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Database: UniProt
Entry: Q9QP61_9HEPC
LinkDB: Q9QP61_9HEPC
Original site: Q9QP61_9HEPC 
ID   Q9QP61_9HEPC            Unreviewed;      3010 AA.
AC   Q9QP61;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 161.
DE   RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS   Hepatitis C virus subtype 1b.
OC   Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Flasuviricetes;
OC   Amarillovirales; Flaviviridae; Hepacivirus; Hepacivirus hominis.
OX   NCBI_TaxID=31647 {ECO:0000313|EMBL:AAD50312.1, ECO:0000313|Proteomes:UP000160335};
RN   [1] {ECO:0007829|PDB:2A4G}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1678-1696.
RX   PubMed=16087332; DOI=10.1016/j.bmcl.2005.06.091;
RA   Arasappan A., Njoroge F.G., Chan T.Y., Bennett F., Bogen S.L., Chen K.,
RA   Gu H., Hong L., Jao E., Liu Y.T., Lovey R.G., Parekh T., Pike R.E.,
RA   Pinto P., Santhanam B., Venkatraman S., Vaccaro H., Wang H., Yang X.,
RA   Zhu Z., Mckittrick B., Saksena A.K., Girijavallabhan V., Pichardo J.,
RA   Butkiewicz N., Ingram R., Malcolm B., Prongay A., Yao N., Marten B.,
RA   Madison V., Kemp S., Levy O., Lim-Wilby M., Tamura S., Ganguly A.K.;
RT   "Hepatitis C virus NS3-4A serine protease inhibitors: SAR of P'2 moiety
RT   with improved potency.";
RL   Bioorg. Med. Chem. Lett. 15:4180-4184(2005).
RN   [2] {ECO:0000313|EMBL:AAD50312.1, ECO:0000313|Proteomes:UP000160335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=274933RU {ECO:0000313|EMBL:AAD50312.1};
RX   PubMed=16442623; DOI=10.1016/j.molimm.2005.11.018;
RA   Sominskaya I., Alekseeva E., Skrastina D., Mokhonov V., Starodubova E.,
RA   Jansons J., Levi M., Prilipov A., Kozlovska T., Smirnov V., Pumpens P.,
RA   Isaguliants M.G.;
RT   "Signal sequences modulate the immunogenic performance of human hepatitis C
RT   virus E2 gene.";
RL   Mol. Immunol. 43:1941-1952(2006).
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; AF176573; AAD50312.1; -; Genomic_RNA.
DR   PIR; A61196; A61196.
DR   PIR; PQ0246; PQ0246.
DR   PIR; PS0329; PS0329.
DR   PDB; 2A4G; X-ray; 2.50 A; B/D=1676-1696.
DR   PDBsum; 2A4G; -.
DR   SMR; Q9QP61; -.
DR   MEROPS; S29.001; -.
DR   euHCVdb; AF176573; -.
DR   EvolutionaryTrace; Q9QP61; -.
DR   Proteomes; UP000160335; 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; 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; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:2A4G};
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        718..740
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        752..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..835
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        872..896
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   TRANSMEM        2990..3007
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..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2187..2219
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        2194..2217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2351..2385
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3010 AA;  327072 MW;  9105F69483DD5BBA CRC64;
     MSTNPKPQRK TKRNTNRRPQ DVKFPGGGQI VGGVYLLPRR GPRLGVRATR KTSERSQPRG
     RRQPIPKARH PEGRTWAQPG YPWPLYGNEG LGWAGWLLSP RGSRPSWGPT DPRRRSRNLG
     KVIDTLTCGF ADLMGYIPLV GAPLGGVARA LAHGVRVLED GVNYATGNLP GCSFSIFLLA
