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Protein

Genome polyprotein

Gene
N/A
Organism
Classical swine fever virus (strain Alfort) (CSFV) (Hog cholera virus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E(rns), E1 and E2 are responsible of cell attachment and subsequent fusion of viral and cellular membrane.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 annotation1 Publication
Active sitei49 – 491For N-terminal protease activityPROSITE-ProRule annotation1 Publication
Active sitei69 – 691For N-terminal protease activityPROSITE-ProRule annotation1 Publication
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 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

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, 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 entry into host cell

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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
OrganismiClassical swine fever virus (strain Alfort) (CSFV) (Hog cholera virus)
Taxonomic identifieri11097 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaePestivirus
Virus hostiSus scrofa (Pig) [TaxID: 9823]
Proteomesi
  • UP000008568 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
Transmembranei1140 – 116425HelicalPROSITE-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

  • host cell cytoplasm 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: UniProtKB-KW
  • virion membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host membrane, Membrane, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi22 – 221E → V: Almost complete loss of cleavage between N-pro and C. 1 Publication
Mutagenesisi40 – 401H → L: No effect. 1 Publication
Mutagenesisi49 – 491H → L: Complete loss of cleavage between N-pro and C. 1 Publication
Mutagenesisi69 – 691C → A: Complete loss of cleavage between N-pro and C. 1 Publication
Mutagenesisi69 – 691C → S: Complete loss of cleavage between N-pro and C. 1 Publication
Mutagenesisi99 – 991H → L: No effect. 1 Publication
Mutagenesisi112 – 1121C → A: No effect. 1 Publication
Mutagenesisi112 – 1121C → S: No effect. 1 Publication
Mutagenesisi130 – 1301H → L: No effect. 1 Publication
Mutagenesisi134 – 1341C → A: No effect. 1 Publication
Mutagenesisi134 – 1341C → S: No effect. 1 Publication
Mutagenesisi138 – 1381C → A: No effect. 1 Publication
Mutagenesisi138 – 1381C → S: No effect. 1 Publication
Mutagenesisi161 – 1611C → A: No effect. 1 Publication
Mutagenesisi161 – 1611C → S: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 168168N-terminal proteasePRO_0000038050Add
BLAST
Chaini169 – 26799Capsid protein CBy similarityPRO_0000038051Add
BLAST
Chaini268 – 494227E(rns) glycoproteinPRO_0000038052Add
BLAST
Chaini495 – 656162Envelope glycoprotein E1PRO_0000038053Add
BLAST
Chaini657 – 1062406Envelope glycoprotein E2PRO_0000038054Add
BLAST
Chaini1063 – 113270p7By similarityPRO_0000038055Add
BLAST
Chaini1133 – 22721140Non-structural protein 2-3By similarityPRO_0000038056Add
BLAST
Chaini1133 – 1589457Cysteine protease NS2PROSITE-ProRule annotationPRO_0000349361Add
BLAST
Chaini1590 – 2272683Serine protease NS3By similarityPRO_0000038057Add
BLAST
Chaini2273 – 233664Non-structural protein 4ABy similarityPRO_0000038058Add
BLAST
Chaini2337 – 2683347Non-structural protein 4BBy similarityPRO_0000038059Add
BLAST
Chaini2684 – 3180497Non-structural protein 5ABy similarityPRO_0000038060Add
BLAST
Chaini3181 – 3898718RNA-directed RNA polymeraseBy similarityPRO_0000038061Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi157 – 1571N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi269 – 2691N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi274 – 2741N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi278 – 2781N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi293 – 2931N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi332 – 3321N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi362 – 3621N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi367 – 3671N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi410 – 4101N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi425 – 4251N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi500 – 5001N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi594 – 5941N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi805 – 8051N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi810 – 8101N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi874 – 8741N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi918 – 9181N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi949 – 9491N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi986 – 9861N-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
Glycosylationi2787 – 27871N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2815 – 28151N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi2891 – 28911N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi3211 – 32111N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi3316 – 33161N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi3689 – 36891N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi3698 – 36981N-linked (GlcNAc...); by hostSequence analysis
Glycosylationi3794 – 37941N-linked (GlcNAc...); by hostSequence analysis

