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Sequence of POLG_CSFVA

EC Number:3.4.21.113

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
pestivirus NS3 polyprotein peptidase
P19712
Classical swine fever virus (strain Alfort)
3898
438578
Reaction
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
Other sequences found for EC No. 3.4.21.113

General information:

Sequence
show sequence in fasta format
   0 MELNHFELLY KTSKQKPVGV EEPVYDTAGR PLFGNPSEVH PQSTLKLPHD RGRGDIRTTL
  60 RDLPRKGDCR SGNHLGPVSG IYIKPGPVYY QDYTGPVYHR APLEFFDEAQ FCEVTKRIGR
 120 VTGSDGKLYH IYVCVDGCIL LKLAKRGTPR TLKWIRNFTN CPLWVTSCSD DGASGSKDKK
 180 PDRMNKGKLK IAPREHEKDS KTKPPDATIV VEGVKYQIKK KGKVKGKNTQ DGLYHNKNKP
 240 PESRKKLEKA LLAWAVITIL LYQPVAAENI TQWNLSDNGT NGIQRAMYLR GVNRSLHGIW
 300 PEKICKGVPT HLATDTELKE IRGMMDASER TNYTCCRLQR HEWNKHGWCN WYNIDPWIQL
 360 MNRTQTNLTE GPPDKECAVT CRYDKNTDVN VVTQARNRPT TLTGCKKGKN FSFAGTVIEG
 420 PCNFNVSVED ILYGDHECGS LLQDTALYLL DGMTNTIENA RQGAARVTSW LGRQLSTAGK
 480 KLERRSKTWF GAYALSPYCN VTRKIGYIWY TNNCTPACLP KNTKIIGPGK FDTNAEDGKI
 540 LHEMGGHLSE FLLLSLVILS DFAPETASTL YLILHYAIPQ SHEEPEGCDT NQLNLTVKLR
 600 TEDVVPSSVW NIGKYVCVRP DWWPYETKVA LLFEEAGQVI KLVLRALRDL TRVWNSASTT
 660 AFLICLIKVL RGQVVQGIIW LLLVTGAQGR LACKEDYRYA ISSTNEIGLL GAEGLTTTWK
 720 EYSHGLQLDD GTVKAVCTAG SFKVTALNVV SRRYLASLHK RALPTSVTFE LLFDGTNPAI
 780 EEMDDDFGFG LCPFDTSPVI KGKYNTTLLN GSAFYLVCPI GWTGVVECTA VSPTTLRTEV
 840 VKTFRRDKPF PHRVDCVTTI VEKEDLFHCK LGGNWTCVKG DPVTYKGGQV KQCRWCGFEF
 900 KEPYGLPHYP IGKCILTNET GYRVVDSTDC NRDGVVISTE GEHECLIGNT TVKVHALDER
 960 LGPMPCRPKE IVSSEGPVRK TSCTFNYTKT LRNKYYEPRD SYFQQYMLKG EYQYWFNLDV
1020 TDHHTDYFAE FVVLVVVALL GGRYVLWLIV TYIILTEQLA AGLQLGQGEV VLIGNLITHT
1080 DNEVVVYFLL LYLVIRDEPI KKWILLLFHA MTNNPVKTIT VALLMISGVA KGGKIDGGWQ
1140 RQPVTSFDIQ LALAVVVVVV MLLAKRDPTT FPLVITVATL RTAKITNGFS TDLVIATVSA
1200 ALLTWTYISD YYKYKTWLQY LVSTVTGIFL IRVLKGIGEL DLHAPTLPSH RPLFYILVYL
1260 ISTAVVTRWN LDVAGLLLQC VPTLLMVFTM WADILTLILI LPTYELTKLY YLKEVKIGAE
1320 RGWLWKTNYK RVNDIYEVDQ TSEGVYLFPS KQRTSAITST MLPLIKAILI SCISNKWQLI
1380 YLLYLIFEVS YYLHKKVIDE IAGGTNFVSR LVAALIEVNW AFDNEEVKGL KKFFLLSSRV
