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Protein

Genome polyprotein

Gene
N/A
Organism
Human enterovirus 71 (strain 7423/MS/87) (Ev 71)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Capsid protein VP1: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome. Capsid protein VP1 mainly forms the vertices of the capsid. Capsid protein VP1 interacts with host cell receptor to provide virion attachment to target host cells. This attachment induces virion internalization. Tyrosine kinases are probably involved in the entry process. After binding to its receptor, the capsid undergoes conformational changes. Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized. Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm. After genome has been released, the channel shrinks (By similarity).By similarity
Capsid protein VP2: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).By similarity
Capsid protein VP3: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity).By similarity
Capsid protein VP4: Lies on the inner surface of the capsid shell. After binding to the host receptor, the capsid undergoes conformational changes. 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. After genome has been released, the channel shrinks (By similarity).By similarity
Capsid protein VP0: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation. Allows the capsid to remain inactive before the maturation step (By similarity).By similarity
Protein 2A: Cysteine protease that cleaves viral polyprotein and specific host proteins. It is responsible for the cleavage between the P1 and P2 regions, first cleavage occurring in the polyprotein. Cleaves also the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA translation. Inhibits the host nucleus-cytoplasm protein and RNA trafficking by cleaving host members of the nuclear pores (By similarity).By similarity
Protein 2B: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cyctoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication (By similarity).By similarity
Protein 2C: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3 (By similarity).By similarity
Protein 3AB: Localizes the viral replication complex to the surface of membranous vesicles. Together with protein 3CD binds the Cis-Active RNA Element (CRE) which is involved in RNA synthesis initiation. Acts as a cofactor to stimulate the activity of 3D polymerase, maybe through a nucleid acid chaperone activity (By similarity).By similarity
Protein 3A: Localizes the viral replication complex to the surface of membranous vesicles. It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the dissassembly of the Golgi complex, possibly through GBF1 interaction. This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity).By similarity
Viral protein genome-linked: acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome. VPg may be removed in the cytoplasm by an unknown enzyme termed "unlinkase". VPg is not cleaved off virion genomes because replicated genomic RNA are encapsidated at the site of replication (By similarity).By similarity
Protein 3CD: Is involved in the viral replication complex and viral polypeptide maturation. It exhibits protease activity with a specificity and catalytic efficiency that is different from protease 3C. Protein 3CD lacks polymerase activity. The 3C domain in the context of protein 3CD may have an RNA binding activity (By similarity).By similarity
Protease 3C: cleaves host DDX58/RIG-I and thus contributes to the inhibition of type I interferon production. Cleaves also host PABPC1 (By similarity).By similarity
RNA-directed RNA polymerase: Replicates the viral genomic RNA on the surface of intracellular membranes. May form linear arrays of subunits that propagate along a strong head-to-tail interaction called interface-I. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss+RNA genomes are either translated, replicated or encapsidated (By similarity).PROSITE-ProRule annotation

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).PROSITE-ProRule annotation
Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein.
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.
NTP + H2O = NDP + phosphate.

Enzyme regulationi

RNA-directed RNA polymerase: replication or transcription is subject to high level of random mutations by the nucleotide analog ribavirin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei883For Protease 2A activityBy similarity1
Active sitei901For Protease 2A activityBy similarity1
Active sitei972For Protease 2A activityBy similarity1
Active sitei1588For Protease 3C activitySequence analysis1
Active sitei1619For Protease 3C activitySequence analysis1
Active sitei1695For Protease 3C activityBy similarity1
Active sitei2060For RdRp activityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi1240 – 1247ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel

Keywords - Biological processi

Activation of host autophagy by virus, Clathrin-mediated endocytosis of virus by host, DNA replication, Eukaryotic host gene expression shutoff by virus, Eukaryotic host translation shutoff by virus, Host gene expression shutoff by virus, Host mRNA suppression by virus, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host mRNA nuclear export by virus, Inhibition of host RIG-I by virus, Inhibition of host RLR pathway by virus, Ion transport, Pore-mediated penetration of viral genome into host cell, Transport, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Viral RNA replication, Virus endocytosis by host, Virus entry into host cell

