ID W5RM18_9HEPC Unreviewed; 2996 AA.
AC W5RM18;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE Flags: Fragment;
OS Hepacivirus hominis.
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC Amarillovirales; Flaviviridae; Hepacivirus.
OX NCBI_TaxID=3052230 {ECO:0000313|EMBL:AHA15792.1};
RN [1] {ECO:0000313|EMBL:AHA15792.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UMI013 {ECO:0000313|EMBL:AHA15792.1};
RX PubMed=25079603;
RA Donlin M.J., Lomonosova E., Kiss A., Cheng X., Cao F., Curto T.M.,
RA Di Bisceglie A., Tavis J.E.;
RT "HCV genome-wide genetic analyses in context of disease progression and
RT hepatocellular carcinoma.";
RL PLoS ONE 9:E103748-E103748(2014).
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; KC439499; AHA15792.1; -; Genomic_RNA.
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; 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 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 718..739
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 751..778
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 784..803
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 815..836
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 1825..1845
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1851..1870
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1882..1902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 903..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 2633..2751
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 2351..2407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2351..2369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 2996
FT /evidence="ECO:0000313|EMBL:AHA15792.1"
SQ SEQUENCE 2996 AA; 325378 MW; 6644C3AEA8046F72 CRC64;
MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG
RRQPIPKARR PEGRTWAQPG YPWPLYGNEG MGWAGWLLSP RGSRPSWGPT DPRRKSRNLG
KVIDTLTCGF ADLMGYIPLV GAPLGGVARA LAHGVRVVED GVNYATGNLP GCSFSIFLLA
LLSCLTIPAS AYEVHNVSGV YHVTNDCSNA SIVYEAADMI MHTPGCVPCV RENNSSRCWV
ALTPTLAARN ASVPTATIRR HVDLLVGAAA LCSAMYVGDL CGSVFLVSQL FTFSPRQHTT
VQDCNCSIYP GHVSGHRMAW DMMMNWSPTT ALVVSQLLRI PQAVVDMVAG SHWGILAGLA
YYSMAGNWAK VLIVMLLFAG VDGTTYVTGG AIARSTGSLT SLFSTGASQK IQLINTNGSW
HINRTALNCN DTLHTGFLAA LFYVNKFNAS GCPERMAKCR PIDKFKQGWG PITYAEPDSL
DQRPYCWHYA PRPCGIVPAA KVCGPVYCFT PSPVVVGTTD RFGVPTYRWG ENETDVLLLN
NTRPPQGNWF GCTWMNGTGF TKTCGGPPCN IGGVGNDSLI CPTDCFRKHP EATYAKCGSG
PWLTPRCLVD YPYRLWHYPC TVNFTIFKVR MYVGGVEHRL TAACNWTRGE RCDLEDRDRS
ELSPLLLSTT EWQILPCSFT TLPALSTGLI HLHQNIVDVQ YLYGIGSAVV SFAIKWEYIV
