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Protein

Genome polyprotein

Gene
N/A
Organism
Human rhinovirus 1A (HRV-1A)
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 sitei875For Protease 2A activityBy similarity1
Active sitei892For Protease 2A activityBy similarity1
Active sitei963For Protease 2A activityBy similarity1
Active sitei1554For Protease 3C activitySequence analysis1
Active sitei1585For Protease 3C activitySequence analysis1
Active sitei1661For Protease 3C activityBy similarity1
Active sitei2024For RdRp activityBy similarity1

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, 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

MEROPSiC03.007.
TCDBi1.A.85.1.7. the poliovirus 2b viroporin (2b viroporin) family.

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 rhinovirus 1A (HRV-1A)
Taxonomic identifieri12134 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusRhinovirus A
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000013736 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 – 1470CytoplasmicSequence analysisAdd BLAST1469
Intramembranei1471 – 1486Sequence analysisAdd BLAST16
Topological domaini1487 – 2157CytoplasmicSequence analysisAdd BLAST671

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_00004264762 – 2157Genome polyproteinBy similarityAdd BLAST2156
ChainiPRO_00004264772 – 857P1By similarityAdd BLAST856
ChainiPRO_00004264782 – 332Capsid protein VP0Sequence analysisAdd BLAST331
ChainiPRO_00004264792 – 69Capsid protein VP4Sequence analysisAdd BLAST68
ChainiPRO_000042648070 – 332Capsid protein VP2Sequence analysisAdd BLAST263
ChainiPRO_0000426481333 – 567Capsid protein VP3Sequence analysisAdd BLAST235
ChainiPRO_0000426482567 – 857Capsid protein VP1Sequence analysisAdd BLAST291
ChainiPRO_0000426483858 – 1416P2By similarityAdd BLAST559
ChainiPRO_0000426484858 – 999Protease 2ASequence analysisAdd BLAST142
ChainiPRO_50004383671000 – 1094Protein 2BSequence analysisAdd BLAST95
ChainiPRO_50004383681095 – 1416Protein 2CSequence analysisAdd BLAST322
ChainiPRO_00004264851417 – 2157P3By similarityAdd BLAST741
ChainiPRO_00004264861417 – 1514Protein 3ABSequence analysisAdd BLAST98
ChainiPRO_50004383691417 – 1493Protein 3ASequence analysisAdd BLAST77
ChainiPRO_00004264871494 – 1514Viral protein genome-linkedSequence analysisAdd BLAST21
ChainiPRO_00004264881515 – 2157Protein 3CDSequence analysisAdd BLAST643
ChainiPRO_00004264891515 – 1696Protease 3CSequence analysisAdd BLAST182
ChainiPRO_00004264901697 – 2157RNA-directed RNA polymeraseBy similarityAdd BLAST461

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostBy similarity1
Modified residuei1496O-(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
Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle.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
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
Sitei332 – 333Cleavage; by Protease 3CSequence analysis2
Sitei857 – 858Cleavage; by Protease 2ASequence analysis2
Sitei999 – 1000Cleavage; by Protease 3CSequence analysis2
Sitei1416 – 1417Cleavage; by Protease 3CSequence analysis2
Sitei1493 – 1494Cleavage; by Protease 3CSequence analysis2
Sitei1514 – 1515Cleavage; by Protease 3CSequence analysis2
Sitei1697 – 1698Cleavage; 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

