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Protein

Genome polyprotein

Gene
N/A
Organism
Classical swine fever virus (strain Brescia) (CSFV) (Hog cholera virus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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)DescriptionActionsGraphical viewLength
Active sitei22For N-terminal protease activityPROSITE-ProRule annotation1
Active sitei49For N-terminal protease activityPROSITE-ProRule annotation1
Active sitei69For N-terminal protease activityPROSITE-ProRule annotation1
Active sitei1447For cysteine protease NS2 activityPROSITE-ProRule annotation1
Active sitei1461For cysteine protease NS2 activityPROSITE-ProRule annotation1
Active sitei1512For cysteine protease NS2 activityPROSITE-ProRule annotation1
Active sitei1658Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1695Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1
Active sitei1752Charge relay system; for serine protease NS3 activityPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Serine protease, Thiol protease, Transferase, Viral ion channel

Keywords - Biological processi

Activation of host autophagy by virus, 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

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
OrganismiClassical swine fever virus (strain Brescia) (CSFV) (Hog cholera virus)
Taxonomic identifieri11098 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageFlaviviridaePestivirus
Virus hostiSus scrofa (Pig) [TaxID: 9823]
Proteomesi
  • UP000008569 Componenti: Genome

Subcellular locationi

E(rns) glycoprotein :
Cysteine protease NS2 :
  • Host membrane PROSITE-ProRule annotation; Multi-pass membrane protein PROSITE-ProRule annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei1140 – 1164HelicalPROSITE-ProRule annotationAdd BLAST25
Transmembranei1189 – 1209HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei1217 – 1237HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei1247 – 1267HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei1281 – 1301HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei1360 – 1380HelicalPROSITE-ProRule annotationAdd BLAST21
Transmembranei1568 – 1588HelicalPROSITE-ProRule annotationAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000380621 – 168N-terminal proteaseBy similarityAdd BLAST168
ChainiPRO_0000038063169 – 267Capsid protein CBy similarityAdd BLAST99
ChainiPRO_0000038064268 – 494E(rns) glycoproteinBy similarityAdd BLAST227
ChainiPRO_0000038065495 – 656Envelope glycoprotein E1By similarityAdd BLAST162
ChainiPRO_0000038066657 – 1062Envelope glycoprotein E2By similarityAdd BLAST406
ChainiPRO_00000380671063 – 1132p7By similarityAdd BLAST70
ChainiPRO_00000380681133 – 2272Non-structural protein 2-3By similarityAdd BLAST1140
ChainiPRO_00003493621133 – 1589Cysteine protease NS2PROSITE-ProRule annotationAdd BLAST457
ChainiPRO_00000380691590 – 2272Serine protease NS3By similarityAdd BLAST683
ChainiPRO_00000380702273 – 2336Non-structural protein 4ABy similarityAdd BLAST64
ChainiPRO_00000380712337 – 2683Non-structural protein 4BBy similarityAdd BLAST347
ChainiPRO_00000380722684 – 3180Non-structural protein 5ABy similarityAdd BLAST497
ChainiPRO_00000380733181 – 3898RNA-directed RNA polymeraseBy similarityAdd BLAST718

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi157N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi269N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi278N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi332N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi362N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi410N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi425N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi500N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi594N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi805N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi810N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi874N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi918N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi949N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1713N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2134N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2217N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2419N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2494N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2787N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2815N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi2891N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi3103N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi3211N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi3316N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi3689N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi3698N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi3794N-linked (GlcNAc...); by hostSequence analysis1

