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Q01499 (POLG_BVDVS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Genome polyprotein

Cleaved into the following 13 chains:

  1. N-terminal protease
    Short name=N-pro
    EC=3.4.22.-
    Alternative name(s):
    Autoprotease p20
  2. Capsid protein C
  3. E(rns) glycoprotein
    Alternative name(s):
    gp44/48
  4. Envelope glycoprotein E1
    Alternative name(s):
    gp33
  5. Envelope glycoprotein E2
    Alternative name(s):
    gp55
  6. p7
  7. Non-structural protein 2-3
  8. Cysteine protease NS2
    EC=3.4.22.-
    Alternative name(s):
    Non-structural protein 2
  9. Serine protease NS3
    EC=3.4.21.113
    EC=3.6.1.15
    EC=3.6.4.13
    Alternative name(s):
    Non-structural protein 3
  10. Non-structural protein 4A
    Short name=NS4A
  11. Non-structural protein 4B
    Short name=NS4B
  12. Non-structural protein 5A
    Short name=NS5A
  13. RNA-directed RNA polymerase
    EC=2.7.7.48
    Alternative name(s):
    NS5B
OrganismBovine viral diarrhea virus (strain SD-1) (BVDV) (Mucosal disease virus) [Complete proteome]
Taxonomic identifier31656 [NCBI]
Taxonomic lineageVirusesssRNA positive-strand viruses, no DNA stageFlaviviridaePestivirus
Virus hostBos taurus (Bovine) [TaxID: 9913]

Protein attributes

Sequence length3898 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

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 By similarity.

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 By similarity.

Catalytic activity

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).

NTP + H2O = NDP + phosphate.

ATP + H2O = ADP + phosphate.

Subunit structure

The E(rns) glycoprotein is found as a homodimer; disulfide-linked By similarity. The E1 and E2 envelope glycoproteins form disulfide-linked homodimers as well as heterodimers By similarity.

Subcellular location

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.

Envelope glycoprotein E2: Host cell surface By similarity.

Cysteine protease NS2: Host membrane; Multi-pass membrane protein Potential.

Post-translational modification

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.

Cleavage between E2 and p7 is partial By similarity.

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.

Sequence similarities

Belongs to the pestivirus polyprotein family.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Contains 1 peptidase C53 domain.

Contains 1 peptidase C74 domain.

Contains 1 peptidase S31 domain.

Contains 1 RdRp catalytic domain.

Ontologies

Keywords
   Biological processActivation 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
   Cellular componentHost membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
Ion channel
Nucleotidyltransferase
Protease
RNA-directed RNA polymerase
Serine protease
Thiol protease
Transferase
Viral ion channel
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processclathrin-mediated endocytosis of virus by host cell

Inferred from electronic annotation. Source: UniProtKB-KW

fusion of virus membrane with host endosome membrane

Inferred from electronic annotation. Source: UniProtKB-KW

induction by virus of host autophagy

Inferred from electronic annotation. Source: UniProtKB-KW

pore formation by virus in membrane of host cell

Inferred from electronic annotation. Source: UniProtKB-KW

protein oligomerization

Inferred from electronic annotation. Source: UniProtKB-KW

suppression by virus of host IRF3 activity

Inferred from electronic annotation. Source: UniProtKB-KW

viral RNA genome replication

Inferred from electronic annotation. Source: InterPro

viral protein processing

Inferred from electronic annotation. Source: InterPro

virion attachment to host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenthost cell surface

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

integral to membrane of host cell

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

RNA binding

Inferred from electronic annotation. Source: InterPro

RNA-directed RNA polymerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

cysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

ion channel activity

Inferred from electronic annotation. Source: UniProtKB-KW

ribonuclease T2 activity

Inferred from electronic annotation. Source: InterPro

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

serine-type exopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 168168N-terminal protease By similarity
PRO_0000038037
Chain169 – 270102Capsid protein C By similarity
PRO_0000038038
Chain271 – 497227E(rns) glycoprotein By similarity
PRO_0000038039
Chain498 – 659162Envelope glycoprotein E1 By similarity
PRO_0000038040
Chain660 – 1066407Envelope glycoprotein E2 By similarity
PRO_0000038041
Chain1067 – 113670p7 By similarity
PRO_0000038042
Chain1137 – 22721136Non-structural protein 2-3 By similarity
PRO_0000038043
Chain1137 – 1589453Cysteine protease NS2 By similarity
PRO_0000038044
Chain1590 – 2272683Serine protease NS3 By similarity
PRO_0000038045
Chain2273 – 233664Non-structural protein 4A By similarity
PRO_0000038046
Chain2337 – 2683347Non-structural protein 4B By similarity
PRO_0000038047
Chain2684 – 3179496Non-structural protein 5A By similarity
PRO_0000038048
Chain3180 – 3898719RNA-directed RNA polymerase By similarity
PRO_0000038049

