POLG_HKV1
ID POLG_HKV1 Reviewed; 2370 AA.
AC C6KEF6;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Leader protein;
DE Short=L;
DE Contains:
DE RecName: Full=Capsid protein VP0;
DE Contains:
DE RecName: Full=Capsid protein VP3;
DE AltName: Full=P1C;
DE AltName: Full=Virion protein 3;
DE Contains:
DE RecName: Full=Capsid protein VP1;
DE AltName: Full=P1D;
DE AltName: Full=Virion protein 1;
DE Contains:
DE RecName: Full=Protein 2A;
DE Short=P2A;
DE Contains:
DE RecName: Full=Protein 2B;
DE Short=P2B;
DE Contains:
DE RecName: Full=Protein 2C;
DE Short=P2C;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:P03300};
DE Contains:
DE RecName: Full=Protein 3A;
DE Short=P3A;
DE Contains:
DE RecName: Full=VPg;
DE Short=P3B;
DE AltName: Full=Protein 3B;
DE Contains:
DE RecName: Full=Protein 3CD;
DE EC=3.4.22.28;
DE Contains:
DE RecName: Full=Protease 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE EC=3.4.22.28 {ECO:0000255|PROSITE-ProRule:PRU01222};
DE AltName: Full=Picornain 3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE Short=P3C {ECO:0000255|PROSITE-ProRule:PRU01222};
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE Short=RdRp;
DE EC=2.7.7.48 {ECO:0000255|PROSITE-ProRule:PRU00539};
DE AltName: Full=3D polymerase;
DE Short=3Dpol;
DE AltName: Full=Protein 3D;
DE Short=3D;
OS Human klassevirus 1 (HKV-1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Picornaviridae; Salivirus.
OX NCBI_TaxID=655603;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=02394-01 {ECO:0000312|EMBL:ACS91540.1};
RX PubMed=19538752; DOI=10.1186/1743-422x-6-82;
RA Greninger A.L., Runckel C., Chiu C.Y., Haggerty T., Parsonnet J., Ganem D.,
RA DeRisi J.L.;
RT "The complete genome of klassevirus - a novel picornavirus in pediatric
RT stool.";
RL Virol. J. 6:82-82(2009).
RN [2]
RP MYRISTOYLATION AT GLY-1597.
RX PubMed=22258260; DOI=10.1128/jvi.06778-11;
RA Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L., Derisi J.L.;
RT "The 3A protein from multiple picornaviruses utilizes the golgi adaptor
RT protein ACBD3 to recruit PI4KIIIbeta.";
RL J. Virol. 86:3605-3616(2012).
RN [3]
RP INTERACTION WITH HOST ACBD3.
RX PubMed=23572552; DOI=10.1128/mbio.00098-13;
RA Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L., DeRisi J.L.;
RT "ACBD3 interaction with TBC1 domain 22 protein is differentially affected
RT by enteroviral and kobuviral 3A protein binding.";
RL MBio 4:E00098-E00098(2013).
CC -!- FUNCTION: [Leader protein]: Required for viral RNA replication and
CC viral RNA encapsidation (By similarity). Does not have any proteolytic
CC activity (By similarity). {ECO:0000250|UniProtKB:O91464}.
CC -!- FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP0 and VP3 (By similarity). Together
CC they form an icosahedral capsid composed of 60 copies of each VP0, VP1,
CC and VP3 (By similarity). All the three latter proteins contain a beta-
CC sheet structure called beta-barrel jelly roll (By similarity).
CC {ECO:0000250|UniProtKB:O91464}.
CC -!- FUNCTION: [Capsid protein VP0]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP1 and VP3 (By similarity). Together
CC they form an icosahedral capsid composed of 60 copies of each VP0, VP1,
CC and VP3 (By similarity). All the three latter proteins contain a beta-
CC sheet structure called beta-barrel jelly roll (By similarity).
CC {ECO:0000250|UniProtKB:O91464}.
CC -!- FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo
CC T=3 symmetry with capsid proteins VP0 and VP1 (By similarity). Together
CC they form an icosahedral capsid composed of 60 copies of each VP0, VP1,
CC and VP3 (By similarity). All the three latter proteins contain a beta-
CC sheet structure called beta-barrel jelly roll (By similarity).