12157
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 6Combined sources4
Beta strandi27 – 30Combined sources4
Beta strandi33 – 35Combined sources3
Helixi36 – 38Combined sources3
Beta strandi83 – 86Combined sources4
Beta strandi91 – 96Combined sources6
Helixi103 – 105Combined sources3
Turni113 – 115Combined sources3
Beta strandi127 – 131Combined sources5
Beta strandi146 – 150Combined sources5
Helixi151 – 154Combined sources4
Beta strandi156 – 158Combined sources3
Helixi161 – 164Combined sources4
Beta strandi167 – 180Combined sources14
Beta strandi190 – 198Combined sources9
Beta strandi203 – 208Combined sources6
Turni214 – 216Combined sources3
Beta strandi223 – 226Combined sources4
Beta strandi231 – 233Combined sources3
Turni240 – 246Combined sources7
Helixi252 – 254Combined sources3
Beta strandi255 – 261Combined sources7
Turni262 – 264Combined sources3
Beta strandi266 – 272Combined sources7
Beta strandi276 – 282Combined sources7
Turni283 – 285Combined sources3
Beta strandi289 – 297Combined sources9
Beta strandi310 – 325Combined sources16
Turni340 – 343Combined sources4
Beta strandi355 – 357Combined sources3
Helixi375 – 379Combined sources5
Helixi391 – 393Combined sources3
Helixi398 – 400Combined sources3
Beta strandi401 – 404Combined sources4
Beta strandi408 – 411Combined sources4
Beta strandi413 – 418Combined sources6
Beta strandi421 – 423Combined sources3
Helixi432 – 435Combined sources4
Beta strandi438 – 443Combined sources6
Beta strandi445 – 451Combined sources7
Beta strandi458 – 466Combined sources9
Helixi476 – 480Combined sources5
Beta strandi482 – 488Combined sources7
Beta strandi490 – 492Combined sources3
Beta strandi494 – 499Combined sources6
Beta strandi504 – 511Combined sources8
Beta strandi520 – 530Combined sources11
Beta strandi533 – 535Combined sources3
Beta strandi539 – 547Combined sources9
Beta strandi552 – 556Combined sources5
Helixi576 – 580Combined sources5
Beta strandi584 – 586Combined sources3
Helixi607 – 609Combined sources3
Helixi617 – 620Combined sources4
Beta strandi633 – 636Combined sources4
Helixi637 – 641Combined sources5
Beta strandi645 – 653Combined sources9
Beta strandi656 – 660Combined sources5
Beta strandi667 – 670Combined sources4
Helixi679 – 683Combined sources5
Beta strandi686 – 703Combined sources18
Beta strandi713 – 718Combined sources6
Beta strandi720 – 722Combined sources3
Beta strandi726 – 729Combined sources4
Helixi732 – 734Combined sources3
Beta strandi738 – 743Combined sources6
Beta strandi751 – 754Combined sources4
Beta strandi759 – 765Combined sources7
Beta strandi789 – 793Combined sources5
Beta strandi803 – 821Combined sources19
Beta strandi831 – 834Combined sources4
Beta strandi840 – 842Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AYMX-ray2.1542-69[»]
1AYNX-ray2.9042-69[»]
1R1AX-ray3.201571-857[»]
270-332[»]
3333-570[»]
42-45[»]
2HWDX-ray3.801571-857[»]
270-332[»]
3333-570[»]
42-45[»]
2HWEX-ray3.801571-857[»]
270-332[»]
3333-570[»]
42-45[»]
2HWFX-ray3.801571-857[»]
270-332[»]
3333-570[»]
42-45[»]
ProteinModelPortaliP23008.
SMRiP23008.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23008.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1188 – 1350SF3 helicasePROSITE-ProRule annotationAdd BLAST163
Domaini1515 – 1680Peptidase C3Add BLAST166
Domaini1925 – 2038RdRp catalyticPROSITE-ProRule annotationAdd BLAST114

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni567 – 584Amphipatic alpha-helixSequence analysisAdd BLAST18
Regioni1417 – 1431DisorderedBy similarityAdd BLAST15

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.
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.
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]
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.

