UniProtKB - P08544 (POLG_TMEVB)
Genome polyprotein
Functioni
Forms a complex with host RAN and probably binds to exportins carrying activated MAPK in order to mediate the hyperphosphorylation of host Phe/Gly containing nuclear pore proteins (Nups) resulting in cessation of active nucleocytoplasmic transport (Probable). Proteins with NLS signals fail to import, cellular mRNAs fail to export, and some proteins small enough for diffusion are not retained anymore (efflux) (By similarity).
The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity).
The leader protein also inhibits host interferon regulatory factor 3 (IRF3) dimerization, thereby blocking the transcriptional activation of IFN genes (By similarity).
Binds to host RNase L thereby preventing its activation by 2'-5' oligoadenylates in order to counteract the antiviral interferon-inducible OAS/RNase L pathway (By similarity).
By similarity1 PublicationForms 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).
Inhibits the phosphorylation of the leader protein (PubMed:25210192).
By similarity1 PublicationAffects 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).
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).
By similarityReplicates the genomic and antigenomic RNAs by recognizing replications specific signals (By similarity).
Performs VPg uridylylation (By similarity).
By similarityMiscellaneous
Catalytic 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 | 1680 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1714 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1793 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 2077 | For RdRp activityBy similarity | 1 | |
Active sitei | 2175 | For RdRp activityBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 3 – 14 | By similarityAdd BLAST | 12 | |
Nucleotide bindingi | 1312 – 1319 | 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
- metal ion binding 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
- induction by virus of host autophagy Source: UniProtKB
- 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
- suppression by virus of host gene expression Source: UniProtKB-KW
- suppression by virus of host mRNA export from nucleus Source: UniProtKB
- suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity 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
Protein family/group databases
MEROPSi | C03.010 |
Names & Taxonomyi
Protein namesi | Recommended name: Genome polyproteinCleaved into the following 13 chains: Alternative name(s): VP4-VP2 Alternative name(s): P1A Virion protein 4 Alternative name(s): P1B Virion protein 2 Alternative name(s): P1C Virion protein 3 Alternative name(s): P1D Virion protein 1 Alternative name(s): Protein 3B Alternative name(s): Picornain 3C Alternative name(s): 3D polymerase Short name: 3Dpol Protein 3D Short name: 3D |
Organismi | Theiler's murine encephalomyelitis virus (strain BeAn 8386) (TMEV) |
Taxonomic identifieri | 12125 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Pisuviricota › Pisoniviricetes › Picornavirales › Picornaviridae › Cardiovirus › |
Virus hosti | Mus musculus (Mouse) [TaxID: 10090] |
