UniProtKB - Q66765 (POLG_EMCVR)
Genome polyprotein
Functioni
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 | 1673 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1707 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1786 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 2067 | For RdRp activityBy similarity | 1 | |
Active sitei | 2165 | For RdRp activityBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 10 – 22 | By similarityAdd BLAST | 13 | |
Nucleotide bindingi | 1313 – 1320 | ATPPROSITE-ProRule annotation | 8 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- 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 RIG-I activity Source: UniProtKB
- suppression by virus of host translation Source: UniProtKB
- 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 | C03.009 |
Names & Taxonomyi
Protein namesi | Recommended name: Genome polyproteinCleaved into the following 13 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 E Protein 3D Short name: 3D |
Organismi | Encephalomyocarditis virus (strain Rueckert) (EMCV) |
Taxonomic identifieri | 650129 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Pisuviricota › Pisoniviricetes › Picornavirales › Picornaviridae › Cardiovirus › |
Virus hosti | Homo sapiens (Human) [TaxID: 9606] Mus musculus (Mouse) [TaxID: 10090] Sigmodon hispidus (Hispid cotton rat) [TaxID: 42415] Sus scrofa (Pig) [TaxID: 9823] |
Proteomesi |
|
Subcellular locationi
- Virion By similarity
- Host cytoplasm Curated
- Virion By similarity
- Host cytoplasm Curated
- Virion By similarity
- Host cytoplasm Curated
- host nucleolus 2 Publications
- 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, VirionPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 19 | C → A: Complete loss of inhibitory activity of nucleocytoplasmic transport. 2 Publications | 1 | |
Mutagenesisi | 35 | K → Q: 25% loss of 2A-Leader interaction. 1 Publication | 1 | |
Mutagenesisi | 37 | D → A: 30% loss of 2A-Leader interaction. 1 Publication | 1 | |
Mutagenesisi | 40 | W → A: 20% loss of 2A-Leader interaction. 1 Publication | 1 | |
Mutagenesisi | 41 | Y → F: No effect on the inhibitory activity of nucleocytoplasmic transport. 1 Publication | 1 | |
Mutagenesisi | 47 | T → A: No effect on the inhibitory activity of nucleocytoplasmic transport. 1 Publication | 1 | |
Mutagenesisi | 993 – 994 | YY → AA: 5-10 fold decreased viral growth. 1 Publication | 2 | |
Mutagenesisi | 996 | R → A: No effect on viral growth. 1 Publication | 1 | |
Mutagenesisi | 998 | R → E: 5-10 fold decreased viral growth. 1 Publication | 1 | |
Mutagenesisi | 1006 | Q → A: No effect on viral growth. 1 Publication | 1 | |
Mutagenesisi | 1035 | L → A: Complete loss of interaction with host EIF4E. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000446100 | 1 – 2292 | Genome polyproteinAdd BLAST | 2292 | |
ChainiPRO_0000423146 | 1 – 67 | Leader proteinAdd BLAST | 67 | |
ChainiPRO_0000423147 | 68 – 393 | Capsid protein VP0Add BLAST | 326 | |
ChainiPRO_5000143569 | 68 – 137 | Capsid protein VP4Add BLAST | 70 | |
ChainiPRO_5000143570 | 138 – 393 | Capsid protein VP2Add BLAST | 256 | |
ChainiPRO_5000143571 | 394 – 624 | Capsid protein VP3Add BLAST | 231 | |
ChainiPRO_5000143572 | 625 – 901 | Capsid protein VP1Add BLAST | 277 | |
ChainiPRO_5000143573 | 902 – 1044 | Protein 2AAdd BLAST | 143 | |
ChainiPRO_5000143574 | 1045 – 1194 | Protein 2BAdd BLAST | 150 | |
ChainiPRO_5000143575 | 1195 – 1519 | Protein 2CAdd BLAST | 325 | |
ChainiPRO_5000143576 | 1520 – 1607 | Protein 3AAdd BLAST | 88 | |
ChainiPRO_0000423148 | 1608 – 1627 | VPgAdd BLAST | 20 | |
ChainiPRO_5000143577 | 1628 – 1832 | Protease 3CAdd BLAST | 205 | |
ChainiPRO_5000143578 | 1833 – 2292 | RNA-directed RNA polymeraseAdd BLAST | 460 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 41 | Phosphotyrosine; by host SYK1 Publication | 1 | |
Modified residuei | 47 | Phosphothreonine; by host CK21 Publication | 1 | |
Lipidationi | 68 | N-myristoyl glycine; by hostBy similarity | 1 | |
Modified residuei | 1610 | O-(5'-phospho-RNA)-tyrosineBy similarity | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 137 – 138 | CleavageSequence analysis | 2 | |
Sitei | 393 – 394 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 624 – 625 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 901 – 902 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1044 – 1045 | Cleavage; by ribosomal skipBy similarity | 2 | |
Sitei | 1194 – 1195 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1519 – 1520 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1607 – 1608 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1627 – 1628 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1832 – 1833 | Cleavage; by protease 3CBy similarity | 2 |
Keywords - PTMi
Covalent protein-RNA linkage, Lipoprotein, Myristate, PhosphoproteinPTM databases
iPTMneti | Q66765 |
Interactioni
Subunit structurei
Interacts with host TRIM22; this interaction leads to the ubiquitination of protease 3C and may restrict the virus replication (By similarity).