Post-translational modificationi

The E(rns) glycoprotein is heavily glycosylated.1 Publication
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.2 Publications
Cleavage between E2 and p7 is partial.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei168 – 1692Cleavage; by autolysis
Sitei267 – 2682Cleavage; by host signal peptidase
Sitei494 – 4952Cleavage
Sitei656 – 6572Cleavage; by host signal peptidase
Sitei1062 – 10632Cleavage; by host signal peptidase; partialBy similarity
Sitei1132 – 11332Cleavage; by host signal peptidaseBy similarity
Sitei1589 – 15902Cleavage; partial; cysteine protease NS2PROSITE-ProRule annotation
Sitei2272 – 22732Cleavage; by serine protease NS3By similarity
Sitei2336 – 23372Cleavage; by serine protease NS3By similarity
Sitei2683 – 26842Cleavage; by serine protease NS3By similarity
Sitei3180 – 31812Cleavage; by serine protease NS3By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Miscellaneous databases

PMAP-CutDBP19712.

Expressioni

Inductioni

Translated cap independently from an internal ribosome entry site (IRES).1 Publication

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.

Protein-protein interaction databases

IntActiP19712. 93 interactions.

Structurei

Secondary structure

1
3898
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1792 – 180312Combined sources
Beta strandi1810 – 18145Combined sources
Beta strandi1817 – 18193Combined sources
Beta strandi1821 – 18233Combined sources
Helixi1824 – 183310Combined sources
Beta strandi1839 – 18457Combined sources
Helixi1846 – 185914Combined sources
Beta strandi1865 – 18717Combined sources
Beta strandi1880 – 18856Combined sources
Helixi1886 – 18894Combined sources
Helixi1894 – 19018Combined sources
Beta strandi1905 – 19106Combined sources
Helixi1912 – 19143Combined sources
Helixi1917 – 192711Combined sources
Helixi1928 – 19325Combined sources
Beta strandi1935 – 19395Combined sources
Beta strandi1956 – 19583Combined sources
Turni1970 – 19723Combined sources
Beta strandi1973 – 19764Combined sources
Beta strandi1979 – 19824Combined sources
Helixi1983 – 19875Combined sources
Beta strandi1990 – 19934Combined sources
Helixi1997 – 200913Combined sources
Beta strandi2014 – 20174Combined sources
Helixi2024 – 20307Combined sources
Beta strandi2032 – 20343Combined sources
Beta strandi2036 – 20416Combined sources
Helixi2042 – 20454Combined sources
Beta strandi2054 – 20574Combined sources
Beta strandi2061 – 20688Combined sources
Beta strandi2070 – 20734Combined sources
Beta strandi2075 – 20828Combined sources
Helixi2086 – 20938Combined sources
Beta strandi2096 – 21005Combined sources
Beta strandi2103 – 21053Combined sources
Beta strandi2112 – 21143Combined sources
Helixi2118 – 21247Combined sources
Helixi2125 – 21284Combined sources
Turni2129 – 21324Combined sources
Helixi2135 – 214612Combined sources
Helixi2153 – 216614Combined sources
Helixi2173 – 21819Combined sources
Helixi2188 – 21936Combined sources
Turni2194 – 21963Combined sources
Beta strandi2204 – 22074Combined sources
Beta strandi2210 – 22156Combined sources
Beta strandi2234 – 22374Combined sources
Helixi2238 – 22469Combined sources
Helixi2257 – 227014Combined sources
Helixi2272 – 22754Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CBGX-ray2.82A/B/C/D1782-2280[»]
4CBHX-ray2.51A/B/C/D1782-2280[»]
4CBIX-ray3.00A/B/C/D1782-2280[»]
4CBLX-ray3.05A/B/C/D1792-2176[»]
A/B/C/D2178-2280[»]
4CBMX-ray3.27A/B/C/D1782-2280[»]
ProteinModelPortaliP19712.
SMRiP19712. Positions 3273-3854.
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 – 2179202Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini3519 – 3642124RdRp 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.
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.