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 Curated; 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.Curated
- Host cytoplasmic vesicle membrane Curated; 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.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 Curated; 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.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 |
---|---|---|---|---|
ChainiPRO_0000446097 | 1 – 2303 | Genome polyproteinAdd BLAST | 2303 | |
ChainiPRO_0000040168 | 1 – 76 | Leader proteinAdd BLAST | 76 | |
ChainiPRO_0000310970 | 77 – 414 | Capsid protein VP0Add BLAST | 338 | |
ChainiPRO_0000040169 | 77 – 147 | Capsid protein VP4Add BLAST | 71 | |
ChainiPRO_0000040170 | 148 – 414 | Capsid protein VP2Add BLAST | 267 | |
ChainiPRO_0000040171 | 415 – 646 | Capsid protein VP3Add BLAST | 232 | |
ChainiPRO_0000040172 | 647 – 922 | Capsid protein VP1Add BLAST | 276 | |
ChainiPRO_0000040173 | 923 – 1055 | Protein 2AAdd BLAST | 133 | |
ChainiPRO_0000040174 | 1056 – 1191 | Protein 2BAdd BLAST | 136 | |
ChainiPRO_0000040175 | 1192 – 1517 | Protein 2CAdd BLAST | 326 | |
ChainiPRO_0000040176 | 1518 – 1605 | Protein 3AAdd BLAST | 88 | |
ChainiPRO_0000040177 | 1606 – 1625 | VPgAdd BLAST | 20 | |
ChainiPRO_0000040178 | 1626 – 1842 | Protease 3CAdd BLAST | 217 | |
ChainiPRO_0000040179 | 1843 – 2303 | RNA-directed RNA polymeraseAdd BLAST | 461 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 77 | N-myristoyl glycine; by hostBy similarity | 1 | |
Disulfide bondi | 501 ↔ 503 | By similarity | ||
Modified residuei | 1608 | O-(5'-phospho-RNA)-tyrosineBy similarity | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 147 – 148 | CleavageSequence analysis | 2 | |
Sitei | 414 – 415 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 646 – 647 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 922 – 923 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1055 – 1056 | Cleavage; by ribosomal skipBy similarity | 2 | |
Sitei | 1191 – 1192 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1517 – 1518 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1605 – 1606 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1625 – 1626 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1842 – 1843 | Cleavage; by protease 3CBy similarity | 2 |
Keywords - PTMi
Covalent protein-RNA linkage, Disulfide bond, Lipoprotein, Myristate, PhosphoproteinInteractioni
Subunit structurei
Interacts with host EIF4E (By similarity).
Interacts with the leader protein (PubMed:25210192).
By similarity1 PublicationInteracts with host RAN; the complex L-RAN recruits cellular kinases responsible for the L-induced nucleocytoplasmic trafficking inhibition (By similarity). The complex L-RAN can further bind to the host exportins XPO1/CRM1 and CSE1L/CAS (By similarity).
Interacts with the protein 2A (PubMed:25210192).
Interacts with host RNASEL; this interaction prevents RNASEL activation by its substrate 2'-5' oligoadenylates (By similarity).
By similarity1 PublicationStructurei
Secondary structure
3D structure databases