Post-translational modificationi

The E(rns) glycoprotein is heavily glycosylated.By similarity
The viral RNA of pestiviruses is expressed as a single polyprotein which undergoes post-translational proteolytic processing resulting in the production of at least eleven individual proteins. The N-terminal protease cleaves itself from the nascent polyprotein autocatalytically and thereby generates the N-terminus of the adjacent viral capsid protein C.
Cleavage between E2 and p7 is partial.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei168 – 169Cleavage; by autolysisBy similarity2
Sitei267 – 268Cleavage; by host signal peptidaseBy similarity2
Sitei494 – 495CleavageBy similarity2
Sitei656 – 657Cleavage; by host signal peptidaseBy similarity2
Sitei1062 – 1063Cleavage; by host signal peptidase; partialBy similarity2
Sitei1132 – 1133Cleavage; by host signal peptidaseBy similarity2
Sitei1589 – 1590Cleavage; partial; by cysteine protease NS2By similarity2
Sitei2272 – 2273Cleavage; by serine protease NS3By similarity2
Sitei2336 – 2337Cleavage; by serine protease NS3By similarity2
Sitei2683 – 2684Cleavage; by serine protease NS3By similarity2
Sitei3180 – 3181Cleavage; by serine protease NS3By similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein

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.By similarity

Protein-protein interaction databases

IntActiP21530. 51 interactors.

Structurei

3D structure databases

ProteinModelPortaliP21530.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 168Peptidase C53Add BLAST168
Domaini1441 – 1589Peptidase C74PROSITE-ProRule annotationAdd BLAST149
Domaini1590 – 1763Peptidase S31PROSITE-ProRule annotationAdd BLAST174
Domaini1802 – 1960Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST159
Domaini1978 – 2179Helicase C-terminalPROSITE-ProRule annotationAdd BLAST202
Domaini3519 – 3642RdRp catalyticPROSITE-ProRule annotationAdd BLAST124

