ID F1BZ95_9FLAV Unreviewed; 3897 AA.
AC F1BZ95;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Bovine viral diarrhea virus 2.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Pestivirus; Pestivirus tauri.
OX NCBI_TaxID=54315 {ECO:0000313|EMBL:ADX31696.1, ECO:0000313|Proteomes:UP000155957};
RN [1] {ECO:0000313|EMBL:ADX31696.1, ECO:0000313|Proteomes:UP000155957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=446 {ECO:0000313|EMBL:ADX31696.1};
RX PubMed=21470568; DOI=10.1016/j.virusres.2011.03.024;
RA Neill J.D., Newcomer B.W., Marley S.D., Ridpath J.F., Givens M.D.;
RT "Genetic change in the open reading frame of bovine viral diarrhea virus is
RT introduced more rapidly during the establishment of a single persistent
RT infection than from multiple acute infections.";
RL Virus Res. 158:140-145(2011).
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; HQ174297; ADX31696.1; -; Genomic_RNA.
DR MEROPS; S31.001; -.
DR Proteomes; UP000155957; 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: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:0005525; F:GTP binding; IEA:UniProtKB-KW.
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; IPR049486; NS3-hel_C_flaviviridae.
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:SF234; ATP-DEPENDENT RNA HELICASE DHX40-RELATED; 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 1033..1052
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1072..1096
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1108..1132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1183..1203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1215..1233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1254..1276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1282..1302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1358..1385
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 1439..1587
FT /note="Peptidase C74"
FT /evidence="ECO:0000259|PROSITE:PS51692"
FT DOMAIN 1588..1761
FT /note="Peptidase S31"
FT /evidence="ECO:0000259|PROSITE:PS51535"
FT DOMAIN 1800..1958
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1971..2141
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 3517..3640
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 170..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..208
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 1656
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00868"
FT ACT_SITE 1693
FT /note="Charge relay system; for serine protease NS3
FT activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00868"
FT ACT_SITE 1750
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 3897 AA; 437848 MW; 9952C74B4AEC1B64 CRC64;
MELFSNELLY KTYKQKPAGI VEPVYDINGC PLFGESSGIH PQSTLKLPHQ RGSANILTDA
RSLPRKGDCR KGNVNGAVSG IYIKPGPVYY QDYTGPVYHR APLELCREAS MCETTRRIGR
VTGSNGNLYH IYVCIDGCIL LKRATRDQPE VLKWVYNRLN CPLWVTSCSD EGGKGATSKK
QPKPDRIEKG KMKIAPKETE KDSKTRPPDA TIVVEGVKYQ VKKKGKVRGK NTQDGLYHNK
NKPPESRKKL EKALLAWAIL AAVLLQLVTG ENITQWNLMD NGTEGIQQAM FLRGVNRSLH
GIWPEKICTG VPTHLATDYE LKEIVGMMDA SEKTNYTCCR LQRHEWNKHG WCNWFHIEPW
IWLMNKTQNN LTGGQPPREC AVTCRYDRET ELNIVTQARD RPTTLTGCKK GKNFSFAGTV
LDGPCNFKVS AEDVLFKEHD CGNLLQETAI QLLDGATNTI EGARAGTAKL TTWLGKQLGI
LGKKLENKSK AWFGAHAASP YCDVERKIGY IWYTKNCTPA CLPRNTKIIG PGKFDTNAED
GKILHEMGGH LSEFVLLSLV VLSDFAPETA SAIYLVLHFA IPQSYVSVDT CDKNQLNLTV
ATTVAEVIPG SVWNLGKYVC IRPDWWPYET TTVFVLEEAG QVVKLGLRAI RDLTRIWNAA
TTTAFLVFLV KALRGQLIQG LLWLMLITGA QGFPECKEGF QYAISKDKKM GLLGPESLTT
