UniProtKB - B8XTP8 (POLG_COSAA)
Genome polyprotein
Functioni
Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes.
By similarityForms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes.
By similarityForms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes.
By similarityLies on the inner surface of the capsid shell (By similarity).
After binding to the host receptor, the capsid undergoes conformational changes (By similarity).
Capsid protein VP4 is released, capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm (By similarity).
After genome has been released, the channel shrinks (By similarity).
By similarityVP0 precursor is a component of immature procapsids.
By similarityInvolved in host translation shutoff by inhibiting cap-dependent mRNA translation (By similarity).
Nuclear localization is required for this function (By similarity).
The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity).
By similarityAffects membrane integrity and causes an increase in membrane permeability.
By similarityAssociates with and induces structural rearrangements of intracellular membranes (By similarity).
It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).
Interacts with IFIH1/MDA5 to inhibit the induction of the IFN-beta signal pathway (By similarity).
By similarityServes as membrane anchor via its hydrophobic domain.
By similarityForms a primer, VPg-pU, which is utilized by the polymerase for the initiation of RNA chains.
By similarityCysteine protease that generates mature viral proteins from the precursor polyprotein (By similarity).
In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate cooperatively bind to the protease. Cleaves host PABP1, this cleavage is important for viral replication (By similarity).
Cleaves host TANK and disrupts the TANK-TBK1-IKKepsilon-IRF3 complex, thereby inhibiting the induction of the IFN-beta signal pathway (By similarity).
By similarityReplicates the genomic and antigenomic RNAs by recognizing replications specific signals (By similarity).
Performs VPg uridylylation (By similarity).
By similarityCatalytic activityi
- Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.PROSITE-ProRule annotation EC:3.4.22.28
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 1501 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1535 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1612 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1899 | For RdRp activityBy similarity | 1 | |
Active sitei | 1997 | For RdRp activityBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 1130 – 1137 | ATPPROSITE-ProRule annotation | 8 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- ATP hydrolysis activity Source: RHEA
- cysteine-type endopeptidase activity Source: UniProtKB-EC
- ion channel activity Source: UniProtKB-KW
- RNA binding Source: UniProtKB-KW
- RNA-directed 5'-3' RNA polymerase activity Source: UniProtKB-KW
- RNA helicase activity Source: UniProtKB-EC
- structural molecule activity Source: InterPro
GO - Biological processi
- pore formation by virus in membrane of host cell Source: UniProtKB-KW
- protein complex oligomerization Source: UniProtKB-KW
- RNA-protein covalent cross-linking Source: UniProtKB-KW
- transcription, DNA-templated Source: InterPro
- viral entry into host cell Source: UniProtKB-KW
- viral RNA genome replication Source: InterPro
- virion attachment to host cell Source: UniProtKB-KW
Keywordsi
Molecular function | Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel |
Biological process | Host-virus interaction, Ion transport, Transport, Viral attachment to host cell, Viral RNA replication, Virus entry into host cell |
Ligand | ATP-binding, Nucleotide-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Genome polyproteinCleaved into the following 12 chains: Alternative name(s): VP4-VP2 Alternative name(s): P1A Rho Virion protein 4 Alternative name(s): Beta P1B Virion protein 2 Alternative name(s): Gamma P1C Virion protein 3 Alternative name(s): Alpha P1D Virion protein 1 Alternative name(s): G Alternative name(s): H Protein 3B Alternative name(s): Picornain 3C p22 Alternative name(s): 3D polymerase Short name: 3Dpol Protein 3D Short name: 3D |
Organismi | Cosavirus A (isolate Human/Pakistan/0553/-) (HCoSV-A) |
Taxonomic identifieri | 1554483 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Pisuviricota › Pisoniviricetes › Picornavirales › Picornaviridae › Cosavirus › |
Virus hosti | Homo sapiens (Human) [TaxID: 9606] |
Proteomesi |
|
Subcellular locationi
- Virion By similarity
- Host cytoplasm Curated
- Virion By similarity
- Host cytoplasm Curated
- Virion By similarity
- Host cytoplasm Curated
- host nucleolus By similarity
- Host cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles.Curated
- Host cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles.Curated
- Host cytoplasmic vesicle membrane By similarity; Peripheral membrane protein Curated; Cytoplasmic side Curated Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles.By similarity
- Host cytoplasm Curated
- Host cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity Note: Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are probably autophagosome-like vesicles.Curated
Keywords - Cellular componenti
Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Host nucleus, Membrane, T=pseudo3 icosahedral capsid protein, VirionPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed; by hostCurated | |||
ChainiPRO_0000446193 | 2 – 2124 | Genome polyproteinAdd BLAST | 2123 | |
ChainiPRO_0000446194 | 2 – 333 | Capsid protein VP0Add BLAST | 332 | |
ChainiPRO_0000446195 | 2 – 68 | Capsid protein VP4Add BLAST | 67 | |
ChainiPRO_0000446196 | 69 – 333 | Capsid protein VP2Add BLAST | 265 | |
ChainiPRO_0000446197 | 334 – 568 | Capsid protein VP3Add BLAST | 235 | |
ChainiPRO_0000446198 | 569 – 859 | Capsid protein VP1Add BLAST | 291 | |
ChainiPRO_0000446199 | 860 – 889 | Protein 2AAdd BLAST | 30 | |
ChainiPRO_0000446200 | 890 – 1010 | Protein 2BAdd BLAST | 121 | |
ChainiPRO_0000446201 | 1011 – 1331 | Protein 2CAdd BLAST | 321 | |
ChainiPRO_0000446202 | 1332 – 1434 | Protein 3AAdd BLAST | 103 | |
ChainiPRO_0000446203 | 1435 – 1458 | VPgAdd BLAST | 24 | |
ChainiPRO_0000446204 | 1459 – 1661 | Protease 3CAdd BLAST | 203 | |
ChainiPRO_0000446205 | 1662 – 2123 | RNA-directed RNA polymeraseAdd BLAST | 462 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 2 | N-myristoyl glycine; by hostBy similarity | 1 | |
Modified residuei | 1442 | O-(5'-phospho-RNA)-tyrosineBy similarity | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 68 – 69 | Cleavage | 2 | |
Sitei | 333 – 334 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 568 – 569 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 859 – 860 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 889 – 890 | Cleavage; by ribosomal skipBy similarity | 2 | |
Sitei | 1010 – 1011 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1331 – 1332 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1434 – 1435 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1458 – 1459 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1661 – 1662 | Cleavage; by protease 3CBy similarity | 2 |