CC {ECO:0000250|UniProtKB:O91464}.
CC -!- FUNCTION: [Protein 2A]: Required for viral RNA replication (By
CC similarity). Does not have any proteolytic activity (By similarity).
CC {ECO:0000250|UniProtKB:O91464}.
CC -!- FUNCTION: [Protein 2B]: Affects membrane integrity and causes an
CC increase in membrane permeability. {ECO:0000250}.
CC -!- FUNCTION: [Protein 2C]: Induces and associates with structural
CC rearrangements of intracellular membranes. Displays RNA-binding,
CC nucleotide binding and NTPase activities. May play a role in virion
CC morphogenesis and viral RNA encapsidation by interacting with the
CC capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.
CC -!- FUNCTION: [Protein 3A]: Serves as membrane anchor via its hydrophobic
CC domain. Plays an essential role in viral RNA replication by recruiting
CC PI4KB at the viral replication sites, thereby allowing the formation of
CC rearranged membranous structures where viral replication takes place
CC (By similarity). {ECO:0000250|UniProtKB:O91464}.
CC -!- FUNCTION: [VPg]: Forms a primer, VPg-pU, which is utilized by the
CC polymerase for the initiation of RNA chains.
CC {ECO:0000250|UniProtKB:P03304}.
CC -!- FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral
CC proteins from the precursor polyprotein (By similarity). In addition to
CC its proteolytic activity, it binds to viral RNA, and thus influences
CC viral genome replication. RNA and substrate cooperatively bind to the
CC protease (By similarity). {ECO:0000250|UniProtKB:P03304,
CC ECO:0000250|UniProtKB:P12296}.
CC -!- FUNCTION: [RNA-directed RNA polymerase]: Replicates the genomic and
CC antigenomic RNAs by recognizing replications specific signals (By
CC similarity). Performs VPg uridylylation (By similarity).
CC {ECO:0000250|UniProtKB:P12296}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus
CC polyprotein. In other picornavirus reactions Glu may be substituted
CC for Gln, and Ser or Thr for Gly.; EC=3.4.22.28;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01222};
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:0000250|UniProtKB:P03300};
CC -!- SUBUNIT: [Capsid protein VP0]: Interacts with capsid protein VP1 (By
CC similarity). Interacts with capsid protein VP3 (By similarity).
CC {ECO:0000250|UniProtKB:O91464}.
CC -!- SUBUNIT: [Capsid protein VP1]: Interacts with capsid protein VP0 (By
CC similarity). Interacts with capsid protein VP3 (By similarity).
CC {ECO:0000250|UniProtKB:O91464}.
CC -!- SUBUNIT: [Capsid protein VP3]: Interacts with capsid protein VP0 (By
CC similarity). Interacts with capsid protein VP1 (By similarity).
CC {ECO:0000250|UniProtKB:O91464}.
CC -!- SUBUNIT: [Protein 2A]: Homodimer. Interacts with protein 2B (By
CC similarity). Interacts with protein 2C (By similarity).
CC {ECO:0000250|UniProtKB:O91464}.
CC -!- SUBUNIT: [Protein 2B]: Homodimer. Interacts with host ABCD3. Interacts
CC with protein 2A (By similarity). Interacts with host ACBD3 (By
CC similarity). {ECO:0000250|UniProtKB:O91464}.
CC -!- SUBUNIT: [Protein 2C]: Homodimer. Interacts with host ABCD3 (By
CC similarity). Interacts with protein 2A (By similarity). Interacts with
CC protein 3A (By similarity). Interacts with protein 3C (By similarity).
CC Interacts with host ACBD3 (By similarity).
CC {ECO:0000250|UniProtKB:O91464}.
CC -!- SUBUNIT: [Protein 3A]: Homodimer (By similarity). Interacts with host
CC ABCD3 (via GOLD domain) and PI4KB; these interactions allow the
CC formation of a viral protein/ACBD3/PI4KB complex in order to synthesize
CC PI4P at the viral RNA replication sites (Probable). Interacts with
CC protein 2C (By similarity). Interacts with protein 3C (By similarity).
CC Protein 3C: Interacts with protein 2A (By similarity). Protein 3C:
CC Interacts with protein 2C (By similarity).
