ID A8DF27_9HEPC Unreviewed; 3011 AA.
AC A8DF27;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 2.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS hepatitis C virus genotype 1a.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Hepacivirus; Hepacivirus hominis.
OX NCBI_TaxID=2847144 {ECO:0000313|EMBL:ABV46076.2, ECO:0000313|Proteomes:UP000103762};
RN [1] {ECO:0000313|EMBL:ABV46076.2, ECO:0000313|Proteomes:UP000103762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HCV-1a/US/BID-V445/2006 {ECO:0000313|EMBL:ABV46076.2};
RX PubMed=19026009; DOI=10.1002/hep.22549;
RA Kuntzen T., Timm J., Berical A., Lennon N., Berlin A.M., Young S.K.,
RA Lee B., Heckerman D., Carlson J., Reyor L.L., Kleyman M., McMahon C.M.,
RA Birch C., Schulze Zur Wiesch J., Ledlie T., Koehrsen M., Kodira C.,
RA Roberts A.D., Lauer G.M., Rosen H.R., Bihl F., Cerny A., Spengler U.,
RA Liu Z., Kim A.Y., Xing Y., Schneidewind A., Madey M.A., Fleckenstein J.F.,
RA Park V.M., Galagan J.E., Nusbaum C., Walker B.D., Lake-Bakaar G.V.,
RA Daar E.S., Jacobson I.M., Gomperts E.D., Edlin B.R., Donfield S.M.,
RA Chung R.T., Talal A.H., Marion T., Birren B.W., Henn M.R., Allen T.M.;
RT "Naturally occurring dominant resistance mutations to hepatitis C virus
RT protease and polymerase inhibitors in treatment-naive patients.";
RL Hepatology 48:1769-1778(2008).
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}.
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DR EMBL; EU155233; ABV46076.2; -; Genomic_RNA.
DR MEROPS; S29.001; -.
DR Proteomes; UP000103762; 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; cd17931; DEXHc_viral_Ns3; 1.
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; HepC_NS3_protease.
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; 1.
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 SMART; SM00490; HELICc; 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 264..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 718..741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 753..778
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 785..802
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 814..831
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 873..901
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1660..1688
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1816..1840
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1847..1870
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1882..1902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2991..3008
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 899..1026
FT /note="Peptidase C18"
FT /evidence="ECO:0000259|PROSITE:PS51693"
FT DOMAIN 1027..1208
FT /note="Peptidase S29"
FT /evidence="ECO:0000259|PROSITE:PS51822"
FT DOMAIN 1217..1369
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1361..1538
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 2634..2752
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2188..2220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2313..2334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2352..2409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2195..2220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2313..2329
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2352..2373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3011 AA; 327527 MW; B973272DEFA23674 CRC64;
MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG
RRQPIPKARQ PEGRTWAQPG YPWPLYGNEG CGWAGWLLSP RGSRPSWGPT DPRRRSRNLG
KVIDTLTCGF ADLMGYIPLV GAPLGGAARA LAHGVRVLED GVNYATGNLP GCSFSIFLLA
LLSCLTVPAS AYQVRNSSGL YHVTNDCPNS SIVYETADTI LHSPGCVPCV REGNASKCWV
PVAPTVATRD GKLPTTQLRR HIDLLVGSAT LCSALYVGDL CGSVFLVGQL FTFSPRRHWT
TQDCNCSIYP GHITGHRMAW DMMMNWSPTA ALVVAQLLRV PQAILDMIAG AHWGVLAGIA
YFSMVGNWAK VLIVLLLFAG VDATTYVTGG AAASATSAFA GFFTQGPKQN IQLVNTNGSW
HINRTALNCN ASLDTGWVAG LIYYHRFNSS GCPERMASCR PLADFDQGWG PISYANGSGP
EHRPYCWHYP PKPCGIVPAQ TVCGPVYCFT PSPVVVGTTD KLGVPTYNWG SNDTDVFVLN
NTRPPLGNWF GCTWMNSSGY TKVCGAPPCV IGGVGNNTLH CPTDCFRKHP EATYSRCGSG
PWVTPRCLVH YPYRLWHYPC TINYTLFKVR MYVGGVEHRL EVACNWTRGE RCDLDDRDRS
ELSPLLLSTT QWQVLPCSFT TLPALTTGLI HLHQNIVDVQ YLYGVGSSIV SWAIKWEYVI
LLFLLLADAR ICSCLWMMLL ISQAEAALEN LVLLNVASLA GTHGLASFLV FFCFAWYLKG
RWVPGVAYAF YGMWPFLLLL LALPQRAYAL DTEMAASCGG VVLVGLMVLT LSPHYKRYIS
WCFWWLQYFL TRTEAQLHEW IPPLNVRGGR DAVILLMCVV HPALVFDITK LLLAIFGPLW
ILQASLLKVP YFVRVQGLLR ICALARKIAG GHYVQMAIIK VGALTGTYIY NHLTPLRDWA
HNGLRDLAVA VEPVVFSQME TKLITWGADT AACGDIIDGL PVSARRGREI LLGPADGMDS
KGWRLLAPIT AYAQQTRGLL GCIITSLTGR DKNQVEGEVQ IVSTAAQTFL ATCINGVCWT
VYHGAGTRTI ASPKGPVIQM YTNVDQDLVG WPAPQGARSL TPCTCGSSDL YLVTRHADVI
PVRRRGDSRG SLLSPRPISY LKGSSGGPLL CPAGHAVGIF RAAVCTRGVA KAVDFIPVES
LETTMRSPVF TDNSSPPAVP QSFQVAHLHA PTGSGKSTKV PAAYAAQGYK VLVLNPSVAA
TLGFGAYMSK AHGIDPNIRT GVRTITTGSP ITYSTYGKFL ADGGCSGGAY DIIICDECHS
TDATSILGIG TVLDQAETAG ARLVVLATAT PPGSVTVPHP NIEEVALSTT GEIPFYGKAI
PLEAIKGGRH LIFCHSKKKC DELAAKLVAL GVNAVAYYRG LDVSVIPTSG DVVVVATDAL
MTGYTGDFDS VIDCNTCVTQ TVDFSLDPTF TIETTTLPQD AVSRTQRRGR TGRGKPGIYR
FVAPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETTVRLR AYMNTPGLPV CQDHLEFWEG
VFTGLTHIDA HFLSQTKQSG ENLPYLVAYQ ATVCARAQAP PPSWDQMWKC LIRLKPTLHG
PTPLLYRLGA VQNEVTLTHP VTKYIMTCMS ADLEVVTSTW VLVGGVLAAL AAYCLSTGCV
VIVGRIVLSG KPAVIPDREV LYREFDEMEE CSQHLPYIEQ GMMLAEQFKQ KALGLLQTAS
HQAEVIAPAV QTNWQKLEAF WAKHMWNFIS GIQYLAGLST LPGNPAIASL MAFTAAVTSP
LTTSQTLLFN ILGGWVAAQL AAPGAATAFV GAGLAGAAIG SVGLGKVLVD ILAGYGAGVA
GALVAFKIMS GEVPSTEDLV NLLPAILSPG ALVVGVVCAA ILRRHVGPGE GAVQWMNRLI
AFASRGNHVS PTHYVPESDA AARVTAILSS LTVTQLLRRL HQWISSECTT PCSDSWLRDI
WDWICEVLSD FKTWLKAKLM PQLPGIPFVS CQRGYRGVWR GDGIMHTRCH CGAEITGHVK
NGTMRIVGPK TCRNMWSGTF PINAYTTGPS TPLPAPNYTF ALWRVSAEEY VEVRRVGDFH
YITGMTTDNL KCPCQVPSPE FFTELDGVRL HRFAPPCKPL LRDEVSFSVG LHSYPVGSQL
PCEPEPDVAV LTSMLTDPSH ITAEAARRRL ARGSPPSEAS SSASQLSAPS LKATCTTNHD
SPDAELISAN LLWRQEMGGN ITRVESENKV VVLDSFDPLV AEEDEREVSV EAEILRKSRR
FTPALPIWAR PDYNPPLLET WRKPDYEPPV VHGCPLPPPR SPPVPPPRKK RTVVLTESTV
SDALAELATK SFGSSSTSGI TGDNTTESSE PAPSACPPDS DVESYSSMPP LEGEPGDPDL
SDGSWSTVSS GADTEDVVCC SMSYTWTGAL ITPCAAEEQK LPINALSNSL LRHHNLVYST
TSRSACQRQK KVTFDRLQVL DSHYQDVLKE VKAAASKVKA SLLSVEEACS LTPPHSARSK
FGYGAKDVRC HARKAVNHIN SVWKDLLEDS VTPIDTTIMA KNEVFCVQPE KGGRKPARLI
VFPDLGVRVC EKMALYDVVK KLPLAVMGSS YGFQYSPGQR VEFLVQAWKS KKTPMGFSYD
TRCFDSTVTE SDIRTEEAIY QCCDLDPQAR VAIKSLTERL YVGGPLTNSR GENCGYRRCR
ASGVLTTSCG NTLTCYIKAQ AACRAAGLRD CTMLVCGDDL VVICESQGVQ EDAASLRAFT
EAMTRYSAPP GDPPQPEYDL ELITSCSSNV SVAHDGAGKR VYYLTRDPTT PLARAAWETA
RHTPVNSWLG NIIMFAPTLW ARMILMTHFF SVLIARDQLE QALDCEIYGA CYSIEPLDLP
PIIQRLHGLS AFSLHSYSPG EINRVAACLR KLGVPPLRAW RHRARSVRAK LLSRGGRAAI
CGRYLFNWAV RTKLKLTPIA AASQLDLSGW FTAGYSGGDI YHSVSRARPR WIWFCLLLLT
AGVGIYLLPN R
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