P03303 (POLG_HRV14) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Genome polyprotein Cleaved into the following 12 chains: Protein VP0 Alternative name(s): VP4-VP2 Protein VP4 Alternative name(s): P1A Virion protein 4 Protein VP2 Alternative name(s): P1B Virion protein 2 Protein VP3 Alternative name(s): P1C Virion protein 3 Protein VP1 Alternative name(s): P1D Virion protein 1 Picornain 2A Short name=P2A Short name=Protein 2A EC=3.4.22.29 Protein 2B Short name=P2B Protein 2C Short name=P2C EC=3.6.1.15 Protein 3A Short name=P3A Protein 3B Short name=P3B Alternative name(s): VPg Picornain 3C EC=3.4.22.28 Alternative name(s): Protease 3C Short name=P3C RNA-directed RNA polymerase 3D-POL Short name=P3D-POL EC=2.7.7.48
Organism	Human rhinovirus 14 (HRV-14) [Complete proteome]
Taxonomic identifier	12131 [NCBI]
Taxonomic lineage	Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Picornavirales › Picornaviridae › Enterovirus › Rhinovirus B
Virus host	Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	2179 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Capsid proteins VP1, VP2, VP3 and VP4 form a closed capsid enclosing the viral positive strand RNA genome. VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes By similarity. The capsid interacts with human ICAM1 to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis. VP0 precursor is a component of immature procapsids By similarity. Protein 2A is a cysteine protease that is responsible for the cleavage between the P1 and P2 regions. It cleaves the host translation initiation factor EIF4G1, in order to shut down the capped cellular mRNA transcription By similarity. Protein 2B affects membrane integrity and cause an increase in membrane permeability By similarity. Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities By similarity. Protein 3A, via its hydrophobic domain, serves as membrane anchor By similarity. Protein 3C is a cysteine protease that generates mature viral proteins from the precursor polyprotein. In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind co-operatively to the protease By similarity. RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity.
Catalytic activity	Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). 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.
Subunit structure	Capsid proteins interact with host ICAM1.
Subcellular location	Protein VP2: Virion. Host cytoplasm Potential. Protein VP3: Virion. Host cytoplasm Potential. Protein VP1: Virion. Host cytoplasm Potential. Protein 2B: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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 By similarity. Protein 2C: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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 By similarity. Protein 3A: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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 By similarity. Protein 3B: Virion Potential. Picornain 3C: Host cytoplasm Potential. RNA-directed RNA polymerase 3D-POL: Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Potential. 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 By similarity.
Post-translational modification	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. 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. Myristoylation of VP4 is required during RNA encapsidation and formation of the mature virus particle By similarity.
Sequence similarities	Belongs to the picornaviruses polyprotein family. Contains 2 peptidase C3 domains. Contains 1 RdRp catalytic domain. Contains 1 SF3 helicase domain.
Caution	The PDB data bank contains the 3D-structure coordinates of proteins VP1, VP2, VP3 and VP4.

Ontologies

Keywords
Biological process	Activation of host autophagy by virus Clathrin- and caveolin-independent endocytosis of virus by host Host-virus interaction Inhibition of host IFN-mediated response initiation by virus Inhibition of host RIG-I by virus Inhibition of host innate immune response by virus Ion transport Transport Viral RNA replication Viral attachment to host cell Viral immunoevasion Viral penetration into host cytoplasm Viral penetration via lysis of host organellar membrane Virus endocytosis by host Virus entry into host cell
Cellular component	Host cytoplasm Host cytoplasmic vesicle Host membrane Membrane Virion
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Capsid protein Helicase Hydrolase Ion channel Nucleotidyltransferase Protease RNA-directed RNA polymerase Thiol protease Transferase Viral ion channel
PTM	Covalent protein-RNA linkage Lipoprotein Myristate Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	RNA-protein covalent cross-linking Inferred from electronic annotation. Source: UniProtKB-KW induction by virus of host autophagy Inferred from electronic annotation. Source: UniProtKB-KW ion transport Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host RIG-I activity Inferred from electronic annotation. Source: UniProtKB-KW suppression by virus of host type I interferon production Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro viral attachment to host cell Inferred from electronic annotation. Source: UniProtKB-KW viral entry into host cell via endocytosis Inferred from electronic annotation. Source: UniProtKB-KW viral genome replication Inferred from electronic annotation. Source: InterPro
Cellular_component	host cell cytoplasmic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-KW viral capsid Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA helicase activity Inferred from electronic annotation. Source: InterPro RNA-directed RNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro structural molecule activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed; by host By similarity