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Protein family/group databases

MEROPSiN08.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved into the following 17 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
Protease 2A (EC:3.4.22.29)
Short name:
P2A
Alternative name(s):
Picornain 2A
Protein 2A
Protein 2B
Short name:
P2B
Protein 2C (EC:3.6.1.15)
Short name:
P2C
Protein 3A
Short name:
P3A
Alternative name(s):
Protein 3B
Short name:
P3B
Protease 3C (EC:3.4.22.28)
Short name:
P3C
Alternative name(s):
3D polymerase
Short name:
3Dpol
Protein 3D
Short name:
3D
OrganismiHuman enterovirus 71 (strain 7423/MS/87) (Ev 71)
Taxonomic identifieri103922 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus A
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000008117 Componenti: Genome

Subcellular locationi

Capsid protein VP0 :
Capsid protein VP4 :
Capsid protein VP2 :
Capsid protein VP3 :
Capsid protein VP1 :
Protein 2B :
Protein 2C :
Protein 3A :
Protein 3AB :
Protease 3C :
Protein 3CD :
RNA-directed RNA polymerase :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini2 – 1503CytoplasmicSequence analysisAdd BLAST1502
Intramembranei1504 – 1519Sequence analysisAdd BLAST16
Topological domaini1520 – 2193CytoplasmicSequence analysisAdd BLAST674

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Membrane, T=pseudo3 icosahedral capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostBy similarity
ChainiPRO_00004261502 – 2193Genome polyproteinBy similarityAdd BLAST2192
ChainiPRO_00004261512 – 862P1By similarityAdd BLAST861
ChainiPRO_00004261522 – 323Capsid protein VP0Sequence analysisAdd BLAST322
ChainiPRO_00004261532 – 69Capsid protein VP4Sequence analysisAdd BLAST68
ChainiPRO_000042615470 – 323Capsid protein VP2Sequence analysisAdd BLAST254
ChainiPRO_0000426155324 – 567Capsid protein VP3Sequence analysisAdd BLAST244
ChainiPRO_0000426156568 – 862Capsid protein VP1Sequence analysisAdd BLAST295
ChainiPRO_0000426157863 – 1440P2By similarityAdd BLAST578
ChainiPRO_0000039496863 – 1012Protease 2ASequence analysisAdd BLAST150
ChainiPRO_00000394971013 – 1111Protein 2BSequence analysisAdd BLAST99
ChainiPRO_00000394981112 – 1440Protein 2CSequence analysisAdd BLAST329
ChainiPRO_00004261581441 – 2193P3By similarityAdd BLAST753
ChainiPRO_00004261591441 – 1548Protein 3ABSequence analysisAdd BLAST108
ChainiPRO_00000394991441 – 1526Protein 3ASequence analysisAdd BLAST86
ChainiPRO_00004261601527 – 1548Viral protein genome-linkedSequence analysisAdd BLAST22
ChainiPRO_00004261611549 – 2193Protein 3CDSequence analysisAdd BLAST645
ChainiPRO_00004261621549 – 1730Protease 3CSequence analysisAdd BLAST182
ChainiPRO_00004261631731 – 2193RNA-directed RNA polymeraseBy similarityAdd BLAST463

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostBy similarity1
Modified residuei1529O-(5'-phospho-RNA)-tyrosineBy similarity1

