P04936 (POLG_HRV2) 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 2 (HRV-2) [Complete proteome]
Taxonomic identifier	12130 [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	2150 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 VLDLR to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis. VP4 and VP1 subsequently undergo conformational changes leading to the formation of a pore in the endosomal membrane, thereby delivering the viral genome into the cytoplasm. Ref.3 Ref.4 VP0 precursor is a component of immature procapsids By similarity. Ref.3 Ref.4 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. Ref.3 Ref.4 Protein 2B affects membrane integrity and cause an increase in membrane permeability By similarity. Ref.3 Ref.4 Protein 2C associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities By similarity. Ref.3 Ref.4 Protein 3A, via its hydrophobic domain, serves as membrane anchor By similarity. Ref.3 Ref.4 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. Ref.3 Ref.4 RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity. Ref.3 Ref.4
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 VLDLR.
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-mediated 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 Pore-mediated penetration of viral genome into host cell 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 pore-mediated entry of viral genome into host cell 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 clathrin-mediated 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_0000311072

Chain

2 – 69

68

Protein VP4 Potential

PRO_0000040010

Chain

70 – 330

261

Protein VP2 Potential

PRO_0000040011

Chain

331 – 567

237

Protein VP3 Potential

PRO_0000040012

Chain

568 – 856

289

Protein VP1 Potential

PRO_0000040013

Chain

857 – 992

136

Picornain 2A Potential

PRO_0000040014

Chain

993 – 1087

95

Protein 2B Potential

PRO_0000040015

Chain

1088 – 1409

322

Protein 2C Potential

PRO_0000040016

Chain

1410 – 1486

77

Protein 3A Potential

PRO_0000040017

Chain

1487 – 1507

21

Protein 3B Potential

PRO_0000040018

Chain

1508 – 1690

183

Picornain 3C Potential

PRO_0000040019

Chain

1691 – 2150

460

RNA-directed RNA polymerase 3D-POL Potential

PRO_0000040020

Regions

Topological domain

2 – 1463

1462

Cytoplasmic Potential

Intramembrane

1464 – 1479

16

Potential

Topological domain

1480 – 2150

671

Cytoplasmic Potential

Domain

1181 – 1343

163

SF3 helicase

Domain

1918 – 2031

114

RdRp catalytic

Nucleotide binding

1211 – 1218

8

ATP Potential

Sites

Active site

868

1

For picornain 2A activity

Active site

885

1

For picornain 2A activity

Active site

956

1

For picornain 2A activity

Active site

1547

1

For picornain 3C activity Potential

Active site

1578

1

For picornain 3C activity Potential

Active site

1654

1

For picornain 3C activity Probable

Site

69 – 70

2

Cleavage Potential

Site

330 – 331

2

Cleavage; by picornain 3C Potential

Site

856 – 857

2

Cleavage; by picornain 2A Potential

Site

992 – 993

2

Cleavage; by picornain 3C Potential

Site

1409 – 1410

2

Cleavage; by picornain 3C Potential

Site

1486 – 1487

2

Cleavage; by picornain 3C Potential

Site

1507 – 1508

2

Cleavage; by picornain 3C Potential

Site

1690 – 1691

2

Cleavage; by picornain 3C Potential

Amino acid modifications

Modified residue

1489

1

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

Lipidation

2

1

N-myristoyl glycine; by host By similarity

Secondary structure

1

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2150

Helix Strand Turn

Details...

