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Protein

Genome polyprotein

Gene
N/A
Organism
Human rhinovirus 2 (HRV-2)
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 VLDLR 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 sitei868For Protease 2A activity1
Active sitei885For Protease 2A activity1
Active sitei956For Protease 2A activity1
Active sitei1547For Protease 3C activitySequence analysis1
Active sitei1578For Protease 3C activitySequence analysis1
Active sitei1654For Protease 3C activityCurated1
Active sitei2017For 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

Enzyme and pathway databases

SABIO-RKP04936.

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 rhinovirus 2 (HRV-2)
Taxonomic identifieri12130 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeEnterovirusRhinovirus A
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000007682 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 – 1463CytoplasmicSequence analysisAdd BLAST1462
Intramembranei1464 – 1479Sequence analysisAdd BLAST16
Topological domaini1480 – 2150CytoplasmicSequence 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_00004265062 – 2150Genome polyproteinBy similarityAdd BLAST2149
ChainiPRO_00004265072 – 844P1By similarityAdd BLAST843
ChainiPRO_00004265082 – 330Capsid protein VP0Sequence analysisAdd BLAST329
ChainiPRO_00004265092 – 69Capsid protein VP4Sequence analysisAdd BLAST68
ChainiPRO_000042651070 – 330Capsid protein VP2Sequence analysisAdd BLAST261
ChainiPRO_0000426511331 – 565Capsid protein VP3Sequence analysisAdd BLAST235
ChainiPRO_0000426512565 – 850Capsid protein VP1Sequence analysisAdd BLAST286
ChainiPRO_0000426513851 – 1409P2By similarityAdd BLAST559
ChainiPRO_0000426514851 – 992Protease 2ASequence analysisAdd BLAST142
ChainiPRO_0000040015993 – 1087Protein 2BSequence analysisAdd BLAST95
ChainiPRO_00000400161088 – 1409Protein 2CSequence analysisAdd BLAST322
ChainiPRO_00004265151410 – 2150P3By similarityAdd BLAST741
ChainiPRO_00004265161410 – 1507Protein 3ABSequence analysisAdd BLAST98
ChainiPRO_00000400171410 – 1486Protein 3ASequence analysisAdd BLAST77
ChainiPRO_00004265171487 – 1507Viral protein genome-linkedSequence analysisAdd BLAST21
ChainiPRO_00004265181508 – 2150Protein 3CDSequence analysisAdd BLAST643
ChainiPRO_00004265191508 – 1689Protease 3CSequence analysisAdd BLAST182
ChainiPRO_00004265201690 – 2150RNA-directed RNA polymeraseBy similarityAdd BLAST461

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycine; by hostBy similarity1
Modified residuei1489O-(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
Sitei330 – 331Cleavage; by Protease 3CSequence analysis2
Sitei850 – 851Cleavage; by Protease 2ASequence analysis2
Sitei992 – 993Cleavage; by Protease 3CSequence analysis2
Sitei1409 – 1410Cleavage; by Protease 3CSequence analysis2
Sitei1486 – 1487Cleavage; by Protease 3CSequence analysis2
Sitei1507 – 1508Cleavage; by Protease 3CSequence analysis2
Sitei1690 – 1691Cleavage; 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). Interacts with host VLDLR. 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

