Q82122 (POLG_HRV16) 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 16 (HRV-16) [Complete proteome]
Taxonomic identifier	31708 [NCBI]
Taxonomic lineage	Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Picornavirales › Picornaviridae › Enterovirus › Rhinovirus A
Virus host	Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	2153 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. 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 By similarity. 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 By similarity.
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.

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 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 – 330

329

Protein VP0 Potential

PRO_0000311075

Chain

2 – 69

68

Protein VP4 Potential

PRO_0000040036

Chain

70 – 330

261

Protein VP2 Potential

PRO_0000040037

Chain

331 – 568

238

Protein VP3 Potential

PRO_0000040038

Chain

569 – 853

285

Protein VP1 Potential

PRO_0000040039

Chain

854 – 995

142

Picornain 2A Potential

PRO_0000040040

Chain

996 – 1090

95

Protein 2B Potential

PRO_0000040041

Chain

1091 – 1412

322

Protein 2C Potential

PRO_0000040042

Chain

1413 – 1489

77

Protein 3A Potential

PRO_0000040043

Chain

1490 – 1510

21

Protein 3B Potential

PRO_0000040044

Chain

1511 – 1693

183

Picornain 3C Potential

PRO_0000040045

Chain

1694 – 2153

460

RNA-directed RNA polymerase 3D-POL Potential

PRO_0000040046

Regions

Topological domain

2 – 1466

1465

Cytoplasmic Potential

Intramembrane

1467 – 1482

16

Potential

Topological domain

1483 – 2153

671

Cytoplasmic Potential

Domain

1186 – 1346

161

SF3 helicase

Domain

1921 – 2034

114

RdRp catalytic

Nucleotide binding

1214 – 1221

8

ATP Potential

Sites

Active site

871

1

For picornain 2A activity By similarity

Active site

888

1

For picornain 2A activity By similarity

Active site

959

1

For picornain 2A activity By similarity

Active site

1550

1

For picornain 3C activity Potential

Active site

1581

1

For picornain 3C activity Potential

Active site

1657

1

For picornain 3C activity By similarity

Site

69 – 70

2

Cleavage Potential

Site

330 – 331

2

Cleavage; by picornain 3C Potential

Site

853 – 854

2

Cleavage; by picornain 2A Potential

Site

995 – 996

2

Cleavage; by picornain 3C Potential

Site

1412 – 1413

2

Cleavage; by picornain 3C Potential

Site

1489 – 1490

2

Cleavage; by picornain 3C Potential

Site

1510 – 1511

2

Cleavage; by picornain 3C Potential

Site

1693 – 1694

2

Cleavage; by picornain 3C Potential

Amino acid modifications

Modified residue

1492

1

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

Lipidation

2

1

N-myristoyl glycine; by host By similarity

Experimental info

Sequence conflict

547 – 548

2

KD → NH in AAA69862. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

2153

Helix Strand Turn

Details...