P19712-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELNHFELLY KTSKQKPVGV EEPVYDTAGR PLFGNPSEVH PQSTLKLPHD
60 70 80 90 100
RGRGDIRTTL RDLPRKGDCR SGNHLGPVSG IYIKPGPVYY QDYTGPVYHR
110 120 130 140 150
APLEFFDEAQ FCEVTKRIGR VTGSDGKLYH IYVCVDGCIL LKLAKRGTPR
160 170 180 190 200
TLKWIRNFTN CPLWVTSCSD DGASGSKDKK PDRMNKGKLK IAPREHEKDS
210 220 230 240 250
KTKPPDATIV VEGVKYQIKK KGKVKGKNTQ DGLYHNKNKP PESRKKLEKA
260 270 280 290 300
LLAWAVITIL LYQPVAAENI TQWNLSDNGT NGIQRAMYLR GVNRSLHGIW
310 320 330 340 350
PEKICKGVPT HLATDTELKE IRGMMDASER TNYTCCRLQR HEWNKHGWCN
360 370 380 390 400
WYNIDPWIQL MNRTQTNLTE GPPDKECAVT CRYDKNTDVN VVTQARNRPT
410 420 430 440 450
TLTGCKKGKN FSFAGTVIEG PCNFNVSVED ILYGDHECGS LLQDTALYLL
460 470 480 490 500
DGMTNTIENA RQGAARVTSW LGRQLSTAGK KLERRSKTWF GAYALSPYCN
510 520 530 540 550
VTRKIGYIWY TNNCTPACLP KNTKIIGPGK FDTNAEDGKI LHEMGGHLSE
560 570 580 590 600
FLLLSLVILS DFAPETASTL YLILHYAIPQ SHEEPEGCDT NQLNLTVKLR
610 620 630 640 650
TEDVVPSSVW NIGKYVCVRP DWWPYETKVA LLFEEAGQVI KLVLRALRDL
660 670 680 690 700
TRVWNSASTT AFLICLIKVL RGQVVQGIIW LLLVTGAQGR LACKEDYRYA
710 720 730 740 750
ISSTNEIGLL GAEGLTTTWK EYSHGLQLDD GTVKAVCTAG SFKVTALNVV
760 770 780 790 800
SRRYLASLHK RALPTSVTFE LLFDGTNPAI EEMDDDFGFG LCPFDTSPVI
810 820 830 840 850
KGKYNTTLLN GSAFYLVCPI GWTGVVECTA VSPTTLRTEV VKTFRRDKPF
860 870 880 890 900
PHRVDCVTTI VEKEDLFHCK LGGNWTCVKG DPVTYKGGQV KQCRWCGFEF
910 920 930 940 950
KEPYGLPHYP IGKCILTNET GYRVVDSTDC NRDGVVISTE GEHECLIGNT
960 970 980 990 1000
TVKVHALDER LGPMPCRPKE IVSSEGPVRK TSCTFNYTKT LRNKYYEPRD
1010 1020 1030 1040 1050
SYFQQYMLKG EYQYWFNLDV TDHHTDYFAE FVVLVVVALL GGRYVLWLIV
1060 1070 1080 1090 1100
TYIILTEQLA AGLQLGQGEV VLIGNLITHT DNEVVVYFLL LYLVIRDEPI
1110 1120 1130 1140 1150
KKWILLLFHA MTNNPVKTIT VALLMISGVA KGGKIDGGWQ RQPVTSFDIQ
1160 1170 1180 1190 1200
LALAVVVVVV MLLAKRDPTT FPLVITVATL RTAKITNGFS TDLVIATVSA
1210 1220 1230 1240 1250
ALLTWTYISD YYKYKTWLQY LVSTVTGIFL IRVLKGIGEL DLHAPTLPSH
1260 1270 1280 1290 1300
RPLFYILVYL ISTAVVTRWN LDVAGLLLQC VPTLLMVFTM WADILTLILI
1310 1320 1330 1340 1350
LPTYELTKLY YLKEVKIGAE RGWLWKTNYK RVNDIYEVDQ TSEGVYLFPS
1360 1370 1380 1390 1400
KQRTSAITST MLPLIKAILI SCISNKWQLI YLLYLIFEVS YYLHKKVIDE
1410 1420 1430 1440 1450
IAGGTNFVSR LVAALIEVNW AFDNEEVKGL KKFFLLSSRV KELIIKHKVR
1460 1470 1480 1490 1500
NEVVVRWFGD EEIYGMPKLI GLVKAATLSR NKHCMLCTVC EDRDWRGETC