12150
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi33 – 35Combined sources3
Helixi36 – 38Combined sources3
Turni52 – 54Combined sources3
Beta strandi83 – 86Combined sources4
Beta strandi91 – 96Combined sources6
Helixi103 – 105Combined sources3
Turni113 – 115Combined sources3
Beta strandi117 – 119Combined sources3
Helixi126 – 128Combined sources3
Beta strandi138 – 140Combined sources3
Beta strandi147 – 151Combined sources5
Helixi153 – 155Combined sources3
Helixi159 – 167Combined sources9
Beta strandi168 – 180Combined sources13
Beta strandi187 – 197Combined sources11
Beta strandi203 – 208Combined sources6
Helixi213 – 216Combined sources4
Helixi219 – 221Combined sources3
Helixi233 – 235Combined sources3
Helixi241 – 243Combined sources3
Turni244 – 247Combined sources4
Helixi253 – 255Combined sources3
Beta strandi256 – 262Combined sources7
Turni263 – 265Combined sources3
Beta strandi267 – 273Combined sources7
Beta strandi278 – 282Combined sources5
Turni284 – 286Combined sources3
Beta strandi290 – 305Combined sources16
Beta strandi309 – 325Combined sources17
Turni338 – 341Combined sources4
Beta strandi353 – 355Combined sources3
Beta strandi367 – 372Combined sources6
Helixi374 – 377Combined sources4
Turni389 – 393Combined sources5
Helixi395 – 398Combined sources4
Beta strandi399 – 403Combined sources5
Beta strandi411 – 416Combined sources6
Beta strandi418 – 421Combined sources4
Helixi424 – 426Combined sources3
Helixi428 – 433Combined sources6
Beta strandi436 – 441Combined sources6
Beta strandi443 – 449Combined sources7
Beta strandi456 – 464Combined sources9
Beta strandi466 – 468Combined sources3
Helixi474 – 478Combined sources5
Beta strandi480 – 489Combined sources10
Beta strandi492 – 497Combined sources6
Beta strandi502 – 504Combined sources3
Beta strandi506 – 509Combined sources4
Beta strandi517 – 524Combined sources8
Beta strandi530 – 532Combined sources3
Beta strandi534 – 544Combined sources11
Beta strandi549 – 553Combined sources5
Turni572 – 579Combined sources8
Beta strandi581 – 583Combined sources3
Beta strandi599 – 602Combined sources4
Helixi604 – 606Combined sources3
Helixi614 – 617Combined sources4
Helixi630 – 632Combined sources3
Helixi634 – 638Combined sources5
Beta strandi642 – 650Combined sources9
Turni654 – 658Combined sources5
Beta strandi661 – 665Combined sources5
Helixi672 – 678Combined sources7
Beta strandi681 – 698Combined sources18
Beta strandi707 – 713Combined sources7
Helixi726 – 729Combined sources4
Beta strandi731 – 733Combined sources3
Beta strandi735 – 739Combined sources5
Beta strandi746 – 749Combined sources4
Beta strandi754 – 760Combined sources7
Turni774 – 777Combined sources4
Beta strandi782 – 787Combined sources6
Beta strandi796 – 814Combined sources19
Beta strandi855 – 866Combined sources12
Helixi867 – 869Combined sources3
Helixi874 – 876Combined sources3
Beta strandi878 – 881Combined sources4
Helixi882 – 884Combined sources3
Beta strandi886 – 896Combined sources11
Beta strandi906 – 911Combined sources6
Turni912 – 915Combined sources4
Beta strandi916 – 921Combined sources6
Beta strandi923 – 930Combined sources8
Beta strandi938 – 948Combined sources11
Beta strandi959 – 962Combined sources4
Beta strandi965 – 973Combined sources9
Beta strandi975 – 982Combined sources8
Helixi983 – 986Combined sources4
Helixi1509 – 1521Combined sources13
Beta strandi1522 – 1527Combined sources6
Beta strandi1530 – 1539Combined sources10
Beta strandi1541 – 1545Combined sources5
Helixi1546 – 1548Combined sources3
Beta strandi1552 – 1556Combined sources5
Beta strandi1559 – 1570Combined sources12
Beta strandi1576 – 1584Combined sources9
Helixi1594 – 1596Combined sources3
Beta strandi1604 – 1611Combined sources8
Beta strandi1615 – 1617Combined sources3
Beta strandi1619 – 1634Combined sources16
Beta strandi1637 – 1647Combined sources11
Helixi1651 – 1653Combined sources3
Beta strandi1657 – 1660Combined sources4
Beta strandi1663 – 1671Combined sources9
Beta strandi1676 – 1680Combined sources5
Helixi1683 – 1685Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A3RX-ray2.10P225-239[»]
1CQQX-ray1.85A1508-1687[»]
1FPNX-ray2.601568-856[»]
270-330[»]
3331-567[»]
42-69[»]
1V9UX-ray3.601568-856[»]
270-330[»]
3331-567[»]
42-69[»]
2HRVX-ray1.95A/B851-992[»]
2XYAX-ray2.40A1508-1687[»]
3DPRX-ray3.50A568-856[»]
B70-330[»]
C331-567[»]
D2-69[»]
3TN9X-ray3.001568-856[»]
270-330[»]
3331-567[»]
3VDDX-ray3.20A568-850[»]
B70-330[»]
C331-567[»]
D1-69[»]
4L3BX-ray6.50A568-856[»]
B70-330[»]
C331-567[»]
5FX5X-ray1.70A1508-1687[»]
5FX6X-ray1.45A1508-1687[»]
ProteinModelPortaliP04936.
SMRiP04936.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04936.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1181 – 1343SF3 helicasePROSITE-ProRule annotationAdd BLAST163
Domaini1508 – 1673Peptidase C3Add BLAST166
Domaini1918 – 2031RdRp catalyticPROSITE-ProRule annotationAdd BLAST114

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni565 – 581Amphipatic alpha-helixSequence analysisAdd BLAST17
Regioni1410 – 1424DisorderedBy 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.
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.

