ID X2FTB9_9FLAV Unreviewed; 3897 AA.
AC X2FTB9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 57.
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:AHN05530.1, ECO:0000313|Proteomes:UP000142864};
RN [1] {ECO:0000313|EMBL:AHN05530.1, ECO:0000313|Proteomes:UP000142864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=108 {ECO:0000313|EMBL:AHN05530.1};
RX PubMed=24708266; DOI=10.1186/1297-9716-45-38;
RA Passler T., Riddell K.P., Edmondson M.A., Chamorro M.F., Neill J.D.,
RA Brodersen B.W., Walz H.L., Galik P.K., Zhang Y., Walz P.H.;
RT "Experimental infection of pregnant goats with bovine viral diarrhea virus
RT (BVDV) 1 or 2.";
RL Vet. Res. 45:38-38(2014).
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; KF835701; AHN05530.1; -; Genomic_RNA.
DR Proteomes; UP000142864; 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 656..673
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
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 1144..1162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1183..1206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1212..1229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1250..1269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1275..1299
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 169..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..206
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; 438195 MW; B7305F8786DC7D1C CRC64;
MELFSNELLY KTYKQKPAGV VEPVYDVNGR PLFGEGSDLH PQSTLKLPHQ RGSANILTNA
RSLPRKGDCR RGNVNGAVSG IYIKPGPIYY QDYMGPVYHR APLELCREAS MCETTRRVGR
VTGSDGKLYH IYICIDGCIL LKRATRNQPE VLKWVYNRLN CPLWVTSCSD EGSKGATSKK
QPKPDRIEKG KMKIAPKETE KDCKTRPPDA TIVVEGVKYQ VKKKGKVRGK NTQDGLYHNK
NKPPESRKKL EKALLAWAIL AAVLLQLVTG ENITQWNLMD NGTKGIQQAM FLRGVNRSLH
GIWPEKICTG VPTHLATDYE LKEIVGMMDA SERTNYTCCR LQRHEWNKHG WCNWFHIEPW
IWLMNKTQNN LTEGQPLREC AVTCRYDKEA ELNIVTQARD RPTTLTGCKK GKNFSFAGVV
LDGPCNFKVS VEDVLFKEHD CGNMLQETAI QLLDGATNTI EGARVGTAKL TTWLGKQLGI
LGKKLENKSK AWFGAHAASP YCGVERKVGY VWYTKNCTPA CLPRNTKIIG PGKFDTNAED
GKILHEMGGH LSEFALLSLV VLSDFAPETA SVIYLVLHFA IPQSHVDVDT CDKNQLNLTV
ATTVAEVIPG TVWNLGKYVC IRPDWWPYET TTVFVLEEAG QVIKLGLRAI RDLTRIWNAA
TTTAFLIFLV KALRGQLIQG LLWLMLITGA QGFPECKEGF QYAISKDRKM GLLGPESLTT
TWHLPTKKLV DSMVQVWCEG KDLKILKTCT KEERYLVAVH ERALPTSAEF MQISDGTIGP
DVIDMPDDFE FGLCPCDSKP VIKGKFNASL LNGPAFQMVC PQGWTGRIEC TLANQDTLDT
TVVRTYRRTT PFQRRKWCTY EKIIGEDIHE CVLGGNWTCI TGDHSRLKDG PIKKCKWCGY
DFVNSEGLPH YPIGKCMHIN ESGYRYVDDT SCDRGGVAIV PTGTVKCRIG NVTVQVIATN
NDLGPMPCSP AEVIASEGPV EKTACTFNYS KTLPNKYYEP RDRYFQQYML KGEWQYWFDL
DSVDHHKDYF SEFIIIAVVA LLGGKYVLWL LITYTILSEQ MAMGAGVNTE EIVMIGNLLT
HSDIEVVVYF LLLYLIVKEE LVRKWIILVY HILVANPMKT IGVILLMLGG VVKASRISAD