1440 KELIIKHKVR NEVVVRWFGD EEIYGMPKLI GLVKAATLSR NKHCMLCTVC EDRDWRGETC
1500 PKCGRFGPPV VCGMTLADFE EKHYKRIFIR EDQSGGPLRE EHAGYLQYKA RGQLFLRNLP
1560 VLATKVKMLL VGNLGTEIGD LEHLGWVLRG PAVCKKVTEH ERCTTSIMDK LTAFFGVMPR
1620 GTTPRAPVRF PTSLLKIRRG LETGWAYTHQ GGISSVDHVT CGKDLLVCDT MGRTRVVCQS
1680 NNKMTDESEY GVKTDSGCPE GARCYVFNPE AVNISGTKGA MVHLQKTGGE FTCVTASGTP
1740 AFFDLKNLKG WSGLPIFEAS SGRVVGRVKV GKNEDSKPTK LMSGIQTVSK SATDLTEMVK
1800 KITTMNRGEF RQITLATGAG KTTELPRSVI EEIGRHKRVL VLIPLRAAAE SVYQYMRQKH
1860 PSIAFNLRIG EMKEGDMATG ITYASYGYFC QMSQPKLRAA MVEYSFIFLD EYHCATPEQL
1920 AIMGKIHRFS ENLRVVAMTA TPAGTVTTTG QKHPIEEFIA PEVMKGEDLG SEYLDIAGLK
1980 IPVEEMKNNM LVFVPTRNMA VEAAKKLKAK GYNSGYYYSG EDPSNLRVVT SQSPYVVVAT
2040 NAIESGVTLP DLDVVVDTGL KCEKRIRLSP KMPFIVTGLK RMAVTIGEQA QRRGRVGRVK
2100 PGRYYRSQET PVGSKDYHYD LLQAQRYGIE DGINITKSFR EMNYDWSLYE EDSLMITQLE
2160 ILNNLLISEE LPMAVKNIMA RTDHPEPIQL AYNSYETQVP VLFPKIRNGE VTDTYDNYTF
2220 LNARKLGDDV PPYVYATEDE DLAVELLGLD WPDPGNQGTV EAGRALKQVV GLSTAENALL
2280 VALFGYVGYQ ALSKRHIPVV TDIYSVEDHR LEDTTHLQYA PNAIKTEGKE TELKELAQGD
2340 VQRCVEAVTN YAREGIQFMK SQALKVRETP TYKETMNTVA DYVKKFIEAL TDSKEDIIKY
2400 GLWGAHTALY KSIGARLGHE TAFATLVVKW LAFGGESISD HIKQAATDLV VYYIINRPQF
2460 PGDTETQQEG RKFVASLLVS ALATYTYKSW NYNNLSKIVE PALATLPYAA KALKLFAPTR
2520 LESVVILSTA IYKTYLSIRR GKSDGLLGTG VSAAMEIMSQ NPVSVGIAVM LGVGAVAAHN
2580 AIEASEQKRT LLMKVFVKNF LDQAATDELV KESPEKIIMA LFEAVQTVGN PLRLVYHLYG
2640 VFYKGWEAKE LAQRTAGRNL FTLIMFEAVE LLGVDSEGKI RQLSSNYILE LLYKFRDNIK
2700 SSVREIAISW APAPFSCDWT PTDDRIGLPH ENYLRVETKC PCGYRMKAVK NCAGELRLLE
2760 EGGSFLCRNK FGRGSQNYRV TKYYDDNLSE IKPVIRMEGH VELYYKGATI KLDFNNSKTV
2820 LATDKWEVDH STLVRALKRY TGAGYRGAYL GEKPNHKHLI QRDCATITKD KVCFIKMKRG
2880 CAFTYDLSLH NLTRLIELVH KNNLEDREIP AVTVTTWLAY TFVNEDIGTI KPTFGEKVTP
2940 EKQEEVVLQP AVVVDTTDVA VTVVGETSTM TTGETPTTFT SLGSDSKVRQ VLKLGVDDGQ
3000 YPGPNQQRAS LLEAIQGVDE RPSVLILGSD KATSNRVKTA KNVKIYRSRD PLELREMMKR
3060 GKILVVALSR VDTALLKFVD YKGTFLTRET LEALSLGKPK KRDITKAEAQ WLLRLEDQIE
3120 ELPDWFAAKE PIFLEANIKR DKYHLVGDIA TIKEKAKQLG ATDSTKISKE VGAKVYSMKL