Sequence similaritiesi

Belongs to the pestivirus polyprotein family.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
Contains 1 peptidase C53 domain.Curated
Contains 1 peptidase C74 domain.PROSITE-ProRule annotation
Contains 1 peptidase S31 domain.PROSITE-ProRule annotation
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
3.90.730.10. 1 hit.
InterProiIPR021824. Capsid-C_pestivirus.
IPR011492. DEAD_Flavivir.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR022120. NS2.
IPR030399. NS2_C74.
IPR027417. P-loop_NTPase.
IPR008751. Peptidase_C53.
IPR032521. Pestivirus_E2.
IPR000280. Pestivirus_NS3_S31.
IPR007094. RNA-dir_pol_PSvirus.
IPR002166. RNA_pol_HCV.
IPR001568. RNase_T2-like.
IPR033130. RNase_T2_His_AS_2.
[Graphical view]
PfamiPF11889. DUF3409. 1 hit.
PF07652. Flavi_DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF05550. Peptidase_C53. 1 hit.
PF12387. Peptidase_C74. 1 hit.
PF05578. Peptidase_S31. 1 hit.
PF16329. Pestivirus_E2. 1 hit.
PF00998. RdRP_3. 1 hit.
[Graphical view]
PRINTSiPR00729. CDVENDOPTASE.
ProDomiPD003091. Peptidase_C53. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF55895. SSF55895. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51692. PESTIVIRUS_NS2_PRO. 1 hit.
PS51535. PESTIVIRUS_NS3PRO. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
PS00531. RNASE_T2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21530-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELNHFELLY KTNKQKPMGV EEPVYDVTGR PLFGDPSEVH PQSTLKLPHD
60 70 80 90 100
RGRGNIKTTL KNLPRRGDCR SGNHLGPVSG IYVKPGPVFY QDYMGPVYHR
110 120 130 140 150
APLEFFDEAQ FCEVTKRIGR VTGSDGKLYH IYVCIDGCIL LKLAKRGEPR
160 170 180 190 200
TLKWIRNLTD CPLWVTSCSD DGASASKEKK PDRINKGKLK IAPKEHEKDS
210 220 230 240 250
RTKPPDATIV VEGVKYQVKK KGKVKGKNTQ DGLYHNKNKP PESRKKLEKA
260 270 280 290 300
LLAWAVIAIM LYQPVAAENI TQWNLRDNGT NGIQHAMYLR GVSRSLHGIW
310 320 330 340 350
PEKICKGVPT YLATDTELRE IQGMMVASEG TNYTCCKLQR HEWNKHGWCN
360 370 380 390 400
WYNIDPWIQL MNRTQANLAE GPPSKECAVT CRYDKNADIN VVTQARNRPT
410 420 430 440 450
TLTGCKKGTN FSFAGTVIEG PCNFNVSVED ILYGDHECGS LLQDTALYLV
460 470 480 490 500
DGMTNTIERA RQGAARVTSW LGRQLRIAGK RLEGRSKTWF GAYALSPYCN
510 520 530 540 550
VTTKIGYIWY TNNCTPACLP KNTKIIGPGK FDTNAEDGKI LHEMGGHLSE
560 570 580 590 600
FLLLSLVVLS DFAPETASAL YLILHYVIPQ SHEEPEGCDT NQLNLTVELR
610 620 630 640 650
TEDVIPSSVW NVGKYVCVRP DWWPYETKVA LLFEEAGQVV KLALRALRDL
660 670 680 690 700
TRVWNSASTT AFLICLIKVL RGQVVQGVIW LLLVTGAQGR LACKEDHRYA
710 720 730 740 750
ISTTNEIGLH GAEGLTTTWK EYNHNLQLDD GTVKAICMAG SFKVTALNVV
760 770 780 790 800
SRRYLASLHK DALPTSVTFE LLFDGTSPLT EEMGDDFGFG LCPYDTSPVV
810 820 830 840 850
KGKYNTTLLN GSAFYLVCPI GWTGVIECTA VSPTTLRTEV VKTFRREKPF
860 870 880 890 900
PYRRDCVTTT VENEDLFYCK WGGNWTCVKG EPVTYTGGPV KQCRWCGFDF
910 920 930 940 950
NEPDGLPHYP IGKCILANET GYRIVDSTDC NRDGVVISTE GSHECLIGNT
960 970 980 990 1000
TVKVHALDER LGPMPCRPKE IVSSAGPVRK TSCTFNYAKT LRNRYYEPRD
1010 1020 1030 1040 1050
SYFQQYMLKG EYQYWFDLDV TDRHSDYFAE FIVLVVVALL GGRYVLWLIV
1060 1070 1080 1090 1100
TYIVLTEQLA AGLQLGQGEV VLIGNLITHT DIEVVVYFLL LYLVMRDEPI
1110 1120 1130 1140 1150
KKWILLLFHA MTNNPVKTIT VALLMVSGVA KGGKIDGGWQ RLPETNFDIQ
1160 1170 1180 1190 1200
LALTVIVVAV MLLAKKDPTT VPLVITVATL RTAKITNGLS TDLAIATVST
1210 1220 1230 1240 1250
ALLTWTYISD YYKYKTLLQY LISTVTGIFL IRVLKGVGEL DLHTPTLPSY
1260 1270 1280 1290 1300
RPLFFILVYL ISTAVVTRWN LDIAGLLLQC VPTLLMVFTM WADILTLILI
1310 1320 1330 1340 1350
LPTYELTKLY YLKEVKIGAE RGWLWKTNFK RVNDIYEVDQ AGEGVYLFPS
1360 1370 1380 1390 1400
KQKTGTITGT MLPLIKAILI SCISNKWQFI YLLYLIFEVS YYLHKKIIDE
1410 1420 1430 1440 1450
IAGGTNFISR LVAALIEANW AFDNEEVRGL KKFFLLSSRV KELIIKHKVR
1460 1470 1480 1490 1500
NEVMVHWFGD EEVYGMPKLV GLVKAATLSK NKHCILCTVC ENREWRGETC
1510 1520 1530 1540 1550
PKCGRFGPPV TCGMTLADFE EKHYKRIFFR EDQSEGPVRE EYAGYLQYRA
1560 1570 1580 1590 1600
