P19712 (POLG_CSFVA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Genome polyprotein Cleaved into the following 13 chains: N-terminal protease Short name=N-pro EC=3.4.22.- Alternative name(s): Autoprotease p20 Capsid protein C E(rns) glycoprotein Alternative name(s): gp44/48 Envelope glycoprotein E1 Alternative name(s): gp33 Envelope glycoprotein E2 Alternative name(s): gp55 p7 Non-structural protein 2-3 Short name=NS2-3 Cysteine protease NS2 EC=3.4.22.- Alternative name(s): Non-structural protein 2 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 Non-structural protein 4A Short name=NS4A Non-structural protein 4B Short name=NS4B Non-structural protein 5A Short name=NS5A RNA-directed RNA polymerase EC=2.7.7.48 Alternative name(s): NS5B
Organism	Classical swine fever virus (strain Alfort) (CSFV) (Hog cholera virus) [Complete proteome]
Taxonomic identifier	11097 [NCBI]
Taxonomic lineage	Viruses › ssRNA positive-strand viruses, no DNA stage › Flaviviridae › Pestivirus
Virus host	Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length	3898 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 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. The E1 and E2 envelope glycoproteins form disulfide-linked homodimers as well as heterodimers. Ref.3
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. Ref.7 Envelope glycoprotein E2: Host cell surface By similarity Ref.7. Cysteine protease NS2: Host membrane; Multi-pass membrane protein Potential Ref.7.
Post-translational modification	The E(rns) glycoprotein is heavily glycosylated. Ref.3 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. Cleavage between E2 and p7 is partial By similarity.
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 process	Fusion of virus membrane with host endosomal membrane Fusion of virus membrane with host membrane Host-virus interaction Inhibition of host IFN-mediated response initiation by virus Inhibition of host IRF3 by virus Inhibition of host innate immune response by virus Initiation of viral infection Ion transport RNA replication Transport Viral attachment to host cell Viral immunoevasion Viral penetration into host cytoplasm
Cellular component	Host membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Helicase Hydrolase Ionic channel Nucleotidyltransferase Protease RNA-directed RNA polymerase Serine protease Thiol protease Transferase Viral ionic channel
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	evasion by virus of host immune response Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro viral genome replication Inferred from electronic annotation. Source: InterPro viral protein processing Inferred from electronic annotation. Source: InterPro
Cellular component	host cell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell host cell surface Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 168	168	N-terminal protease		PRO_0000038050
	Chain	169 – 267	99	Capsid protein C By similarity		PRO_0000038051
	Chain	268 – 494	227	E(rns) glycoprotein		PRO_0000038052
	Chain	495 – 656	162	Envelope glycoprotein E1		PRO_0000038053
	Chain	657 – 1062	406	Envelope glycoprotein E2		PRO_0000038054
	Chain	1063 – 1132	70	p7 By similarity		PRO_0000038055
	Chain	1133 – 2272	1140	Non-structural protein 2-3 By similarity		PRO_0000038056