Chain

2 – 331

330

Protein VP0 Potential

PRO_0000311074

Chain

2 – 69

68

Protein VP4 Potential

PRO_0000040025

Chain

70 – 331

262

Protein VP2 Potential

PRO_0000040026

Chain

332 – 567

236

Protein VP3 Potential

PRO_0000040027

Chain

568 – 856

289

Protein VP1 Potential

PRO_0000040028

Chain

857 – 1002

146

Picornain 2A Potential

PRO_0000040029

Chain

1003 – 1099

97

Protein 2B Potential

PRO_0000040030

Chain

1100 – 1429

330

Protein 2C Potential

PRO_0000040031

Chain

1430 – 1514

85

Protein 3A Potential

PRO_0000040032

Chain

1515 – 1537

23

Protein 3B Potential

PRO_0000040033

Chain

1538 – 1719

182

Picornain 3C Potential

PRO_0000040034

Chain

1720 – 2179

460

RNA-directed RNA polymerase 3D-POL Potential

PRO_0000040035

Regions

Topological domain

2 – 1491

1490

Cytoplasmic Potential

Intramembrane

1492 – 1507

16

Potential

Topological domain

1508 – 2179

672

Cytoplasmic Potential

Domain

1205 – 1361

157

SF3 helicase

Domain

1946 – 2060

115

RdRp catalytic

Nucleotide binding

1229 – 1236

8

ATP Potential

Sites

Active site

876

1

For picornain 2A activity By similarity

Active site

894

1

For picornain 2A activity By similarity

Active site

965

1

For picornain 2A activity By similarity

Active site

1577

1

For picornain 3C activity Potential

Active site

1608

1

For picornain 3C activity Potential

Active site

1683

1

For picornain 3C activity By similarity

Site

69 – 70

2

Cleavage Potential

Site

331 – 332

2

Cleavage; by picornain 3C Potential

Site

856 – 857

2

Cleavage; by picornain 2A Potential

Site

1002 – 1003

2

Cleavage; by picornain 3C Potential

Site

1099 – 1100

2

Cleavage; by picornain 3C Potential

Site

1429 – 1430

2

Cleavage; by picornain 3C Potential

Site

1514 – 1515

2

Cleavage; by picornain 3C Potential

Site

1537 – 1538

2

Cleavage; by picornain 3C Potential

Site

1719 – 1720

2

Cleavage; by picornain 3C Potential

Amino acid modifications

Modified residue

1517

1

O-(5'-phospho-RNA)-tyrosine By similarity

Lipidation

2

1

N-myristoyl glycine; by host By similarity

Experimental info

Sequence conflict

368

1

P → L in AAA45756. Ref.3

Sequence conflict

459

1

I → T in AAA45756. Ref.3

Sequence conflict

722

1

P → H in AAA45756. Ref.3

Sequence conflict

726 – 727

2

NP → KS Ref.3

Sequence conflict

729 – 731

3

EWD → RVG Ref.3

Sequence conflict

913

1

C → R in AAA45756. Ref.3

Sequence conflict

942

1

N → S in AAA45756. Ref.3

Sequence conflict

962

1

P → L in AAA45756. Ref.3

Sequence conflict

982

1

G → E in AAA45756. Ref.3

Sequence conflict

1193

1

L → F in AAA45756. Ref.3

Sequence conflict

1193

1

L → H in AAA45758. Ref.2

Sequence conflict

1220

1

I → T Ref.2

Sequence conflict

1220

1

I → T Ref.3

Sequence conflict

1399

1

I → V Ref.2

Sequence conflict

1399

1

I → V Ref.3

Sequence conflict

1446

1

P → S in AAA45756. Ref.3

Sequence conflict

1739

1

P → A in AAA45756. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

2179

Helix Strand Turn

Details...