Helix

233 – 235

3

Beta strand

855 – 866

12

Helix

867 – 869

3

Helix

874 – 876

3

Beta strand

878 – 881

4

Helix

882 – 884

3

Beta strand

886 – 896

11

Beta strand

906 – 911

6

Turn

912 – 915

4

Beta strand

916 – 921

6

Beta strand

923 – 930

8

Beta strand

938 – 948

11

Beta strand

959 – 962

4

Beta strand

965 – 973

9

Beta strand

975 – 982

8

Helix

983 – 986

4

Helix

1509 – 1521

13

Beta strand

1522 – 1527

6

Beta strand

1530 – 1539

10

Beta strand

1541 – 1545

5

Helix

1546 – 1548

3

Beta strand

1552 – 1556

5

Beta strand

1559 – 1570

12

Beta strand

1576 – 1584

9

Helix

1593 – 1596

4

Beta strand

1604 – 1611

8

Beta strand

1615 – 1617

3

Beta strand

1619 – 1628

10

Beta strand

1632 – 1634

3

Beta strand

1637 – 1639

3

Beta strand

1641 – 1645

5

Helix

1651 – 1653

3

Beta strand

1657 – 1660

4

Beta strand

1663 – 1671

9

Beta strand

1676 – 1680

5

Helix

1683 – 1685

3

Sequences

	Sequence		Length	Mass (Da)
	P04936 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 6E0DF9F4945D9D0C	FASTA	2,150	241,978
	10 20 30 40 50 60 MGAQVSRQNV GTHSTQNSVS NGSSLNYFNI NYFKDAASNG ASKLEFTQDP SKFTDPVKDV 70 80 90 100 110 120 LEKGIPTLQS PTVEACGYSD RIIQITRGDS TITSQDVANA IVAYGVWPHY LSSKDASAID 130 140 150 160 170 180 KPSQPDTSSN RFYTLRSVTW SSSSKGWWWK LPDALKDMGI FGENMFYHYL GRSGYTIHVQ 190 200 210 220 230 240 CNASKFHQGT LIVALIPEHQ IASALHGNVN VGYNYTHPGE TGREVKAETR LNPDLQPTEE 250 260 270 280 290 300 YWLNFDGTLL GNITIFPHQF INLRSNNSAT IIAPYVNAVP MDSMRSHNNW SLVIIPICPL 310 320 330 340 350 360 ETSSAINTIP ITISISPMCA EFSGARAKRQ GLPVFITPGS GQFLTTDDFQ SPCALPWYHP 370 380 390 400 410 420 TKEISIPGEV KNLVEICQVD SLVPINNTDT YINSENMYSV VLQSSINAPD KIFSIRTDVA 430 440 450 460 470 480 SQPLATTLIG EISSYFTHWT GSLRFSFMFC GTANTTVKLL LAYTPPGIAE PTTRKDAMLG 490 500 510 520 530 540 THVIWDVGLQ STISMVVPWI SASHYRNTSP GRSTSGYITC WYQTRLVIPP QTPPTARLLC 550 560 570 580 590 600 FVSGCKDFCL RMARDTNLHL QSGAIAQNPV ENYIDEVLNE VLVVPNINSS NPTTSNSAPA 610 620 630 640 650 660 LDAAETGHTS SVQPEDVIET RYVQTSQTRD EMSLESFLGR SGCIHESKLE VTLANYNKEN 670 680 690 700 710 720 FTVWAINLQE MAQIRRKFEL FTYTRFDSEI TLVPCISALS QDIGHITMQY MYVPPGAPVP 730 740 750 760 770 780 NSRDDYAWQS GTNASVFWQH GQAYPRFSLP FLSVASAYYM FYDGYDEQDQ NYGTANTNNM 790 800 810 820 830 840 GSLCSRIVTE KHIHKVHIMT RIYHKAKHVK AWCPRPPRAL EYTRAHRTNF KIEDRSIQTA 850 860 870 880 890 900 IVTRPIITTA GPSDMYVHVG NLIYRNLHLF NSEMHESILV SYSSDLIIYR TNTVGDDYIP 910 920 930 940 950 960 SCDCTQATYY CKHKNRYFPI TVTSHDWYEI QESEYYPKHI QYNLLIGEGP CEPGDCGGKL 970 980 990 1000 1010 1020 LCKHGVIGIV TAGGDNHVAF IDLRHFHCAE EQGVTDYIHM LGEAFGNGFV DSVKEHIHAI 1030 1040 1050 1060 1070 1080 NPVGNISKKI IKWMLRIISA MVIIIRNSSD PQTILATLTL IGCSGSPWRF LKEKFCKWTQ 1090 1100 1110 1120 1130 1140 LNYIHKESDS WLKKFTEACN AARGLEWIGN KISKFIEWMK SMLPQAQLKV KYLNELKKLN 1150 1160 1170 1180 1190 1200 LYEKQVESLR VADMKTQEKI KMEIDTLHDL SRKFLPLYAS EAKRIKTLYI KCDNIIKQKK 1210 1220 1230 1240 1250 1260 RCEPVAIVIH GPPGAGKSIT TNFLAKMITN DSDIYSLPPD PKYFDGYDQQ SVVIMDDIMQ 1270 1280 1290 1300 1310 1320 NPAGDDMTLF CQMVSSVTFI PPMADLPDKG KAFDSRFVLC STNHSLLTPP TITSLPAMNR 1330 1340 1350 1360 1370 1380 RFFLDLDIIV HDNFKDPQGK LNVAAAFRPC DVDNRIGNAR CCPFVCGKAV SFKDRNSCNK 1390 1400 1410 1420 1430 1440 YSLAQVYNIM IEEDRRRRQV VDVMTAIFQG PIDMKNPPPP AITDLLQSVR TPEVIKYCEG 1450 1460 1470 1480 1490 1500 NRWIIPAECK IEKELNLANT IITIIANVIG MARIIYVIYK LFCTLQGPYS GEPKPKTKIP 1510 1520 1530 1540 1550 1560 ERRVVTQGPE EEFGMSLIKH NSCVITTENG KFTGLGVYDR FVVVPTHADP GKEIQVDGIT 1570 1580 1590 1600 1610 1620 TKVIDSYDLY NKNGIKLEIT VLKLDRNEKF RDIRRYIPNN EDDYPNCNLA LLANQPEPTI 1630 1640 1650 1660 1670 1680 INVGDVVSYG NILLSGNQTA RMLKYSYPTK SGYCGGVLYK IGQVLGIHVG GNGRDGFSAM 1690 1700 1710 1720 1730 1740 LLRSYFTDVQ GQITLSKKTS ECNLPSIHTP CKTKLQPSVF YDVFPGSKEP AVLSEKDARL 1750 1760 1770 1780 1790 1800 QVDFNEALFS KYKGNTDCSI NDHIRIASSH YAAQLITLDI DPKPITLEDS VFGTDGLEAL 1810 1820 1830 1840 1850 1860 DLNTSAGFPY IAMGVKKRDL INNKTKDISK LKEAIDKYGV DLPMVTFLKD ELRKHEKVIK 1870 1880 1890 1900 1910 1920 GKTRVIEASS VNDTLLFRTT FGNLFSKFHL NPGIVTGSAV GCDPEVFWSK IPAMLDDKCI 1930 1940 1950 1960 1970 1980 MAFDYTNYDG SIHPIWFEAL KQVLVDLSFN PTLIDRLCKS KHIFKNTYYE VEGGVPSGCS 1990 2000 2010 2020 2030 2040 GTSIFNTMIN NIIIRTLVLD AYKNIDLDKL KIIAYGDDVI FSYIHELDME AIAIEGVKYG 2050 2060 2070 2080 2090 2100 LTITPADKSN TFVKLDYSNV TFLKRGFKQD EKYNFLIHPT FPEDEIFESI RWTKKPSQMH 2110 2120 2130 2140 2150 EHVLSLCHLM WHNGRDAYKK FVEKIRSVSA GRALYIPPYD LLLHEWYEKF