1510 1520 1530 1540 1550
PKCGRFGPPV VCGMTLADFE EKHYKRIFIR EDQSGGPLRE EHAGYLQYKA
1560 1570 1580 1590 1600
RGQLFLRNLP VLATKVKMLL VGNLGTEIGD LEHLGWVLRG PAVCKKVTEH
1610 1620 1630 1640 1650
ERCTTSIMDK LTAFFGVMPR GTTPRAPVRF PTSLLKIRRG LETGWAYTHQ
1660 1670 1680 1690 1700
GGISSVDHVT CGKDLLVCDT MGRTRVVCQS NNKMTDESEY GVKTDSGCPE
1710 1720 1730 1740 1750
GARCYVFNPE AVNISGTKGA MVHLQKTGGE FTCVTASGTP AFFDLKNLKG
1760 1770 1780 1790 1800
WSGLPIFEAS SGRVVGRVKV GKNEDSKPTK LMSGIQTVSK SATDLTEMVK
1810 1820 1830 1840 1850
KITTMNRGEF RQITLATGAG KTTELPRSVI EEIGRHKRVL VLIPLRAAAE
1860 1870 1880 1890 1900
SVYQYMRQKH PSIAFNLRIG EMKEGDMATG ITYASYGYFC QMSQPKLRAA
1910 1920 1930 1940 1950
MVEYSFIFLD EYHCATPEQL AIMGKIHRFS ENLRVVAMTA TPAGTVTTTG
1960 1970 1980 1990 2000
QKHPIEEFIA PEVMKGEDLG SEYLDIAGLK IPVEEMKNNM LVFVPTRNMA
2010 2020 2030 2040 2050
VEAAKKLKAK GYNSGYYYSG EDPSNLRVVT SQSPYVVVAT NAIESGVTLP
2060 2070 2080 2090 2100
DLDVVVDTGL KCEKRIRLSP KMPFIVTGLK RMAVTIGEQA QRRGRVGRVK
2110 2120 2130 2140 2150
PGRYYRSQET PVGSKDYHYD LLQAQRYGIE DGINITKSFR EMNYDWSLYE
2160 2170 2180 2190 2200
EDSLMITQLE ILNNLLISEE LPMAVKNIMA RTDHPEPIQL AYNSYETQVP
2210 2220 2230 2240 2250
VLFPKIRNGE VTDTYDNYTF LNARKLGDDV PPYVYATEDE DLAVELLGLD
2260 2270 2280 2290 2300
WPDPGNQGTV EAGRALKQVV GLSTAENALL VALFGYVGYQ ALSKRHIPVV
2310 2320 2330 2340 2350
TDIYSVEDHR LEDTTHLQYA PNAIKTEGKE TELKELAQGD VQRCVEAVTN
2360 2370 2380 2390 2400
YAREGIQFMK SQALKVRETP TYKETMNTVA DYVKKFIEAL TDSKEDIIKY
2410 2420 2430 2440 2450
GLWGAHTALY KSIGARLGHE TAFATLVVKW LAFGGESISD HIKQAATDLV
2460 2470 2480 2490 2500
VYYIINRPQF PGDTETQQEG RKFVASLLVS ALATYTYKSW NYNNLSKIVE
2510 2520 2530 2540 2550
PALATLPYAA KALKLFAPTR LESVVILSTA IYKTYLSIRR GKSDGLLGTG
2560 2570 2580 2590 2600
VSAAMEIMSQ NPVSVGIAVM LGVGAVAAHN AIEASEQKRT LLMKVFVKNF
2610 2620 2630 2640 2650
LDQAATDELV KESPEKIIMA LFEAVQTVGN PLRLVYHLYG VFYKGWEAKE
2660 2670 2680 2690 2700
LAQRTAGRNL FTLIMFEAVE LLGVDSEGKI RQLSSNYILE LLYKFRDNIK
2710 2720 2730 2740 2750
SSVREIAISW APAPFSCDWT PTDDRIGLPH ENYLRVETKC PCGYRMKAVK
2760 2770 2780 2790 2800
NCAGELRLLE EGGSFLCRNK FGRGSQNYRV TKYYDDNLSE IKPVIRMEGH
2810 2820 2830 2840 2850
VELYYKGATI KLDFNNSKTV LATDKWEVDH STLVRALKRY TGAGYRGAYL
2860 2870 2880 2890 2900
GEKPNHKHLI QRDCATITKD KVCFIKMKRG CAFTYDLSLH NLTRLIELVH
2910 2920 2930 2940 2950