3180 SNWVIQEENK QGSLAPLFEE LLQQCPPGGQ NKTTHMVSAY QLAQGNWVPV SCHVFMGTIP
3240 ARRTKTHPYE AYVKLRELVD EHKMKALCGG SGLSKHNEWV IGKVKYQGNL RTKHMLNPGK
3300 VAEQLHREGY RHNVYNKTIG SVMTATGIRL EKLPVVRAQT DTTNFHQAIR DKIDKEENLQ
3360 TPGLHKKLME VFNALKRPEL EASYDAVDWE ELERGINRKG AAGFFERKNI GEVLDSEKNK
3420 VEEVIDSLKK GRNIRYYETA IPKNEKRDVN DDWTAGDFVD EKKPRVIQYP EAKTRLAITK
3480 VMYKWVKQKP VVIPGYEGKT PLFQIFDKVK KEWDQFQNPV AVSFDTKAWD TQVTTRDLEL
3540 IRDIQKFYFK KKWHKFIDTL TKHMSEVPVI SADGEVYIRK GQRGSGQPDT SAGNSMLNVL
3600 TMVYAFCEAT GVPYKSFDRV AKIHVCGDDG FLITERALGE KFASKGVQIL YEAGKPQKIT
3660 EGDKMKVAYQ FDDIEFCSHT PVQVRWSDNT SSYMPGRNTT TILAKMATRL DSSGERGTIA
3720 YEKAVAFSFL LMYSWNPLIR RICLLVLSTE LQVRPGKSTT YYYEGDPISA YKEVIGHNLF
3780 DLKRTSFEKL AKLNLSMSTL GVWTRHTSKR LLQDCVNVGT KEGNWLVNAD RLVSSKTGNR
3840 YIPGEGHTLQ GKHYEELILA RKPIGNFEGT DRYNLGPIVN VVLRRLKIMM MALIGRGV
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
842273
Meyers G.,Ruemenapf T.,Thiel H.-J.
Molecular cloning and nucleotide sequence of the genome of hog cholera virus.
Virology
171
555-567
1989
842275
Weiland E.,Stark R.,Haas B.,Ruemenapf T.,Meyers G.,Thiel H.J.
Pestivirus glycoprotein which induces neutralizing antibodies forms part of a disulfide-linked heterodimer.
J. Virol.
64
3563-3569
1990
842276
Thiel H.-J.,Stark R.,Weiland E.,Ruemenapf T.,Meyers G.
Hog cholera virus: molecular composition of virions from a pestivirus.
J. Virol.
65
4705-4712
1991
842277
Ruemenapf T.,Unger G.,Strauss J.H.,Thiel H.-J.
Processing of the envelope glycoproteins of pestiviruses.
J. Virol.
67
3288-3294
1993
842278
Stark R.,Meyers G.,Ruemenapf T.,Thiel H.-J.
Processing of pestivirus polyprotein: cleavage site between autoprotease and nucleocapsid protein of classical swine fever virus.
J. Virol.
67
7088-7095
1993
842279
Schneider R.,Unger G.,Stark R.,Schneider-Scherzer E.,Thiel H.J.
Identification of a structural glycoprotein of an RNA virus as a ribonuclease.
Science
261
1169-1171
1993
842280
Ruemenapf T.,Stark R.,Heimann M.,Thiel H.-J.
N-terminal protease of pestiviruses: identification of putative catalytic residues by site-directed mutagenesis.