CC {ECO:0000250|UniProtKB:O91464, ECO:0000305|PubMed:23572552}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion
CC {ECO:0000250|UniProtKB:O91464}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P12296}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion
CC {ECO:0000250|UniProtKB:O91464}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P12296}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion
CC {ECO:0000250|UniProtKB:O91464}. Host cytoplasm
CC {ECO:0000250|UniProtKB:P12296}.
CC -!- SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P03304}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P03304}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P03304}. Note=Probably localizes to the surface
CC of intracellular membrane vesicles that are induced after virus
CC infection as the site for viral RNA replication. These vesicles are
CC probably autophagosome-like vesicles. {ECO:0000250|UniProtKB:P03304}.
CC -!- SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P03304}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P03304}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P03304}. Note=Probably localizes to the surface
CC of intracellular membrane vesicles that are induced after virus
CC infection as the site for viral RNA replication. These vesicles are
CC probably autophagosome-like vesicles. {ECO:0000250|UniProtKB:P03304}.
CC -!- SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P03304}; Single-pass membrane protein
CC {ECO:0000255}. Host Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:O91464}; Single-pass membrane protein
CC {ECO:0000255}. Note=Probably localizes to intracellular membrane
CC vesicles that are induced after virus infection as the site for viral
CC RNA replication. {ECO:0000250|UniProtKB:P03304}.
CC -!- SUBCELLULAR LOCATION: [VPg]: Virion {ECO:0000250|UniProtKB:P03304}.
CC -!- SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm
CC {ECO:0000250|UniProtKB:P03304}.
CC -!- SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host cytoplasmic
CC vesicle membrane {ECO:0000250|UniProtKB:P03304}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P03304}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P03304}. Note=Probably localizes to the surface
CC of intracellular membrane vesicles that are induced after virus
CC infection as the site for viral RNA replication. These vesicles are
CC probably autophagosome-like vesicles. {ECO:0000250|UniProtKB:P03304}.
CC -!- PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral
CC protease in vivo yield a variety of precursors and mature proteins (By
CC similarity). The leader protein-VP0 junction is cleaved by 3C
CC proteinase (By similarity). The VP1/2A junction is cleaved by the
CC protein 3CD in association with protein 2A (By similarity).
CC {ECO:0000250|UniProtKB:O91464, ECO:0000250|UniProtKB:P03300}.
CC -!- PTM: [VPg]: Uridylylated by the polymerase and is covalently linked to
CC the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-
CC peptide primer for the polymerase. {ECO:0000250|UniProtKB:P12296}.
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DR EMBL; GQ184145; ACS91540.1; -; Genomic_RNA.
DR RefSeq; YP_003065643.1; NC_012986.1.
DR SMR; C6KEF6; -.
DR IntAct; C6KEF6; 1.
DR iPTMnet; C6KEF6; -.
DR GeneID; 8187145; -.
DR KEGG; vg:8187145; -.
DR Proteomes; UP000126165; Genome.
DR GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
DR GO; GO:0039618; C:T=pseudo3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
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-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0039707; P:pore formation by virus in membrane of host cell; 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:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
DR GO; GO:0039522; P:suppression by virus of host mRNA export from nucleus; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; 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 CDD; cd00205; rhv_like; 3.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.60.120.20; -; 4.
DR Gene3D; 3.30.70.270; -; 2.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001676; Picornavirus_capsid.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR033703; Rhv-like.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00073; Rhv; 2.
DR Pfam; PF00910; RNA_helicase; 1.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Capsid protein; Covalent protein-RNA linkage;
KW Eukaryotic host gene expression shutoff by virus;
KW Eukaryotic host translation shutoff by virus; Helicase; Host cytoplasm;
KW Host cytoplasmic vesicle; Host gene expression shutoff by virus;
KW Host Golgi apparatus; Host membrane; Host mRNA suppression by virus;
KW Host-virus interaction; Hydrolase;
KW Inhibition of host mRNA nuclear export by virus; Ion channel;
KW Ion transport; Lipoprotein; Membrane; Myristate; Nucleotide-binding;
KW Nucleotidyltransferase; Phosphoprotein; Protease; RNA-binding;
KW RNA-directed RNA polymerase; T=pseudo3 icosahedral capsid protein;
KW Thiol protease; Transferase; Transmembrane; Transmembrane helix; Transport;
KW Viral attachment to host cell; Viral ion channel; Viral RNA replication;
KW Virion; Virus entry into host cell.
