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O91734

- POLG_EC01F

UniProt

O91734 - POLG_EC01F

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Protein

Genome polyprotein

Gene
N/A
Organism
Echovirus 1 (strain Human/Egypt/Farouk/1951) (E-1)
Status
Reviewed - 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 integrin ITGA2/ITGB1 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)LengthDescriptionGraphical viewFeature identifierActions
Sitei69 – 702Cleavage; by autolysisSequence Analysis
Sitei330 – 3312Cleavage; by Protease 3CSequence Analysis
Active sitei871 – 8711For Protease 2A activityBy similarity
Active sitei889 – 8891For Protease 2A activityBy similarity
Active sitei960 – 9601For Protease 2A activityBy similarity
Sitei1000 – 10012Cleavage; by Protease 3CSequence Analysis
Sitei1428 – 14292Cleavage; by Protease 3CSequence Analysis
Sitei1517 – 15182Cleavage; by Protease 3CSequence Analysis
Sitei1539 – 15402Cleavage; by Protease 3CSequence Analysis
Active sitei1579 – 15791For Protease 3C activitySequence Analysis
Active sitei1610 – 16101For Protease 3C activitySequence Analysis
Active sitei1686 – 16861For Protease 3C activityBy similarity
Sitei1722 – 17232Cleavage; by Protease 3CSequence Analysis
Active sitei2051 – 20511For RdRp activityBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cysteine-type endopeptidase activity Source: InterPro
  3. ion channel activity Source: UniProtKB-KW
  4. RNA binding Source: UniProtKB-KW
  5. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  6. RNA helicase activity Source: InterPro
  7. structural molecule activity Source: InterPro

GO - Biological processi

  1. caveolin-mediated endocytosis of virus by host cell Source: UniProtKB-KW
  2. DNA replication Source: UniProtKB-KW
  3. induction by virus of host autophagy Source: UniProtKB
  4. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  5. pore-mediated entry of viral genome into host cell Source: UniProtKB-KW
  6. protein oligomerization Source: UniProtKB-KW
  7. RNA-protein covalent cross-linking Source: UniProtKB-KW
  8. suppression by virus of host gene expression Source: UniProtKB-KW
  9. suppression by virus of host mRNA export from nucleus Source: UniProtKB-KW
  10. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
  11. suppression by virus of host translation initiation factor activity Source: UniProtKB
  12. transcription, DNA-templated Source: InterPro
  13. viral RNA genome replication Source: InterPro
  14. virion attachment to host cell Source: UniProtKB-KW
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, Caveolin-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

MEROPSiC03.020.

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
OrganismiEchovirus 1 (strain Human/Egypt/Farouk/1951) (E-1)
Taxonomic identifieri103908 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusEnterovirus B
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000002694: Genome

Subcellular locationi

Chain Capsid protein VP0 : Virion By similarity. Host cytoplasm By similarity
Chain Capsid protein VP2 : Virion By similarity. Host cytoplasm By similarity
Chain Capsid protein VP3 : Virion By similarity. Host cytoplasm By similarity
Chain Capsid protein VP1 : Virion By similarity. Host cytoplasm By similarity
Chain Protein 2B : 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 derived from the endoplasmic reticulum.
Chain Protein 2C : 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 derived from the endoplasmic reticulum.
Chain Protein 3A : 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 derived from the endoplasmic reticulum.
Chain Protein 3AB : 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 derived from the endoplasmic reticulum.
Chain Protein 3CD : 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 derived from the endoplasmic reticulum.
Chain RNA-directed RNA polymerase : 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 derived from the endoplasmic reticulum.