SMRi | P08544 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P08544 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1283 – 1448 | SF3 helicasePROSITE-ProRule annotationAdd BLAST | 166 | |
Domaini | 1636 – 1829 | Peptidase C3PROSITE-ProRule annotationAdd BLAST | 194 | |
Domaini | 2071 – 2189 | RdRp catalyticPROSITE-ProRule annotationAdd BLAST | 119 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 30 – 46 | AcidicCuratedAdd BLAST | 17 | |
Regioni | 60 – 73 | TheiloBy similarityAdd BLAST | 14 | |
Regioni | 74 – 93 | DisorderedSequence analysisAdd BLAST | 20 | |
Regioni | 1041 – 1047 | Host EIF4E bindingBy similarity | 7 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 3 – 14 | By similarityAdd BLAST | 12 |
Keywords - Domaini
Zinc-fingerFamily and domain databases
CDDi | cd00205, rhv_like, 3 hits |
Gene3Di | 2.40.10.10, 1 hit 2.60.120.20, 3 hits 3.30.70.270, 2 hits 4.10.90.10, 1 hit |
InterProi | View protein in InterPro IPR015031, Capsid_VP4_Picornavir 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 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 PF08935, VP4_2, 1 hit |
PRINTSi | PR00918, CALICVIRUSNS |
SUPFAMi | SSF50494, SSF50494, 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
MACKHGYPDV CPICTAVDAT PGFEYLLMAD GEWYPTDLLC VDLDDDVFWP
60 70 80 90 100
SDTSNQSQTM DWTDVPLIRD IVMEPQGNSS SSDKSNSQSS GNEGVIINNF
110 120 130 140 150
YSNQYQNSID LSASGGNAGD APQTNGQLSN ILGGAANAFA TMAPLLLDQN
160 170 180 190 200
TEEMENLSDR VASDKAGNSA TNTQSTVGRL CGYGKSHHGE HPASCADTAT
210 220 230 240 250
DKVLAAERYY TIDLASWTTS QEAFSHIRIP LPHVLAGEDG GVFGATLRRH
260 270 280 290 300
YLCKTGWRVQ VQCNASQFHA GSLLVFMAPE FYTGKGTKTG TMEPSDPFTM
310 320 330 340 350
DTEWRSPQGA PTGYRYDSRT GFFATNHQNQ WQWTVYPHQI LNLRTNTTVD
360 370 380 390 400
LEVPYVNVAP SSSWTQHANW TLVVAVLSPL QYATGSSPDV QITASLQPVN
410 420 430 440 450
PVFNGLRHET VIAQSPIPVT VREHKGCFYS TNPDTTVPIY GKTISTPSDY
460 470 480 490 500
MCGEFSDLLE LCKLPTFLGN PNTNNKRYPY FSATNSVPAT SMVDYQVALS
510 520 530 540 550
CSCMANSMLA AVARNFNQYR GSLNFLFVFT GAAMVKGKFL IAYTPPGAGK
560 570 580 590 600
PTTRDQAMQS TYAIWDLGLN SSFNFTAPFI SPTHYRQTSY TSPTITSVDG
610 620 630 640 650
WVTVWKLTPL TYPSGTPTNS DILTLVSAGD DFTLRMPISP TKWVPQGVDN
660 670 680 690 700
AEKGKVSNDD ASVDFVAEPV KLPENQTRVA FFYDRAVPIG MLRPGQNMET
710 720 730 740 750
TFNYQENDYR LNCLLLTPLP SFCPDSSSGP QKTKAPVQWR WVRSGGVNGA
760 770 780 790 800
NFPLMTKQDY AFLCFSPFTF YKCDLEVTVS ALGMTRVASV LRWAPTGAPA
810 820 830 840 850
DVTDQLIGYT PSLGETRNPH MWLVGAGNSQ VSFVVPYNSP LSVLPAAWFN
860 870 880 890 900
GWSDFGNTKD FGVAPNADFG RLWIQGNTSA SVRIRYKKMK VFCPRPTLFF
910 920 930 940 950
PWPTPTTTKI NADNPVPILE LENPAALYRI DLFITFTDEF ITFDYKVHGR
960 970 980 990 1000
PVLTFRIPGF GLTPAGRMLV CMGEQPAHGP FTSSRSLYHV IFTATCSSFS
1010 1020 1030 1040 1050
FSIYKGRYRS WKKPIHDELV DRGYTTFGEF FKAVRGYHAD YYRQRLIHDV
1060 1070 1080 1090 1100
ETNPGPVQSV FQPQGAVLTK SLAPQAGIQN LLLRLLGIDG DCSEVSKAIT
1110 1120 1130 1140 1150
VVTDLVAAWE KAKTTLVSPE FWSKLILKTT KFIAASVLYL HNPDFTTTVC
1160 1170 1180 1190 1200
LSLMTGVDLL TNDSVFDWLK QKLSSFFRTP PPACPNVMQP QGPLREANEG
1210 1220 1230 1240 1250
FTFAKNIEWA MKTIQSVVNW LTSWFKQEED HPQSKLDKLL MEFPDHCRNI
1260 1270 1280 1290 1300
MDMRNGRKAY CECTASFKYF DELYNLAVTC KRIPLASLCE KFKNRHDHSV
