ID B1PVV8_9FLAV Unreviewed; 3898 AA.
AC B1PVV8;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 24-JAN-2024, entry version 105.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Classical swine fever virus.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Pestivirus; Pestivirus suis.
OX NCBI_TaxID=11096 {ECO:0000313|EMBL:ACA60749.1, ECO:0000313|Proteomes:UP000099917};
RN [1] {ECO:0000313|EMBL:ACA60749.1, ECO:0000313|Proteomes:UP000099917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JL1 {ECO:0000313|EMBL:ACA60749.1};
RA Qiu H.-J., Jin M.-L., Chen D., Sun Y.;
RT "Isolation and characterization of Classical swine fever virus strain
RT JL1(06).";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a cofactor for the NS3 protease activity.
CC {ECO:0000256|ARBA:ARBA00023576}.
CC -!- FUNCTION: Packages viral RNA to form a viral nucleocapsid and thereby
CC protects viral RNA. Also plays a role in transcription regulation.
CC Protects the incoming virus against IFN-induced effectors.
CC {ECO:0000256|ARBA:ARBA00034097}.
CC -!- FUNCTION: Plays a role in the regulation of viral RNA replication.
CC {ECO:0000256|ARBA:ARBA00023574}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Leu is conserved at position P1 for all four cleavage sites.
CC Alanine is found at position P1' of the NS4A-NS4B cleavage site,
CC whereas serine is found at position P1' of the NS3-NS4A, NS4B-NS5A
CC and NS5A-NS5B cleavage sites.; EC=3.4.21.113;
CC Evidence={ECO:0000256|ARBA:ARBA00001160};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC Evidence={ECO:0000256|ARBA:ARBA00001491};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host
CC cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Virion membrane
CC {ECO:0000256|ARBA:ARBA00004650}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004650}.
CC -!- SIMILARITY: Belongs to the pestivirus polyprotein family.
CC {ECO:0000256|ARBA:ARBA00010133}.
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DR EMBL; EU497410; ACA60749.1; -; Genomic_RNA.
DR IntAct; B1PVV8; 2.
DR MEROPS; S31.001; -.
DR Proteomes; UP000099917; Genome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW.
DR GO; GO:0044228; C:host cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:InterPro.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003968; F:RNA-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0039520; P:induction by virus of host autophagy; IEA:UniProtKB-KW.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019082; P:viral protein processing; IEA:UniProtKB-UniRule.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0039707; P:virus-mediated pore formation in host cell membrane; IEA:UniProtKB-KW.
DR CDD; cd17931; DEXHc_viral_Ns3; 1.
DR CDD; cd23201; Pestivirus_RdRp; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.60.40.4200; Pestivirus envelope glycoprotein E2, C-terminal domain; 1.
DR Gene3D; 2.60.320.20; Pestivirus envelope glycoprotein E2, domain A; 1.
DR Gene3D; 2.60.40.3000; Pestivirus envelope glycoprotein E2, domain B; 1.
DR Gene3D; 2.30.140.40; Pestivirus Npro endopeptidase C53, interaction domain; 1.
DR Gene3D; 3.90.730.10; Ribonuclease T2-like; 1.
DR InterPro; IPR021824; Capsid-C_pestivirus.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR011492; Flavi_DEAD.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR022120; NS2.
DR InterPro; IPR030399; NS2_C74.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008751; Peptidase_C53.
DR InterPro; IPR042542; Peptidase_C53_interaction.
DR InterPro; IPR032521; Pestivirus_E2.
DR InterPro; IPR042309; Pestivirus_E2_A.
DR InterPro; IPR042310; Pestivirus_E2_B.
DR InterPro; IPR042311; Pestivirus_E2_D.
DR InterPro; IPR000280; Pestivirus_NS3_S31.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR002166; RNA_pol_HCV.
DR InterPro; IPR036430; RNase_T2-like_sf.
DR InterPro; IPR033130; RNase_T2_His_AS_2.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 1.
DR Pfam; PF11889; Capsid_pestivir; 1.
DR Pfam; PF20907; Flav_NS3-hel_C; 1.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF05550; Peptidase_C53; 1.