GO - Cellular componenti

  1. host cell cytoplasmic vesicle Source: UniProtKB-KW
  2. integral to membrane of host cell Source: UniProtKB-KW
  3. membrane Source: UniProtKB-KW
  4. T=pseudo3 icosahedral viral capsid Source: UniProtKB-KW
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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by hostBy similarity
Chaini2 – 21842183Genome polyproteinBy similarityPRO_0000426356Add
BLAST
Chaini2 – 850849P1By similarityPRO_0000426357Add
BLAST
Chaini2 – 330329Capsid protein VP0Sequence AnalysisPRO_0000426358Add
BLAST
Chaini2 – 6968Capsid protein VP4Sequence AnalysisPRO_0000426359Add
BLAST
Chaini70 – 330261Capsid protein VP2Sequence AnalysisPRO_0000426360Add
BLAST
Chaini331 – 567237Capsid protein VP3Sequence AnalysisPRO_0000426361Add
BLAST
Chaini567 – 850284Capsid protein VP1Sequence AnalysisPRO_0000426362Add
BLAST
Chaini850 – 1428579P2By similarityPRO_0000426363Add
BLAST
Chaini850 – 1000151Protease 2ASequence AnalysisPRO_0000426364Add
BLAST
Chaini1001 – 109999Protein 2BSequence AnalysisPRO_0000039653Add
BLAST
Chaini1100 – 1428329Protein 2CSequence AnalysisPRO_0000039654Add
BLAST
Chaini1429 – 2184756P3By similarityPRO_0000426365Add
BLAST
Chaini1429 – 1539111Protein 3ABSequence AnalysisPRO_0000426366Add
BLAST
Chaini1429 – 151789Protein 3ASequence AnalysisPRO_0000039655Add
BLAST
Chaini1518 – 153922Viral protein genome-linkedSequence AnalysisPRO_0000426367Add
BLAST
Chaini1540 – 2184645Protein 3CDSequence AnalysisPRO_0000426368Add
BLAST
Chaini1540 – 1721182Protease 3CSequence AnalysisPRO_0000426369Add
BLAST
Chaini1722 – 2184463RNA-directed RNA polymeraseBy similarityPRO_0000426370Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity
Modified residuei1520 – 15201O-(5'-phospho-RNA)-tyrosineBy similarity

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

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). Interact with host integrin ITGA2/ITGB1 heterodimer. 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

1
2184
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74
Beta strandi26 – 294
Beta strandi33 – 353
Helixi36 – 383
Helixi51 – 544
Beta strandi57 – 593
Beta strandi83 – 864
Beta strandi91 – 966
Helixi103 – 1053
Turni113 – 1153
Helixi126 – 1283
Beta strandi138 – 1403
Beta strandi147 – 1515
Helixi153 – 1575
Helixi159 – 1679
Beta strandi168 – 18013
Beta strandi188 – 19710
Beta strandi203 – 2053
Helixi212 – 2143
Beta strandi225 – 2284
Helixi239 – 2413
Turni242 – 2454
Helixi248 – 2536
Beta strandi254 – 2607
Turni261 – 2633
Beta strandi265 – 2717
Beta strandi276 – 2805
Turni282 – 2843
Beta strandi288 – 29912
Beta strandi308 – 32417
Turni338 – 3414
Beta strandi353 – 3553
Helixi374 – 3774
Helixi390 – 3934
Helixi397 – 3993
Beta strandi400 – 4056
Beta strandi412 – 4176
Turni420 – 4223
Helixi424 – 4274
Helixi430 – 4356
Beta strandi438 – 4436
Beta strandi445 – 4539
Beta strandi460 – 4667
Helixi476 – 4816
Beta strandi482 – 4887
Beta strandi490 – 4923
Beta strandi494 – 4996
Beta strandi504 – 5063
Beta strandi508 – 5114
Helixi514 – 5163
Beta strandi520 – 5278
Beta strandi537 – 54711
Beta strandi552 – 5565
Helixi603 – 6053
Helixi613 – 6153
Helixi633 – 6375
Beta strandi641 – 65010
Helixi656 – 6583
Beta strandi659 – 6635
Helixi666 – 6683
Helixi671 – 6766
Beta strandi679 – 69618
Turni700 – 7034
Beta strandi710 – 7167
Helixi729 – 7324
Beta strandi734 – 7363
Beta strandi738 – 7425
Beta strandi748 – 7525
Beta strandi757 – 7637
Beta strandi767 – 7704
Turni771 – 7733
Beta strandi774 – 7785
Helixi779 – 7813
Beta strandi787 – 7926
Beta strandi801 – 81919
Beta strandi830 – 8323