J. Virol.
72
2544-2547
1998
842281
Sizova D.V.,Kolupaeva V.G.,Pestova T.V.,Shatsky I.N.,Hellen C.U.
Specific interaction of eukaryotic translation initiation factor 3 with the 5' nontranslated regions of hepatitis C virus and classical swine fever virus RNAs.
J. Virol.
72
4775-4782
1998
842282
Liu J.J.,Wong M.L.,Chang T.J.
The recombinant nucleocapsid protein of classical swine fever virus can act as a transcriptional regulator.
Virus Res.
53
75-80
1998
842283
Weiland F.,Weiland E.,Unger G.,Saalmuller A.,Thiel H.-J.
Localization of pestiviral envelope proteins E(rns) and E2 at the cell surface and on isolated particles.
J. Gen. Virol.
80
1157-1165
1999
842284
Moser C.,Stettler P.,Tratschin J.D.,Hofmann M.A.
Cytopathogenic and noncytopathogenic RNA replicons of classical swine fever virus.
J. Virol.
73
7787-7794
1999
842285
Wang Z.,Nie Y.,Wang P.,Ding M.,Deng H.
Characterization of classical swine fever virus entry by using pseudotyped viruses: E1 and E2 are sufficient to mediate viral entry.
Virology
330
332-341
2004
842286
Moulin H.R.,Seuberlich T.,Bauhofer O.,Bennett L.C.,Tratschin J.D.,Hofmann M.A.,Ruggli N.
Nonstructural proteins NS2-3 and NS4A of classical swine fever virus: essential features for infectious particle formation.
Virology
365
376-389
2007
842287
Bauhofer O.,Summerfield A.,Sakoda Y.,Tratschin J.D.,Hofmann M.A.,Ruggli N.
Classical swine fever virus Npro interacts with interferon regulatory factor 3 and induces its proteasomal degradation.
J. Virol.
81
3087-3096
2007
842288
Tews B.A.,Schuermann E.M.,Meyers G.
Mutation of cysteine 171 of pestivirus E rns RNase prevents homodimer formation and leads to attenuation of classical swine fever virus.
J. Virol.
83
4823-4834
2009
842289
Luo X.,Ling D.,Li T.,Wan C.,Zhang C.,Pan Z.
Classical swine fever virus Erns glycoprotein antagonizes induction of interferon-beta by double-stranded RNA.
Can. J. Microbiol.
55
698-704
2009
842290
Wen G.,Xue J.,Shen Y.,Zhang C.,Pan Z.
Characterization of classical swine fever virus (CSFV) nonstructural protein 3 (NS3) helicase activity and its modulation by CSFV RNA-dependent RNA polymerase.
Virus Res.
141
63-70
2009
842291
Sheng C.,Chen Y.,Xiao J.,Xiao J.,Wang J.,Li G.,Chen J.,Xiao M.
Classical swine fever virus NS5A protein interacts with 3'-untranslated region and regulates viral RNA synthesis.
Virus Res.
163
636-643
2012
842292
Chen Y.,Xiao J.,Xiao J.,Sheng C.,Wang J.,Jia L.,Zhi Y.,Li G.,Chen J.,Xiao M.
Classical swine fever virus NS5A regulates viral RNA replication through binding to NS5B and 3'UTR.
Virology
432
376-388
2012
842293
Gladue D.P.,Holinka L.G.,Largo E.,Fernandez Sainz I.,Carrillo C.,O'Donnell V.,Baker-Branstetter R.,Lu Z.,Ambroggio X.,Risatti G.R.,Nieva J.L.,Borca M.V.
Classical swine fever virus p7 protein is a viroporin involved in virulence in swine.
J. Virol.
86
6778-6791
2012
842294
Gottipati K.,Acholi S.,Ruggli N.,Choi K.H.
Autocatalytic activity and substrate specificity of the pestivirus N-terminal protease Npro.
Virology
452
303-309
2014
842295
Gladue D.P.,O'Donnell V.,Fernandez-Sainz I.J.,Fletcher P.,Baker-Branstetter R.,Holinka L.G.,Sanford B.,Carlson J.,Lu Z.,Borca M.V.