DR Pfam; PF12387; Peptidase_C74; 1.
DR Pfam; PF05578; Peptidase_S31; 1.
DR Pfam; PF16329; Pestivirus_E2; 1.
DR Pfam; PF00998; RdRP_3; 1.
DR PRINTS; PR00729; CDVENDOPTASE.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF55895; Ribonuclease Rh-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51692; PESTIVIRUS_NS2_PRO; 1.
DR PROSITE; PS51535; PESTIVIRUS_NS3PRO; 1.
DR PROSITE; PS51876; PV_NPRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS00531; RNASE_T2_2; 1.
PE 3: Inferred from homology;
KW Activation of host autophagy by virus {ECO:0000256|ARBA:ARBA00023050};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Fusion of virus membrane with host endosomal membrane
KW {ECO:0000256|ARBA:ARBA00022510};
KW Fusion of virus membrane with host membrane
KW {ECO:0000256|ARBA:ARBA00022506};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00868};
KW Inhibition of host innate immune response by virus
KW {ECO:0000256|ARBA:ARBA00022632, ECO:0000256|PROSITE-ProRule:PRU01224};
KW Inhibition of host IRF3 by virus {ECO:0000256|ARBA:ARBA00022931,
KW ECO:0000256|PROSITE-ProRule:PRU01224};
KW Inhibition of host RLR pathway by virus {ECO:0000256|ARBA:ARBA00022482,
KW ECO:0000256|PROSITE-ProRule:PRU01224};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU00868};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU00868};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW ProRule:PRU01224}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280};
KW Viral ion channel {ECO:0000256|ARBA:ARBA00023039};
KW Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022595};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022844};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296}.
FT TRANSMEM 1031..1055
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1076..1095
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1115..1133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1145..1164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1189..1208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1220..1238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1250..1271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1283..1304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..168
FT /note="Peptidase C53"
FT /evidence="ECO:0000259|PROSITE:PS51876"
FT DOMAIN 1441..1589
FT /note="Peptidase C74"
FT /evidence="ECO:0000259|PROSITE:PS51692"
FT DOMAIN 1590..1763
FT /note="Peptidase S31"
FT /evidence="ECO:0000259|PROSITE:PS51535"
FT DOMAIN 1802..1960
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1978..2179