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EV1X-ray3.551570-850[»]
277-330[»]
3331-569[»]
42-69[»]
ProteinModelPortaliO91734.
SMRiO91734. Positions 2-69, 77-1000, 1540-2184.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO91734.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 14941493CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini1511 – 2184674CytoplasmicSequence AnalysisAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei1495 – 151016Sequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1204 – 1360157SF3 helicasePROSITE-ProRule annotationAdd
BLAST
Domaini1540 – 1705166Peptidase C3Add
BLAST
Domaini1949 – 2065117RdRp catalyticPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni567 – 58317Amphipatic alpha-helixSequence AnalysisAdd
BLAST
Regioni1429 – 145224DisorderedBy similarityAdd
BLAST

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

Gene3Di2.60.120.20. 3 hits.
4.10.80.10. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR014838. P3A.
IPR000081. Peptidase_C3.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
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]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
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.

O91734-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MGAQVSTQKT GAHETSLSAT GNSIIHYTNI NYYKDAASNS ANRQDFTQDP
60 70 80 90 100
GKFTEPMKDV MIKTLPALNS PTVEECGYSD RVRSITLGNS TITTQECANV
110 120 130 140 150
VVGYGEWPEY LSDNEATAED QPTQPDVATC RFYTLDSVQW ENGSPGWWWK
160 170 180 190 200
FPDALRDMGL FGQNMYYHYL GRAGYTIHVQ CNASKFHQGC ILVVCVPEAE
210 220 230 240 250
MGSAQTSGVV NYEHISKGEI ASRFTTTTTA EDHGVQAAVW NAGMGVGVGN
260 270 280 290 300
LTIFPHQWIN LRTNNSATIV MPYVNSVPMD NMYRHHNFTL MIIPFVPLDF
310 320 330 340 350
SAGASTYVPI TVTVAPMCAE YNGLRLAGHQ GLPTMNTPGS NQFLTSDDFQ
360 370 380 390 400
SPSAMPQFDV TPEMHIPGEV RNLMEIAEVD SVMPINNDSA AKVSSMEAYR
410 420 430 440 450
VELSTNTNAG TQVFGFQLNP GAESVMNRTL MGEILNYYAH WSGSIKITFV
460 470 480 490 500
FCGSAMTTGK FLLSYAPPGA GAPKTRKDAM LGTHVVWDVG LQSSCVLCIP
510 520 530 540 550
WISQTHYRFV EKDPYTNAGF VTCWYQTSVV SPASNQPKCY MMCMVSACND
560 570 580 590 600
FSVRMLRDTK FIEQTSFYQG DVQNAVEGAM VRVADTVQTS ATNSERVPNL
610 620 630 640 650
TAVETGHTSQ AVPGDTMQTR HVINNHVRSE STIENFLARS ACVFYLEYKT
660 670 680 690 700
GTKEDSNSFN NWVITTRRVA QLRRKLEMFT YLRFDMEITV VITSSQDQST
710 720 730 740 750
SQNQNAPVLT HQIMYVPPGG PIPVSVDDYS WQTSTNPSIF WTEGNAPARM
760 770 780 790 800
SIPFISIGNA YSNFYDGWSH FSQAGVYGFT TLNNMGQLFF RHVNKPNPAA
810 820 830 840 850
ITSVARIYFK PKHVRAWVPR PPRLCPYINS TNVNFEPKPV TEVRTNIITT
860 870 880 890 900
GAFGQQSGAV YVGNYRVVNR HLATHIDWQN CVWEDYNRDL LVSTTTAHGC
910 920 930 940 950
DTIARCQCTT GVYFCLSRNK HYPVSFEGPG LVEVQESEYY PKRYQSHVLL
960 970 980 990 1000
AAGFSEPGDC GGILRCEHGV IGIVTMGGEG VVGFADVRDL LWLEDDAMEQ
1010 1020 1030 1040 1050
GVKDYVEQLG NAFGSGFTNQ ICEQVNLLKE SLVGQDSILE KSLKALVKII
1060 1070 1080 1090 1100
SALVIVVRNH DDLITVTATL ALIGCTSSPW RWLKQKVSQY YGIPMAERQN
1110 1120 1130 1140 1150