Regions

Transmembrane1144 – 116421Helical; Potential
Transmembrane1189 – 120921Helical; Potential
Transmembrane1217 – 123721Helical; Potential
Transmembrane1247 – 126721Helical; Potential
Transmembrane1281 – 130121Helical; Potential
Transmembrane1360 – 138021Helical; Potential
Transmembrane1568 – 158821Helical; Potential
Domain1 – 168168Peptidase C53
Domain1441 – 1589149Peptidase C74
Domain1590 – 1763174Peptidase S31
Domain1802 – 1960159Helicase ATP-binding
Domain1978 – 2143166Helicase C-terminal
Domain3518 – 3641124RdRp catalytic

Sites

Active site221For N-terminal protease activity By similarity
Active site491For N-terminal protease activity By similarity
Active site691For N-terminal protease activity By similarity
Active site14471For cysteine protease NS2 activity By similarity
Active site14611For cysteine protease NS2 activity By similarity
Active site15121For cysteine protease NS2 activity By similarity
Active site16581Charge relay system; for serine protease NS3 activity By similarity
Active site16951Charge relay system; for serine protease NS3 activity By similarity
Active site17521Charge relay system; for serine protease NS3 activity By similarity
Site168 – 1692Cleavage; by autolysis By similarity
Site270 – 2712Cleavage; by host signal peptidase By similarity
Site497 – 4982Cleavage By similarity
Site659 – 6602Cleavage; by host signal peptidase By similarity
Site1066 – 10672Cleavage; by host signal peptidase; partial By similarity
Site1136 – 11372Cleavage; by host signal peptidase By similarity
Site1589 – 15902Cleavage; partial; cysteine protease NS2 By similarity
Site2272 – 22732Cleavage; by serine protease NS3 By similarity
Site2336 – 23372Cleavage; by serine protease NS3 By similarity
Site2683 – 26842Cleavage; by serine protease NS3 By similarity
Site3179 – 31802Cleavage; by serine protease NS3 By similarity

Amino acid modifications

Glycosylation2721N-linked (GlcNAc...); by host Potential
Glycosylation2811N-linked (GlcNAc...); by host Potential
Glycosylation2961N-linked (GlcNAc...); by host Potential
Glycosylation3351N-linked (GlcNAc...); by host Potential
Glycosylation3651N-linked (GlcNAc...); by host Potential
Glycosylation3701N-linked (GlcNAc...); by host Potential
Glycosylation4131N-linked (GlcNAc...); by host Potential
Glycosylation4871N-linked (GlcNAc...); by host Potential
Glycosylation5971N-linked (GlcNAc...); by host Potential
Glycosylation8091N-linked (GlcNAc...); by host Potential
Glycosylation8781N-linked (GlcNAc...); by host Potential
Glycosylation9221N-linked (GlcNAc...); by host Potential
Glycosylation9901N-linked (GlcNAc...); by host Potential
Glycosylation13571N-linked (GlcNAc...); by host Potential
Glycosylation14191N-linked (GlcNAc...); by host Potential
Glycosylation14511N-linked (GlcNAc...); by host Potential
Glycosylation17131N-linked (GlcNAc...); by host Potential
Glycosylation21341N-linked (GlcNAc...); by host Potential
Glycosylation22171N-linked (GlcNAc...); by host Potential
Glycosylation24941N-linked (GlcNAc...); by host Potential
Glycosylation26821N-linked (GlcNAc...); by host Potential
Glycosylation27511N-linked (GlcNAc...); by host Potential
Glycosylation28911N-linked (GlcNAc...); by host Potential
Glycosylation29881N-linked (GlcNAc...); by host Potential
Glycosylation36881N-linked (GlcNAc...); by host Potential
Glycosylation37771N-linked (GlcNAc...); by host Potential
Glycosylation37931N-linked (GlcNAc...); by host Potential

Secondary structure

........................................................................... 3898
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q01499 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 31ACEE140D407ED3

FASTA3,898437,808
        10         20         30         40         50         60 
MELITNELLY KTYKQKPVGV EEPVYDQAGN PLFGERGAIH PQSTLKLPHK RGERNVPTSL 