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 3519..3642
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 170..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 49
FT /note="For N-terminal protease activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01224"
FT ACT_SITE 69
FT /note="For N-terminal protease activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01224"
FT ACT_SITE 1658
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00868"
FT ACT_SITE 1695
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00868"
FT ACT_SITE 1752
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00868"
FT SITE 168..169
FT /note="Cleavage; by autolysis"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01224"
SQ SEQUENCE 3898 AA; 437893 MW; 09E540B043FEDCA3 CRC64;
MELNHFELLY KTNKQKPMGV EEPVYDVTGR PLFGDPSEVH PQSTLKLPHD RGRGNIKTTL
NNLPRKGDCR SGNHLGPVSG IYVKPGPVFY QDYMGPVYHR APLEFFNETQ FCEVTKRIGR
VTGSDGKLYH MYVCIDGCIL LKLAKRGEPR TLKWIRNFTD CPLWVTSCSD DGASGSKEKK
PDRINKGKLK IAPKEHEKDS RTKPPDATIV VEGVKYQVKK KGKVKGKNTQ DGLYHNKNKP
PESRKKLEKA LLAWAVITIM LYQPVEAENI TQWNLSDNGT NGIQHAMYLR GVSRSLHGIW
PEKICKGVPT YLATDTELKE IQGMMDASEG TNYTCCKLQR HEWNKHGWCN WYNIDPWVQL
MNRTQANLAE GPPAKECAVT CRYDKDADIN VVTQARNRPT TLTGCKKGKN FSFAGTIIEG
PCNFNVSVED ILYGDHECGS LLQDTALYLV DGMTNTIENA RQGAARVTSW LGRQLSTAGK
RLEGRSKTWF GAYALSPYCN VTSKIGYIWY TNNCTPACLP KNTKIIGPGK FDTNAEDGKI
LHEMGGHLSE FLLLSLVVLS DFAPETASAL YLILHYVIPQ SYEEPEGCDT NQLNLTVELR
TEDVIPSSVW NVGKYVCVRP DWWPYETKVA LLFEEAGQVV KLALRALRDL TRVWNSASTT
AFLICLIKVL RGQIVQGVIW LLLVTGAQGR LACKEDYRYA ISSTNEIGLL GAGGLTTTWK
EYSHDLQLND GTVKAICVAG SFKVTALNVV SRRYLASLHK GALLTSVTFE LLFDGTNPST
EEMGDDFGFG LCPFDTSPVV KGKYNTTLLN GSAFYLVCPI GWTGVIECTA VSPTTLRTEV
VKTFRREKPF PHRMDCVTTT VENEDLFYCK LGGNWTCVKG EPVVYTGGQV KQCKWCGFDF
NEPDGLPHYP IGKCILANET GYRIVDSTDC NRDGVVISAE GSHECLIGNT TVKVHASDER
LGPMPCRPKE IVSSAGPVRK TSCTFNYAKT LKNKYYEPRD SYFQQYMLKG EYQYWFDLDV
TDRHSDYFAE FVVLVVVALL GGRYVLWLIV TYIVLTEQLA AGLPLGQGEV VLIGNLITHT
DIEVVVYFLL LYLVMRDEPI KKWILLLFHA MTNNPVKTIT VALLMVSGVA KGGKIDGGWQ
RLPETSFDIQ LALTVIVVAV MLLAKRDPTT VPLVITVATL RTAKMTNGLS TDIAIATVST
ALLTWTYISD YYRYKTWLQY LISTVTGIFL IRVLKGIGEL DLHTPTLPSY RPLFFILVYL
ISTAVVTRWN LDIAGLLLQC VPTLLMVFTM WADILTLILI LPTYELTKLY YLKEVKIGAE
RGWLWKTNFK RVNDIYEVDQ AGEGVYLFPS KQKTSSITGT MLPLIKAILI SCISNKWQFI
YLLYLIFEVS YYLHKKIIDE IAGGTNFISR LVAALIEANW AFDNEEVRGL KKFFLLSSRV
KELIIKHKVR NEVMVHWFGD EEVYGMPKLV GLVKAATLSK NKHCILCTVC EDREWKGETC
PKCGRFGPPM TCGMTLADFE EKHYKRIFFR EDQSEGPVRE EYAGYLQYRA RGQLFLRNLP
