ID F8WTP1_9HEPC Unreviewed; 3033 AA.
AC F8WTP1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 76.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Hepatitis C virus subtype 2b.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Hepacivirus; Hepacivirus hominis.
OX NCBI_TaxID=31650 {ECO:0000313|EMBL:BAK61658.1, ECO:0000313|Proteomes:UP000118683};
RN [1] {ECO:0000313|Proteomes:UP000118683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21935415;
RA Kadokura M., Maekawa S., Sueki R., Miura M., Komase K., Shindo H.,
RA Amemiya F., Uetake T., Inoue T., Sakamoto M., Nakagawa M., Sakamoto N.,
RA Watanabe M., Enomoto N.;
RT "Analysis of the complete open reading frame of genotype 2b hepatitis C
RT virus in association with the response to peginterferon and ribavirin
RT therapy.";
RL PLoS ONE 6:e24514-e24514(2011).
CC -!- FUNCTION: RNA-dependent RNA polymerase that performs primer-template
CC recognition and RNA synthesis during viral replication.
CC {ECO:0000256|ARBA:ARBA00023584}.
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=Hydrolysis of four peptide bonds in the viral precursor
CC polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr
CC in P1 and Ser or Ala in P1'.; EC=3.4.21.98;
CC Evidence={ECO:0000256|ARBA:ARBA00001117};
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endoplasmic reticulum
CC membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004406}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004389}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004115}. Host cell membrane
CC {ECO:0000256|ARBA:ARBA00004165}. Host cytoplasm, host perinuclear
CC region {ECO:0000256|ARBA:ARBA00004407}. Host endoplasmic reticulum
CC membrane {ECO:0000256|ARBA:ARBA00004153}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004153}. Host endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004291}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004291}. Host endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004517}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004517}. Host endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004482}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004482}. Host lipid droplet
CC {ECO:0000256|ARBA:ARBA00004338}. Host mitochondrion membrane
CC {ECO:0000256|ARBA:ARBA00004458}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004458}. Host nucleus
CC {ECO:0000256|ARBA:ARBA00004147}. Lipid droplet
CC {ECO:0000256|ARBA:ARBA00004502}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Mitochondrion membrane
CC {ECO:0000256|ARBA:ARBA00004583}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004583}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Virion membrane
CC {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004563}.
CC -!- SIMILARITY: Belongs to the hepacivirus polyprotein family.
CC {ECO:0000256|ARBA:ARBA00008286}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB661426; BAK61658.1; -; Genomic_RNA.
DR Proteomes; UP000118683; Genome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044186; C:host cell lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0044191; C:host cell mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
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:InterPro.
DR GO; GO:0005216; F:monoatomic ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039563; P:disruption by virus of host JAK-STAT cascade via inhibition of STAT1 activity; IEA:UniProtKB-KW.
DR GO; GO:0039527; P:disruption by virus of host TRAF-mediated signal transduction; IEA:UniProtKB-KW.
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:0039645; P:perturbation by virus of host G1/S transition checkpoint; 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:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0039545; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity; IEA:UniProtKB-KW.
DR GO; GO:0019087; P:transformation of host cell by virus; IEA:InterPro.
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; cd20903; HCV_p7; 1.
DR CDD; cd23202; Hepacivirus_RdRp; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 6.10.250.1610; -; 1.
DR Gene3D; 6.10.250.1750; -; 1.
DR Gene3D; 6.10.250.2920; -; 1.
DR Gene3D; 2.20.25.210; Hepatitis C NS5A, domain 1B; 1.
DR Gene3D; 3.30.160.890; Hepatitis C virus envelope glycoprotein E1, chain C; 1.
DR Gene3D; 2.30.30.710; Hepatitis C virus non-structural protein NS2, C-terminal domain; 1.
DR Gene3D; 1.20.1280.150; Hepatitis C virus non-structural protein NS2, N-terminal domain; 1.
DR Gene3D; 2.20.25.220; Hepatitis C virus NS5A, 1B domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.820.10; RNA Helicase Chain A , domain 3; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR011492; Flavi_DEAD.