1310 1320 1330 1340 1350
TRPEPVVVVL RGAAGQGKSV TSQIIAQSVS KMAFGRQSVY SMPPDSEYFD
1360 1370 1380 1390 1400
GYENQFSVIM DDLGQNPDGE DFTVFCQMVS STNFLPNMAH LERKGTPFTS
1410 1420 1430 1440 1450
SFIVATTNLP KFRPVTVAHY PAVDRRITFD FTVTAGPHCK TPAGMLDVEK
1460 1470 1480 1490 1500
AFDEIPGSKP QLACFSADCP LLHKRGVMFT CNRTQTVYNL QQVVKMVNDT
1510 1520 1530 1540 1550
ITRKTENVKK MNSLVAQSPP DWEHFENILT CLRQNNAALQ DQLDELQEAF
1560 1570 1580 1590 1600
AQARERSDFL SDWLKVSAII FAGIASLSAV IKLASKFKES IWPTPVRVEL
1610 1620 1630 1640 1650
SEGEQAAYAG RARAQKQALQ VLDIQGGGKV LAQAGNPVMD FELFCAKNIV
1660 1670 1680 1690 1700
APITFYYPDK AEVTQSCLLL RAHLFVVNRH VAETDWTAFK LKDVRHERHT
1710 1720 1730 1740 1750
VALRSVNRSG AKTDLTFIKV TKGPLFKDNV NKFCSNKDDF PARNDTVTGI
1760 1770 1780 1790 1800
MNTGLAFVYS GNFLIGNQPV NTTTGACFNH CLHYRAQTRR GWCGSAIICN
1810 1820 1830 1840 1850
VNGKKAVYGM HSAGGGGLAA ATIITKELIE AAEKSMLALE PQGAIVDIAT
1860 1870 1880 1890 1900
GSVVHVPRKT KLRRTVAHDV FQPKFEPAVL SRYDPRTDKD VDVVAFSKHT
1910 1920 1930 1940 1950
TNMESLPPIF DVVCGEYANR VFTILGKENG LLTVEQAVLG LPGMDPMEKD
1960 1970 1980 1990 2000
TSPGLPYTQQ GLRRTDLLNF ITAKMTPQLD YAHSKLVIGV YDDVVYQSFL
2010 2020 2030 2040 2050
KDEIRPIEKI HEAKTRIVDV PPFAHCIWGR QLLGRFASKF QTKPGLELGS
2060 2070 2080 2090 2100
AIGTDPDVDW TRYAVELSGF NYVYDVDYSN FDASHSTAMF ECLINNFFTE
2110 2120 2130 2140 2150
QNGFDRRIAE YLRSLAVSRH AYEDRRVLIR GGLPSGCAAT SMLNTIMNNV
2160 2170 2180 2190 2200
IIRAALYLTY SNFDFDDIKV LSYGDDLLIG TNYQIDFNLV KERLAPFGYK
2210 2220 2230 2240 2250
ITPANKTTTF PLTSHLQDVT FLKRRFVRFN SYLFRPQMDA VNLKAMVSYC
2260 2270 2280 2290 2300
KPGTLKEKLM SIALLAVHSG PDIYDEIFLP FRNVGIVVPT YSSMLYRWLS
LFR
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M16020 Genomic RNA Translation: AAA47930.1 |
PIRi | A29535, GNNYTM |
Similar proteinsi
Cross-referencesi
Web resourcesi
Virus Particle ExploreR db Icosahedral capsid structure |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M16020 Genomic RNA Translation: AAA47930.1 |
PIRi | A29535, GNNYTM |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1TMF | X-ray | 3.50 | 1 | 647-922 | [»] | |
2 | 148-414 | [»] | ||||
3 | 415-646 | [»] | ||||
SMRi | P08544 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein family/group databases
MEROPSi | C03.010 |
Miscellaneous databases
EvolutionaryTracei | P08544 |
Family and domain databases
CDDi | cd00205, rhv_like, 3 hits |
Gene3Di | 2.40.10.10, 1 hit 2.60.120.20, 3 hits 3.30.70.270, 2 hits 4.10.90.10, 1 hit |
InterProi | View protein in InterPro IPR015031, Capsid_VP4_Picornavir 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 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 PF08935, VP4_2, 1 hit |
PRINTSi | PR00918, CALICVIRUSNS |
SUPFAMi | SSF50494, SSF50494, 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_TMEVB | |
Accessioni | P08544Primary (citable) accession number: P08544 Secondary accession number(s): Q88583 Q88592 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1988 |
Last sequence update: | August 1, 1988 | |
Last modified: | February 23, 2022 | |
This is version 178 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
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families