VLATKVKMLL VGNLGTEVGD LEHLGWVLRG PAVCKKVTEH EKCTTSIMDK LTAFFGVMPR
GTTPRAPVRF PTSLLKIRRG LETGWAYTHQ GGISSVDHVT CGKDLLVCDT MGRTRVVCQS
NNKMTDESEY GVKTDSGCPE GARCYVFNPE AVNISGTKGA MVHLQKTGGE FTCVTASGTP
AFFDLKNLKG WSGLPIFEAS SGRVVGRVKV GKNEDSKPTK LMSGIQTVSK STTDLTEMVK
KITTMNRGEF RQITLATGAG KTTELPRSVI EEIGRHKRVL VLIPLRAAAE SVYQYMRQKH
PSIAFNLRIG EMKEGDMATG ITYASYGYFC QMPQPKLRAA MVEYSFIFLD EYHCATPEQL
AIMGKIHRFS ENLRVVAMTA TPAGTVTTTG QKHPIEEFIA PEVMKGEDLG SEYLDIAGLK
IPVEEMKSNM LVFVPTRNMA VETAKKLKAK GYNSGYYYSG EDPSNLRVVT SQSPYVVVAT
NAIESGVTLP DLDVVVDTGL KCEKRIRLSS KMPFIVTGLK RMAVTIGEQA QRRGRVGRVK
PGRYYRSQET PVGSKDYHYD LLQAQRYGIE DGINITKSFR EMNYDWSLYE EDSLMITQLE
ILNNLLISEE LPMAVKNIMA RTDHPEPIQL AYNSYETQVP VLFPKIRNGE VTDSYDNYTF
LNARKLGDDV PPYVYATEDE DLAVELLGLD WPDPGNQGTV EAGRALKQVV GLSTAENALL
VALFGYVGYQ ALSKRHIPVV TDIYSIEDHR LEDTTHLQYA PNAIKTEGKE TELKELAQGD
VQRCVEAMTN YAREGIQFMK SQALKVKETP TYKETMDTVT DYVKKFMEAL KDSKEDIMKY
GLWGTHTALY KSISARLGSE TAFATLVVKW LAFGGESIAD HVKQAATDLV VYYIINRPQF
PGDTETQQEG RKFVASLLVS ALATYTYKSW NYNNLSKIVE PALATLPYAA TALKLFAPTR
LESVVILSTA IYKTYLSIRR GKSDGLLGTG VSAAMEIMSQ NPVSVGIAVM LGVGAVAAHN
AIEASEQKRT LLMKVFVKNF LDQAATDELV KESPEKIIMA LFEALQTVGN PLRLVYHLYG
VFYKGWEAKE LAQRTAGRNL FTLIMFEAVE LLGVDSEGKI RQLSSNYILE LLYKFRDSIK
SSVREMAISW APAPFSCDWT PTDNRIGLPQ DNFLQVETKC PCGYKMKAVK NCAGELRLLE
EEGSFLCRNK FGRGSRNYKV TKYYDDNLSE IKPVIKMEGH VELYYKGATI KLDFNNSKTI
LATDKWEVDH STLVRVLKRH TGAGYNGAYL GEKPNHKHLI ERDCATITKD KVCFLKMKRG
CAFTYDLSLH NLTRLIELVH KNNLEDKEIP AVTVTTWLAY TFVNEDIGTI RPAFGEKVTP
EMQEEITLQP AVVVDTTDVT VTVVGEAPTM TTGETPTAFT SSGSDPKGQQ VLKLGVGEGQ
YPGTNPQRAS LHEAIQGADE RPSVLILGSD KATSNRVKTA KNVKVYRGRD PLEVRDMMRR
GKILVIALSR VDNALLKFVD YKGTFLTRET LEALSLGRPK KKDITKAEAQ WLLCLEDQME
ELPDWFAAGE PIFLEANIKH DRYHLVGDIA TIKEKAKQLG ATDSTKISKE VGAKVYSMKL
SNWVMQEENK QGNLTPLFEE LLQQCPPGGQ NKTAHMVSAY QLAQGNWMPT SCHVFMGTIS
ARRIKTHPYE AYVKLRELVE EHKMKTLCPG SSLGKHNDWI IGKIKYQGNL RTKHMLNPGK
VAEQLCREGH RHNVYNKTIG SVMTATGIRL EKLPVVRAQT DTTNFHQAIR DKIDKEENLQ
TPGLHKKLME VFNALKRPEL ESSYDAVEWE ELERGINRKG AAGFFERKNI GEILDSEKNK
VEEIIDNLKK GRNIKYYETA IPKNEKRDVN DDWTAGDFVD EKKPRVIQYP EAKTRLAITK
VMYKWVKQKP VVIPGYEGKT PLFQIFDKVK KEWDQFQNPV AVSFDTKAWD TQVTTKDLEL
IKDIQKYYFK KKWHKFIDTL TMHMTEVPVI CADGEVYIRK GQRGSGQPDT SAGNSMLNVL
TMVYAFCEAT GVPYKSFDRV AKIHVCGDDG FLITERALGE KFASKGVQIL YEAGKPQKIT
EGDKMKVAYQ FDDIEFCSHT PIQVRWSDNT SSYMPGRNTT TILAKMATRL DSSGERGTIA
YEKAVAFSFL LMYSWNPLIR RICLLVLSTE LQVKPGKSTT YYYEGDPISA YKEVIGHNLF
DLKRTSFEKL AKLNLSMSVL GAWTRHTSKR LLQDCVNMGV KEGNWLVNAD RLVSSKTGNR
YIPGEGHTLQ GRHYEELVLA RKQINNFQGT DRYNLGPIVN MVLRRLRVMM MTLIGRGV
//