By similarityInteracts with host RAN; the complex L-RAN recruits cellular kinases responsible for the L-induced nucleocytoplasmic trafficking inhibition (PubMed:16888036). The complex L-RAN can further bind to the host exportins XPO1/CRM1 and CSE1L/CAS (PubMed:26492198).
Interacts with the protein 2A (PubMed:25210192).
3 PublicationsInteracts 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 | 1281 – 1447 | SF3 helicasePROSITE-ProRule annotationAdd BLAST | 167 | |
Domaini | 1630 – 1822 | Peptidase C3PROSITE-ProRule annotationAdd BLAST | 193 | |
Domaini | 2061 – 2179 | RdRp catalyticPROSITE-ProRule annotationAdd BLAST | 119 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 37 – 61 | AcidicCuratedAdd BLAST | 25 | |
Regioni | 1030 – 1036 | Host EIF4E binding1 Publication | 7 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 995 – 1003 | Nuclear localization signal1 Publication | 9 |
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 10 – 22 | By similarityAdd BLAST | 13 |
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 IPR021573, Leader_pept_picornaV 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 IPR037243, Viral_lead_polypep_zc_finger |
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 PF11475, VP_N-CPKC, 1 hit |
PRINTSi | PR00918, CALICVIRUSNS |
SUPFAMi | SSF144251, SSF144251, 1 hit 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 |
s (2)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsiribosomal frameshifting. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MATTMEQETC AHSLTFEECP KCSALQYRNG FYLLKYDEEW YPEELLTDGE
60 70 80 90 100
DDVFDPELDM EVVFELQGNS TSSDKNNSSS EGNEGVIINN FYSNQYQNSI
110 120 130 140 150
DLSANAAGSD PPRTYGQFSN LFSGAVNAFS NMLPLLADQN TEEMENLSDR
160 170 180 190 200
VSQDTAGNTV TNTQSTVGRL VGYGTVHDGE HPASCADTAS EKILAVERYY
210 220 230 240 250
TFKVNDWTST QKPFEYIRIP LPHVLSGEDG GVFGAALRRH YLVKTGWRVQ
260 270 280 290 300
VQCNASQFHA GGLLVFMAPE YPTLDAFAMD NRWSKDNLPN GTRTQTNKKG
310 320 330 340 350
PFAMDHQNFW QWTLYPHQFL NLRTNTTVDL EVPYVNIAPT SSWTQHASWT
360 370 380 390 400
LVIAVVAPLT YSTGASTSLD ITASIQPVRP VFNGLRHETL SRQSPIPVTI
410 420 430 440 450
REHAGTWYST LPDSTVPIYG KTPVAPSNYM VGEYKDFLEI AQIPTFIGNK
460 470 480 490 500
IPNAVPYIEA SNTAVKTQPL ATYQVTLSCS CLANTFLAAL SRNFAQYRGS
510 520 530 540 550
LVYTFVFTGT AMMKGKFLIA YTPPGAGKPT SRDQAMQATY AIWDLGLNSS
560 570 580 590 600
YSFTVPFISP THFRMVGTDQ VNITNADGWV TVWQLTPLTY PPGCPTSAKI
610 620 630 640 650
LTMVSAGKDF SLKMPISPAP WSPQGVENAE KGVTENTNAT ADFVAQPVYL
660 670 680 690 700
PENQTKVAFF YNRSSPIGAF TVKSGSLESG FAPFSNGTCP NSVILTPGPQ
710 720 730 740 750
FDPAYDQLRP QRLTEIWGNG NEETSKVFPL KSKQDYSFCL FSPFVYYKCD
760 770 780 790 800
LEVTLSPHTS GNHGLLVRWC PTGTPTKPTT QVLHEVSSLS EGRTPQVYSA
810 820 830 840 850
GPGISNQISF VVPYNSPLSV LSAVWYNGHK RFDNTGSLGI APNSDFGTLF
860 870 880 890 900
FAGTKPDIKF TVYLRYKNKR VFCPRPTVFF PWPTSGDKID MTPRAGVLML
910 920 930 940 950
ESPNALDISR TYPTLHVLIQ FNHRGLEVRL FRHGHFWAET RADVILRSKT
960 970 980 990 1000
KQVSFLSNGN YPSMDSRAPW NPWKNTYQAV LRAEPCRVTM DIYYKRVRPF
1010 1020 1030 1040 1050
RLPLVQKEWP VREENVFGLY RIFNAHYAGY FADLLIHDIE TNPGPFMFRP
1060 1070 1080 1090 1100
RKQVFQTQGA AVSSMAQTLL PNDLASKAMG SAFTALLDAN EDAQKAMKII
1110 1120 1130 1140 1150