P04936-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAQVSRQNV GTHSTQNSVS NGSSLNYFNI NYFKDAASNG ASKLEFTQDP
60 70 80 90 100
SKFTDPVKDV LEKGIPTLQS PTVEACGYSD RIIQITRGDS TITSQDVANA
110 120 130 140 150
IVAYGVWPHY LSSKDASAID KPSQPDTSSN RFYTLRSVTW SSSSKGWWWK
160 170 180 190 200
LPDALKDMGI FGENMFYHYL GRSGYTIHVQ CNASKFHQGT LIVALIPEHQ
210 220 230 240 250
IASALHGNVN VGYNYTHPGE TGREVKAETR LNPDLQPTEE YWLNFDGTLL
260 270 280 290 300
GNITIFPHQF INLRSNNSAT IIAPYVNAVP MDSMRSHNNW SLVIIPICPL
310 320 330 340 350
ETSSAINTIP ITISISPMCA EFSGARAKRQ GLPVFITPGS GQFLTTDDFQ
360 370 380 390 400
SPCALPWYHP TKEISIPGEV KNLVEICQVD SLVPINNTDT YINSENMYSV
410 420 430 440 450
VLQSSINAPD KIFSIRTDVA SQPLATTLIG EISSYFTHWT GSLRFSFMFC
460 470 480 490 500
GTANTTVKLL LAYTPPGIAE PTTRKDAMLG THVIWDVGLQ STISMVVPWI
510 520 530 540 550
SASHYRNTSP GRSTSGYITC WYQTRLVIPP QTPPTARLLC FVSGCKDFCL
560 570 580 590 600
RMARDTNLHL QSGAIAQNPV ENYIDEVLNE VLVVPNINSS NPTTSNSAPA
610 620 630 640 650
LDAAETGHTS SVQPEDVIET RYVQTSQTRD EMSLESFLGR SGCIHESKLE
660 670 680 690 700
VTLANYNKEN FTVWAINLQE MAQIRRKFEL FTYTRFDSEI TLVPCISALS
710 720 730 740 750
QDIGHITMQY MYVPPGAPVP NSRDDYAWQS GTNASVFWQH GQAYPRFSLP
760 770 780 790 800
FLSVASAYYM FYDGYDEQDQ NYGTANTNNM GSLCSRIVTE KHIHKVHIMT
810 820 830 840 850
RIYHKAKHVK AWCPRPPRAL EYTRAHRTNF KIEDRSIQTA IVTRPIITTA
860 870 880 890 900
GPSDMYVHVG NLIYRNLHLF NSEMHESILV SYSSDLIIYR TNTVGDDYIP
910 920 930 940 950
SCDCTQATYY CKHKNRYFPI TVTSHDWYEI QESEYYPKHI QYNLLIGEGP
960 970 980 990 1000
CEPGDCGGKL LCKHGVIGIV TAGGDNHVAF IDLRHFHCAE EQGVTDYIHM
1010 1020 1030 1040 1050
LGEAFGNGFV DSVKEHIHAI NPVGNISKKI IKWMLRIISA MVIIIRNSSD
1060 1070 1080 1090 1100
PQTILATLTL IGCSGSPWRF LKEKFCKWTQ LNYIHKESDS WLKKFTEACN
1110 1120 1130 1140 1150
AARGLEWIGN KISKFIEWMK SMLPQAQLKV KYLNELKKLN LYEKQVESLR
1160 1170 1180 1190 1200
VADMKTQEKI KMEIDTLHDL SRKFLPLYAS EAKRIKTLYI KCDNIIKQKK
1210 1220 1230 1240 1250
RCEPVAIVIH GPPGAGKSIT TNFLAKMITN DSDIYSLPPD PKYFDGYDQQ
1260 1270 1280 1290 1300
SVVIMDDIMQ NPAGDDMTLF CQMVSSVTFI PPMADLPDKG KAFDSRFVLC
1310 1320 1330 1340 1350
STNHSLLTPP TITSLPAMNR RFFLDLDIIV HDNFKDPQGK LNVAAAFRPC
1360 1370 1380 1390 1400
DVDNRIGNAR CCPFVCGKAV SFKDRNSCNK YSLAQVYNIM IEEDRRRRQV
1410 1420 1430 1440 1450
VDVMTAIFQG PIDMKNPPPP AITDLLQSVR TPEVIKYCEG NRWIIPAECK
1460 1470 1480 1490 1500
IEKELNLANT IITIIANVIG MARIIYVIYK LFCTLQGPYS GEPKPKTKIP
1510 1520 1530 1540 1550
ERRVVTQGPE EEFGMSLIKH NSCVITTENG KFTGLGVYDR FVVVPTHADP
1560 1570 1580 1590 1600
GKEIQVDGIT TKVIDSYDLY NKNGIKLEIT VLKLDRNEKF RDIRRYIPNN
1610 1620 1630 1640 1650
EDDYPNCNLA LLANQPEPTI INVGDVVSYG NILLSGNQTA RMLKYSYPTK
1660 1670 1680 1690 1700
SGYCGGVLYK IGQVLGIHVG GNGRDGFSAM LLRSYFTDVQ GQITLSKKTS
1710 1720 1730 1740 1750
ECNLPSIHTP CKTKLQPSVF YDVFPGSKEP AVLSEKDARL QVDFNEALFS
1760 1770 1780 1790 1800
KYKGNTDCSI NDHIRIASSH YAAQLITLDI DPKPITLEDS VFGTDGLEAL
1810 1820 1830 1840 1850
DLNTSAGFPY IAMGVKKRDL INNKTKDISK LKEAIDKYGV DLPMVTFLKD
1860 1870 1880 1890 1900
ELRKHEKVIK GKTRVIEASS VNDTLLFRTT FGNLFSKFHL NPGIVTGSAV
1910 1920 1930 1940 1950
GCDPEVFWSK IPAMLDDKCI MAFDYTNYDG SIHPIWFEAL KQVLVDLSFN
1960 1970 1980 1990 2000
PTLIDRLCKS KHIFKNTYYE VEGGVPSGCS GTSIFNTMIN NIIIRTLVLD
2010 2020 2030 2040 2050
AYKNIDLDKL KIIAYGDDVI FSYIHELDME AIAIEGVKYG LTITPADKSN
2060 2070 2080 2090 2100
TFVKLDYSNV TFLKRGFKQD EKYNFLIHPT FPEDEIFESI RWTKKPSQMH
2110 2120 2130 2140 2150
EHVLSLCHLM WHNGRDAYKK FVEKIRSVSA GRALYIPPYD LLLHEWYEKF
Length:2,150
Mass (Da):241,978
Last modified:January 23, 2007 - v3
Checksum:i6E0DF9F4945D9D0C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02316 Genomic RNA. Translation: CAA26181.1.
PIRiA03902. GNNYH2.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure associated with cellular receptor

