ID T2C5Z3_9HEPC Unreviewed; 3033 AA.
AC T2C5Z3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Hepacivirus hominis.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Hepacivirus.
OX NCBI_TaxID=3052230 {ECO:0000313|EMBL:AGV23517.1, ECO:0000313|Proteomes:UP000107766};
RN [1] {ECO:0000313|EMBL:AGV23517.1, ECO:0000313|Proteomes:UP000107766}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PTR2795 {ECO:0000313|EMBL:AGV23517.1};
RX PubMed=23861126; DOI=10.1002/jmv.23674;
RA Jordier F., Deligny M.-L., Barre R., De Micco P., Cantaloube J.-F.;
RT "Evidence for two phylogenetic clusters within hepatitis C virus (HCV)
RT genotype 2 inferred from analysis of complete coding sequences of 15 HCV
RT strains.";
RL J. Med. Virol. 85:1754-1764(2013).
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: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:ARBA00004482}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004482}. Host lipid droplet
CC {ECO:0000256|ARBA:ARBA00004338}. Host mitochondrion
CC {ECO:0000256|ARBA:ARBA00004181}. 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:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Mitochondrion
CC {ECO:0000256|ARBA:ARBA00004173}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Virion membrane
CC {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004563}.
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DR EMBL; KC197233; AGV23517.1; -; Genomic_RNA.
DR Proteomes; UP000107766; 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:0033650; C:host cell mitochondrion; 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: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:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
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; 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 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 4: Predicted;
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 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 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 entry into host cell {ECO:0000256|ARBA:ARBA00023296};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 174..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 722..743
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 763..782
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 789..808
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 820..839
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 877..897
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1664..1687
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1851..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 903..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..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2193..2218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2351..2432
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 2199..2218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2357..2391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2399..2413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3033 AA; 329567 MW; 594F69D7F7E20620 CRC64;
MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG
RRQPIPKDRR ATGKSWGRPG YPWPLYGNEG LGWAGWLLSP RGSRPSWGPT DPRHRSRNLG