Beta strand

1695 – 1701

7

Helix

1702 – 1705

4

Turn

1722 – 1726

5

Helix

1747 – 1751

5

Helix

1752 – 1754

3

Helix

1765 – 1779

15

Helix

1790 – 1795

6

Beta strand

1805 – 1807

3

Turn

1811 – 1817

7

Helix

1820 – 1823

4

Turn

1826 – 1829

4

Helix

1832 – 1841

10

Beta strand

1847 – 1851

5

Beta strand

1854 – 1856

3

Helix

1859 – 1862

4

Beta strand

1868 – 1871

4

Helix

1874 – 1893

20

Turn

1897 – 1900

4

Helix

1907 – 1917

11

Beta strand

1920 – 1930

11

Helix

1931 – 1934

4

Helix

1937 – 1949

13

Helix

1958 – 1961

4

Beta strand

1962 – 1967

6

Beta strand

1970 – 1977

8

Helix

1985 – 2004

20

Helix

2010 – 2012

3

Beta strand

2014 – 2018

5

Beta strand

2021 – 2028

8

Helix

2032 – 2037

6

Helix

2038 – 2042

5

Beta strand

2046 – 2049

4

Turn

2060 – 2062

3

Beta strand

2068 – 2072

5

Beta strand

2079 – 2083

5

Helix

2086 – 2093

8

Beta strand

2095 – 2097

3

Helix

2099 – 2101

3

Helix

2102 – 2113

12

Helix

2114 – 2116

3

Helix

2118 – 2128

11

Helix

2132 – 2135

4

Helix

2142 – 2150

9

Sequences

	Sequence		Length	Mass (Da)
	Q82122 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 6B11D0D93DF11C04	FASTA	2,153	242,244
	10 20 30 40 50 60 MGAQVSRQNV GTHSTQNMVS NGSSLNYFNI NYFKDAASSG ASRLDFSQDP SKFTDPVKDV 70 80 90 100 110 120 LEKGIPTLQS PSVEACGYSD RIIQITRGDS TITSQDVANA VVGYGVWPHY LTPQDATAID 130 140 150 160 170 180 KPTQPDTSSN RFYTLDSKMW NSTSKGWWWK LPDALKDMGI FGENMFYHFL GRSGYTVHVQ 190 200 210 220 230 240 CNASKFHQGT LLVVMIPEHQ LATVNKGNVN AGYKYTHPGE AGREVGTQVE NEKQPSDDNW 250 260 270 280 290 300 LNFDGTLLGN LLIFPHQFIN LRSNNSATLI VPYVNAVPMD SMVRHNNWSL VIIPVCQLQS 310 320 330 340 350 360 NNISNIVPIT VSISPMCAEF SGARAKTVVQ GLPVYVTPGS GQFMTTDDMQ SPCALPWYHP 370 380 390 400 410 420 TKEIFIPGEV KNLIEMCQVD TLIPINSTQS NIGNVSMYTV TLSPQTKLAE EIFAIKVDIA 430 440 450 460 470 480 SHPLATTLIG EIASYFTHWT GSLRFSFMFC GTANTTLKVL LAYTPPGIGK PRSRKEAMLG 490 500 510 520 530 540 THVVWDVGLQ STVSLVVPWI SASQYRFTTP DTYSSAGYIT CWYQTNFVVP PNTPNTAEML 550 560 570 580 590 600 CFVSGCKDFC LRMARDTDLH KQTGPITQNP VERYVDEVLN EVLVVPNINQ SHPTTSNAAP 610 620 630 640 650 660 VLDAAETGHT NKIQPEDTIE TRYVQSSQTL DEMSVESFLG RSGCIHESVL DIVDNYNDQS 670 680 690 700 710 720 FTKWNINLQE MAQIRRKFEM FTYARFDSEI TMVPSVAAKD GHIGHIVMQY MYVPPGAPIP 730 740 750 760 770 780 TTRDDYAWQS GTNASVFWQH GQPFPRFSLP FLSIASAYYM FYDGYDGDTY KSRYGTVVTN 790 800 810 820 830 840 DMGTLCSRIV TSEQLHKVKV VTRIYHKAKH TKAWCPRPPR AVQYSHTHTT NYKLSSEVHN 850 860 870 880 890 900 DVAIRPRTNL TTVGPSDMYV HVGNLIYRNL HLFNSDIHDS ILVSYSSDLI IYRTSTQGDG 910 920 930 940 950 960 YIPTCNCTEA TYYCKHKNRY YPINVTPHDW YEIQESEYYP KHIQYNLLIG EGPCEPGDCG 970 980 990 1000 1010 1020 GKLLCKHGVI GIITAGGEGH VAFIDLRHFH CAEEQGITDY IHMLGEAFGS GFVDSVKDQI 1030 1040 1050 1060 1070 1080 NSINPINNIS SKMVKWMLRI ISAMVIIIRN SSDPQTIIAT LTLIGCNGSP WRFLKEKFCK 1090 1100 1110 1120 1130 1140 WTQLTYIHKE SDSWLKKFTE MCNAARGLEW IGNKISKFID WMKSMLPQAQ LKVKYLSELK 1150 1160 1170 1180 1190 1200 KLNFLEKQVE NLRAADTNTQ EKIKCEIDTL HDLSCKFLPL YASEAKRIKV LYHKCTNIIK 1210 1220 1230 1240 1250 1260 QKKRSEPVAV MIHGPPGTGK SITTSFLARM ITNESDIYSL PPDPKYFDGY DNQSVVIMDD 1270 1280 1290 1300 1310 1320 IMQNPGGEDM TLFCQMVSSV TFIPPMADLP DKGKPFDSRF VLCSTNHSLL APPTISSLPA 1330 1340 1350 1360 1370 1380 MNRRFYLDLD ILVHDNYKDN QGKLDVSRAF RLCDVDSKIG NAKCCPFVCG KAVTFKDRNT 1390 1400 1410 1420 1430 1440 CRTYSLSQIY NQILEEDKRR RQVVDVMSAI FQGPISMDKP PPPAITDLLR SVRTPEVIKY 1450 1460 1470 1480 1490 1500 CQDNKWIVPA DCQIERDLNI ANSIITIIAN IISIAGIIYI IYKLFCSLQG PYSGEPKPKT 1510 1520 1530 1540 1550 1560 KVPERRVVAQ GPEEEFGMSI IKNNTCVVTT TNGKFTGLGI YDRILILPTH ADPGSEIQVN 1570 1580 1590 1600 1610 1620 GIHTKVLDSY DLFNKEGVKL EITVLKLDRN EKFRDIRKYI PESEDDYPEC NLALVANQTE 1630 1640 1650 1660 1670 1680 PTIIKVGDVV SYGNILLSGT QTARMLKYNY PTKSGYCGGV LYKIGQILGI HVGGNGRDGF 1690 1700 1710 1720 1730 1740 SSMLLRSYFT EQQGQIQISK HVKDVGLPSI HTPTKTKLQP SVFYDIFPGS KEPAVLTEKD 1750 1760 1770 1780 1790 1800 PRLKVDFDSA LFSKYKGNTE CSLNEHIQVA VAHYSAQLAT LDIDPQPIAM EDSVFGMDGL 1810 1820 1830 1840 1850 1860 EALDLNTSAG YPYVTLGIKK KDLINNKTKD ISKLKLALDK YDVDLPMITF LKDELRKKDK 1870 1880 1890 1900 1910 1920 IAAGKTRVIE ASSINDTILF RTVYGNLFSK FHLNPGVVTG CAVGCDPETF WSKIPLMLDG 1930 1940 1950 1960 1970 1980 DCIMAFDYTN YDGSIHPIWF KALGMVLDNL SFNPTLINRL CNSKHIFKST YYEVEGGVPS 1990 2000 2010 2020 2030 2040 GCSGTSIFNS MINNIIIRTL VLDAYKHIDL DKLKIIAYGD DVIFSYKYKL DMEAIAKEGQ 2050 2060 2070 2080 2090 2100 KYGLTITPAD KSSEFKELDY GNVTFLKRGF RQDDKYKFLI HPTFPVEEIY ESIRWTKKPS 2110 2120 2130 2140 2150 QMQEHVLSLC HLMWHNGPEI YKDFETKIRS VSAGRALYIP PYELLRHEWY EKF