P23008-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAQVSRQNV GTHSTQNSVS NGSSLNYFNI NYFKDAASSG ASRLDFSQDP
60 70 80 90 100
SKFTDPVKDV LEKGIPTLQS PSVEACGYSD RIMQITRGDS TITSQDVANA
110 120 130 140 150
VVGYGVWPHY LTPQDATAID KPTQPDTSSN RFYTLESKHW NGSSKGWWWK
160 170 180 190 200
LPDALKDMGI FGENMYYHFL GRSGYTVHVQ CNASKFHQGT LLVAMIPEHQ
210 220 230 240 250
LASAKHGSVT AGYKLTHPGE AGRDVSQERD ASLRQPSDDS WLNFDGTLLG
260 270 280 290 300
NLLIFPHQFI NLRSNNSATL IVPYVNAVPM DSMLRHNNWS LVIIPISPLR
310 320 330 340 350
SETTSSNIVP ITVSISPMCA EFSGARAKNI KQGLPVYITP GSGQFMTTDD
360 370 380 390 400
MQSPCALPWY HPTKEISIPG EVKNLIEMCQ VDTLIPVNNV GNNVGNVSMY
410 420 430 440 450
TVQLGNQTGM AQKVFSIKVD ITSQPLATTL IGEIASYYTH WTGSLRFSFM
460 470 480 490 500
FCGTANTTLK LLLAYTPPGI DEPTTRKDAM LGTHVVWDVG LQSTISLVVP
510 520 530 540 550
WVSASHFRLT ADNKYSMAGY ITCWYQTNLV VPPSTPQTAD MLCFVSACKD
560 570 580 590 600
FCLRMARDTD LHIQSGPIEQ NPVENYIDEV LNEVLVVPNI KESHHTTSNS
610 620 630 640 650
APLLDAAETG HTSNVQPEDA IETRYVITSQ TRDEMSIESF LGRSGCVHIS
660 670 680 690 700
RIKVDYTDYN GQDINFTKWK ITLQEMAQIR RKFELFTYVR FDSEITLVPC
710 720 730 740 750
IAGRGDDIGH IVMQYMYVPP GAPIPSKRND FSWQSGTNMS IFWQHGQPFP
760 770 780 790 800
RFSLPFLSIA SAYYMFYDGY DGDNTSSKYG SVVTNDMGTI CSRIVTEKQK
810 820 830 840 850
HSVVITTHIY HKAKHTKAWC PRPPRAVPYT HSHVTNYMPE TGDVTTAIVR
860 870 880 890 900
RNTITTAGPS DLYVHVGNLI YRNLHLFNSE MHDSILISYS SDLIIYRTNT
910 920 930 940 950
IGDDYIPNCN CTEATYYCRH KNRYYPIKVT PHDWYEIQES EYYPKHIQYN
960 970 980 990 1000
LLIGEGPCEP GDCGGKLLCR HGVIGIITAG GEGHVAFIDL RQFHCAEEQG
1010 1020 1030 1040 1050
ITDYIHMLGE AFGNGFVDSV KEQINAINPI NNISKKVIKW LLRIISAMVI
1060 1070 1080 1090 1100
IIRNSSDPQT IIATLTLIGC NGSPWRFLKE KFCKWTQLTY IHKESDSWLK
1110 1120 1130 1140 1150
KFTEMCNAAR GLEWIGNKIS KFIDWMKSML PQAQLKVKYL NEIKKLSLLE
1160 1170 1180 1190 1200
KQIENLRAAD SATQEKIKCE IDTLHDLSCK FLPLYAHEAK RIKVLYNKCS
1210 1220 1230 1240 1250
NIIKQRKRSE PVAVMIHGPP GTGKSITTNF LARMITNESD VYSLPPDPKY
1260 1270 1280 1290 1300
FDGYDNQSVV IMDDIMQNPD GEDMTLFCQM VSSVTFIPPM ADLPDKGKPF
1310 1320 1330 1340 1350
DSRFILCSTN HSLLAPPTIS SLPAMNRRFF FDLDIVVHDN YKDTQGKLDV
1360 1370 1380 1390 1400
SKAFRPCNVN TKIGNAKCCP FVCGKAVXFK DRSTCSTYTL AQVYNHILEE
1410 1420 1430 1440 1450
DKRRRQVVDV MSAIFQGPIS LDXPPPPAIX DLLQSVRTPE VIKYCQDNKW
1460 1470 1480 1490 1500
VIPAECQVER DLNIANSIIA IIANIISIAG IIFVIYKLFC SLQGPYSGEP
1510 1520 1530 1540 1550
KPKTKVPERR VVAQGPEEEF GRSILKNNTC VITTGNGKFT GLGIHDRILI
1560 1570 1580 1590 1600
IPTHADPGRE VQVNGVHTKV LDSYDLYNRD GVKLEITVIQ LDRNEKFRDI
1610 1620 1630 1640 1650
RKYIPETEDD YPECNLALSA NQDEPTIIKV GDVVSYGNIL LSGNQTARML
1660 1670 1680 1690 1700
KYNYPTKSGY CGGVLYKIGQ ILGIHVGGNG RDGFSAMLLR SYFTDTQGQI
1710 1720 1730 1740 1750
KVNKHATECG LPTIHTPSKT KLQPSVFYDV FPGSKEPAVL TDNDPRLEVN
1760 1770 1780 1790 1800
FKEALFSKYK GNVECNLNEH MEIAIAHYSA QLMTLDIDSR PIALEDSVFG
1810 1820 1830 1840 1850
IEGLEALDLN TSAGFPYVTM GIKKRDLINN KTKDISRLKE ALDKYGVDLP
1860 1870 1880 1890 1900
MITFLKDELR KKEKISTGKT RVIEASSIND TILFRTTFGN LFSKFHLNPG
1910 1920 1930 1940 1950
VVTGSAVGCD PETFWSKIPV MLDGDCIMAF DYTNYDGSIH PVWFQALKKV
1960 1970 1980 1990 2000
LENLSFQSNL IDRLCYSKHL FKSTYYEVAG GVPSGCSGTS IFNTMINNII
2010 2020 2030 2040 2050
IRTLVLDAYK NIDLDKLKII AYGDDVIFSY KYTLDMEAIA NEGKKYGLTI
2060 2070 2080 2090 2100
TPADKSNEFK KLDYSNVTFL KRGFKQDERH TFLIHPTFPV EEIHESIRWT
2110 2120 2130 2140 2150
KKPSQMQEHV LSLCHLMWHN GRKVYEDFSS KIRSVSAGRA LYIPPYDLLK