Keywords - PTMi
Covalent protein-RNA linkage, Lipoprotein, Myristate, PhosphoproteinInteractioni
Subunit structurei
Interacts with host IFIH1/MDA5; this interaction inhibits the induction of the IFN-beta signal pathway (By similarity).
By similarityFamily & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1102 – 1264 | SF3 helicasePROSITE-ProRule annotationAdd BLAST | 163 | |
Domaini | 1459 – 1648 | Peptidase C3PROSITE-ProRule annotationAdd BLAST | 190 | |
Domaini | 1893 – 2011 | RdRp catalyticPROSITE-ProRule annotationAdd BLAST | 119 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 873 – 880 | Host EIF4E bindingBy similarity | 8 | |
Regioni | 1415 – 1446 | DisorderedSequence analysisAdd BLAST | 32 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 1415 – 1437 | Basic and acidic residuesSequence analysisAdd BLAST | 23 |
Sequence similaritiesi
Family and domain databases
CDDi | cd00205, rhv_like, 2 hits |
Gene3Di | 2.40.10.10, 2 hits 2.60.120.20, 3 hits 3.30.70.270, 2 hits 4.10.90.10, 1 hit |
InterProi | View protein in InterPro IPR037080, Capsid_VP4_sf_Picornavirus IPR043502, DNA/RNA_pol_sf IPR004004, Helic/Pol/Pept_Calicivir-typ IPR000605, Helicase_SF3_ssDNA/RNA_vir IPR014759, Helicase_SF3_ssRNA_vir IPR027417, P-loop_NTPase IPR044067, PCV_3C_PRO IPR000199, Peptidase_C3A/C3B_picornavir IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR001676, Picornavirus_capsid IPR043128, Rev_trsase/Diguanyl_cyclase IPR033703, Rhv-like IPR001205, RNA-dir_pol_C IPR007094, RNA-dir_pol_PSvirus IPR029053, Viral_coat |
Pfami | View protein in Pfam PF00548, Peptidase_C3, 1 hit PF00680, RdRP_1, 1 hit PF00073, Rhv, 2 hits PF00910, RNA_helicase, 1 hit |
PRINTSi | PR00918, CALICVIRUSNS |
SUPFAMi | SSF50494, SSF50494, 1 hit SSF52540, SSF52540, 1 hit SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS51874, PCV_3C_PRO, 1 hit PS50507, RDRP_SSRNA_POS, 1 hit PS51218, SF3_HELICASE_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MGANNSKESV SSNGNEGTIV NNFYSNQYYA SIDASAQGVG TSTTPENGNV
60 70 80 90 100
SGFLGLAGSA FNALSLLASP RTETGMMMED RVLSRTAGNT SVNSQAAEGV
110 120 130 140 150
LQAYGTETDS NSPTSCGDDP SKGTHATDRA FVIQLLPWKQ TTNSYFAQWV
160 170 180 190 200
RLTQKLSNNL HGNVMAKNIK SHAFAKMGFE VMLQANTSPF HNGILGLFLV
210 220 230 240 250
PEFVRKGEIT DEWIDLTPTS SLVSNTELYN PQTYANFPFD AKHSFDYSDI
260 270 280 290 300
TPEQFMIFPH QLINPKDTNV ATVRVPYINI APTNDTTVHT VWTAVVMVLV
310 320 330 340 350
PLNFSSGASP TVSLTLTITP INSVFNGLHH TAQGPIPVRP FHNFQQFSTT
360 370 380 390 400
VPLRTEPCYG MTVTPPVDYM PLPITDLVEL AKVPSFVTVA NSDTTSERSF
410 420 430 440 450
PYFSVSNTEQ GRNLFKSSVV LSDLHYQHTL VANLARYFCN YRGSLQFDFI
460 470 480 490 500
AATTAMTRGK LLISYTPPGA GEPQSIDQAM MGTYAIWDLG LQSTFNFVVP
510 520 530 540 550
FISASDFRFN TSSVSNALNS DGWITVWLMN PLTYPPSTPP TQQILMLMSA
560 570 580 590 600
GSDFSYRLPI SPGFAEGETS EHPMDNAECG KIDDKDAGMF SGHSVGLPTP
610 620 630 640 650
HTSTSFFYDR YRFVGIVKSV VNNTPKPVNI YDDTGKVKNL QQVFPTSDTL
660 670 680 690 700
LPHSLMSLSP CASVCGQPIS SFLFAQRANP KKTLKLRSGD EFLYRCCPFS
710 720 730 740 750
YIKCDLEFTV VPPANSTRDY IVHWYPPGAT LDAGEVAVGN TSGSNGFDDN
760 770 780 790 800
GMNAGSSLFS YNPTFHARAP SKVSAVIPFC LPVSLLPLYF DGFPDYSTTK
810 820 830 840 850
GMYGCSPSFS FGTIYIESGL QETYSVYIRY KDFKGYAPRP LIRTPHIRLS
860 870 880 890 900
ERARYIMADS VLPRPLTRAE RDVARDLLLI AGDIESNPGP AFNPEYTAHG
910 920 930 940 950
PVTELIQLAR KPETVDNVNR LLTTLNTLMA KWNNLKDTVT DAVFLRDMVC
960 970 980 990 1000
LLVKLTSLMY LVHGQGPGAY FAAASILLAD GITFFDWYEK IKIFMARKLR
1010 1020 1030 1040 1050
VSPPFFPAAQ GPDLRDFVTF FNAARGAQWM IDSLKSLITC IKQWLELEEE
1060 1070 1080 1090 1100