        70         80         90        100        110        120 
ASLPKRGDCR SGNSKGPVSG IYLKPGPLFY QDYKGPVYHR APLELFEEGS MCETTKRIGR 

       130        140        150        160        170        180 
VTGSDGKLYH IYICIDGCIT VKSATRSHQR VLRWVHNRLD CPLWVTSCSD TKEEGATKKK 

       190        200        210        220        230        240 
QQKPDRLEKG RMKIVPKESE KDSKTKPPDA TIVVDGVKYQ VKKKGKVKSK NTQDGLYHNK 

       250        260        270        280        290        300 
NKPPESRKKL EKALLAWAIL AVVLIEVTMG ENITQWNLQD NGTEGIQRAM FQRGVNRSLH 

       310        320        330        340        350        360 
GIWPEKICTG VPSHLATDVE LKTIHGMMDA SEKTNYTCCR LQRHEWNKHG WCNWYNIEPW 

       370        380        390        400        410        420 
ILIMNRTQAN LTEGQPPREC AVTCRYDRDS DLNVVTQARD SPTPLTGCKK GKNFSFAGVL 

       430        440        450        460        470        480 
TRGPCNFEIA ASDVLFKEHE CTGVFQDTAH YLVDGVTNSL ESARQGTAKL TTWLGKQLGI 

       490        500        510        520        530        540 
LGKKLENKSK TWFGAYAASP YCDVDRKIGY IWFTKNCTPA CLPKNTKIIG PGKFDTNAED 

       550        560        570        580        590        600 
GKILHEMGGH LSEVLLLSLV VLSDFAPETA SAMYLILHFS IPQSHVDITD CDKTQLNLTI 

       610        620        630        640        650        660 
ELTTADVIPG SVWNLGKYVC IRPDWWPYET AAVLAFEEVG QVVKIVLRAL RDLTRIWNAA 

       670        680        690        700        710        720 
TTTAFLVCLI KMVRGQVVQG ILWLLLITGV QGHLDCKPEY SYAIAKNDRV GPLGAEGLTT 

       730        740        750        760        770        780 
VWKDYSHEMK LEDTMVIAWC KGGKFTYLSR CTRETRYLAI LHSRALPTSV VFKKLFEGQK 

       790        800        810        820        830        840 
QEDTVEMDDD FEFGLCPCDA KPIVRGKFNT TLLNGPAFQM VCPIGWTGTV SCMLANRDTL 

       850        860        870        880        890        900 
DTAVVRTYRR SVPFPYRQGC ITQKTLGEDL YDCALGGNWT CVTGDQSRYT GGLIESCKWC 

       910        920        930        940        950        960 
GYKFQKSEGL PHYPIGKCRL NNETGYRLVD DTSCDREGVA IVPHGLVKCK IGDTTVQVIA 

       970        980        990       1000       1010       1020 
TDTKLGPMPC KPHEIISSEG PIEKTACTFN YTRTLKNKYF EPRDSYFQQY MLKGDYQYWF 

      1030       1040       1050       1060       1070       1080 
DLEVTDHHRD YFAESILVVV VALLGGRYVL WLLVTYMVLS EQKASGAQYG AGEVVMMGNL 

      1090       1100       1110       1120       1130       1140 
LTHDNVEVVT YFFLLYLLLR EESVKKWVLL LYHILVAHPL KSVIVILLMI GDVVKADPGG 

      1150       1160       1170       1180       1190       1200 
QGYLGQIDVC FTMVVIIIIG LIIARRDPTI VPLITIVASL RVTGLTYSPG VDAAMAVITI 

      1210       1220       1230       1240       1250       1260 
TLLMVSYVTD YFRYKRWLQC ILSLVSGVFL IRCLIHLGRI ETPEVTIPNW RPLTLILFYL 

      1270       1280       1290       1300       1310       1320 
ISTTVVTMWK IDLAGLLLQG VPILLLITTL WADFLTLILI LPTYELVKLY YLKTIKTDIE 

      1330       1340       1350       1360       1370       1380 
KSWLGGLDYK RVDSIYDVDE SGEGVYLFPS RQKAQKNFSM LLPLVRATLI SCVSSKWQLI 

      1390       1400       1410       1420       1430       1440 
YMAYLSVDFM YYMHRKVIEE ISGGTNMISR IVAALIELNW SMEEEESKGL KKFYLLSGRL 