Interaction of structural core protein of classical swine fever virus with endoplasmic reticulum-associated degradation pathway protein OS9.
Virology
460
173-179
2014
842296
Largo E.,Gladue D.P.,Huarte N.,Borca M.V.,Nieva J.L.
Pore-forming activity of pestivirus p7 in a minimal model system supports genus-specific viroporin function.
Antiviral Res.
101
30-36
2014
842297
Li S.,Wang J.,He W.R.,Feng S.,Li Y.,Wang X.,Liao Y.,Qin H.Y.,Li L.F.,Dong H.,Sun Y.,Luo Y.,Qiu H.J.
Thioredoxin 2 Is a Novel E2-Interacting Protein That Inhibits the Replication of Classical Swine Fever Virus.
J. Virol.
89
8510-8524
2015
842298
Chen J.,He W.R.,Shen L.,Dong H.,Yu J.,Wang X.,Yu S.,Li Y.,Li S.,Luo Y.,Sun Y.,Qiu H.J.
The laminin receptor is a cellular attachment receptor for classical Swine Fever virus.
J. Virol.
89
4894-4906
2015
842299
Gottipati K.,Holthauzen L.M.,Ruggli N.,Choi K.H.
Pestivirus Npro Directly Interacts with Interferon Regulatory Factor 3 Monomer and Dimer.
J. Virol.
90
7740-7747
2016
842300
Riedel C.,Lamp B.,Hagen B.,Indik S.,Ruemenapf T.
The core protein of a pestivirus protects the incoming virus against IFN-induced effectors.
Sci. Rep.
7
44459-44459
2017
842301
Lv H.,Dong W.,Cao Z.,Li X.,Wang J.,Qian G.,Lv Q.,Wang C.,Guo K.,Zhang Y.
TRAF6 is a novel NS3-interacting protein that inhibits classical swine fever virus replication.
Sci. Rep.
7
6737-6737
2017
842302
Lin J.,Wang C.,Zhang L.,Wang T.,Zhang J.,Liang W.,Li C.,Qian G.,Ouyang Y.,Guo K.,Zhang Y.
Rab5 Enhances Classical Swine Fever Virus Proliferation and Interacts with Viral NS4B Protein to Facilitate Formation of NS4B Related Complex.
Front. Microbiol.
8
1468-1468
2017
842303
Tucakov A.K.,Yavuz S.,Schuermann E.M.,Mischler M.,Klingebeil A.,Meyers G.
dimerization via pseudoreversion partially restores virulence of classical swine fever virus.
J. Gen. Virol.
99
86-96
2018
842304
Qian G.,Lv H.,Lin J.,Li X.,Lv Q.,Wang T.,Zhang J.,Dong W.,Guo K.,Zhang Y.
FHC, an NS4B-interacting Protein, Enhances Classical Swine Fever Virus Propagation and Acts Positively in Viral Anti-apoptosis.
Sci. Rep.
8
8318-8318
2018
842305
Xu C.,Feng L.,Chen P.,Li A.,Guo S.,Jiao X.,Zhang C.,Zhao Y.,Jin X.,Zhong K.,Guo Y.,Zhu H.,Han L.,Yang G.,Li H.,Wang Y.
Viperin inhibits classical swine fever virus replication by interacting with viral nonstructural 5A protein.
J. Med. Virol.
92
149-160
2020
842306
Tortorici M.A.,Duquerroy S.,Kwok J.,Vonrhein C.,Perez J.,Lamp B.,Bricogne G.,Ruemenapf T.,Vachette P.,Rey F.A.
X-ray structure of the pestivirus NS3 helicase and its conformation in solution.
J. Virol.
89
4356-4371
2015
842307
Dubrau D.,Tortorici M.A.,Rey F.A.,Tautz N.
A positive-strand RNA virus uses alternative protein-protein interactions within a viral protease/cofactor complex to switch between RNA replication and virion morphogenesis.
PLoS Pathog.
13
0-0
2017