FT CHAIN 1..2370
FT /note="Genome polyprotein"
FT /id="PRO_0000448032"
FT CHAIN 1..111
FT /note="Leader protein"
FT /id="PRO_0000448033"
FT CHAIN 112..479
FT /note="Capsid protein VP0"
FT /id="PRO_0000448034"
FT CHAIN 480..702
FT /note="Capsid protein VP3"
FT /id="PRO_0000448035"
FT CHAIN 703..952
FT /note="Capsid protein VP1"
FT /id="PRO_0000448036"
FT CHAIN 953..1097
FT /note="Protein 2A"
FT /id="PRO_0000448037"
FT CHAIN 1098..1250
FT /note="Protein 2B"
FT /id="PRO_0000448038"
FT CHAIN 1251..1596
FT /note="Protein 2C"
FT /id="PRO_0000448039"
FT CHAIN 1597..1673
FT /note="Protein 3A"
FT /id="PRO_0000448040"
FT CHAIN 1674..1702
FT /note="VPg"
FT /id="PRO_0000448041"
FT CHAIN 1703..2362
FT /note="Protein 3CD"
FT /id="PRO_0000448042"
FT CHAIN 1703..1897
FT /note="Protease 3C"
FT /id="PRO_0000448043"
FT CHAIN 1898..2362
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000448044"
FT TRANSMEM 1646..1666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1358..1522
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1697..1886
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 2122..2239
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 140..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1674..1696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2007..2026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1745
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1776
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1849
FT /note="For protease 3C activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 2128
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT ACT_SITE 2225
FT /note="For RdRp activity"
FT /evidence="ECO:0000250|UniProtKB:P12296"
FT BINDING 1384..1391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 111..112
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000305"
FT SITE 479..480
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 702..703
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 952..953
FT /note="Cleavage; by protein 3CD"
FT /evidence="ECO:0000250|UniProtKB:O91464"
FT SITE 1097..1098
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1250..1251
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1596..1597
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1673..1674
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1702..1703
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT SITE 1897..1898
FT /note="Cleavage; by protease 3C"
FT /evidence="ECO:0000250|UniProtKB:P03304"
FT MOD_RES 1676
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT LIPID 112
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250|UniProtKB:P03300"
FT LIPID 1597