KNNLEDREIP AVTVTTWLAY TFVNEDIGTI KPTFGEKVTP EKQEEVVLQP
2960 2970 2980 2990 3000
AVVVDTTDVA VTVVGETSTM TTGETPTTFT SLGSDSKVRQ VLKLGVDDGQ
3010 3020 3030 3040 3050
YPGPNQQRAS LLEAIQGVDE RPSVLILGSD KATSNRVKTA KNVKIYRSRD
3060 3070 3080 3090 3100
PLELREMMKR GKILVVALSR VDTALLKFVD YKGTFLTRET LEALSLGKPK
3110 3120 3130 3140 3150
KRDITKAEAQ WLLRLEDQIE ELPDWFAAKE PIFLEANIKR DKYHLVGDIA
3160 3170 3180 3190 3200
TIKEKAKQLG ATDSTKISKE VGAKVYSMKL SNWVIQEENK QGSLAPLFEE
3210 3220 3230 3240 3250
LLQQCPPGGQ NKTTHMVSAY QLAQGNWVPV SCHVFMGTIP ARRTKTHPYE
3260 3270 3280 3290 3300
AYVKLRELVD EHKMKALCGG SGLSKHNEWV IGKVKYQGNL RTKHMLNPGK
3310 3320 3330 3340 3350
VAEQLHREGY RHNVYNKTIG SVMTATGIRL EKLPVVRAQT DTTNFHQAIR
3360 3370 3380 3390 3400
DKIDKEENLQ TPGLHKKLME VFNALKRPEL EASYDAVDWE ELERGINRKG
3410 3420 3430 3440 3450
AAGFFERKNI GEVLDSEKNK VEEVIDSLKK GRNIRYYETA IPKNEKRDVN
3460 3470 3480 3490 3500
DDWTAGDFVD EKKPRVIQYP EAKTRLAITK VMYKWVKQKP VVIPGYEGKT
3510 3520 3530 3540 3550
PLFQIFDKVK KEWDQFQNPV AVSFDTKAWD TQVTTRDLEL IRDIQKFYFK
3560 3570 3580 3590 3600
KKWHKFIDTL TKHMSEVPVI SADGEVYIRK GQRGSGQPDT SAGNSMLNVL
3610 3620 3630 3640 3650
TMVYAFCEAT GVPYKSFDRV AKIHVCGDDG FLITERALGE KFASKGVQIL
3660 3670 3680 3690 3700
YEAGKPQKIT EGDKMKVAYQ FDDIEFCSHT PVQVRWSDNT SSYMPGRNTT
3710 3720 3730 3740 3750
TILAKMATRL DSSGERGTIA YEKAVAFSFL LMYSWNPLIR RICLLVLSTE
3760 3770 3780 3790 3800
LQVRPGKSTT YYYEGDPISA YKEVIGHNLF DLKRTSFEKL AKLNLSMSTL
3810 3820 3830 3840 3850
GVWTRHTSKR LLQDCVNVGT KEGNWLVNAD RLVSSKTGNR YIPGEGHTLQ
3860 3870 3880 3890
GKHYEELILA RKPIGNFEGT DRYNLGPIVN VVLRRLKIMM MALIGRGV
Length:3,898
Mass (Da):438,578
Last modified:July 11, 2001 - v2
Checksum:i2C1F17B8A359D0F6
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti387 – 3871T → A.
Natural varianti3542 – 35421R → S.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04358 Genomic RNA. Translation: AAA43844.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04358 Genomic RNA. Translation: AAA43844.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4CBGX-ray2.82A/B/C/D1782-2280[»]
4CBHX-ray2.51A/B/C/D1782-2280[»]
4CBIX-ray3.00A/B/C/D1782-2280[»]
4CBLX-ray3.05A/B/C/D1792-2176[»]
A/B/C/D2178-2280[»]
4CBMX-ray3.27A/B/C/D1782-2280[»]
ProteinModelPortaliP19712.
SMRiP19712. Positions 3273-3854.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP19712. 93 interactions.