NEAVQLEKML IDSPRHCKAI NDYNRGDSFQ RPTNSFEFMD RLVECATKLG
1110 1120 1130 1140 1150
KVQIATYFRN FTTADSDTSR PEPVVVVLRG KPGVGKSAAA TVMAAAVSKL
1160 1170 1180 1190 1200
LVGSQSVYTL SPDTEHMDGY HGQFVTLMDD LGQNPDGEDF RCFCQMVSCA
1210 1220 1230 1240 1250
QYRPAMADLK DKGILFTSRL LIATTNLPDF NPVTISDPRA LDRRITFDIL
1260 1270 1280 1290 1300
VTPGSAATKN GKLDLAAALK PDGPGEHPYT SDCPILHTTG LLLKNLRNNQ
1310 1320 1330 1340 1350
TMNLKDLVDM IVKRIKHKKE VGNMLDSLVA QGPTMIVGYT KDDDGIAIVD
1360 1370 1380 1390 1400
CLEEWNKIKD KKKKQLALEM VAQELKDKHE EHKGTIKLLK MFVTGLGVVA
1410 1420 1430 1440 1450
AVAGAYATMK YFTKDKPKEE EEEPEEKKEK KTEESKEAAG PYNGPTKKEI
1460 1470 1480 1490 1500
KTLKLKAQSP LMDMEKKIAQ NVMPFQIFYN GKRYTQSCLA IGKRVILVNK
1510 1520 1530 1540 1550
HAFESVEHKF VVDQKEYTLD QVTAISLDCG SGVTDVCAVC LPPGPDFKSI
1560 1570 1580 1590 1600
KKHFLPFNTT MFPGTRLTIL SNDHYPMSRE GSFLRFEDEV PTNVGNMPFV
1610 1620 1630 1640 1650
MLYKSTSYFG MCGSVVCSRF VDGGGIIGMH CAGGGGVSVG TRLTARMIES
1660 1670 1680 1690 1700
VFDYFYPPVA QGIIENTETG PRVHVPRTSK LKRTNATYPA TEKYGPAALS
1710 1720 1730 1740 1750
RYDPRLNEGV NLDEVIFSKH TQNTLVEKGS TFRSALDMAA EIYGEKFRGN
1760 1770 1780 1790 1800
DFSPLSVEDA ILGIPGLDRL DPNTASGLPY TKTRRQMIDF NTGQILDDTL
1810 1820 1830 1840 1850
KCRLGQWLAG RPPQEVHYQT FLKDEIRPIE KVKAGKTRII DVPPLDHVIA
1860 1870 1880 1890 1900
FRMLFGRFIA HYHLNFGFKT GSAIGCDPDV AWASFGFELS GFPYLYDFDY
1910 1920 1930 1940 1950
SNFDASHSTS IFEILEQKFF SPELGFDPRC SLLLKSLAVS THCYENKRLQ
1960 1970 1980 1990 2000
IAGGLPSGTA GTSVLNTVIN NIIFHGALYH TYTNFERDDI SMLAYGDDIV
2010 2020 2030 2040 2050
VASKFELDLV MVKAFMNRIG YKITPADKSD EFRPKCMDDI CFLKRRFVKV
2060 2070 2080 2090 2100
AGVWAPVMET ENLEAMLSWY KPGTLNEKLQ SVSRLAHFSG RDVYDHLFKP
2110 2120
FIRDGFDVTP WKQLHLEWLN KLSA
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | FJ438902 Genomic RNA Translation: ACL15185.1 |
RefSeqi | YP_002956074.1, NC_012800.1 |
Genome annotation databases
GeneIDi | 7986820 |
KEGGi | vg:7986820 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | FJ438902 Genomic RNA Translation: ACL15185.1 |
RefSeqi | YP_002956074.1, NC_012800.1 |
3D structure databases
SMRi | B8XTP8 |
ModBasei | Search... |
Genome annotation databases
GeneIDi | 7986820 |
KEGGi | vg:7986820 |
Family and domain databases
CDDi | cd00205, rhv_like, 2 hits |
Gene3Di | 2.40.10.10, 2 hits 2.60.120.20, 3 hits 3.30.70.270, 2 hits 4.10.90.10, 1 hit |
InterProi | View protein in InterPro IPR037080, Capsid_VP4_sf_Picornavirus IPR043502, DNA/RNA_pol_sf IPR004004, Helic/Pol/Pept_Calicivir-typ IPR000605, Helicase_SF3_ssDNA/RNA_vir IPR014759, Helicase_SF3_ssRNA_vir IPR027417, P-loop_NTPase IPR044067, PCV_3C_PRO IPR000199, Peptidase_C3A/C3B_picornavir IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR001676, Picornavirus_capsid IPR043128, Rev_trsase/Diguanyl_cyclase IPR033703, Rhv-like IPR001205, RNA-dir_pol_C IPR007094, RNA-dir_pol_PSvirus IPR029053, Viral_coat |
Pfami | View protein in Pfam PF00548, Peptidase_C3, 1 hit PF00680, RdRP_1, 1 hit PF00073, Rhv, 2 hits PF00910, RNA_helicase, 1 hit |
PRINTSi | PR00918, CALICVIRUSNS |
SUPFAMi | SSF50494, SSF50494, 1 hit SSF52540, SSF52540, 1 hit SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS51874, PCV_3C_PRO, 1 hit PS50507, RDRP_SSRNA_POS, 1 hit PS51218, SF3_HELICASE_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | POLG_COSAA | |
Accessioni | B8XTP8Primary (citable) accession number: B8XTP8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 16, 2019 |
Last sequence update: | March 3, 2009 | |
Last modified: | February 23, 2022 | |
This is version 94 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families