Virus Particle ExploreR db

Icosahedral capsid structure complexed with cellular receptor fragment

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02316 Genomic RNA. Translation: CAA26181.1.
PIRiA03902. GNNYH2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A3RX-ray2.10P225-239[»]
1CQQX-ray1.85A1508-1687[»]
1FPNX-ray2.601568-856[»]
270-330[»]
3331-567[»]
42-69[»]
1V9UX-ray3.601568-856[»]
270-330[»]
3331-567[»]
42-69[»]
2HRVX-ray1.95A/B851-992[»]
2XYAX-ray2.40A1508-1687[»]
3DPRX-ray3.50A568-856[»]
B70-330[»]
C331-567[»]
D2-69[»]
3TN9X-ray3.001568-856[»]
270-330[»]
3331-567[»]
3VDDX-ray3.20A568-850[»]
B70-330[»]
C331-567[»]
D1-69[»]
4L3BX-ray6.50A568-856[»]
B70-330[»]
C331-567[»]
5FX5X-ray1.70A1508-1687[»]
5FX6X-ray1.45A1508-1687[»]
ProteinModelPortaliP04936.
SMRiP04936.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiN08.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP04936.

Miscellaneous databases

EvolutionaryTraceiP04936.

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_HRV2
AccessioniPrimary (citable) accession number: P04936
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 172 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.