	Chain	1133 – 1589	457	Cysteine protease NS2 By similarity		PRO_0000349361
	Chain	1590 – 2272	683	Serine protease NS3 By similarity		PRO_0000038057
	Chain	2273 – 2336	64	Non-structural protein 4A By similarity		PRO_0000038058
	Chain	2337 – 2683	347	Non-structural protein 4B By similarity		PRO_0000038059
	Chain	2684 – 3180	497	Non-structural protein 5A By similarity		PRO_0000038060
	Chain	3181 – 3898	718	RNA-directed RNA polymerase By similarity		PRO_0000038061
Regions
	Transmembrane	1140 – 1164	25	Helical; Potential
	Transmembrane	1189 – 1209	21	Helical; Potential
	Transmembrane	1217 – 1237	21	Helical; Potential
	Transmembrane	1247 – 1267	21	Helical; Potential
	Transmembrane	1281 – 1301	21	Helical; Potential
	Transmembrane	1360 – 1380	21	Helical; Potential
	Transmembrane	1568 – 1588	21	Helical; Potential
	Domain	1 – 168	168	Peptidase C53
	Domain	1441 – 1589	149	Peptidase C74
	Domain	1590 – 1763	174	Peptidase S31
	Domain	1802 – 1960	159	Helicase ATP-binding
	Domain	1978 – 2179	202	Helicase C-terminal
	Domain	3519 – 3642	124	RdRp catalytic
Sites
	Active site	22	1	For N-terminal protease activity Ref.6
	Active site	49	1	For N-terminal protease activity Ref.6
	Active site	69	1	For N-terminal protease activity Ref.6
	Active site	1447	1	For cysteine protease NS2 activity By similarity
	Active site	1461	1	For cysteine protease NS2 activity By similarity
	Active site	1512	1	For cysteine protease NS2 activity By similarity
	Active site	1658	1	Charge relay system; for serine protease NS3 activity By similarity
	Active site	1695	1	Charge relay system; for serine protease NS3 activity By similarity
	Active site	1752	1	Charge relay system; for serine protease NS3 activity By similarity
	Site	168 – 169	2	Cleavage; by autolysis
	Site	267 – 268	2	Cleavage; by host signal peptidase
	Site	494 – 495	2	Cleavage
	Site	656 – 657	2	Cleavage; by host signal peptidase
	Site	1062 – 1063	2	Cleavage; by host signal peptidase; partial By similarity
	Site	1132 – 1133	2	Cleavage; by host signal peptidase By similarity
	Site	1589 – 1590	2	Cleavage; partial; cysteine protease NS2 By similarity
	Site	2272 – 2273	2	Cleavage; by serine protease NS3 By similarity
	Site	2336 – 2337	2	Cleavage; by serine protease NS3 By similarity
	Site	2683 – 2684	2	Cleavage; by serine protease NS3 By similarity
	Site	3180 – 3181	2	Cleavage; by serine protease NS3 By similarity
Amino acid modifications
	Glycosylation	157	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	269	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	274	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	278	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	293	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	332	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	362	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	367	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	410	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	425	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	500	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	594	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	805	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	810	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	874	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	918	