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POLG_SALVA
ID   POLG_SALVA              Reviewed;        2374 AA.
AC   C5MSH2;
DT   16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 89.
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   Salivirus A (isolate Human/Nigeria/NG-J1/2007) (SV-A).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Picornaviridae; Salivirus.
OX   NCBI_TaxID=651733;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19759142; DOI=10.1128/jvi.01241-09;
RA   Li L., Victoria J., Kapoor A., Blinkova O., Wang C., Babrzadeh F.,
RA   Mason C.J., Pandey P., Triki H., Bahri O., Oderinde B.S., Baba M.M.,
RA   Bukbuk D.N., Besser J.M., Bartkus J.M., Delwart E.L.;
RT   "A novel picornavirus associated with gastroenteritis.";
RL   J. Virol. 83:12002-12006(2009).
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=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=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=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 (By similarity). Interacts with
CC       protein 2B (By similarity). Interacts with protein 2C (By similarity).
CC       {ECO:0000250|UniProtKB:O91464}.
CC   -!- SUBUNIT: [Protein 2B]: Homodimer. Interacts with host ABCD3 (By
CC       similarity). Interacts with protein 2A (By similarity). Interacts with
CC       host ACBD3 (By 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 (By similarity). 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}.
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; GQ179640; ACS32214.2; -; Genomic_RNA.
DR   RefSeq; YP_003038594.1; NC_012957.1.
DR   SMR; C5MSH2; -.
DR   DNASU; 11242466; -.
DR   GeneID; 11242466; -.
DR   KEGG; vg:11242466; -.
DR   Proteomes; UP000029742; 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; -; 2.
DR   Gene3D; 2.60.120.20; -; 3.
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   3: Inferred from homology;
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; Reference proteome;
KW   RNA-binding; RNA-directed RNA polymerase;
KW   T=pseudo3 icosahedral capsid protein; Thiol protease; Transferase;
KW   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..2374
FT                   /note="Genome polyprotein"
FT                   /id="PRO_0000448019"
FT   CHAIN           1..114
FT                   /note="Leader protein"
FT                   /id="PRO_0000448020"
FT   CHAIN           115..482
FT                   /note="Capsid protein VP0"
FT                   /id="PRO_0000448021"
FT   CHAIN           483..705
FT                   /note="Capsid protein VP3"
FT                   /id="PRO_0000448022"
FT   CHAIN           706..955
FT                   /note="Capsid protein VP1"
FT                   /id="PRO_0000448023"
FT   CHAIN           956..1100
FT                   /note="Protein 2A"
FT                   /id="PRO_0000448024"
FT   CHAIN           1101..1253
FT                   /note="Protein 2B"
FT                   /id="PRO_0000448025"
FT   CHAIN           1254..1599
FT                   /note="Protein 2C"
FT                   /id="PRO_0000448026"
FT   CHAIN           1600..1676
FT                   /note="Protein 3A"
FT                   /id="PRO_0000448027"
FT   CHAIN           1677..1705
FT                   /note="VPg"
FT                   /id="PRO_0000448028"
FT   CHAIN           1706..2366
FT                   /note="Protein 3CD"
FT                   /id="PRO_0000448029"
FT   CHAIN           1706..1900
FT                   /note="Protease 3C"
FT                   /id="PRO_0000448030"
FT   CHAIN           1901..2366
FT                   /note="RNA-directed RNA polymerase"
FT                   /id="PRO_0000448031"
FT   TRANSMEM        1649..1669
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1361..1525
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   DOMAIN          1700..1889
FT                   /note="Peptidase C3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   DOMAIN          2126..2243
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT   REGION          144..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          707..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1677..1699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1748
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1779
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        1852
FT                   /note="For protease 3C activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT   ACT_SITE        2132