      1450       1460       1470       1480       1490       1500 
RNLIIKHKVR NETVAGWYGE EEVYGMPKIM TIIKASTLNK NKHCIICTVC EGRKWKGGTC 

      1510       1520       1530       1540       1550       1560 
PKCGRHGKPI TCGMSLADFE ERHYKRIFIR EGNFEGPFRQ EYNGFIQYTA RGQLFLRNLP 

      1570       1580       1590       1600       1610       1620 
ILATKVKMLM VGNLGEEVGD LEHLGWILRG PAVCKKITEH ERCHINILDK LTAFFGIMPR 

      1630       1640       1650       1660       1670       1680 
GTTPRAPVRF PTSLLKVRRG LETGWAYTHQ GGISSVDHVT AGKDLLVCDS MGRTRVVCQS 

      1690       1700       1710       1720       1730       1740 
NNKLTDETEY GVKTDSGCPD GARCYVLNPE AVNISGSKGA VVHLQKTGGE FTCVTASGTP 

      1750       1760       1770       1780       1790       1800 
AFFDLKNLKG WSGLPIFEAS SGRVVGRVKV GKNEESKPTK IMSGIQTVSK NTADLTEMVK 

      1810       1820       1830       1840       1850       1860 
KITSMNRGDF KQITLATGAG KTTELPKAVI EEIGRHKRVL VLIPLRAAAE SVYQYMRLKH 

      1870       1880       1890       1900       1910       1920 
PSISFNLRIG DMKEGDMATG ITYASYGYFC QMPQPKLRAA MVEYSYIFLD EYHCATPEQL 

      1930       1940       1950       1960       1970       1980 
AIIGKIHRFS ESIRVVAMTA TPAGSVTTTG QKHPIEEFIA PEVMEGEDLG SQFLDIAGLK 

      1990       2000       2010       2020       2030       2040 
IPVDEMKGNM LVFVPTRNMA VEVAKKLKAK GYNSGYYYSG EDPANLRVVT SQSPYVIVAT 

      2050       2060       2070       2080       2090       2100 
NAIESGVTLP DLDTVVDTGL KCEKRVRVSS KIPFIVTGLK RMAVTVGEQA QRRGRVGRVK 

      2110       2120       2130       2140       2150       2160 
PGRYYRSQET ATGSKDYHYD LLQAQRYGIE DGINVTKSFR EMNYDWSLYE EDSLLITQLE 

      2170       2180       2190       2200       2210       2220 
ILNNLLISED LPAAVKNIMA RTDHPEPIQL AYNSYEVQVP VLFPKIRNGE VTDTYENYSF 

      2230       2240       2250       2260       2270       2280 
LNARKLGEDV PVYIYATEDE DLAVDLLGLD WPDPGNQQVV ETGKALKQVA GLSSAENALL 

      2290       2300       2310       2320       2330       2340 
VALFGYVGYQ ALSKRHVPMI TDIYTIEDQR LEDTTHLQYA PNAIKTEGTE TELKELASGD 

      2350       2360       2370       2380       2390       2400 
VEKIMGAISD YAAGGLDFVK SQAEKIKTAP LFKENVEAAR GYVQKLIDSL IEDKDVIIRY 

      2410       2420       2430       2440       2450       2460 
GLWGTHTALY KSIAARLGHE TAFATLVLKW LAFGGETVSD HIRQAAVDLV VYYVMNKPSF 

      2470       2480       2490       2500       2510       2520 
PGDTETQQEG RRFVASLFIS ALATYTYKTW NYNNLSKVVE PALAYLPYAT SALKMFTPTR 

      2530       2540       2550       2560       2570       2580 
LESVVILSTT IYKTYLSIRK GKSDGLLGTG ISAAMEILSQ NPVSVGISVM LGVGAIAAHN 

      2590       2600       2610       2620       2630       2640 
AIESSEQKRT LLMKVFVKNF LDQAATDELV KENPEKIIMA LFEAVQTIGN PLRLIYHLYG 

      2650       2660       2670       2680       2690       2700 
VYYKGWEAKE LSERTAGRNL FTLIMFEAFE LLGMDSEGKI RNLSGNYILD LIHGLHKQIN 

      2710       2720       2730       2740       2750       2760 
RGLKKIVLGW APAPFSCDWT PSDERIRLPT DSYLRVETKC PCGYEMKALK NVSGKLTKVE 

      2770       2780       2790       2800       2810       2820 
ESGPFLCRNR PGRGPVNYRV TKYYDDNLRE IRPVAKLEGQ VEHYYKGVTA RIDYSKGKTL 