NGWLKKFTEM TNACKGMEWI AIKIQKFIEW LKVKILPEVK EKHEFLNRLK
1160 1170 1180 1190 1200
QLPLLESQIA TIEQSAPSQG DQEQLFSNVQ YFAHYCRKYA PLYAAEAKRV
1210 1220 1230 1240 1250
FSLEKKMSNY IQFKSKCRIE PVCLLLHGSP GAGKSVATNL IGRSLAEKLN
1260 1270 1280 1290 1300
SSVYSLPPDP DHFDGYKQQA VVIMDDLCQN PDGKDVSLFC QMVSSVDFVP
1310 1320 1330 1340 1350
PMAALEEKGI LFTSPFVLAS TNAGSINAPT VSDSRALARR FHFDMNIEVI
1360 1370 1380 1390 1400
SMYSQNGKIN MPMSVKTCDE DCCPVNFKKC CPLVCGKAIQ FIDRKTQVRY
1410 1420 1430 1440 1450
SLDMLVTEMF REYNHRHSVG ATLEALFQGP PVYREIKISV APETPPPPAI
1460 1470 1480 1490 1500
ADLLKSVDSE AVREYCKEKG WLVPEISSTL QIEKHVSRAF ICLQALTTFV
1510 1520 1530 1540 1550
SVAGIIYIIY KLFAGFQGAY TGMPNQKPKV PTLRQAKVQG PAFEFAVAMM
1560 1570 1580 1590 1600
KRNASTVKTE YGEFTMLGIY DRWAVLPRHA KPGPTILMND QEVGVLDAKE
1610 1620 1630 1640 1650
LVDKDGTNLE LTLLKLNRNE KFRDIRGFLA REEAEVNEAV LAINTSKFPN
1660 1670 1680 1690 1700
MYIPVGQVTD YGFLNLGGTP TKRMLMYNFP TRAGQCGGVL MSTGKVLGIH
1710 1720 1730 1740 1750
VGGNGHQGFS AALLRHYFNE EQGEIEFIES SKDAGFPVIN TPSKTKLEPS
1760 1770 1780 1790 1800
VFHQVFEGNK EPAVLRNGDP RLKVNFEEAI FSKYIGNVNT HVDEYMQEAV
1810 1820 1830 1840 1850
DHYAGQLATL DISTEPMKLE DAVYGTEGLE ALDLTTSAGY PYVALGIKKR
1860 1870 1880 1890 1900
DILSKKTKDL TKLKECMDKY GLNLPMVTYV KDELRSAEKV AKGKSRLIEA
1910 1920 1930 1940 1950
SSLNDSVAMR QTFGNLYKTF HLNPGIVTGS AVGCDPDVFW SKIPVMLDGH
1960 1970 1980 1990 2000
LIAFDYSGYD ASLSPVWFAC LKLLLEKLGY TNKETNYIDY LCNSHHLYRD
2010 2020 2030 2040 2050
KHYFVRGGMP SGCSGTSIFN SMINNIIIRT LMLKVYKGID LDQFRMIAYG
2060 2070 2080 2090 2100
DDVIASYPWP IDASLLAEAG KDYGLIMTPA DKGECFNEVT WTNVTFLKRY
2110 2120 2130 2140 2150
FRADEQYPFL VHPVMPMKDI HESIRWTKDP KNTQDHVRSL CLLAWHNGEH
2160 2170 2180
EYEEFIRKIR SVPVGRCLTL PAFSTLRRKW LDSF
Length:2,184
Mass (Da):244,004
Last modified:January 23, 2007 - v4
Checksum:iCBBB937D0AC18EA9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti69 – 691N → M in CAA61710. (PubMed:8627260)Curated
Sequence conflicti238 – 2381A → R in CAA61710. (PubMed:8627260)Curated
Sequence conflicti611 – 6111A → V in AAD17718. (PubMed:9971773)Curated
Sequence conflicti645 – 6451Y → F in AAD17718. (PubMed:9971773)Curated
Sequence conflicti724 – 7241V → I in AAD17718. (PubMed:9971773)Curated
Sequence conflicti774 – 7741A → T in AAD17718. (PubMed:9971773)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF029859 Genomic RNA. Translation: AAC63944.2.
X89531 Genomic RNA. Translation: CAA61710.1.
AF081314 Genomic RNA. Translation: AAD17718.1.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF029859 Genomic RNA. Translation: AAC63944.2 .
X89531 Genomic RNA. Translation: CAA61710.1 .
AF081314 Genomic RNA. Translation: AAD17718.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EV1 X-ray 3.55 1 570-850 [» ]
2 77-330 [» ]
3 331-569 [» ]
4 2-69 [» ]
ProteinModelPortali O91734.
SMRi O91734. Positions 2-69, 77-1000, 1540-2184.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C03.020.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei O91734.