FT                   /note="For RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   ACT_SITE        2229
FT                   /note="For RdRp activity"
FT                   /evidence="ECO:0000250|UniProtKB:P12296"
FT   BINDING         1387..1394
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT   SITE            114..115
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000305"
FT   SITE            482..483
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            705..706
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            955..956
FT                   /note="Cleavage; by protein 3CD"
FT                   /evidence="ECO:0000250|UniProtKB:O91464"
FT   SITE            1100..1101
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1253..1254
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1599..1600
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1676..1677
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1705..1706
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   SITE            1900..1901
FT                   /note="Cleavage; by protease 3C"
FT                   /evidence="ECO:0000250|UniProtKB:P03304"
FT   MOD_RES         1679
FT                   /note="O-(5'-phospho-RNA)-tyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   LIPID           115
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P03300"
FT   LIPID           1600
FT                   /note="N-myristoyl glycine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:C6KEF6"
SQ   SEQUENCE   2374 AA;  255475 MW;  DD94E33770F73453 CRC64;
     MEGSNGFSSS LAGLSSSRSS LRLLTHFLSL PTLPVNIYLN ARRHSGWYRS PPTLPVNIYL
     NEQFDNLCLA ALRYPGHKLY PSVHTLFPDV SPLKIPHSVP AFAHLVQRQG LRRQGNSITN
     IYGNGNDVTT DVGANGMSLP IAVGDMPTAS TSEAPLGSNK GGSSTSPKST SNGNVVRGSR
     YSKWWEPAAA RALDRALDHA VDATDAVAGA ASKGIKAGAA KLSNKLSGSQ TTALLALPGN
     IAGGAPSATV NANNTSISSQ ALLPSVNPYP STPAVSLPNP DAPTQVGPAA DRQWLVDTLS
     WSETIAPLTV FSGPKALTPG VYPPTIEPNT GVYPLPAALC VSHPESVFST AYNAHAYFNC
     GFDVTVVVNA SQFHGGSLIV LAMAEGLGDI TPADSSTWFN FPHTIINLAN SNAATLKLPY
     IGVTPNTSTE GLHNYWTILF APLTPLAVPT GSPTTVKVSL FVSPIDSAFY GLRFPVPFPA
     PQHWKTRAVP GAGTYGSVVA GQEIPLVGYA PAAPPRDYLP GRVHNWLEYA ARHSWERNLT
     WTSADEVGDQ LVSYPIQPEA LANTQTNTAF VLSLFSQWRG SLQISLIFTG PAQCYGRLLL
     AYTPPSANPP TTIDEANNGT YDVWDVNGDS TYTFTIPFCS QAYWKTVDIG TSSGLVSNNG
     YFTVFVMNPL VTPGPSPPSA TVAAFLHVAD DFDVRLPQCP ALGFQSGADG AEVQPAPTSD
     LSDGNPTTDP APRDNFDYPH HPVDPSTDLA FYFSQYRWFG LNESLTPLDA TGGLFYHISL
     NPINFQQSSL LSVLGAFTYV YANLSLNINV SAPSQPCTFY VFYAPPGASV PSVQTLAELS
     FFTHTATPLN LAAPTNITVS IPYSSPQSVL CTSFGGFGLQ NGGDAGNLHS NTWGTLILYV
     DLPQSDSVSV SAYISFRDFE AYVPRQTPGV GPVPTSTSIV RVARPTPKPR TARRQGGTLA
     DLILSPESRC FIVAHTTAPF YSILLVNPDE EYAISMFSHG DESILQYSSR SGTRLTPTAP
     AFFLCAAASV DTVLPYSISQ SHLWLTDLTG IPLRAVPPLT LFLSAGAALC AGAQTLIAVA
     QGGSTPETPP TPNRALLRRQ GLGDLPDAAK GLSAALESVA RVAGDANIAT SSQAIATSIN
     SLSNSIDGAT SFMQNFFSGL APRNPTSPLQ HLFAKLIKWV TKIIGSLIII CNNPTPSALI
     GVSLMLCGDL AEDITEFFSN LGNPLAAVFY RCARALGLSP TPQSAAQAAG GRQGVRDYND
     IMSALRNTDW FFEKIMTHIK NLLEWLGVLV KDDPRTKLNG QHEKILELYT DSVTASSTPP
     SELSADAIRS NLDLAKQLLT LSHAANSVTH IQLCTRAITN YSTALSAISL VGTPGTRPEP
     LVVYLYGPPG TGKSLLASLL ASTLAQALSG DPNNYYSPSS PDCKFYDGYS GQPVHYIDDI
     GQDPDGADWA DFVNIVSSAP FIVPMADVND KGRFYTSRVV IVTSNFPGPN PRSARCVAAL
     ERRLHIRLNV TARDGVAFSA AAALQPSNPP SATRYCKFAN PLTQFSMFNL AVDYKSVVLP
     NTPLTCFDEL VDFVLSSLRD RASVNSLLSG MVRTDVTRQG GNADAPAPSA APLPSVIPSV
     PSQDPFTRAV NENRPVSFLS KIWSWRAPIF AASSFLSLIA ATLTIVRCLR DLRSTQGAYS
     GTPVPKPRKK DLPKQPVYSG PVRRQGFDPA VMKIMGNVDS FVTLSGTKPI WTMSCLWIGG
     RNLIAPSHAF VSDEYEITHI RVGSRTLDVS RVTRVDDGEL SLLSVPDGPE HKSLIRYIRS
     ASPKSGILAS KFSDTPVFVS FWNGKSHSTP LPGVVDEKDS FTYRCSSFQG LCGSPMIATD
     PGGLGILGIH VAGVAGYNGF SARLTPERVQ AFLSHLATPQ SVLYFHPPMG PPAHVSRRSR
     LHPIPPAFGA FPITKEPAAL SRKDPRLPEG TDLDAITLAK HDKGDIATPW PCMEEAADWY
     FSQLPDNLPV LSQEDAIRGL DHMDAIDLSQ SPGYPWTTQG RSRRSLFDED GNPLPELQEA
     IDSVWDGGSY IYQSFLKDEL RPTAKARAGK TRIVEAAPIQ AIVVGRRLLG SLINHLQGNP
     LQHGSAVGCN PDIHWTQIFH SLTSFSNVWS IDYSCFDATI PSVLLSAIAS RIAARSDQPG
     RVLDYLSYTT TSYHVYDSLW YTMIGGNPSG CVGTSILNTI ANNIAVISAM MYCNKFDPRD
     PPVLYCYGDD LIWGSNQDFH PRELQAFYQK FTNFVVTPAD KASDFPDSSS IFDITFLKRY
     FVPDDIHPHL IHPVMDEQTL TNSIMWLRGG EFEEVLRSLE TLAFHSGPKN YSAWCEKIKA
     KIRENGCDAT FTPYSVLQRG WVSTCMTGPY PLTG
 
 
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