References

[1]	"Complete sequence of the RNA genome of human rhinovirus 16, a clinically useful common cold virus belonging to the ICAM-1 receptor group." Lee W.M., Wang W., Rueckert R.R. Virus Genes 9:177-181(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	"The structure of human rhinovirus 16." Oliveira M.A., Zhao R., Lee W.M., Kremer M.J., Minor I., Rueckert R.R., Diana G.D., Pevear D.C., Dutko F.J., McKinlay M.A., Rossmann M.G. Structure 1:51-68(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-853.
[3]	"The refined structure of human rhinovirus 16 at 2.15-A resolution: implications for the viral life cycle." Hadfield A.T., Lee W.M., Zhao R., Oliveira M.A., Minor I., Rueckert R.R., Rossmann M.G. Structure 5:427-441(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-853, SEQUENCE REVISION TO 547-548.
+	Additional computationally mapped references.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure at high resolution

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral drug VP63843 (pleconaril)

Virus Particle ExploreR db

Icosahedral capsid structure in complex with a two-domain fragment of its cellular receptor ICAM1

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound pleconaril

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound pleconaril

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound VP61209

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound WIN68934

Virus Particle ExploreR db

Icosahedral capsid structure in complex with antiviral compound VP65099

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L24917 Genomic RNA. Translation: AAA69862.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AYM	X-ray	2.15	1	569-853	[»]
			2	70-330	[»]
			3	331-568	[»]
1AYN	X-ray	2.90	1	569-853	[»]
			2	70-330	[»]
			3	331-568	[»]
			4	2-69	[»]
1C8M	X-ray	2.80	1	569-852	[»]
			2	79-329	[»]
			3	331-567	[»]
			4	2-77	[»]
1D3E	electron microscopy	28.00	1	574-853	[»]
			2	79-329	[»]
			3	331-567	[»]
			4	2-68	[»]
1NCR	X-ray	2.70	A	569-853	[»]
			B	70-330	[»]
			C	331-568	[»]
			D	2-69	[»]
1ND2	X-ray	2.50	A	569-853	[»]
			B	70-330	[»]
			C	331-568	[»]
			D	2-69	[»]
1ND3	X-ray	2.80	A	569-853	[»]
			B	70-330	[»]
			C	331-568	[»]
			D	2-69	[»]
1QJU	X-ray	2.80	1	569-853	[»]
			2	70-330	[»]
			3	331-568	[»]
			4	2-69	[»]
1QJX	X-ray	2.80	1	569-853	[»]
			2	70-330	[»]
			3	331-568	[»]
			4	2-69	[»]
1QJY	X-ray	2.80	1	569-853	[»]
			2	70-330	[»]
			3	331-568	[»]
			4	2-69	[»]
1TP7	X-ray	2.40	A/B/C/D	1694-2153	[»]
1XR7	X-ray	2.30	A/B	1694-2153	[»]

ProteinModelPortal

Q82122.

SMR

Q82122. Positions 2-69, 79-992, 1511-1690, 1694-2153.

ModBase

Search...

Protein family/group databases

MEROPS

C03.007.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

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.
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.

PROSITE

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

ProtoNet

Search...

Other

BindingDB

Q82122.

ChEMBL

CHEMBL5296.

EvolutionaryTrace

Q82122.

Entry information

Entry name

POLG_HRV16

Accession

Primary (citable) accession number: Q82122

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 130 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program