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	949	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	986	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	1713	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	2134	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	2217	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	2494	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	2787	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	2815	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	2891	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	3211	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	3316	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	3689	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	3698	1	N-linked (GlcNAc...); by host Potential
	Glycosylation	3794	1	N-linked (GlcNAc...); by host Potential
Natural variations
	Natural variant	387	1	T → A.
	Natural variant	3542	1	R → S.
Experimental info
	Mutagenesis	22	1	E → V: Almost complete loss of cleavage between N-pro and C. Ref.6
	Mutagenesis	40	1	H → L: No effect. Ref.6
	Mutagenesis	49	1	H → L: Complete loss of cleavage between N-pro and C. Ref.6
	Mutagenesis	69	1	C → A: Complete loss of cleavage between N-pro and C. Ref.6
	Mutagenesis	69	1	C → S: Complete loss of cleavage between N-pro and C. Ref.6
	Mutagenesis	99	1	H → L: No effect. Ref.6
	Mutagenesis	112	1	C → A: No effect. Ref.6
	Mutagenesis	112	1	C → S: No effect. Ref.6
	Mutagenesis	130	1	H → L: No effect. Ref.6
	Mutagenesis	134	1	C → A: No effect. Ref.6
	Mutagenesis	134	1	C → S: No effect. Ref.6
	Mutagenesis	138	1	C → A: No effect. Ref.6
	Mutagenesis	138	1	C → S: No effect. Ref.6
	Mutagenesis	161	1	C → A: No effect. Ref.6
	Mutagenesis	161	1	C → S: No effect. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P19712 [UniParc]. Last modified July 11, 2001. Version 2. Checksum: 2C1F17B8A359D0F6	FASTA	3,898	438,578
	10 20 30 40 50 60 MELNHFELLY KTSKQKPVGV EEPVYDTAGR PLFGNPSEVH PQSTLKLPHD RGRGDIRTTL 70 80 90 100 110 120 RDLPRKGDCR SGNHLGPVSG IYIKPGPVYY QDYTGPVYHR APLEFFDEAQ FCEVTKRIGR 130 140 150 160 170 180 VTGSDGKLYH IYVCVDGCIL LKLAKRGTPR TLKWIRNFTN CPLWVTSCSD DGASGSKDKK 190 200 210 220 230 240 PDRMNKGKLK IAPREHEKDS KTKPPDATIV VEGVKYQIKK KGKVKGKNTQ DGLYHNKNKP 250 260 270 280 290 300 PESRKKLEKA LLAWAVITIL LYQPVAAENI TQWNLSDNGT NGIQRAMYLR GVNRSLHGIW 310 320 330 340 350 360 PEKICKGVPT HLATDTELKE IRGMMDASER TNYTCCRLQR HEWNKHGWCN WYNIDPWIQL 370 380 390 400 410 420 MNRTQTNLTE GPPDKECAVT CRYDKNTDVN VVTQARNRPT TLTGCKKGKN FSFAGTVIEG 430 440 450 460 470 480 PCNFNVSVED ILYGDHECGS LLQDTALYLL DGMTNTIENA RQGAARVTSW LGRQLSTAGK 490 500 510 520 530 540 KLERRSKTWF GAYALSPYCN VTRKIGYIWY TNNCTPACLP KNTKIIGPGK FDTNAEDGKI 550 560 570 580 590 600 LHEMGGHLSE FLLLSLVILS DFAPETASTL YLILHYAIPQ SHEEPEGCDT NQLNLTVKLR 610 620 630 640 650 660 TEDVVPSSVW NIGKYVCVRP DWWPYETKVA LLFEEAGQVI KLVLRALRDL TRVWNSASTT 670 680 690 700 710 720 AFLICLIKVL RGQVVQGIIW LLLVTGAQGR LACKEDYRYA ISSTNEIGLL GAEGLTTTWK 730 740 750 760 770 780 EYSHGLQLDD GTVKAVCTAG SFKVTALNVV SRRYLASLHK RALPTSVTFE LLFDGTNPAI 790 800 810 820 830 840 EEMDDDFGFG LCPFDTSPVI KGKYNTTLLN GSAFYLVCPI GWTGVVECTA VSPTTLRTEV 850 860 870 880 890 900 VKTFRRDKPF PHRVDCVTTI VEKEDLFHCK LGGNWTCVKG DPVTYKGGQV KQCRWCGFEF 910 920 930 940 950 960 KEPYGLPHYP IGKCILTNET