DR InterPro; IPR002521; HCV_Core_C.
DR InterPro; IPR044896; HCV_core_chain_A.
DR InterPro; IPR002522; HCV_core_N.
DR InterPro; IPR002519; HCV_Env.
DR InterPro; IPR002531; HCV_NS1.
DR InterPro; IPR002518; HCV_NS2.
DR InterPro; IPR042205; HCV_NS2_C.
DR InterPro; IPR042209; HCV_NS2_N.
DR InterPro; IPR000745; HCV_NS4a.
DR InterPro; IPR001490; HCV_NS4b.
DR InterPro; IPR002868; HCV_NS5a.
DR InterPro; IPR013192; HCV_NS5A_1a.
DR InterPro; IPR013193; HCV_NS5a_1B_dom.
DR InterPro; IPR038568; HCV_NS5A_1B_sf.
DR InterPro; IPR024350; HCV_NS5a_C.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR004109; NS3_Peptidase_S29.
DR InterPro; IPR038170; NS5A_1a_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR002166; RNA_pol_HCV.
DR Pfam; PF07652; Flavi_DEAD; 1.
DR Pfam; PF01543; HCV_capsid; 1.
DR Pfam; PF01542; HCV_core; 1.
DR Pfam; PF01539; HCV_env; 1.
DR Pfam; PF01560; HCV_NS1; 3.
DR Pfam; PF01538; HCV_NS2; 1.
DR Pfam; PF01006; HCV_NS4a; 1.
DR Pfam; PF01001; HCV_NS4b; 1.
DR Pfam; PF01506; HCV_NS5a; 1.
DR Pfam; PF08300; HCV_NS5a_1a; 1.
DR Pfam; PF08301; HCV_NS5a_1b; 1.
DR Pfam; PF12941; HCV_NS5a_C; 1.
DR Pfam; PF02907; Peptidase_S29; 1.
DR Pfam; PF00998; RdRP_3; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51693; HCV_NS2_PRO; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51822; HV_PV_NS3_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Activation of host autophagy by virus {ECO:0000256|ARBA:ARBA00023050};
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW Clathrin-mediated endocytosis of virus by host
KW {ECO:0000256|ARBA:ARBA00022570};
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 G1/S host cell cycle checkpoint dysregulation by virus
KW {ECO:0000256|ARBA:ARBA00023309};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Host endoplasmic reticulum {ECO:0000256|ARBA:ARBA00023184};
KW Host lipid droplet {ECO:0000256|ARBA:ARBA00023190};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Host mitochondrion {ECO:0000256|ARBA:ARBA00023147};
KW Host nucleus {ECO:0000256|ARBA:ARBA00022562};
KW Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Inhibition of host innate immune response by virus
KW {ECO:0000256|ARBA:ARBA00022632};
KW Inhibition of host interferon signaling pathway by virus
KW {ECO:0000256|ARBA:ARBA00022830};
KW Inhibition of host MAVS by virus {ECO:0000256|ARBA:ARBA00022986};
KW Inhibition of host RLR pathway by virus {ECO:0000256|ARBA:ARBA00022482};
KW Inhibition of host STAT1 by virus {ECO:0000256|ARBA:ARBA00022961};
KW Inhibition of host TRAFs by virus {ECO:0000256|ARBA:ARBA00022647};
KW Interferon antiviral system evasion {ECO:0000256|ARBA:ARBA00023258};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Modulation of host cell cycle by virus {ECO:0000256|ARBA:ARBA00022504};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW 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 Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Viral attachment to host cell {ECO:0000256|ARBA:ARBA00022804};
KW Viral envelope protein {ECO:0000256|ARBA:ARBA00022879};
KW Viral immunoevasion {ECO:0000256|ARBA:ARBA00023280};
KW Viral ion channel {ECO:0000256|ARBA:ARBA00023039};
KW Viral nucleoprotein {ECO:0000256|ARBA:ARBA00023086};
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 endocytosis by host {ECO:0000256|ARBA:ARBA00022890};
KW Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 639..659
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 722..744
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 756..782
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 789..807
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 822..843
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 895..917
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1664..1688
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1828..1848
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1855..1874
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1886..1906
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3013..3032
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 905..1030
FT /note="Peptidase C18"
FT /evidence="ECO:0000259|PROSITE:PS51693"
FT DOMAIN 1031..1212
FT /note="Peptidase S29"
FT /evidence="ECO:0000259|PROSITE:PS51822"
FT DOMAIN 1221..1373
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1365..1542
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2656..2774
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2318..2341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2355..2431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2357..2388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3033 AA; 329747 MW; 752EA9DB58DC9059 CRC64;
MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTPERSQPRG
RRQPIPKDRR STGKSWGKPG YPWPLYGNEG CGWAGWLLSP RGSRPTWGPT DPRHRSRNLG
RVIDTITCGF ADLMGYIPVV GAPVGGVARA LAHGVRVLED GINYATGNLP GCSFSIFLLA
LLSCVTVPVS AVEIRNISSS YYATNDCSNN SITWQLTDAV LHLPGCVPCE NDNGTLRCWI
QVTPNVAVKH RGALTHNLRT HVDMIVMAAT VCSALYVGDV CGAVMIVSQA LIVSPERHNF
TQECNCSIYQ GHITGHRMAW DMMLNWSPTL TMILAYVARV PELALEIVFG GHWGVVFGLA
YFSMQGAWAK VIAILLLVAG VDAHTQVTGG QAASFTRGFV GIFSPGPQQN IQLINSNGSW
HINRTALNCN DSLQTGFIAS LFYAKKFNSS GCPERLSSCR RLDDFRIGWG TLEHESHVTN
DEDMRPYCWH YPPKPCGIVS ARTVCGPVYC FTPSPVVVGT TDRQGVPTYS WGENETDVFL
LNSTRPPQGA WFGCTWMNGT GFTKTCGAPP CRIRRDFNNT TPLLHSTTEW AALPCSFSNL