RGQLFLRNLP VLATKVKMLL VGNLGTEVGD LEHLGWVLRG PAVCKKVTEH
1610 1620 1630 1640 1650
EKCTTSIMDK LTAFFGVMPR GTTPRAPVRF PTSLLKIRRG LETGWAYTHQ
1660 1670 1680 1690 1700
GGISSVDHVT CGKDLLVCDT MGRTRVVCQS NNKMTDESEY GVKTDSGCPE
1710 1720 1730 1740 1750
GARCYVFNRE AVNISGTKGA MVHLQKTGGE FTCVTASGTP AFFDLKNLKG
1760 1770 1780 1790 1800
WSGLPIFEAS SGRVVGRVKV GKNEDSKPTK LMSGIQTVSK STTDLTEMVK
1810 1820 1830 1840 1850
KITTMNRGEF RQITLATGAG KTTELPRSVI EEIGRHKRVL VLIPLRAAAE
1860 1870 1880 1890 1900
SVYQYMRQKH PSIAFNLRIG EMKEGDMATG ITYASYGYFC QMPQPKLRAA
1910 1920 1930 1940 1950
MVEYSFIFLD EYHCSTPEQL AIMGKIHRFS ENLRVVAMTA TPAGTVTTTG
1960 1970 1980 1990 2000
QKHPIEEYIA PEVMKGEDLG PEYLDIAGLK IPVEEMKSNM LVFVPTRNMA
2010 2020 2030 2040 2050
VETAKKLKAK 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
VLFPKIKNGE VTDSYDNYTF LNARKLGDDV PPYVYATEDE DLAVELLGLD
2260 2270 2280 2290 2300
WPDPGNQGTV EAGRALKQVV GLSTAENALL VALFGYVGYQ ALSKRHIPVV
2310 2320 2330 2340 2350
TDIYSIEDHR LEDTTHLQYA PNAIKTEGKE TELKELAQGD VQRCMEAMTN
2360 2370 2380 2390 2400
YARDGIQFMK SQALKVKETP TYKETMDTVA DYVKKFMEAL ADSKEDIIKY
2410 2420 2430 2440 2450
GLWGTHTALY KSIGARLGNE TAFATLVVKW LAFGGESIAD HVKQAATDLV
2460 2470 2480 2490 2500
VYYIINRPQF PGDTETQQEG RKFVASLLVS ALATYTYKSW NYNNLSKIVE
2510 2520 2530 2540 2550
PALATLPYAA TALKLFAPTR LESVVILSTA IYKTYLSIRR GKSDGLLGTG
2560 2570 2580 2590 2600
VSAAMEIMSQ NPVSVGIAVM LGVGAVAAHN AIEASEQKRT LLMKVFVKNF
2610 2620 2630 2640 2650
LDQAATDELV KESPEKIIMA LFEAVQTVGN PLRLVYHVYG VFYKGWEAKE
2660 2670 2680 2690 2700
LAQRTAGRNL FTLIMFEAVE LLGVDSEGKI RQLSSNYILE LLYKFRDSIK
2710 2720 2730 2740 2750
SSVRQMAISW APAPFSCDWT PTDDRIGLPQ DNFLRVETKC PCGYKMKAVK
2760 2770 2780 2790 2800
NCAGELRLLE EEGSFLCRNK FGRGSRNYRV TKYYDDNLSE IKPVIRMEGH
2810 2820 2830 2840 2850
VELYYKGATI KLDFNNSKTI LATDKWEVDH STLVRVLKRH TGAGYCGAYL
2860 2870 2880 2890 2900
GEKPNHKHLI ERDCATITKD KVCFLKMKRG CAFTYDLSLH NLTRLIELVH
2910 2920 2930 2940 2950
KNNLEDKEIP AVTVTTWLAY TFVNEDIGTI KPAFGEKITP EMQEEITLQP
2960 2970 2980 2990 3000
AVLVDATDVT VTVVGETPTM TTGETPTTFT SSGPDPKGQQ VLKLGVGEGQ
3010 3020 3030 3040 3050
YPGTNPQRAS LHEAIQSADE RPSVLILGSD KATSNRVKTV KNVKVYRGRD
3060 3070 3080 3090 3100
PLEVRDMMRR GKILVIALSR VDNALLKFVD YKGTFLTRET LEALSLGRPK
3110 3120 3130 3140 3150
KKNITKAEAQ WLLRLEDQME ELPDWFAAGE PIFLEANIKH DRYHLVGDIA
3160 3170 3180 3190 3200
TIKEKAKQLG ATDSTKISKE VGAKVYSMKL SNWVMQEENK QSNLTPLFEE
3210 3220 3230 3240 3250
LLQQCPPGGQ NKTAHMVSAY QLAQGNWMPT SCHVFMGTIS ARRTKTHPYE
3260 3270 3280 3290 3300
AYVKLRELVE EHKMKTLCPG SSLRNDNEWV IGKIKYQGNL RTKHMLNPGK
3310 3320 3330 3340 3350
VAEQLHREGH RHNVYNKTIG SVMTATGIRL EKLPVVRAQT DTTNFHQAIR
3360 3370 3380 3390 3400
DKIDKEENLQ TPGLHKKLME VFNALKRPEL ESSYDAVEWE ELERGINRKG
3410 3420 3430 3440 3450
AAGFFERKNI GEILDSEKIK VEEIIDNLKK GRNIKYYETA IPKNEKRDVN
3460 3470 3480 3490 3500
DDWTAGDFVD EKKPRVIQYP EAKTRLAITK VMYKWVKQKP VVIPGYEGKT
3510 3520 3530 3540 3550
PLFQIFDKVK KEWDQFQNPV AVSFDTKAWD TQVTTNDLEL IKDIQKYYFK
3560 3570 3580 3590 3600
KKWHKFIDTL TMHMSEVPVI TADGEVYIRK GQRGSGQPDT SAGNSMLNVL
3610 3620 3630 3640 3650
TMVYAFCEAT GVPYKSFDRV AKIHVCGDDG FLITERALGE KFASKGVQIL
3660 3670 3680 3690 3700
YEAGKPQKIT EGDKMKVAYQ FADIEFCSHT PIQVRWSDNT SSYMPGRNTT
3710 3720 3730 3740 3750
TILAKMATRL DSSGERGTIA YEKAVAFSFL LMYSWNPLIR RICLLVLSTE
3760 3770 3780 3790 3800
LQVKPGKSTT YYYEGDPISA YKEVIGHNLF DLKRTSFEKL AKLNLSMSVL
3810 3820 3830 3840 3850
GAWTRHTSKR LLQDCVNMGV KEGNWLVNAD RLVSSKTGNR YVPGEGHTLQ
3860 3870 3880 3890
GRHYEELALA RKQINSFQGT DRYNLGPIVN MVLRRLRVMM MTLIGRGV
Length:3,898
Mass (Da):438,430
Last modified:May 1, 1991 - v1
Checksum:iEC6EB207A09D59FD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31768 Genomic RNA. Translation: AAA43843.1.
PIRiA35317. GNWVHB.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31768 Genomic RNA. Translation: AAA43843.1.
PIRiA35317. GNWVHB.