     LLSCLTIPAS AYEVRNVSGV YHVTNDCSNS SIVYEAADVI MHTPGCVPCV QDGNTSRCWV
     ALTPTLAARN ASVPVTAIRR HVDLLVGTAA FCSAMYVGDL CGSVFPVSQL FTFSPRRHQT
     VQDCNCSIYP GHISGHRMAW DMMMNWSPTA ALVVSQLLRI PQAIVDMVAG AHWGVLAGLA
     YYSMVGNWAK VMIVLLLFAG VDGTTHTTGG AAARATQGFT SFFSLGPSQK IQLINTNGSW
     HINRTALNCN DSLQTGFLAA LFYTYRFNAS GCPERMASCR PIDKFDQGWG PITYAEPDSS
     DQRPYCWHYA PRPCGIVPAS QVCGPVYCFT PSPVVVGTTD RFGVPTYTWG ENETDVLLLN
     NTRPPLGNWF GCTWMNSTGF TKTCGGPPCN IGGAGNTTLT CPTDCFRKHP EATYTKCGSG
     PWLTPRCLVD YPYRLWHYPC AVNFTIFKVR MYVGGVEHRL NAACNWTRGE RCDLEDRDRS
     ELSPLLLSTT EWQVLPCSFT TLPALSTGLI HLHQNIVDVQ YLYGIGSAVI PFAIKWEYVL
     LLFLLLADAR VCACLWMMLL IAQAEAALEN LVVLNAASVA GAHGILSFLV FFCAAWYIKG
     RLVPGAAYAL YGVWPLLLLL LALPPRAYAM DREMAASCGG AVFVGLVLLT LSPHYKVFLA
     RLIWWSQYFT TRAEALLQVW VPPLNIRGGR DAIILLMCAV HSELIFDITK FLLAILGPLM
     MFQARITRVP YFVRAQGLIR ACMLVRKAAG GHYIQMALMK LAALSGTYVY DHLTPLQDWA
     HAGLRDLAAA VEPVVFSDME TKVITWGADT AACGDIISGL PVSARRGREI LLGPADGLEE
     QGWRLLAPIT AYSQQTRGLL GCIITSLTGR DKNQVEGEVQ VVSTATQSFL ATCVNGVCWT
     VYHGAGTKTL AGPKGPITQM YTNVDQDLVG WQAPPGARSL TPCTCGSSDL YLVTRHADVI
     PVRRRGDSRG SLLSPRPISY LKGSSGGPLL CPSGHAVGIF RAAVCTRGVA KAVDFVPVES
     METTMRSPVF TDNSSPPAVP QTFQVAHLHA PTGSGKSTKV PAAYAAQGYK VLVLNPSVAA
     TLGFGAYMSK AHGVDPNLRT GVRTITTGAP ITYSTYGKFL ADGGCSGGAY DIIICDECHS
     TDSTTILGIG TVLDQAETAG ARLVVLATAT PPGSVTVPHP NIEEIALSNT GEIPFYGKAI
     PIEIIKGGRH LIFCHSKKKC DELAAKLSGL GLNAVAYYRG LDVSVIPTSG NVVVVATDAL
     MTGFTGDFDS VIDCNTCVTQ TVDFSLDPTF TIETTTVPQD AVSRSQRRGR TGRGRRGIYR
     FVTPGERPSG MFDSSVLCEC YDAGCAWYEL TPAETSVRLR AYLNTPGLPV CQDHLEFWES
     VFTGLTHIDA HFLSQTKQAG DNFPYLVAYQ ATVCARAQAP PPSWDQMWKC LIRLKPTLHG
     PTPLLYRLGA VQNETTLTHP ITKYIMACMS ADLEVVTSTW VLVGGVLAAL AAYCLTTGSV
     VIVGRIVLSG KPAIIPDREV LYQEFDEMEE CASHLPYIEQ GMQLAEQFKQ KALGLLQTAT
     KQAEAAAPVV ESKWRALEAF WAKHMWNFIS GVQYLAGLST LPGNPAIASL MAFTASITSP
     LTTQYTLLFN ILGGWVAAQL APPSAASAFV GAGIAGAAVG SIGLGKVLVD ILAGYGAGVA
     GALVAFKVMS GEMPSTEDLV NLLPAILSPG ALVVGVVCAA ILRRHVGPGE GAVQWMNRLI
     AFASRGNHVS PTHYVPESDA AARVTQILSN LTITQLLKRL HQWINEDCST PCSGSWLRDV
     WDWICTVLTD FKTWLRSKLL PRLPGVPFLS CQRGYKGVWR GDGIMQTTCP CGAQIAGHVK
     NGSMRIVGPR TCSNTWHGTF PINAYTTGPC TPSPAPNYSR ALWRVAAEEY VEITRVGDFH
     YVTGMTTDNV KCPCQVPAPE FFTEVDGVRL HRYAPVCKPL LHEDVTFQVG LNQYLVGSQL
     PCEPEPDVAV LTSMLTDPSH ITAETAKRRL ARGSSPSLAS SSASQLSAPS LKATCTTRHD
     SPDADLIEAN LLWRQEMGGN ITRVESENKV VILDSFDPLR AEEDEREVSV PAEILRKTRK
     FPSAMPIWAR PDYNPPLLES WKDPDYVPPV VHGCPLPPTK VPPIPPPRRK RTVVLTESTV
     SSALAELATK TFGSSESSAV DSGTAAASPD QPSDNGDTGS DVESYSSMPP LEGEPGDPDL
     SDGSWSTVSE EASEDVVCCS MSYTWTGALI TPCAAEESQL PINALSNSLL RHRNLVYATT
     SRSASQRQKK VTFDRLQVLD DHYQDVLKEM KAKASTVKAK LLSVEEACKL TPPHSAKSKF
     GYGAKDVRNL SSKAVNHIHS VWKDLLEDTE TPIDTTIMAK NEVFCVQPEK GGRKPARLIV
     FPDLGVRVCE KMALYDVVST LPQAVMGSAY GFQYSPGQRV DFLVNAWKSK KCPMGFSYDT
     RCFDSTVTES DIRVEESIYQ CCDLAPEARQ AIRSLTERLY VGGPLTNSKG QNCGYRRCRA
     SGVLTTSCGN TLTCYLKATA ACRAAKLRDC TLLVNGDDLV VICESAGTQE DAASLRVFTE
     AMTRYSAPPG DLPQPEYDLE LITSRSSNVS VAHDASGKRV YYLTRDPTTP LARAAWEAAR
     HTPVNSWLGN IIMYAPTLWA RMILMTHFFS ILLFQEQLEK ALDCQIYGAY YSIEPLDLPQ
     IIQRLHGLSA FSLHSYSPGE INRVASCLRK LGVPPLRAWR HRARNVRAKL LSQGGRAATC
     GKYLFNWAVR TKLKLTPIPA ASQLDLSGWF VAGYGGGDIY HSLSRARPRW PMLCLLLLFV
     GVGIYLLPNR
//
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