PVLCTGLLHL HQNIVDVHHL YGLSPALTKY IVKWEGVSLL FLLLPHALVC ACLWMLIILG
QGHIRVLNLL HSTTEWAVLP CSFSDLPALS TGLLHLHQNI VDVQYLYGLS PALTRYIVKW
EWVVLLFLLL ADARVCACLW MLIILGQAEA ALEKLIILHS ASAASANGPL WFFIFFTAAW
YLKGRVVPVA TYSVLGLWSF LLLVLALPQQ AYALDAAEQG ELGLVILVII SIFTLTPAYK
ILLSRSVWWL SYMLVLAEAQ IQQWVPPLEV RGGRDGIIWV AVILHPRLVF EVTKWLLAIL
GSAHLLKLSL LRVPYFVRAH ALLRVCTLVR HLAGAKYIQM LLITIGRWTG TYIYDHLSPL
STWAAQGLRD LAVAVEPVVF SPMEKKVIVW GAETVACGDI LHGLPVSARL GREVLLGPAD
SYTSKGWKLL APITAYTQQT RGLLGAIVVS LTGRDKNEQA GHIQVLSSVT QSFLGTSISG
VLWTVYHGAG NKTLAGPKGP VTQMYTSAEG DLVGWPSPPG TKSLDPCTCG AVDLYLVTRN
ADVIPVRRKD DRRGALLSPR PLSTLKGSSG GPVLCARGHA VGLFRAAVCA RGVAKSIDFI
PVESLAIATR TPSFSDNSTP PVVPQTYQVG YLHAPTGSGK STKVPAAYAS QGYKVLVLNP
SVAATLGFGA YMSKAYGINP NIRTGVRTVT TGDPITYSTY GKFIADGGCS AGAYDVIICD
ECHSVDATTI LGIGTVLDQA ETAGAKLVVL ATATPPGTVT TPHSNIEEVA LGHEGEIPFY
GKAIPLAFIK GGRHLIFCHS KKKCDELAAA LRGMGVNAVA YYRGLDVSVI PTQGDVVVVA
TDALMTGYTG DFDSVIDCNV AVTQIVDFSL DPTFTITTQT VPQDAVSRSQ RRGRTGRGRL
GIYRYVSSGE RPSGMFDSVV LCECYDAGAA WYELTPAETT VRLRAYFNTP GLPVCQDHLE
FWEAVFTGLT HIDAHFLSQT KQAGDNFAYL TAYQATVCAR AKAPPPSWDV MWKCLTRLKP
TLTGPTPLLY RLGAVTNEVT LTHPVTKYIA TCMQADLEIL TSTWVLAGGV LAAVAAYCLA
TGCISIIGRI HLNDHVVMTP DKEILYEAFD EMEECASKAA LIEEGHRMAE MLKSKVQGLL
QQATRQAQDI QPAIQSSWPK LEQFWAKHMW NFISGIQYLA GLSTLPGNPA VASMMAFSAA
LTSPLPTSTT ILLNIMGGWL ASQIAPPAGA TGFVVSGLVG AAVGSIGLGK ILVDVLAGYG
AGISGALVTF KIMSGEKPSV EDVVNLLPAI LSPGALVVGV ICAAILRRHV GQGEGAVQWM
NRLIAFASRG NHVAPTHYVA ESDASQRVTQ LLSSLTITSL LRRLHAWITE DCPVPCSGSW
LQDIWDWVCS ILTDFKNWLS SKLLPKMPGL PFISCQKGYR GVWAGTGVMT TRCPCGANIS
GHVRLGTMKI TGPKTCFNLW QGTFPINCYT EGPCVPKPPP NYKTAIWRVA ASEYVEVTQR
GSFSYVTGLT SDNLKVPCQV PAPEFFSWVD GVQIHRFAPI PGPFFRDEVT FTVGLNSFVV
GSQLPCDPEP DTEVLASMLT DPSHITAEAA ATRLARGSPP SQASSSASQL SAPSLKATCT
THKMAYDCDM VDANLFMGGD VTRIESDSKV IVLDSLDSMT EVEDDREPSV PSEYLIARKK
FPPALPPWAR PDYNPPVIEL WKRPGYAPPT VLGCALPPTP QVPVPPPRRR RAKVLTQDNV
EGVLREMADK VLSPLQDHTD SGHSTGADTG GDSIQQPPDE TAASEAGSLS SMPPLEGEPG
DPDLEFEPAG STPPSEGECE VIDSDSKSWS TVSDQEDSVI CCSMSYSWTG ALITPCGPEE
EKLPINPLSN SLMRFHNKVY STTSRSASLR AKKVTFDRVQ VLDTYYDSVL QDVKRAASKV
SARLLSIEEA CALTPPHSAK SRYGFGAKEV RSLSRRAVNH IRSVWEDLLE DQHTPIDTTI
MAKNEVFCID PAKGGKKPAR LIVYPDLGVR VCEKMALYDI AQKLPKAVMG PSYGFQYSPA
ERVDFLLKAW GSKKDPMGFS YDTRCFDSTV TERDIRTEES IYQACSLPQE AKTVIHSLTE
RLYVGGPMTN SKGQSCGYRR CRASGVFTTS MGNTMTCYIK ALAACKAAGI RGPTMLVCGD
DLVVISESQG NEEDERNLRA FTEAMTRYSA PPGDLPRPEY DLEPITSCSS NVSGALDSRG
RRRYFLTRDP TTPITRAAWE TVRHSPVNSW LGNIIQYAPT IWVRMVIMTH FFSILLAQDT
LNQNLNFEMY GAVYSVNPLD LPAIIERLHG LEAFSLHTYS PHELSRVAAT LRKLGAPPLR
AWKSRARAVR ASLIAQGGRA AICGRYLFNW AVKTKLKLTP LPEASRLDLS GWFTVGAGGG
DIFHSVSRAR PRLLLLCLLL LTVGVGIFLL PAR
//