References

[1]	"Human rhinovirus 2: complete nucleotide sequence and proteolytic processing signals in the capsid protein region." Skern T., Sommergruber W., Blaas D., Gruendler P., Fraundorfer F., Pieler C., Fogy I., Kuechler E. Nucleic Acids Res. 13:2111-2126(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]	Kuechler E. Submitted (FEB-1986) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A in vitro." Glaser W., Skern T. FEBS Lett. 480:151-155(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF THE LEADER PROTEASE.
[4]	"The concerted conformational changes during human rhinovirus 2 uncoating." Hewat E.A., Neumann E., Blaas D. Mol. Cell 10:317-326(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF VP1 AND VP4.
[5]	"Uncoating of human rhinoviruses." Fuchs R., Blaas D. Rev. Med. Virol. 20:281-297(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[6]	"Three-dimensional structure of the Fab fragment of a neutralizing antibody to human rhinovirus serotype 2." Tormo J., Stadler E., Skern T., Auer H., Kanzler O., Betzel C., Blaas D., Fita I. Protein Sci. 1:1154-1161(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 225-239.
[7]	"The structure of the 2A proteinase from a common cold virus: a proteinase responsible for the shut-off of host-cell protein synthesis." Petersen J.F., Cherney M.M., Liebig H.D., Skern T., Kuechler E., James M.N. EMBO J. 18:5463-5475(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 851-992.
[8]	"Structure-assisted design of mechanism-based irreversible inhibitors of human rhinovirus 3C protease with potent antiviral activity against multiple rhinovirus serotypes." Matthews D.A., Dragovich P.S., Webber S.E., Fuhrman S.A., Patick A.K., Zalman L.S., Hendrickson T.F., Love R.A., Prins T.J., Marakovits J.T., Zhou R., Tikhe J., Ford C.E., Meador J.W., Ferre R.A., Brown E.L., Binford S.L., Brothers M.A., DeLisle D.M., Worland S.T. Proc. Natl. Acad. Sci. U.S.A. 96:11000-11007(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1508-1687.
[9]	"Structure of human rhinovirus serotype 2 (HRV2)." Verdaguer N., Blaas D., Fita I. J. Mol. Biol. 300:1179-1194(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 71-856.
+	Additional computationally mapped references.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure associated with cellular receptor

Virus Particle ExploreR db

Icosahedral capsid structure complexed with cellular receptor fragment

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X02316 Genomic RNA. Translation: CAA26181.1.

PIR

GNNYH2. A03902.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A3R	X-ray	2.10	P	225-239	[»]
1CQQ	X-ray	1.85	A	1508-1687	[»]
1FPN	X-ray	2.60	1	568-856	[»]
			2	70-330	[»]
			3	331-567	[»]
			4	2-69	[»]
1V9U	X-ray	3.60	1	568-856	[»]
			2	70-330	[»]
			3	331-567	[»]
			4	2-69	[»]
2HRV	X-ray	1.95	A/B	851-992	[»]
2XYA	X-ray	2.40	A	1508-1687	[»]
3DPR	X-ray	3.50	A	568-856	[»]
			B	70-330	[»]
			C	331-567	[»]
			D	2-69	[»]
3TN9	X-ray	3.00	1	568-856	[»]
			2	70-330	[»]
			3	331-567	[»]
3VDD	X-ray	3.20	A	568-850	[»]
			B	70-330	[»]
			C	331-567	[»]
			D	1-69	[»]

ProteinModelPortal

P04936.

SMR

P04936. Positions 2-68, 81-567, 582-989, 1508-1687, 1691-2150.

ModBase

Search...

Protein family/group databases

MEROPS

C03.021.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

P04936.

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

EvolutionaryTrace

P04936.

Entry information

Entry name

POLG_HRV2

Accession

Primary (citable) accession number: P04936

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 145 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program