Helix

1539 – 1551

13

Beta strand

1552 – 1557

6

Beta strand

1560 – 1569

10

Beta strand

1571 – 1576

6

Beta strand

1582 – 1586

5

Beta strand

1589 – 1592

4

Beta strand

1594 – 1601

8

Turn

1602 – 1604

3

Beta strand

1605 – 1613

9

Helix

1623 – 1625

3

Beta strand

1634 – 1644

11

Beta strand

1646 – 1663

18

Beta strand

1666 – 1676

11

Beta strand

1686 – 1689

4

Beta strand

1692 – 1701

10

Beta strand

1704 – 1709

6

Helix

1712 – 1716

5

Beta strand

1721 – 1726

6

Helix

1728 – 1731

4

Helix

1748 – 1750

3

Helix

1773 – 1778

6

Helix

1791 – 1805

15

Helix

1816 – 1821

6

Beta strand

1824 – 1826

3

Helix

1839 – 1842

4

Helix

1846 – 1849

4

Turn

1852 – 1855

4

Helix

1858 – 1867

10

Beta strand

1873 – 1877

5

Helix

1884 – 1888

5

Beta strand

1894 – 1897

4

Helix

1900 – 1906

7

Turn

1907 – 1909

3

Helix

1911 – 1919

9

Turn

1923 – 1926

4

Helix

1933 – 1936

4

Helix

1937 – 1939

3

Helix

1940 – 1943

4

Beta strand

1949 – 1955

7

Helix

1957 – 1959

3

Helix

1962 – 1975

14

Turn

1978 – 1981

4

Helix

1982 – 1987

6

Beta strand

1988 – 1992

5

Beta strand

1994 – 2002

9

Beta strand

2008 – 2010

3

Helix

2011 – 2030

20

Helix

2036 – 2038

3

Beta strand

2040 – 2044

5

Beta strand

2047 – 2051

5

Helix

2058 – 2065

8

Turn

2066 – 2069

4

Turn

2086 – 2088

3

Beta strand

2094 – 2098

5

Beta strand

2100 – 2102

3

Beta strand

2105 – 2109

5

Helix

2112 – 2119

8

Beta strand

2121 – 2124

4

Turn

2125 – 2127

3

Helix

2128 – 2139

12

Helix

2140 – 2142

3

Helix

2144 – 2154

11

Helix

2158 – 2162

5

Helix

2168 – 2177

10

Sequences

	Sequence		Length	Mass (Da)
	P03303 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 827201A3032F0285	FASTA	2,179	242,991
	10 20 30 40 50 60 MGAQVSTQKS GSHENQNILT NGSNQTFTVI NYYKDAASTS SAGQSLSMDP SKFTEPVKDL 70 80 90 100 110 120 MLKGAPALNS PNVEACGYSD RVQQITLGNS TITTQEAANA VVCYAEWPEY LPDVDASDVN 130 140 150 160 170 180 KTSKPDTSVC RFYTLDSKTW TTGSKGWCWK LPDALKDMGV FGQNMFFHSL GRSGYTVHVQ 190 200 210 220 230 240 CNATKFHSGC LLVVVIPEHQ LASHEGGNVS VKYTFTHPGE RGIDLSSANE VGGPVKDVIY 250 260 270 280 290 300 NMNGTLLGNL LIFPHQFINL RTNNTATIVI PYINSVPIDS MTRHNNVSLM VIPIAPLTVP 310 320 330 340 350 360 TGATPSLPIT VTIAPMCTEF SGIRSKSIVP QGLPTTTLPG SGQFLTTDDR QSPSALPNYE 370 380 390 400 410 420 PTPRIHIPGK VHNLLEIIQV DTLIPMNNTH TKDEVNSYLI PLNANRQNEQ VFGTNLFIGD 430 440 450 460 470 480 GVFKTTLLGE IVQYYTHWSG SLRFSLMYTG PALSSAKLIL AYTPPGARGP QDRREAMLGT 490 500 510 520 530 540 HVVWDIGLQS TIVMTIPWTS GVQFRYTDPD TYTSAGFLSC WYQTSLILPP ETTGQVYLLS 