Post-translational modificationi

Specific enzymatic cleavages in vivo by the viral proteases yield a variety of precursors and mature proteins. Polyprotein processing intermediates such as VP0 which is a VP4-VP2 precursor are produced. During virion maturation, non-infectious particles are rendered infectious following cleavage of VP0. This maturation cleavage is followed by a conformational change of the particle (By similarity).By similarity
VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity).By similarity
Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle.By similarity
Capsid protein VP0: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion (By similarity).By similarity
Genome polyprotein: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins.By similarity
Capsid protein VP0: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion (By similarity).By similarity
Viral protein genome-linked: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei323 – 324Cleavage; by Protease 3CSequence analysis2
Sitei862 – 863Cleavage; by Protease 2ASequence analysis2
Sitei1012 – 1013Cleavage; by Protease 3CSequence analysis2
Sitei1440 – 1441Cleavage; by Protease 3CSequence analysis2
Sitei1526 – 1527Cleavage; by Protease 3CSequence analysis2
Sitei1548 – 1549Cleavage; by Protease 3CSequence analysis2
Sitei1731 – 1732Cleavage; by Protease 3CSequence analysis2

Keywords - PTMi

Covalent protein-RNA linkage, Lipoprotein, Myristate, Phosphoprotein

Interactioni

Subunit structurei

Capsid protein VP1: Interacts with capsid protein VP0, and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid (By similarity). Capsid protein VP0: interacts with capsid protein VP1 and capsid protein VP3 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Capsid protein VP2: Interacts with capsid protein VP1 and capsid protein VP3 in the mature capsid (By similarity). Capsid protein VP3: interacts with capsid protein VP0 and capsid protein VP1 to form heterotrimeric protomers. Five protomers subsequently associate to form pentamers which serve as building blocks for the capsid. Interacts with capsid protein VP4 in the mature capsid (By similarity). Capsid protein VP4: Interacts with capsid protein VP1 and capsid protein VP3 (By similarity). Protein 2C: interacts with capsid protein VP3; this interaction may be important for virion morphogenesis (By similarity). Protein 3AB: interacts with protein 3CD (By similarity). Viral protein genome-linked: interacts with RNA-directed RNA polymerase (By similarity). Protein 3CD: interacts with protein 3AB and with RNA-directed RNA polymerase. RNA-directed RNA polymerase: interacts with viral protein genome-linked and with protein 3CD (By similarity).By similarity

Structurei

Secondary structure

12193
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi869 – 881Combined sources13
Helixi882 – 884Combined sources3
Helixi887 – 891Combined sources5
Beta strandi893 – 897Combined sources5
Turni898 – 901Combined sources4
Beta strandi902 – 912Combined sources11
Beta strandi922 – 927Combined sources6
Turni928 – 931Combined sources4
Beta strandi932 – 937Combined sources6
Beta strandi941 – 946Combined sources6
Beta strandi954 – 964Combined sources11
Beta strandi975 – 978Combined sources4
Beta strandi981 – 990Combined sources10
Beta strandi993 – 998Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3W95X-ray1.85A863-1012[»]
ProteinModelPortaliQ66479.
SMRiQ66479.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1216 – 1374SF3 helicasePROSITE-ProRule annotationAdd BLAST159
Domaini1549 – 1714Peptidase C3Add BLAST166
Domaini1958 – 2073RdRp catalyticPROSITE-ProRule annotationAdd BLAST116

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni568 – 588Amphipatic alpha-helixSequence analysisAdd BLAST21
Regioni1441 – 1463DisorderedBy similarityAdd BLAST23

Sequence similaritiesi

Belongs to the picornaviruses polyprotein family.Curated
Contains 1 peptidase C3 domain.Curated
Contains 1 RdRp catalytic domain.PROSITE-ProRule annotation
Contains 1 SF3 helicase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