3D structure databases

ProteinModelPortaliP21530.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP21530. 51 interactors.

Protein family/group databases

MEROPSiS31.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
3.90.730.10. 1 hit.
InterProiIPR021824. Capsid-C_pestivirus.
IPR011492. DEAD_Flavivir.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR022120. NS2.
IPR030399. NS2_C74.
IPR027417. P-loop_NTPase.
IPR008751. Peptidase_C53.
IPR032521. Pestivirus_E2.
IPR000280. Pestivirus_NS3_S31.
IPR007094. RNA-dir_pol_PSvirus.
IPR002166. RNA_pol_HCV.
IPR001568. RNase_T2-like.
IPR033130. RNase_T2_His_AS_2.
[Graphical view]
PfamiPF11889. DUF3409. 1 hit.
PF07652. Flavi_DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF05550. Peptidase_C53. 1 hit.
PF12387. Peptidase_C74. 1 hit.
PF05578. Peptidase_S31. 1 hit.
PF16329. Pestivirus_E2. 1 hit.
PF00998. RdRP_3. 1 hit.
[Graphical view]
PRINTSiPR00729. CDVENDOPTASE.
ProDomiPD003091. Peptidase_C53. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF55895. SSF55895. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51692. PESTIVIRUS_NS2_PRO. 1 hit.
PS51535. PESTIVIRUS_NS3PRO. 1 hit.
PS50507. RDRP_SSRNA_POS. 1 hit.
PS00531. RNASE_T2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_CSFVB
AccessioniPrimary (citable) accession number: P21530
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: November 30, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.