LLFLLLADAR VCACLWMMLM IAQAEAALEN LVVLNAASLA GAHGILSFLV FFCAAWYIKG
RLVPGVAYAF YGVWPLLLLL LALPPRAYAM DREMAASCGG AVFVGLALLT LSPHYKVFLA
RLIWWLQYFI TRAEAHLQVW IPPLNIRGGR DAIILLTCVV HPELIFTITK ILLAVLGPLM
VLQAGLTRMP YFVRAQGLIR ACMLVRKAAG GHYVQMAFMK LAALTGTYVY DHLTPLRDWA
HVGLRDLAVA VEPVVFSDME TKIITWGADT AACGDIILGL PVSARRGREI LLGPADSLEG
QGWRLLAPIT AYSQQTRGLL GCIITSLTGR DKNQVEGEVQ VVSTATQSFL ATCVSGVCWT
VYHGAGSKTL AGPKGPIIQM YTNVDQDLVG WPAPPGARSL TPCTCGSSDL YLVTRHADVI
PVRRRGDSRG SLLSPRPISY LKGSSGGPLL CPSGHAVGIF RAAVCTRGVA KAVDFVPVES
METTMRSPVF TDNSSPPAVP QTFQVAHLHA PTGSGKSTKV PAAYAAQGYK VLVLNPSVAA
TLGFGPYMSK AYGTDPNIRT GVRTITTGAP ITYSTYGKFL ADGGCSGGAY DIIICDECHS
TDSTTILGIG TVLDQAETAG ARLVVLATAT PPGSVTVPHP NIEEVALSNT GEIPFYGKAI
PIEAIKGGRH LIFCHSKKKC DELAAKLSGL GLNAVAYYRG LDVSVIPTSG DVVVVATDAL
MTGFTGDFDS VIDCNTCVTQ TVDFSLDPTF TIETTTMPQD AVSRSQRRGR TGRGRTGIYR
FVTPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETSVRLR AYLNTPGLPV CQDHLEFWES
VFTGLTHIDA HFLSQTKQAG ENFPYLTAYQ ATVCARAQAP PPSWDQMWKC LIRLKPTLHG
PTPLLYRLGS VQNEVTLTHP ITKYIMACMS ADLEVVTSTW VLVGGVLAAL AAYCLTTGSV
VIVGRIILSG KPAVIPDREV LYREFDEMEE CASHLPYIEQ GMQLAEQFKQ KALGLLQTAT
KQAEAAAPVV ESRWRALETF WAKHMWNFIS GIQYLAGLST LPGNPAIASL MAFTASITSP
LTTQHTLLFN ILGGWVAAQL APPSAASAFV GAGIAGAAVG SIGLGKVLVD ILAGYGAGVA
GALVAFKVMS GDMPSTEDLV NLLPAILSPG ALVVGVVCAA ILRRHVGPGE GAVQWMNRLI
AFASRGNHVS PTHYVPESDA AARVTQILSS LTITQLLKRL HQWINEDCST PCSGSWLRDV
WDWICTVLTD FKTWLQSKLL PRLPGVPFFS CQRGYKGVWR GDGIMQTTCP CGAQITGHVK
NGSMRIVGPK TCSNTWHGTF PINAYTTGPC TPSPAPNYSR ALWRVAAEEY VEVTRVGDFH
YVTGMTTDNV KCPCQVPAPE FFTEVDGVRL HRYAPACKPL LREEVSFQVG LNQYLVGSQL
PCEPEPDVAV LTSMLTDPSH ITAETAKRRL ARGSPPSLAS SSASQLSAPS LKATCTTRHV
SPDPDLIEAN LLWWQEKGGN ITRVESENKV IILDSFEPLR AEENEGEISV PAEILRKSRK
FPPAMPIWAR PDYNPPLLES WKDPDYVAPT VHGCPLPPAK APPIPPPRRK RTVVLTESTV
SSALAELATK TFGSSESSAA DSGTATAPPD QPSDDGDAGS DVGSYSSMPP LEGEPGDPDL
SDGSWSTVSE EAGEDVVCCS MSYTWTGALI TPCAAEESKL PINALSNSLL RHHNMVYATT
SRSASQRQKK VTFDRLQVLD DHYRDVLKEM KAKASTVKAK LLSIEEACKL TPPHSARSKF
GYGAKDVRNL SSKATRHIRS VWKDLLEDTE TPIDTTIMAK NEVFCVQPEK GGRKPARLIV
YPDLGVRVCE KMALYDVVST LPQAVMGASY GFQYSPGQRV EFLVNAWKSK KSPMGFAYDT
RCFDSTVTES DIRVEESIYQ CCDLAPEARQ AIRSLTERLY VGGPLTNSKG QNCGYRRCRA
SGVLTTSCGN TLTCYLKATA ACRAAKLQDC TMLVCGDDLV VICESAGTQE DAANLRVFTE
AMTRYSAPPG DPPQPEYDLE LITSCSSNVS VAHDASGKRV YYLTRDPTTP LARAAWETAR
HTPVNSWLGN IIMYAPTLWA RMILMTHFFS ILLAQEQLEK ALDCQIYGTC YSIEPLDLPQ
IIQRLHGLSA FSLHSYSPGE INRVASCLRK LGVPPLRTWR HRARSVRAKL LSQGGRAATC
GKYLFNWAVK TKLKLTPIPA ASQLDLSSWF VAGYSGGDIY HSLSRARPRW FMVCLL
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