550 560 570 580 590 600 FISACPDFKL RLMKDTQTIS QTVALTEGLG DELEEVIVEK TKQTVASISS GPKHTQKVPI 610 620 630 640 650 660 LTANETGATM PVLPSDSIET RTTYMHFNGS ETDVECFLGR AACVHVTEIQ NKDATGIDNH 670 680 690 700 710 720 REAKLFNDWK INLSSLVQLR KKLELFTYVR FDSEYTILAT ASQPDSANYS SNLVVQAMYV 730 740 750 760 770 780 PPGAPNPKEW DDYTWQSASN PSVFFKVGDT SRFSVPYVGL ASAYNCFYDG YSHDDAETQY 790 800 810 820 830 840 GITVLNHMGS MAFRIVNEHD EHKTLVKIRV YHRAKHVEAW IPRAPRALPY TSIGRTNYPK 850 860 870 880 890 900 NTEPVIKKRK GDIKSYGLGP RYGGIYTSNV KIMNYHLMTP EDHHNLIAPY PNRDLAIVST 910 920 930 940 950 960 GGHGAETIPH CNCTSGVYYS TYYRKYYPII CEKPTNIWIE GNPYYPSRFQ AGVMKGVGPA 970 980 990 1000 1010 1020 EPGDCGGILR CIHGPIGLLT AGGSGYVCFA DIRQLECIAE EQGLSDYITG LGRAFGVGFT 1030 1040 1050 1060 1070 1080 DQISTKVTEL QEVAKDFLTT KVLSKVVKMV SALVIICRNH DDLVTVTATL ALLGCDGSPW 1090 1100 1110 1120 1130 1140 RFLKMYISKH FQVPYIERQA NDGWFRKFND ACNAAKGLEW IANKISKLIE WIKNKVLPQA 1150 1160 1170 1180 1190 1200 KEKLEFCSKL KQLDILERQI TTMHISNPTQ EKREQLFNNV LWLEQMSQKF APLYAVESKR 1210 1220 1230 1240 1250 1260 IRELKNKMVN YMQFKSKQRI EPVCVLIHGT PGSGKSLTTS IVGRAIAEHF NSAVYSLPPD 1270 1280 1290 1300 1310 1320 PKHFDGYQQQ EVVIMDDLNQ NPDGQDISMF CQMVSSVDFL PPMASLDNKG MLFTSNFVLA 1330 1340 1350 1360 1370 1380 STNSNTLSPP TILNPEALVR RFGFDLDICL HTTYTKNGKL NAGMSTKTCK DCHQPSNFKK 1390 1400 1410 1420 1430 1440 CCPLVCGKAI SLVDRTTNIR YSVDQLVTAI ISDFKSKMQI TDSLETLFQG PVYKDLEIDV 1450 1460 1470 1480 1490 1500 CNTPPPECIN DLLKSVDSEE IREYCKKKKW IIPEIPTNIE RAMNQASMII NTILMFVSTL 1510 1520 1530 1540 1550 1560 GIVYVIYKLF AQTQGPYSGN PPHNKLKAPT LRPVVVQGPN TEFALSLLRK NIMTITTSKG 1570 1580 1590 1600 1610 1620 EFTGLGIHDR VCVIPTHAQP GDDVLVNGQK IRVKDKYKLV DPENINLELT VLTLDRNEKF 1630 1640 1650 1660 1670 1680 RDIRGFISED LEGVDATLVV HSNNFTNTIL EVGPVTMAGL INLSSTPTNR MIRYDYATKT 1690 1700 1710 1720 1730 1740 GQCGGVLCAT GKIFGIHVGG NGRQGFSAQL KKQYFVEKQG QVIARHKVRE FNINPVNTPT 1750 1760 1770 1780 1790 1800 KSKLHPSVFY DVFPGDKEPA VLSDNDPRLE VKLTESLFSK YKGNVNTEPT ENMLVAVDHY 1810 1820 1830 1840 1850 1860 AGQLLSLDIP TSELTLKEAL YGVDGLEPID ITTSAGFPYV SLGIKKRDIL NKETQDTEKM 1870 1880 1890 1900 1910 1920 KFYLDKYGID LPLVTYIKDE LRSVDKVRLG KSRLIEASSL NDSVNMRMKL GNLYKAFHQN 1930 1940 1950 1960 1970 1980 PGVLTGSAVG CDPDVFWSVI PCLMDGHLMA FDYSNFDASL SPVWFVCLEK VLTKLGFAGS 1990 2000 2010 2020 2030 2040 SLIQSICNTH HIFRDEIYVV EGGMPSGCSG TSIFNSMINN IIIRTLILDA YKGIDLDKLK 2050 2060 2070 2080 2090 2100 ILAYGDDLIV SYPYELDPQV LATLGKNYGL TITPPDKSET FTKMTWENLT FLKRYFKPDQ 2110 2120 2130 2140 2150 2160 QFPFLVHPVM PMKDIHESIR WTKDPKNTQD HVRSLCMLAW HSGEKEYNEF IQKIRTTDIG 2170 KCLILPEYSV LRRRWLDLF