HEWYEKF
Length:2,157
Mass (Da):242,487
Last modified:July 24, 2013 - v3
Checksum:i8B7807D279FC0A84
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti4Q → G.1
Natural varianti93 – 95TSQ → SSD.3
Natural varianti120D → N.1
Natural varianti290S → C.1
Natural varianti424Q → T.1
Natural varianti754L → I.1
Natural varianti801H → L.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ445111 Genomic RNA. Translation: ACK37367.1.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound Win56291

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound Win54954

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound R61837

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FJ445111 Genomic RNA. Translation: ACK37367.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AYMX-ray2.1542-69[»]
1AYNX-ray2.9042-69[»]
1R1AX-ray3.201571-857[»]
270-332[»]
3333-570[»]
42-45[»]
2HWDX-ray3.801571-857[»]
270-332[»]
3333-570[»]
42-45[»]
2HWEX-ray3.801571-857[»]
270-332[»]
3333-570[»]
42-45[»]
2HWFX-ray3.801571-857[»]
270-332[»]
3333-570[»]
42-45[»]
ProteinModelPortaliP23008.
SMRiP23008.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiC03.007.
TCDBi1.A.85.1.7. the poliovirus 2b viroporin (2b viroporin) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP23008.

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.
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.
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]
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]
ProtoNetiSearch...

Entry informationi

Entry nameiPOLG_HRV1A
AccessioniPrimary (citable) accession number: P23008
Secondary accession number(s): B9V432
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 24, 2013
Last modified: November 30, 2016
This is version 117 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.