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000269|PubMed:22258260"
SQ SEQUENCE 2370 AA; 255138 MW; D8B0F432F127C715 CRC64;
MMEGSNGFSS SLAGLSSSRS SLRLLTHLLS LPPPNRDARR HSGWYRSPPT LPVNVYLNEQ
FDNLCLAALR YPGCKLYPSV YTLFPDVSPF KIPQSIPAFA HLVQRQGLRR QGNPTTNIYG
NGNEVTTDVG ANGMSLPIAV GDMPTASSSE APLGSNKGGS STSPKSTSNG NVVRGSRYSK
WWEPAAARAL DRALDHAVDA TDAVAGAASK GIKAGATKLS NKLAGSQTTA LLALPGNIAG
GAPSATVNAN NTSISSQALL PSVNPYPSTP AVSLPNPDAP TQVGPAADRQ WLVDTIPWSE
TTPPLTVFSG PKALTPGTYP PTIEPNTGVY PLPAALCVSH PESVFTTAYN AHAYFNCGFD
VTVVVNASQF HGGSLIVLAM AEGLGDITPA DSSTWFNFPH AIINLANSNS ATLKLPYIGV
TPNTSTEGLH NYWTILFAPL TPLAVPTGSP TSVKVSLFVS PIDSAFYGLR FPIPFPTPQH
WKTRAVPGAG SYGSVVAGQE IPLVGYAPAA PPRDYLPGRV RNWLEYAARH SWERNLPWTA
ADEVGDQLVS YPIQPETLAN TQTNTAFVLS LFSQWRGSLQ ISLIFTGPAQ CYGRLLLAYT
PPSANPPTTI EEANNGTYDV WDVNGDSTYT FTIPFCSQAY WKTVDIGTSS GLVSNNGYFT
IFVMNPLVTP GPSPPSATVA AFLHVADDFD VRLPQCPALG FQSGADGAEV QPAPTSDLSD
GNPTTDPAPR DNFDYPHHPV DPSTDLAFYF SQYRWFGLNE DLTPLNVTGG LFYHVSLNPV
NFQQNSLLSV LGAFTYVYAN LSLNINVSAP LQACTFYIFY APPGASVPST QTLAELSFFT
HTATPLNLAA PTNITVSIPY ASPQSVLCTS FGGFGLQNGG DPGNLHSNTW GTLILYVDLP
QSDSVSVSAY ISFRDFEAYV PRQTPGVGPI PTSTSIVRVA RPTPKPRTVR RQGGTLADLI
LTPESRCFIV AHTTAPYYSI LLVNPDEEYA ISMFTHGDES ILRYSSRGGT RLAPTAPAFF
LCAAASVDTI LPYPISQSHL WLSDLTGIPL RAVPPLTLFL SAGAALCAGA QTLIAVAQGG
SAPDTPPTPN RALFRRQGLG DLPDAAKGLS AALENVAKVA GDADIATSSQ AIASSINSLS
NSIDGATTFM QNFFSGLAPK NPTSPLQHLF AKLIKWVTKI IGSLIIICNN PTPSALIGVS
LMLCGDLAED ITEFFSNLGN PLAAVFYRCA RALGLSPTPQ SAAQAAGGRQ GVRDYNDIMS
ALRNTDWFFE KIMSHIKNLL EWLGVLVKDD PRTKLNSQHE KILELYTDSV TASSTPPSEL
SADAIRSNLD LAKQLLTLSH AANSVTHIQL CTRAITNYST ALSAISLVGT PGTRPEPLVV
YLYGPPGTGK SLLASLLAST LAQALSGDPN NYYSPSSPDC KFYDGYSGQP VHYIDDIGQD
PDGADWADFV NIVSSAPFIV PMADVNDKGR FYTSRVVIVT SNFPGPNPRS ARCVAALERR
LHIRLNVTAR DGAAFSAAAA LKPSEPLAAT RYCKFSNPLT QFSMFNLAVD YKSIVLPNTP
LSCFDELIDF ILGSLRDRAS VNSLLSGMVR TDVARQGGNA DAPAPSAAPL PSVLPSVPSQ
DPFVRAVNEN RPVSFLSKIW SWRAPIFAAS SFLSLIAATL TIVRCLRDLR STQGAYSGTP
VPKPRKKDLP KQPVYSGPVR RQGFDPAVMK IMGNVDSFVT LSGSKPIWTM SCLWIGGRNL
IAPSHAFVSD DYEITHIRVG SRTLDVSRVT RVDDGELSLI SVPDGPEHKS LIRYIRSASP
KSGILASKFS DTPVFVSFWN GKPHSTPLPG VVDEKDSFTY RCSSFQGLCG SPMIATDPGG
LGILGIHVAG VAGYNGFSAR LTPERVQAFL SNLATPQSVL HFHPPMGPPA HVSRRSRLHP
SPAFGAFPIT KEPAALSRKD PRLPEGTDLD AITLAKHDKG DIATPWPCME EAADWYFSQL
PDSLPVLSQE DAIRGLDHMD AIDLSQSPGY PWTTQGRSRR SLFDEDGNPV PELQKAIDSV
WDGGSYIYQS FLKDELRPTA KARAGKTRIV EAAPIQAIVV GRRLLGSLIN HLQGNPLQYG
SAVGCNPDIH WTQIFHSLTP FSNVWSIDYS CFDATIPSVL LSAIASRIAS RSDQPGRVLD
YLSYTTTSYH VYDSLWYTMV GGNPSGCVGT SILNTIANNI AIISAMMYCN KFDPRDPPVL
YCYGDDLIWG SNQDFHPREL QAFYQKFTNF VVTPADKASD FPDSSSIYDI TFLKRYFVPD
DIHPHLIHPV MDEATLTNSI MWLRGGEFEE VLRSLETLAF HSGPNNYSTW CEKIKAKIRE
NGCDATFTPY SVLQRGWVST CMTGPYPLTG