References

[1]	"The complete nucleotide sequence of a common cold virus: human rhinovirus 14." Stanway G., Hughes P.J., Mountford R.C., Minor P.D., Almond J.W. Nucleic Acids Res. 12:7859-7875(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"Role of maturation cleavage in infectivity of picornaviruses: activation of an infectosome." Lee W.M., Monroe S., Rueckert R.R. J. Virol. 67:2110-2122(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]	"Molecular cloning and complete sequence determination of RNA genome of human rhinovirus type 14." Callahan P.L., Mizutani S., Colonno R.J. Proc. Natl. Acad. Sci. U.S.A. 82:732-736(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[4]	"Uncoating of human rhinoviruses." Fuchs R., Blaas D. Rev. Med. Virol. 20:281-297(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[5]	"Structure of a human common cold virus and functional relationship to other picornaviruses." Rossman M.G., Arnold E., Erickson J.W., Frankenberger E.A., Griffith J.P., Hecht H.-J., Johnson J.E., Kamer G., Luo M., Mosser A.G., Rueckert R.R., Sherry B., Vriend G. Nature 317:145-153(1985) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[6]	"The use of molecular-replacement phases for the refinement of the human rhinovirus 14 structure." Arnold E., Rossman M.G. Acta Crystallogr. A 44:270-282(1988) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[7]	"Structural studies of two rhinovirus serotypes complexed with fragments of their cellular receptor." Kolatkar P.R., Bella J., Olson N.H., Bator C.M., Baker T.S., Rossmann M.G. EMBO J. 18:6249-6259(1999) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF 70-856 IN COMPLEX WITH ICAM1.
[8]	"Analysis of the structure of a common cold virus, human rhinovirus 14, refined at a resolution of 3.0 A." Arnold E., Rossman M.G. J. Mol. Biol. 211:763-801(1990) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure complexed with antiviral compound SCH 38057

Virus Particle ExploreR db

Icosahedral capsid structure complexed with antiviral compound SDZ 35-682

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X01087 Genomic RNA. Translation: CAA25565.1.
L05355 Genomic RNA. Translation: AAA45758.1.
K02121 Genomic RNA. Translation: AAA45756.1.