Protein family/group databases

MEROPSiC53.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

PMAP-CutDBP19712.

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...

Publicationsi

  1. "Molecular cloning and nucleotide sequence of the genome of hog cholera virus."
    Meyers G., Ruemenapf T., Thiel H.-J.
    Virology 171:555-567(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. Meyers G.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 2731.
  3. "Hog cholera virus: molecular composition of virions from a pestivirus."
    Thiel H.-J., Stark R., Weiland E., Ruemenapf T., Meyers G.
    J. Virol. 65:4705-4712(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION OF E(RNS), GLYCOSYLATION OF E(RNS).
  4. "Processing of the envelope glycoproteins of pestiviruses."
    Ruemenapf T., Unger G., Strauss J.H., Thiel H.-J.
    J. Virol. 67:3288-3294(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN, PROTEIN SEQUENCE OF 169-178.
  5. "Processing of pestivirus polyprotein: cleavage site between autoprotease and nucleocapsid protein of classical swine fever virus."
    Stark R., Meyers G., Ruemenapf T., Thiel H.-J.
    J. Virol. 67:7088-7095(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
  6. "N-terminal protease of pestiviruses: identification of putative catalytic residues by site-directed mutagenesis."
    Ruemenapf T., Stark R., Heimann M., Thiel H.-J.
    J. Virol. 72:2544-2547(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE OF N-PRO, MUTAGENESIS OF GLU-22; HIS-40; HIS-49; CYS-69; HIS-99; CYS-112; HIS-130; CYS-134; CYS-138 AND CYS-161.
  7. "Specific interaction of eukaryotic translation initiation factor 3 with the 5' nontranslated regions of hepatitis C virus and classical swine fever virus RNAs."
    Sizova D.V., Kolupaeva V.G., Pestova T.V., Shatsky I.N., Hellen C.U.
    J. Virol. 72:4775-4782(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "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.

Entry informationi

Entry nameiPOLG_CSFVA
AccessioniPrimary (citable) accession number: P19712
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 11, 2001
Last modified: April 13, 2016
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.