CDDicd00205. rhv_like. 3 hits.
Gene3Di2.60.120.20. 3 hits.
3.40.50.300. 1 hit.
4.10.80.10. 2 hits.
InterProiIPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR014838. P3A.
IPR000081. Peptidase_C3.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR009003. Peptidase_S1_PA.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF08727. P3A. 1 hit.
PF00548. Peptidase_C3. 1 hit.
PF02226. Pico_P1A. 1 hit.
PF00947. Pico_P2A. 1 hit.
PF01552. Pico_P2B. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 3 hits.
PF00910. RNA_helicase. 1 hit.
[Graphical view]
ProDomiPD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF89043. SSF89043. 1 hit.
PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q66479-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSQVSTQRS GSHENSNSAT EGSTINYTTI NYYKDSYAAT AGKQSLKQDP
60 70 80 90 100
DKFANPVKDI FTEMAAPLKS PSAEACGYSD RVAQLTIGNS TITTQEAANI
110 120 130 140 150
IVGYGEWPSY CSDDDATAVD KPTRPDVSVN RFYTLDTKLW EKSSKGWYWK
160 170 180 190 200
FPDVLTETGV FGQNAQFHYL YRSGFCIHVQ CNASKFHQGA LLVAILPEYV
210 220 230 240 250
IGTVAGGTGT EDSHPPYKQT QPGADGFELQ HPYVLDAGIP ISQLTVCPHQ
260 270 280 290 300
WINLRTNNCA TIIVPYMNTL PFDSALNHCN FGLLVVPISP LDFDQGATPV
310 320 330 340 350
IPITITLAPM CSEFGGLRQA VTQGFPTELK PGTNQFLTTD DGVSAPILPN
360 370 380 390 400
FHPTPCIHIP GEVRNLLELC QVETILEVNN VPTNATSLME RLRFPVSAQA
410 420 430 440 450
GKGELCAVFR ADPGRDGPWQ STMLGQLCGY YTQWSGSLEV TFMFTGSFMA
460 470 480 490 500
TGKMLIAYTP PGGPLPKDRA TAMLGTHVIW DFGLQSSVTL VIPWISNTHY
510 520 530 540 550
RAHARDGVFD YYTTGLVSIW YQTNYVVPIG APNTAYILAL AAAQKNFTMK
560 570 580 590 600
LCKDTSHILQ TASIQGDRVA DVIESSIGDS VSRALTQALP APTGQNTQVS
610 620 630 640 650
SHRLDTGEVP ALQAAEIGAS SNTSDESMIE TRCVLNSHST AETTLDSFFS
660 670 680 690 700
RAGLVGEIDL PLEGTTNPNG YANWDIDITG YAQMRRKVEL FTYMRFDAEF
710 720 730 740 750
TFVACTPTGE VVPQLLQYMF VPPGAPKPES RESLAWQTAT NPSVFVKLTD
760 770 780 790 800
PPAQVSVPFM SPASAYQWFY DGYPTFGEHK QEKDLEYGAC PNNMMGTFSV
810 820 830 840 850
RTVGSSKSKY PLVVRIYMRM KHVRAWIPRP MRNQNYLFKA NPNYAGNSIK
860 870 880 890 900
PTGTSRNAIT TLGKFGQQSG AIYVGNFRVV NRHLATHNDW ANLVWEDSSR
910 920 930 940 950
DLLVSSTTAQ GCDTIARCNC QTGVYYCNSK RKHYPVSFSK PSLIYVEASE
960 970 980 990 1000
YYPARYQSHL MLAAGHSESG DCGGILRCQH GVVGIASTGG NGLVGFADVR
1010 1020 1030 1040 1050
DLLWLDEEAM EQGVSDYIKG LGDAFGTGFT DAVSREVEAL RNHLIGSDGA
1060 1070 1080 1090 1100
VEKILKNLIK LISALVIVIR SDYDMVTLTA TLALIGCHGS PWAWIKAKTA
1110 1120 1130 1140 1150
SILGIPIAQK QSASWLKKFN DMASAAKGLE WISNKISKFI DWLREKIVPA
1160 1170 1180 1190 1200
AKEKAEFLTN LKQFPLLENQ ITHLEQSAAS QEDLEAMFGN VSYLAHFCRK
1210 1220 1230 1240 1250
FQPLYATEAK RVYVLEKRMN NYMQFKSTHR IEPVCLIIRG SPGTGKSLAT
1260 1270 1280 1290 1300
GIIARAIADK YHSSVYSLPP DPDHFDGYKQ QVVTVMDDLC QNPDGKDMSL
1310 1320 1330 1340 1350
FYQMVSTVDI IPPMASLEEK GVSFTSKFVI ASTNASNIIV PTVSDSDAIR