KVIDTLTCGF ADLMGYIPVV GAPVGGVARA LAHGVRVLED GINYATGNLP GCSFSIFLLA
LLSCISIPVS AVQVKNTSVS YMVTNDCSNS SIVWQLQDAV LHVPGCVPCE RKGNESRCWI
PVTPNVAVSQ PGALTRGLRT HIDVIVMSAT LCSALYIGDV CGAVMISAQI FIVTPQFHVF
VQDCNCSVYP GHITGHRMAW DMMMNWSPTA TMILAYLLRI PEVVLGIIAE GHWGVMFGLA
YFSMQGAWAK VIVILLLTAG VEAHTRTVAG SVARTAGSLV GMFTNGPQQR LQLIDTNGSW
HINRTALNCN DSLQTGFLAA LFYANKFNSS GCPERLAACR PLDKFPIGWG ALEYEDNVTN
DEDMRPYCWH YPPKPCGIVP ARSVCGPVYC FTPSPVVVGT TDKFGVPTYK WGENETDVFL
LNSTRPPRGA WFGCTWMNAT GFTKTCGAPP CRIRKNFNAS EDLLCPTDCF RKHPDATYLK
CGAGPWLTPK CLVDYPYRLW HYPCTVNYTI FKIRMYVGGV EHRMNAACNF TRGDRCNLED
RDRSQLSPLL HSTTEWAILP CTFSDLPALS TGLLHLHQNI VDVQYMYGLS PALTSYIVKW
EWVVLLFLLL ADARVCACLW MLLLLGQVEA ALEKLITLHA ASAASSNGLL YFLLFFMAAW
YIKGRVVPLT TYSLLGVWPF TLLLLALPQQ AYALDTAEQG QVGLVLLVVI SVITLTPAYK
IIVCRCLWWL SYMPVMAEAL IQEWVPPLEA RGGRDGIIWA ATMLCPGVVF DVTKWLLAIL
GPGYLLRHVL TTVPYFVRAR ALLRICAMVK HLAGGKYIQM ALIAIGNWTG TYIYDHLSPM
TNWAATGLRD LAVAVEPIVF SPMEKKVIIW GAETAACGDI IHGLPVSARL GREVLLGPAD
EYVSRGWSLL APITAYAQQT RGLLGTIVVS LTGRDKTECA GEVQVLSSVT QSFLGTSISG
VLWTVFHGAG NKTLAGSRGP VTQMYTSAEG DLVGWPSPPG TKSLEPCTCG ASDLYLVTRN
ADVIPARRRG DRRGALLSPR PLSTLKGSSG GPVLCPRGHA VGIFRAAVCS RGVAKSIDFI
PVEALDVVAR SPSFTDNSAP PAVPQTYQVG YLHAPTGSGK STKVPAAYAA QGYKVLVLNP
SVAATLGFGA YMSKAHGINP NIRTGVRTVT TGDSITYSTY GKFLADGGCS GGAYDIIICD
ECHSVDSTTI LGIGTVLDQA ETAGARLVVL ATATPPGSVA TPHPNIEEVA LGHEGEIPFY
GKAIPLANIK GGRHLIFCHS KKKCDELASA LRGMGLNAVA YYRGLDVSVI PTQGDVVVVA
TDALMTGYTG DFDSVVDCNV AVTQVVDFSL DPTFTITTQT VPQDAVSRSQ RRGRTGRGRM
GIYRYVSSGE RPSGMFDSVV LCECYDAGTA WYELTPAEAT VRLRAYFNTP GLPVCQDHLE
FWEAVFTGLT HIDAHFLSQT KQSGENFPYL VAYQATVCAR AKAPPPSWDT MWKCLIRLKP
TLVGPTPLLY RLGAVSNEVT LTHPVTKYIA TCMQADLEVM TSTWVLAGGV LAAVAAYCLA
TGCVVIIGRL CINQRTIVAP DKEVLYEAFD EMEECASRAA LVEEGHRIVE MLKSKIQGLL
QQASRQAQDI QPAVQSTWPK LEQFWAKHMW NFISGIQYLA GLSTLPGNPA VASMMAFSAA
LTSPLSTNTT ILLNIMGGWL ASQIAPPAGA TGFVVSGLVG AAVGSIGLGK ILVDVLAGYG
AGISGALVAF KIMSGEKPSV EDVVNLLPGI LSPGALVVGV ICAAILRRHV GQGEGAVQWM
NRLIAFASRG NHVAPTHYVA ESDASQRVTQ MLSSLTITSL LRRLHQWITE DCPVPCSGSW
LRDLWDWIST ILTDFKNWLS SKLFPKMPGI PFVSCQKGYK GVWAGTGIMT TRCPCGANIS
GNVRLGSMRI TGPKTCMNTW QGTFPINCYT EGQCVPKPAP NFKTAIWRVA ATEYAEVTRH
GSYTYVTGLT TDNLKVPCQL PAPEFFSWVD GVQIHRFAPT PKPLIRDEVS FSVGLNSFVV
GSQLPCEPEP DTEVLASMLT DPSHITAEAA ARRLARGSPP SEASSSASQL SAPSLRATCT
SHGRGPDIDM VDANLFMGGD VTRVESNAKV LILDSLDPMV EEEDEREPSV PSEYLLPKKR
FPPALPPWAR PDYNPPLLEN WKKPDYQPPT VAGCALPPSQ QTPVPPPRRR RAIVLDQSSV
GEALKELAIK SFGQPPPSDD SGHSTGALIT DSANQTIPEE SIDSETDSLS SMPPLEGEPG
DPDLEHETVE RQPPPQEGEA APGSDSGSWS TCSEEDDSVI CCSMSYSWTG ALITPCASEE
EKLPINPLSN SLLRFHNKVY CTTSKSASLR AKKVTFDRVQ LLDSHYDSTL KDIKLAASTV
SARLLTIEEA CALTPPHSAR SKYGFGAKEV RSLAKRAVNH IKSVWKDLLE DSITPIPTTI
MAKNEVFCVD PAKGGKKAAR LIVYPDLGVR VCEKVALYDI TQKLPQAVMG ASYGFQYSPA
QRVEFLLKAW KEKKDPMGFS YDTRCFDSTV TERDIRTEES IYLACSLPEE ARRAIHSLTE
RLYVGGPMLN SKGQSCGYRR CRASGVLTTS MGNTITCYVK ALAACKAAGI VNPTMLVCGD
DLVVISESQG AEEDERNLRV FTEAMTRYSA PPGDPPKAEY DLELITSCSS NVSVALDAHG
RRRYYLTRDP TTPLARAAWE TARHSPVNSW LGNIIQYAPT IWVRMVLMTH FFSILMAQDT
PDQDFNFEMY GAVYSVTPLD LPAIIERLHG LEAFSLHTYS PHELTRVAAA LRKLGAPPLR
AWKSRARAVR ASLIARGGRA GICGRYLFNW AVRTKLKLTP LPEAGRLDLS SWFTIGAGGG
DIYHSVSRAR PRFLLFGLLL LLVGVGIFLL PAR
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