Family and domain databases

Gene3Di 2.60.120.20. 3 hits.
4.10.80.10. 2 hits.
InterProi IPR003593. AAA+_ATPase.
IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR027417. P-loop_NTPase.
IPR014838. P3A.
IPR000081. Peptidase_C3.
IPR000199. Peptidase_C3A/C3B_picornavir.
IPR003138. Pico_P1A.
IPR002527. Pico_P2B.
IPR001676. Picornavirus_capsid.
IPR001205. RNA-dir_pol_C.
IPR007094. RNA-dir_pol_PSvirus.
IPR009003. Trypsin-like_Pept_dom.
IPR029053. Viral_coat.
[Graphical view ]
Pfami PF08727. 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 ]
ProDomi PD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 2 hits.
SSF52540. SSF52540. 1 hit.
SSF89043. SSF89043. 1 hit.
PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Receptor interactions, infectious cDNA, and nucleotide sequences of echovirus 1/8."
    Bergelson J.M.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "The major echovirus group is genetically coherent and related to coxsackie B viruses."
    Huttunen P., Santti J., Pulli T., Hyypiae T.
    J. Gen. Virol. 77:715-725(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 69-330.
  3. "Molecular evolution of the human enteroviruses: correlation of serotype with VP1 sequence and application to picornavirus classification."
    Oberste M.S., Maher K., Kilpatrick D.R., Pallansch M.A.
    J. Virol. 73:1941-1948(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 570-853.
  4. "Infection by echoviruses 1 and 8 depends on the alpha 2 subunit of human VLA-2."
    Bergelson J.M., St John N., Kawaguchi S., Chan M., Stubdal H., Modlin J., Finberg R.W.
    J. Virol. 67:6847-6852(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN ITGA2/ITGB1 INTEGRIN.
  5. Cited for: FUNCTION OF CAPSID PROTEINS.
  6. "Echovirus 1 endocytosis into caveosomes requires lipid rafts, dynamin II, and signaling events."
    Pietiainen V., Marjomaki V., Upla P., Pelkmans L., Helenius A., Hyypia T.
    Mol. Biol. Cell 15:4911-4925(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF CAPSID PROTEINS.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (3.55 ANGSTROMS) OF 1-850.

Entry informationi

Entry nameiPOLG_EC01F
AccessioniPrimary (citable) accession number: O91734
Secondary accession number(s): Q66795, Q9YID6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 138 of the entry and version 4 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

External Data

Dasty 3