TWHLSTKKLI DSMVQVWCEG EDLKILRTCT KEERYLVAVH ERALSTSAEF LKISDGTTGP
EVIDMPDDFE FGLCPCDSKP IIRGKFNTSL LNGPAFQMVC PQGWTGTIEC ILANQDTLDT
TVIRTYRRTA PFQRRKWCAY EKIVGEDIYE CILGGNWTCI IGNHSKLKDG LIKKCKWCGY
DFSSPEGLPH YPIGKCMLSN ESGYRYVDDT SCDRGGVAIV PIGTVKCRIG NVTVQVIATN
KDLGPMPCSP SEVIASEGPV EKTACTFNYA ETLPNKYYEP RDRYFQQYML KGKWQYWFDL
DSADHHKDYF SEFIIIAVVA LLGGKYVLWL LVTYMILSEQ IAMGARVNNE EIVMIGNLLT
HSDIEVVVYF LLLYLIIKEE PVRKWIILVY HILVASPMKT IGVILLLLGG MVKASKINTD
DQSTMDPCFL LVTGLVAVLM IARREPATLP LVVALLAIRT SGFLLPASID ITVAVVLTVL
LLASYVTDYF RYKKWLQFTF SLIAGIFIIR SLNHINQMEV PEISIPRWRP LALVLFYIIS
TAITTSWDID LAGFLLQWAP AVIMMATMWA DFLTLIVVLP SYELSKLYFL RNVRTDVEKN
WIGKVKYRQI SSVYDICDSE EAVYLFPSRH KSGSRPDFIL PFVKAVLISC ISSQWQLVYI
SYLILEITYY MHRKIIDEVS GGANFMSRLI AGILELNWAI DDEECKGLKK LYLLSGRVRN
LIVKHKVRNE AVHRWFGEEE IYGVPKVVTI IKASTLSKSK HCIVCTICEG KDWNGANCPK
CGRQGKPITC GMTLADFEEK HYKKIFIREG CHGEPLREEY KGYVQYTARG QLFLRNLPIL
ATKMKLLMVG NLGAEVGDLE HLGWVLRGPA VCKKITNHEK CHVSIMDKLT AFFGIMPRGT
TPRAPVRFPT ALLKVRRGLE TGWAYTHQGG ISSVDHVTAG KDLLVCDSMG RTRVVCHNNN
KMTDETEYGI KTDSGCPEGA RCYVLNPEAV NISGTKGAMV HLQKTGGEFT CVTASGTPAF
FDLKNLKGWS GLPIFEASSG RVVGRVKVGK NEDSKPTKLM SGIQTVSKNQ TDLADIVKKL
TSMNRGEFKQ ITLATGAGKT TELPRSVIEE IGRHKRVLVL IPLRAAAESV YQYMRVKYPS
ISFNLRIGDM KEGDMATGIT YASYGYFCQL PQPKLRAAMV EYSYIFLDEY HCATPEQLAI
IGKIHRFAEN LRVVAMTATP AGTVTTTGQK HPIEEFIAPE VMKGEDLGTE YLDIAGLKIP
TEEMKGNMLV FVPTRNMAVE TAKKLKAKGY NSGYYYSGEN PENLRVVTSQ SPYVVVATNA
IESGVTLPDL DTVVDTGLKC EKRVRISSKM PFIVTGLKRM AVTIGEQAQR RGRVGRVKPG
RYYRSQETAS GSKDYHYDLL QAQRYGIEDG INVTKSFREM NYDWSLYEED SLMITQLEVL
NNLLISEDLP AAVKNIMART DHPEPIQLAY NSYENQIPVL FPKIKNGEVT DSYENYTYLN
ARKLGEDVPA YVYATEDEDL AVDLLGMDWP DPGNQQVVET GRALKQVTGL STAENALLIA
LFGYVGYQTL SKRHIPMITD IYTLEDHRLE DTTHLQFAPN AIRTDGKDSE LKELAVGDLD
KYVDALVDYS KQGMKFIKVQ AEKVKDSQST KEGLQTIKEY VDKFIKSLIE NKEEIIRYGL
WGAHTALYKS LAARLGHETA FATLVVKWLA FGGETLSAHI KQAAVDLVVY YIINKPSFPG
DTETQQEGRR FVASLFISAL ATYTYKTWNY NNLAKVVEPA LAYLPYATSA LKLFTPTRLE
SVVILSSTIY KTYLSIRKGK SDGLLGTGIS AAMEILNQNP ISVGISVMLG VGAIAAHNAI
ESSEQKRTLL MKVFVKNFLD QAATDELVKE NPEKIIMALF EAVQTIGNPL RLIYHLYGVY
YKGWEAKELA EKTAGRNLFT LIMFEAFELL GMDSEGKMRN LSGNYILDLI FNLHNKLNKG
LKKLVLGWAP APFSCDWTPS DERISLPHNN YLRVETRCPC GYEMKAIKNV AGKLTKVEEK
GPFLCRNRLG RGPPNFKTTK FYDDNLIEVK PVAKLEGQVD LYYKGVTARL DYSNGKALLA
TNKWEVDHAF LTRLVKKHTG IGYKGAYLGD RPDHQDLVDR DCATITKNSV QFLKMKKGCA
FTYDLTISNL VRLIELVHKN NLQEREIPTV TVTTWLAYSF VNEDLGTIKP VLGEKVIPEP
PTELSLQPTL ELITTETAIT ITGEAEVMTT GITPVVEMKE EPQQGSQSTF LKVGLKEGEY
PGPGVNPSHL VEVIDEKDDR PFVLVIGNKG SISNRAKTAK NIRVYKGNNP REIRDLMGQG
RILTVALKEL DPELKELVDY KGTFLNREAL EALSLGKPIK RKTTTAMIKR LIEPEVEEEL
PEWFQVEEPL FLEAKIQADT YHLIGSVDSI KSKAKELGAT DNTKIVKEVG ARTYTMKLSS
WSTQITKRHM SLAPLFEELL LKCPPCSKIS RGHMVSAYQL AQGNWEPLGC GVYMGTIPAR
RLKIHPYEAY LKLKELVEAE QSKVAVKESI IKEHNTWILR KVKHEGNLRT KSMINPGKVS
EQLCREGHKR NIYNKIIGST MASVGIRLEK LPVVRAQTDT TNFHQAIREK IDKPENKQTP
ELHGELMKVF DCLKIPELKE SYDEVPWEQL EAGINRKGAA GFLESKNIGE VLDTEKHIVE
QLIRDLRKGK KIRYYETAIP KNEKRDVSDD WEAGEFVDEK KPRVIQYPDA KVRLAIAKVM
YKWVKQQPVV IPGYEGKTPL FDIFNKVKKE WDSFQDPVAV SFDTKAWDTQ VTSRDLMLIR
DIQKYYFKKN IHKFLDTITE HMVEVPVITS DGEVYIRNGQ RGSGQPDTSA GNSMLNVLTM
IYAFCKSTGI PYRGFSRVAR IHVCGDDGFL ITERGLGLKF SEKGMQILHE AGKPQKITEG
DRMKVAYRFE DIEFCSHTPV PVRWADNTSS YMAGRSTATI LAKMATRLDS SGERGSTAYE
KAVAFSFLLM YSWNPIVRRI CLMVLSQYPE VIPSKHTIYY YQGDPIAAYR EVIGKQLCEL
KRTGFEKLAS LNLSMTTLGI WTKHTSKRLI QDCVEIGKKE GNWLVNADRL ISGKTGKFYI
PSTGVTLLGK HYEEINLKQR AGQPPIEGVD RYKLGPIVNI ILRRLRVMLM AVAGGSR
//