KTLSSLSDAW ENVKETLNNP EFWKQLLSRC VQLIAGMTIA VMHPDPLTLL
1160 1170 1180 1190 1200
CLGTLTAAEI TSQTSLCEEI AAKFKTIFIT PPPRFPTISL FQQQSPLKQV
1210 1220 1230 1240 1250
NDIFSLAKNL DWAVKTVEKV VDWFGTWIVQ EEKEQTLDQL LQRFPEHAKR
1260 1270 1280 1290 1300
ISDLRNGMAA YVECKESFDF FEKLYNQAVK EKRTGIAAVC EKFRQKHDHA
1310 1320 1330 1340 1350
TARCEPVVIV LRGDAGQGKS LSSQVIAQAV SKTIFGRQSV YSLPPDSDFF
1360 1370 1380 1390 1400
DGYENQFAAI MDDLGQNPDG SDFTTFCQMV STTNFLPNMA SLERKGTPFT
1410 1420 1430 1440 1450
SQLVVATTNL PEFRPVTIAH YPAVERRITF DYSVSAGPVC SKTEAGYKVL
1460 1470 1480 1490 1500
DVERAFRPTG EAPLPCFQNN CLFLEKAGLQ FRDNRTKEII SLVDVIERAV
1510 1520 1530 1540 1550
ARIERKKKVL TTVQTLVAQG PVDEVSFHSV VQQLKARQQA TDEQLEELQE
1560 1570 1580 1590 1600
AFAKVQERNS VFSDWLKISA MLCAATLALS QVVKMAKAVK QMVKPDLVRV
1610 1620 1630 1640 1650
QLDEQEQGPY NETARVKPKT LQLLDIQGPN PVMDFEKYVA KHVTAPIGFV
1660 1670 1680 1690 1700
YPTGVSTQTC LLVRGRTLVV NRHMAESDWT SIVVRGVTHA RSTVKILAIA
1710 1720 1730 1740 1750
KAGKETDVSF IRLSSGPLFR DNTSKFVKAG DVLPTGAAPV TGIMNTDIPM
1760 1770 1780 1790 1800
MYTGTFLKAG VSVPVETGQT FNHCIHYKAN TRKGWCGSAL LADLGGSKKI
1810 1820 1830 1840 1850
LGIHSAGSMG IAAASIVSQE MIRAVVNAFE PQGALERLPD GPRIHVPRKT
1860 1870 1880 1890 1900
ALRPTVARQV FQPAYAPAVL SKFDPRTEAD VDEVAFSKHT SNQESLPPVF
1910 1920 1930 1940 1950
RMVAKEYANR VFTLLGKDNG RLTVKQALEG LEGMDPMDRN TSPGLPYTAL
1960 1970 1980 1990 2000
GMRRTDVVDW ESATLIPFAA ERLRKMNEGD FSEVVYQTFL KDELRPIEKV
2010 2020 2030 2040 2050
QAAKTRIVDV PPFEHCILGR QLLGKFASKF QTQPGLELGS AIGCDPDVHW
2060 2070 2080 2090 2100
TAFGVAMQGF ERVYDVDYSN FDSTHSVAMF RLLAEEFFTP ENGFDPLTRE
2110 2120 2130 2140 2150
YLESLAISTH AFEEKRFLIT GGLPSGCAAT SMLNTIMNNI IIRAGLYLTY
2160 2170 2180 2190 2200
KNFEFDDVKV LSYGDDLLVA TNYQLDFDKV RASLAKTGYK ITPANTTSTF
2210 2220 2230 2240 2250
PLNSTLEDVV FLKRKFKKEG PLYRPVMNRE ALEAMLSYYR PGTLSEKLTS
2260 2270 2280 2290
ITMLAVHSGK QEYDRLFAPF REVGVVVPSF ESVEYRWRSL FW
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M81861 Genomic RNA Translation: AAA43037.1 |
RefSeqi | NP_056777.1, NC_001479.1 |
Genome annotation databases
GeneIDi | 1493923 |
KEGGi | vg:1493923 |
Keywords - Coding sequence diversityi
Ribosomal frameshiftingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M81861 Genomic RNA Translation: AAA43037.1 |
RefSeqi | NP_056777.1, NC_001479.1 |
3D structure databases
SMRi | Q66765 |
ModBasei | Search... |
Protein family/group databases
MEROPSi | C03.009 |
PTM databases
iPTMneti | Q66765 |
Genome annotation databases
GeneIDi | 1493923 |
KEGGi | vg:1493923 |
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 IPR021573, Leader_pept_picornaV 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 IPR037243, Viral_lead_polypep_zc_finger |
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 PF11475, VP_N-CPKC, 1 hit |
PRINTSi | PR00918, CALICVIRUSNS |
SUPFAMi | SSF144251, SSF144251, 1 hit 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 |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | POLG_EMCVR | |
Accessioni | Q66765Primary (citable) accession number: Q66765 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 24, 2013 |
Last sequence update: | November 1, 1996 | |
Last modified: | April 7, 2021 | |
This is version 127 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