DQSAMDPCFL LVTGLVAVLM IARREPATLP LIVALLAIRT SGFLLPTSID ITVAVVLIVL
LLASYVTDYF RYKKWLQFSF SLIAGIFIIR SLKHINQMEV PEISMPSWRP LALVIFYIIS
TAITTNWDID LAGFLLQWAP AVIMMATMWA DFLTLIIVLP SYELSKLYFL KNVRTDVEKN
WLGKVKYRQI SSVYDICDSE EAVYLFPSRH KSGSRPDFIL PFLKAVLISC ISSQWQVVYI
SYLILEITYY MHRKIIDEVS GGANFLSRLI AAIIELNWAI DDEECKGLKK LYLLSGRVKN
LIVKHKVRNE AVHRWFGEEE IYGAPKVITI IKASTLSKNR HCIICTICEG KDWNGANCPK
CGRQGKPITC GMTLADFEEK HYKKIFIREG CHDGPFREEY KGYIQYTARG QLFLRNLPIL
ATKMKLLMVG NLGAEIGDLE HLGWVLRGPA VCKKITNHEK CHVNIMDKLT AFFGIMPRGT
TPRAPVRFPT ALLKVRRGLE TGWAYTHQGG ISSVDHVTAG KDLLVCDSMG RTRVVCHSNN
KMTDETEYGI KTDSGCPEGA RCYVLNPEAV NISGTKGAMV HLQKTGGEFT CVTASGTPAF
FDLKNLKGWS GLPIFEASSG RVVGRVKVGK NEDSKPTKLM SGIQTVSKNQ TDLVDIVKKL
ASMNRGEFKQ ITLATGAGKT TELPRSVIEE IGRHKRVLVL IPLRAAAESV YQYMRVKYPS
ISFNLRIGDM KEGDMATGIT YASYGYFCQL PQPKLRAAMV EYSYIFLDEY HCATPEQLAI
IGKIHRFAEN LRVVAMTATP AGTVTTTGQK HPIEEFIAPE VMKGEDLGSE 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 KEGLHTIKEY VDKFIQSLTE NKEEIIRYGL
WGAHTALYKS LAARLGHETA FATLVVKWLA FGGETVSAHI KQAAVDLVVY YIINKPSFPG
DTETQQEGRR FVASLFISAL ATYTYKTWNY NNLQRVVEPA LAYLPYATSA LKLFAPTRLE
SVVILSSTIY KTYLSIRKGK SDGLLGTGIS AAMEILNQNP ISVGISVMLG VGAIAAHNAI
ESSEQKRTLL MKVFVKNFLD QAATDELVKE NPEKIIMALF EAVQTIGNPL RLIYHLYGVY
YKGWEAKELA EKTAGRNLFT LIMFEAFELL GMDSEGKIRN LSGNYILDLI FNLHNKLNKG
IKKLVLGWAP APFSCDWTPS DERISLPHNN YLRVETRCPC GYEMKAIKNV AGKLTKVEEK
GPFLCRNRLG RGPPNFKVTK FYDDNLIEVK PVARLEGQVD LYYKGVTARL DYNNGKVLLA
TNKWEVDHAF LTRLVKKHTG IGFKGAYLGD RPDHQDLVDR DCATITKNSV QFLKMKKGCA
FTYDLTISNL VRLIELVHKN NLQEREIPTV TVTTWLAYSF VNEDLGTIKP VLGEKVIPEP
PTELSLQPTV GLVTTETAIT ITGEAELMTT GITPVVEMKE ELQLDHQSTT LKVGLKEGEY
PGPGVNPNHL VEVIDEKDDR PFVLIIGNKG STSNRARTAK NIRLYKGNNP REIRDLMSQG
RILTVALKEL DPELKELVDY KGTFLNREAL EALSLGKPIK RKTTTAMIRR LIEPEVEEEL
PDWFQAEEPL FLEAKIQADL YHLIGSVDSI KSKAKELGAT DNTKIVKEVG ARTYTMKLSS
WSTQVTKKQM SLAPLFEELL LKCPPCSKIS KGHMVSAYQL AQGNWEPLGC GVYMGTIPAR
RLKIHPYEAY LKLKELVEVE LSRTTVKESI IREHNTWILR KVRHEGNLRT KSMINPGKIS
DQLCRDGHKR NIYNKIIGST MASAGIRLEK LPVVRAQTDT TSFHQAIREK IDKPENKQTP
ELHEELMKVF DCLKIPELKE SYDEVSWEQL EAGINRKGAA GYLESKNIGE VLDTEKHIVE
QLIKDLRKGK KIRYYETASP KNEKRDVSDD WEAGEFVDEK KPRVIQYPDA KVRLAIAKVM
YKWVKQKPVV IPGYEGKTPL FDIFNKVKKE WDSFQDPVAV SFDTKAWDTQ VTSRDLMLIK
DIQKYYFKRS THKFLDTITE HMVEVPVITA DGEVYIRSGQ RGSGQPDTSA GNSMLNVLTM
IYAFCKSTGI PYRGFSRVAR IHVCGDDGFL ITERGLGLKF SEKGMQILHE AGKPQKITEG
DKMKVAYRFE DIEFCSHTPV PVRWADNTSS YMAGRSTATI LAKMATRLDS SGERGSTAYE
KAVAFSFLLM YSWNPVVRRI CLLVLSQFPE ISPSKNTIYY YQGDPIAAYR EVIGKQLCEL
KRTGFEKLAS LNLSMTTLGI WTKHTSKRLI QDCVEVGKRE GNWLVNADRL IAGKTGKFYI
PSTGVTLLGK HYEEINLKQK ATQPPIEGVD RYKLGPIVNV ILRRLRVMLM TVASGSW
//