1360 1370 1380 1390 1400
RRFYMDCDIE VTDSSKTDLG RLDAGRAAKL CSENNTANFK RCSPLVCGKA
1410 1420 1430 1440 1450
IQLRDRKSKV RYSVDTVVSE LIREYNSRSA IGNTIEALFQ GPPKFRPIRI
1460 1470 1480 1490 1500
SLEEKPAPDA ISDLLASVDS EEVRQYCREQ GWIIPETPTN VERHLNRAVL
1510 1520 1530 1540 1550
VMQSIATVVA VVSLVYVIYK LFAGFQGAYS GAPNQVLKKP VLRTATVQGP
1560 1570 1580 1590 1600
SLDFALSLLR RNIRQVQTDQ GHFTMLGVRD RLAVLPRHSQ PGKTIWVEHK
1610 1620 1630 1640 1650
LVNILDAAEL VDEQGVNLEL TLVTLDTNEK FRDITKFIPE TISGASDATL
1660 1670 1680 1690 1700
VINTEHMPSM FVPVGDVVQY GFLNLSGKPT HRTMMYNFPT KAGQCGGVVT
1710 1720 1730 1740 1750
SVGKIIGIHI GGNGRQGFCA GLKRSYFASE QGEIQWVKSN KETGRLNING
1760 1770 1780 1790 1800
PTRTKLEPSV FHDVFEANKE PAVLTSKDPR LEVDFEQALF SKYVGNVLHE
1810 1820 1830 1840 1850
PDEYVHQAAL HYANQLKQLD INTKKMSMEE ACYGTDNLEA IDLHTSAGYP
1860 1870 1880 1890 1900
YSALGIKKRD ILDPATRDVS KMKSYMDKYG LDLPYSTYVK DELRSLDKIK
1910 1920 1930 1940 1950
KGKSRLIEAS SLNDSVYLRM TFGHLYEVFH ANPGTVTGSA VGCNPDVFWS
1960 1970 1980 1990 2000
KLPILLPGSL FAFDYSGYDA SLSPVWFRAL EVVLREIGYS EEAVSLIEGI
2010 2020 2030 2040 2050
NHTHHIYRNK TYCVLGGMPS GCSGTSIFNS MINNIIIRTL LIKTFKGIDL
2060 2070 2080 2090 2100
DELNMVAYGD DVLASYPFPI DCLELAKTGK EYGLTMTPAG KSPCFNEVTW
2110 2120 2130 2140 2150
ENATFLKRGF LPDHQFPFLI HPTMPMKEIH ESIRWTKDAR NTQDHVRSLC
2160 2170 2180 2190
LLAWHNGKDE YEKFVSTIRS VPVGKALAIP NFENLRRNWL ELF
Length:2,193
Mass (Da):242,657
Last modified:January 23, 2007 - v3
Checksum:i35E1B3CFF88A50EF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22522 Genomic RNA. Translation: AAB39969.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22522 Genomic RNA. Translation: AAB39969.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3W95X-ray1.85A863-1012[»]
ProteinModelPortaliQ66479.
SMRiQ66479.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiN08.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

CDDicd00205. rhv_like. 3 hits.
Gene3Di2.60.120.20. 3 hits.
3.40.50.300. 1 hit.
4.10.80.10. 2 hits.
InterProiIPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR014838. P3A.
IPR000081. Peptidase_C3.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR009003. Peptidase_S1_PA.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR033703. Rhv-like.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF08727. P3A. 1 hit.
PF00548. Peptidase_C3. 1 hit.
PF02226. Pico_P1A. 1 hit.
PF00947. Pico_P2A. 1 hit.
PF01552. Pico_P2B. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 3 hits.
PF00910. RNA_helicase. 1 hit.
[Graphical view]
ProDomiPD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50494. SSF50494. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF89043. SSF89043. 1 hit.
PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_HE71M
AccessioniPrimary (citable) accession number: Q66479
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.