039Add
BLAST
Chaini498 – 659162Envelope glycoprotein E1By similarityPRO_0000038040Add
BLAST
Chaini660 – 1066407Envelope glycoprotein E2By similarityPRO_0000038041Add
BLAST
Chaini1067 – 113670p7By similarityPRO_0000038042Add
BLAST
Chaini1137 – 22721136Non-structural protein 2-3By similarityPRO_0000038043Add
BLAST
Chaini1137 – 1589453Cysteine protease NS2PROSITE-ProRule annotationPRO_0000038044Add
BLAST
Chaini1590 – 2272683Serine protease NS3By similarityPRO_0000038045Add
BLAST
Chaini2273 – 233664Non-structural protein 4ABy similarityPRO_0000038046Add
BLAST
Chaini2337 – 2683347Non-structural protein 4BBy similarityPRO_0000038047Add
BLAST
Chaini2684 – 3179496Non-structural protein 5ABy similarityPRO_0000038048Add
BLAST
Chaini3180 – 3898719RNA-directed RNA polymeraseBy similarityPRO_0000038049Add
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
Glycosylationi1713 – 17131N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi2134 – 21341N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi2217 – 22171N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi2494 – 24941N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi2682 – 26821N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi2751 – 27511N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi2891 – 28911N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi2988 – 29881N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi3688 – 36881N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi3777 – 37771N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi3793 – 37931N-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

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

1
3898
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi700 – 7067Combined sources
Beta strandi714 – 7163Combined sources
Beta strandi718 – 7203Combined sources
Beta strandi730 – 7323Combined sources
Beta strandi734 – 75017Combined sources
Beta strandi756 – 76510Combined sources
Helixi767 – 7693Combined sources
Beta strandi771 – 7766Combined sources
Beta strandi783 – 7864Combined sources
Beta strandi793 – 7953Combined sources
Helixi797 – 7993Combined sources
Beta strandi801 – 8088Combined sources
Beta strandi811 – 8144Combined sources
Beta strandi817 – 8204Combined sources
Beta strandi828 – 8358Combined sources
Turni837 – 8393Combined sources
Beta strandi842 – 85211Combined sources
Beta strandi863 – 8664Combined sources
Beta strandi869 – 8757Combined sources
Helixi878 – 8803Combined sources
Beta strandi882 – 8865Combined sources
Beta strandi894 – 8996Combined sources
Beta strandi902 – 9065Combined sources
Beta strandi910 – 9145Combined sources
Beta strandi916 – 9205Combined sources
Beta strandi924 – 9285Combined sources
Beta strandi934 – 9363Combined sources
Beta strandi939 – 9413Combined sources
Beta strandi946 – 9516Combined sources
Beta strandi954 – 9618Combined sources
Beta strandi964 – 9674Combined sources
Beta strandi969 – 9735Combined sources
Beta strandi976 – 9827Combined sources
Beta strandi985 – 9939Combined sources
Turni1005 – 10073Combined sources
Beta strandi1011 – 10133Combined sources
Beta strandi1016 – 10249Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YQ2X-ray2.58A/B696-1026[»]
2YQ3X-ray3.29A/B696-1026[»]
ProteinModelPortaliQ01499.
SMRiQ01499. Positions 2684-2711, 3271-3858.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 168168Peptidase C53Add
BLAST
Domaini1441 – 1589149Peptidase C74PROSITE-ProRule annotationAdd
BLAST
Domaini1590 – 1763174Peptidase S31PROSITE-ProRule annotationAdd
BLAST
Domaini1802 – 1960159Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1978 – 2143166Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini3518 – 3641124RdRp 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.
IPR027417. P-loop_NTPase.
IPR022120. Pept_C74_NS2-pestiV.
IPR008751. Peptidase_C53.
IPR000280. Pestivirus_NS3_S31.
IPR007094. RNA-dir_pol_PSvirus.
IPR002166. RNA_pol_HCV.
IPR001568. RNase_T2-like.
IPR018188. RNase_T2_AS.
[Graphical view]
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.
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

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        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 .
PIRi A44217.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YQ2 X-ray 2.58 A/B 696-1026 [» ]
2YQ3 X-ray 3.29 A/B 696-1026 [» ]
ProteinModelPortali Q01499.
SMRi Q01499. Positions 2684-2711, 3271-3858.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S31.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BRENDAi 3.4.21.113. 925.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
3.90.730.10. 1 hit.
InterProi IPR021824. Capsid-C_pestivirus.
IPR011492. DEAD_Flavivir.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR022120. Pept_C74_NS2-pestiV.
IPR008751. Peptidase_C53.
IPR000280. Pestivirus_NS3_S31.
IPR007094. RNA-dir_pol_PSvirus.
IPR002166. RNA_pol_HCV.
IPR001568. RNase_T2-like.
IPR018188. RNase_T2_AS.
[Graphical view ]
Pfami PF11889. DUF3409. 1 hit.
PF07652. Flavi_DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF05550. Peptidase_C53. 1 hit.
PF12387. Peptidase_C74. 1 hit.
PF05578. Peptidase_S31. 1 hit.
PF00998. RdRP_3. 1 hit.
[Graphical view ]
PRINTSi PR00729. CDVENDOPTASE.
ProDomi PD003091. Peptidase_C53. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
SSF55895. SSF55895. 1 hit.
PROSITEi PS51192. 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 ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning and nucleotide sequence of a pestivirus genome, noncytopathic bovine viral diarrhea virus strain SD-1."
    Deng R., Brock K.V.
    Virology 191:867-869(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

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 26, 2014
This is version 123 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

External Data

Dasty 3