PIR

GNNYH4. A03901.

RefSeq

NP_041009.1. NC_001490.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D3I	electron microscopy	26.00	1	568-856	[»]
			2	70-331	[»]
			3	332-567	[»]
			4	2-69	[»]
1HRI	X-ray	3.00	1	568-856	[»]
			2	70-331	[»]
			3	332-567	[»]
			4	2-69	[»]
1HRV	X-ray	3.00	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
1K5M	X-ray	2.70	A	568-856	[»]
			C	332-567	[»]
			D	2-69	[»]
1NA1	X-ray	3.30	A	568-856	[»]
			B	70-331	[»]
			C	332-567	[»]
			D	2-69	[»]
1NCQ	X-ray	2.50	A	568-856	[»]
			B	70-331	[»]
			C	332-567	[»]
			D	2-69	[»]
1R08	X-ray	3.00	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
1R09	X-ray	2.90	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
1RMU	X-ray	3.00	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
1RUC	X-ray	3.10	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
1RUD	X-ray	2.90	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
1RUE	X-ray	2.90	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
1RUF	X-ray	2.90	1	568-856	[»]
			2	70-331	[»]
			3	332-567	[»]
			4	2-69	[»]
1RUG	X-ray	3.00	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
1RUH	X-ray	3.00	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
1RUI	X-ray	3.00	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
1RUJ	X-ray	3.00	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
1RVF	X-ray	4.00	1	568-856	[»]
			2	70-331	[»]
			3	332-567	[»]
			4	2-69	[»]
1VRH	X-ray	3.00	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
1XR5	X-ray	2.80	A	1720-2179	[»]
2B0F	NMR	-	A	1538-1719	[»]
2HWB	X-ray	3.00	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
2HWC	X-ray	3.00	1	568-856	[»]
			2	70-331	[»]
			3	332-567	[»]
			4	2-69	[»]
2IN2	NMR	-	A	1538-1719	[»]
2R04	X-ray	3.00	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
2R06	X-ray	3.00	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
2R07	X-ray	3.00	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
2RM2	X-ray	3.00	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
2RMU	X-ray	3.00	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
2RR1	X-ray	3.00	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
2RS1	X-ray	3.00	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
2RS3	X-ray	3.00	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
2RS5	X-ray	3.00	1	568-855	[»]
			2	70-330	[»]
			3	332-566	[»]
			4	2-68	[»]
4RHV	X-ray	3.00	1	568-856	[»]
			2	70-331	[»]
			3	332-567	[»]
			4	2-69	[»]

ProteinModelPortal

P03303.

SMR

P03303. Positions 2-69, 77-567, 574-856, 1429-1486, 1538-2179.

ModBase

Search...

Protein family/group databases

MEROPS

C03.013.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1461213.

Family and domain databases

Gene3D

4.10.80.10. 2 hits.

InterPro

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.
[Graphical view]

Pfam

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]

ProDom

PD001306. Peptidase_C3. 1 hit.
PD649346. Pico_P2B. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00382. AAA. 1 hit.
[Graphical view]

SUPFAM

SSF89043. P3A. 1 hit.
SSF50494. Pept_Ser_Cys. 2 hits.
SSF52540. SSF52540. 1 hit.

PROSITE

PS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P03303.

Entry information

Entry name

POLG_HRV14

Accession

Primary (citable) accession number: P03303
Secondary accession number(s): Q82083 , Q82123, Q84736, Q84737, Q84738, Q84739, Q84740, Q84741, Q84774, Q84775, Q84776, Q84777, Q84778, Q84779, Q89441, Q89649, Q89763, Q89883

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 159 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program