GYRVVDSTDC NRDGVVISTE GEHECLIGNT TVKVHALDER 970 980 990 1000 1010 1020 LGPMPCRPKE IVSSEGPVRK TSCTFNYTKT LRNKYYEPRD SYFQQYMLKG EYQYWFNLDV 1030 1040 1050 1060 1070 1080 TDHHTDYFAE FVVLVVVALL GGRYVLWLIV TYIILTEQLA AGLQLGQGEV VLIGNLITHT 1090 1100 1110 1120 1130 1140 DNEVVVYFLL LYLVIRDEPI KKWILLLFHA MTNNPVKTIT VALLMISGVA KGGKIDGGWQ 1150 1160 1170 1180 1190 1200 RQPVTSFDIQ LALAVVVVVV MLLAKRDPTT FPLVITVATL RTAKITNGFS TDLVIATVSA 1210 1220 1230 1240 1250 1260 ALLTWTYISD YYKYKTWLQY LVSTVTGIFL IRVLKGIGEL DLHAPTLPSH RPLFYILVYL 1270 1280 1290 1300 1310 1320 ISTAVVTRWN LDVAGLLLQC VPTLLMVFTM WADILTLILI LPTYELTKLY YLKEVKIGAE 1330 1340 1350 1360 1370 1380 RGWLWKTNYK RVNDIYEVDQ TSEGVYLFPS KQRTSAITST MLPLIKAILI SCISNKWQLI 1390 1400 1410 1420 1430 1440 YLLYLIFEVS YYLHKKVIDE IAGGTNFVSR LVAALIEVNW AFDNEEVKGL KKFFLLSSRV 1450 1460 1470 1480 1490 1500 KELIIKHKVR NEVVVRWFGD EEIYGMPKLI GLVKAATLSR NKHCMLCTVC EDRDWRGETC 1510 1520 1530 1540 1550 1560 PKCGRFGPPV VCGMTLADFE EKHYKRIFIR EDQSGGPLRE EHAGYLQYKA RGQLFLRNLP 1570 1580 1590 1600 1610 1620 VLATKVKMLL VGNLGTEIGD LEHLGWVLRG PAVCKKVTEH ERCTTSIMDK LTAFFGVMPR 1630 1640 1650 1660 1670 1680 GTTPRAPVRF PTSLLKIRRG LETGWAYTHQ GGISSVDHVT CGKDLLVCDT MGRTRVVCQS 1690 1700 1710 1720 1730 1740 NNKMTDESEY GVKTDSGCPE GARCYVFNPE AVNISGTKGA MVHLQKTGGE FTCVTASGTP 1750 1760 1770 1780 1790 1800 AFFDLKNLKG WSGLPIFEAS SGRVVGRVKV GKNEDSKPTK LMSGIQTVSK SATDLTEMVK 1810 1820 1830 1840 1850 1860 KITTMNRGEF RQITLATGAG KTTELPRSVI EEIGRHKRVL VLIPLRAAAE SVYQYMRQKH 1870 1880 1890 1900 1910 1920 PSIAFNLRIG EMKEGDMATG ITYASYGYFC QMSQPKLRAA MVEYSFIFLD EYHCATPEQL 1930 1940 1950 1960 1970 1980 AIMGKIHRFS ENLRVVAMTA TPAGTVTTTG QKHPIEEFIA PEVMKGEDLG SEYLDIAGLK 1990 2000 2010 2020 2030 2040 IPVEEMKNNM LVFVPTRNMA VEAAKKLKAK GYNSGYYYSG EDPSNLRVVT SQSPYVVVAT 2050 2060 2070 2080 2090 2100 NAIESGVTLP DLDVVVDTGL KCEKRIRLSP KMPFIVTGLK RMAVTIGEQA QRRGRVGRVK 2110 2120 2130 2140 2150 2160 PGRYYRSQET PVGSKDYHYD LLQAQRYGIE DGINITKSFR EMNYDWSLYE EDSLMITQLE 2170 2180 2190 2200 2210 2220 ILNNLLISEE LPMAVKNIMA RTDHPEPIQL AYNSYETQVP VLFPKIRNGE VTDTYDNYTF 2230 2240 2250 2260 2270 2280 LNARKLGDDV PPYVYATEDE DLAVELLGLD WPDPGNQGTV EAGRALKQVV GLSTAENALL 2290 2300 2310 2320 2330 2340 VALFGYVGYQ ALSKRHIPVV TDIYSVEDHR LEDTTHLQYA PNAIKTEGKE TELKELAQGD 2350 2360 2370 2380 2390 2400 VQRCVEAVTN YAREGIQFMK SQALKVRETP TYKETMNTVA DYVKKFIEAL TDSKEDIIKY 2410 2420 2430 2440 2450 2460 GLWGAHTALY KSIGARLGHE TAFATLVVKW LAFGGESISD HIKQAATDLV VYYIINRPQF 2470 2480 2490 2500 2510 2520 PGDTETQQEG RKFVASLLVS ALATYTYKSW NYNNLSKIVE PALATLPYAA KALKLFAPTR 2530 2540 2550 2560 2570 2580 LESVVILSTA IYKTYLSIRR GKSDGLLGTG VSAAMEIMSQ NPVSVGIAVM LGVGAVAAHN 2590 2600 2610 2620 2630 2640 AIEASEQKRT LLMKVFVKNF LDQAATDELV KESPEKIIMA LFEAVQTVGN PLRLVYHLYG 2650 2660 2670 2680 2690 2700 VFYKGWEAKE LAQRTAGRNL FTLIMFEAVE LLGVDSEGKI RQLSSNYILE LLYKFRDNIK 2710 2720 2730 2740 2750 2760 SSVREIAISW APAPFSCDWT PTDDRIGLPH ENYLRVETKC PCGYRMKAVK NCAGELRLLE 2770 2780 2790 2800 2810 2820 EGGSFLCRNK FGRGSQNYRV TKYYDDNLSE IKPVIRMEGH VELYYKGATI KLDFNNSKTV 2830 2840 2850 2860 2870 2880 LATDKWEVDH STLVRALKRY TGAGYRGAYL GEKPNHKHLI QRDCATITKD KVCFIKMKRG 2890 2900 2910 2920 2930 2940 CAFTYDLSLH NLTRLIELVH KNNLEDREIP AVTVTTWLAY TFVNEDIGTI KPTFGEKVTP 2950 2960 2970 2980 2990 3000 EKQEEVVLQP AVVVDTTDVA VTVVGETSTM TTGETPTTFT SLGSDSKVRQ VLKLGVDDGQ 3010 3020 3030 3040 3050 3060 YPGPNQQRAS LLEAIQGVDE RPSVLILGSD KATSNRVKTA KNVKIYRSRD PLELREMMKR 3070 3080 3090 3100 3110 3120 GKILVVALSR VDTALLKFVD YKGTFLTRET LEALSLGKPK KRDITKAEAQ WLLRLEDQIE 3130 3140 3150 3160 3170 3180 ELPDWFAAKE PIFLEANIKR DKYHLVGDIA TIKEKAKQLG ATDSTKISKE VGAKVYSMKL 3190 3200 3210 3220 3230 3240 SNWVIQEENK QGSLAPLFEE LLQQCPPGGQ NKTTHMVSAY QLAQGNWVPV SCHVFMGTIP 3250 3260 3270 3280 3290 3300 ARRTKTHPYE AYVKLRELVD EHKMKALCGG SGLSKHNEWV IGKVKYQGNL RTKHMLNPGK 3310 3320 3330 3340 3350 3360 VAEQLHREGY RHNVYNKTIG SVMTATGIRL EKLPVVRAQT DTTNFHQAIR DKIDKEENLQ 3370 3380 3390 3400 3410 3420 TPGLHKKLME VFNALKRPEL EASYDAVDWE ELERGINRKG AAGFFERKNI GEVLDSEKNK 3430 3440 3450 3460 3470 3480 VEEVIDSLKK GRNIRYYETA IPKNEKRDVN DDWTAGDFVD EKKPRVIQYP EAKTRLAITK 3490 3500 3510 3520 3530 3540 VMYKWVKQKP VVIPGYEGKT PLFQIFDKVK KEWDQFQNPV AVSFDTKAWD TQVTTRDLEL 3550 3560 3570 3580 3590 3600 IRDIQKFYFK KKWHKFIDTL TKHMSEVPVI SADGEVYIRK GQRGSGQPDT SAGNSMLNVL 3610 3620 3630 3640 3650 3660 TMVYAFCEAT GVPYKSFDRV AKIHVCGDDG FLITERALGE KFASKGVQIL YEAGKPQKIT 3670 3680 3690 3700 3710 3720 EGDKMKVAYQ FDDIEFCSHT PVQVRWSDNT SSYMPGRNTT TILAKMATRL DSSGERGTIA 3730 3740 3750 3760 3770 3780 YEKAVAFSFL LMYSWNPLIR RICLLVLSTE LQVRPGKSTT YYYEGDPISA YKEVIGHNLF 3790 3800 3810 3820 3830 3840 DLKRTSFEKL AKLNLSMSTL GVWTRHTSKR LLQDCVNVGT KEGNWLVNAD RLVSSKTGNR 3850 3860 3870 3880 3890 YIPGEGHTLQ GKHYEELILA RKPIGNFEGT DRYNLGPIVN VVLRRLKIMM MALIGRGV

References

[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: 2763466] [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: 1870198] [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: 8388499] [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: 8230432] [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: 9499122] [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]	"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: 10355762] [Abstract] Cited for: SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J04358 Genomic RNA. Translation: AAA43844.2.
3D structure databases
ProteinModelPortal	P19712.
SMR	P19712. Positions 3273-3854.
ModBase	Search...
Protein family/group databases
MEROPS	C53.001.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR021824. Capsid-C_pestivirus. IPR014001. DEAD-like_helicase. IPR011492. DEAD_Flavivir. IPR001650. Helicase_C. IPR022120. Pept_C74_NS2-pestiV. IPR008751. Peptidase_C53. IPR000280. Peptidase_S31. IPR007094. RNA-dir_pol_PSvirus. IPR002166. RNA_pol_HCV. IPR001568. RNase_T2. IPR018188. RNase_T2_AS. [Graphical view]
Gene3D	G3DSA:3.90.730.10. RNase_T2. 1 hit.
Pfam	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]
PRINTS	PR00729. CDVENDOPTASE.
ProDom	PD003091. Peptidase_C53. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. [Graphical view]
SUPFAM	SSF55895. RNase_T2. 1 hit.
PROSITE	PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. PS51535. PESTIVIRUS_NS3PRO. 1 hit. PS50507. RDRP_SSRNA_POS. 1 hit. PS00531. RNASE_T2_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
PMAP-CutDB	P19712.

Entry information

Entry name

POLG_CSFVA

Accession

Primary (citable) accession number: P19712

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	July 11, 2001
Last modified:	November 16, 2011
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program