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Database: UniProt
Entry: F8WTP1_9HEPC
LinkDB: F8WTP1_9HEPC
Original site: F8WTP1_9HEPC 
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}.
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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
//
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