      2830       2840       2850       2860       2870       2880 
LATDKWEVEH GTLTRLTKRY TGVGFRGAYL GDEPNHRDLV ERDCATITKN TVQFLKMKKG 

      2890       2900       2910       2920       2930       2940 
CAFTYDLTIS NLTRLIELVH RNNLEEKEIP TATVTTWLAY TFVNEDVGTI KPVLGERVIP 

      2950       2960       2970       2980       2990       3000 
DPVVDINLQP EVQVDTSEVG ITIIGKEAVM TTGVTPVMEK VEPDTDNNQS SVKIGLDEGN 

      3010       3020       3030       3040       3050       3060 
YPGPGVQTHT LVEEIHNKDA RPFIMVLGSK SSMSNRAKTA RNINLYTGND PREIRDLMAE 

      3070       3080       3090       3100       3110       3120 
GRILVVALRD IDPDLSELVD FKGTFLDREA LEALSLGQPK PKQVTKAAIR DLLKEERQVE 

      3130       3140       3150       3160       3170       3180 
IPDWFTSDDP VFLDIAMKKD KYHLIGDVVE VKDQAKALGA TDQTRIVKEV GSRTYTMKLS 

      3190       3200       3210       3220       3230       3240 
SWFLQASSKQ MSLTPLFEEL LLRCPPATKS NKGHMASAYQ LAQGNWEPLG CGVHLGTVPA 

      3250       3260       3270       3280       3290       3300 
RRVKMHPYEA YLKLKDLVEE EEKKPRIRDT VIREHNKWIL KKIKFQGNLN TKKMLNPGKL 

      3310       3320       3330       3340       3350       3360 
SEQLDREGHK RNIYNNQIST VMSSAGIRLE KLPIVRAQTD TKSFHEAIRD KIDKNENRQN 

      3370       3380       3390       3400       3410       3420 
PELHNKLLEI FHTIADPSLK HTYGEVTWEQ LEAGINRKGA AGFLEKKNIG EVLDSEKHLV 

      3430       3440       3450       3460       3470       3480 
EQLVRDLKAG RKIRYYETAI PKNEKRDVSD DWQAGDLVDE KKPRVIQYPE AKTRLAITKV 

      3490       3500       3510       3520       3530       3540 
MYNWVKQQPV VIPGYEGKTP LFNIFNKVRK EWDLFNEPVA VSFDTKAWDT QVTSRDLHLI 

      3550       3560       3570       3580       3590       3600 
GEIQKYYYRK EWHKFIDTIT DHMVEVPVIT ADGEVYIRNG QRGSGQPDTS AGNSMLNVLT 

      3610       3620       3630       3640       3650       3660 
MIYAFCESTG VPYKSFNRVA KIHVCGDDGF LITEKGLGLK FSNKGMQILH EAGKPQKLTE 

      3670       3680       3690       3700       3710       3720 
GEKMKVAYKF EDIEFCSHTP VPVRWSDNTS SYMAGRDTAV ILSKMATRLD SSGERGTTAY 

      3730       3740       3750       3760       3770       3780 
EKAVAFSFLL MYSWNPLVRR ICLLVLSQRP ETAPSTQTTY YYKGDPIGAY KDVIGRNLSE 

      3790       3800       3810       3820       3830       3840 
LKRTGFEKLA NLNLSLSTLG IWTKHTSKRI IQDCVAIGKE EGNWLVNADR LISSKTGHLY 

      3850       3860       3870       3880       3890 
IPDKGFTLQG KHYEQLQLGA ETNPVMGVGT ERYKLGPIVN LLLRRLKVLL MAAVGASS 

« Hide

References

[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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96751 Genomic RNA. Translation: AAA42860.1.
PIRA44217.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YQ2X-ray2.58A/B696-1026[»]
2YQ3X-ray3.29A/B696-1026[»]
ProteinModelPortalQ01499.
SMRQ01499. Positions 2684-2711, 3271-3858.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS31.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.4.21.113. 925.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
3.90.730.10. 1 hit.
InterProIPR021824. 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]
PfamPF11889. 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]
PRINTSPR00729. CDVENDOPTASE.
ProDomPD003091. Peptidase_C53. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
SSF55895. SSF55895. 1 hit.
PROSITEPS51192. 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.
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Entry information

Entry namePOLG_BVDVS
AccessionPrimary (citable) accession number: Q01499
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 14, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references