Q9YID8 (POLG_HPE23) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Genome polyprotein Cleaved into the following 10 chains: Protein VP0 Alternative name(s): P1AB Virion protein 0 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 parechovirus 2 (strain CT86-6760) (HPeV-2) (Echovirus 23) [Complete proteome]
Taxonomic identifier	122961 [NCBI]
Taxonomic lineage	Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Picornavirales › Picornaviridae › Parechovirus › Human parechovirus › Human parechovirus 5
Virus host	Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	2188 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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.
Subcellular location	Protein VP3: Virion By similarity. Host cytoplasm Potential. Protein VP1: Virion By similarity. 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	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. Specific enzymatic cleavages yield mature proteins. All cleavages are catalyzed by P3C.
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	Host-virus interaction Ion transport Transport Viral RNA replication Viral attachment to host cell 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	Complete proteome
Gene Ontology (GO)
Biological_process	RNA-protein covalent cross-linking Inferred from electronic annotation. Source: UniProtKB-KW ion transport Inferred from electronic annotation. Source: UniProtKB-KW proteolysis 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 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 viral genome Inferred from electronic annotation. Source: InterPro
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
	Chain	1 – 290	290	Protein VP0 Potential		PRO_0000039740
	Chain	291 – 549	259	Protein VP3 Potential		PRO_0000039741
	Chain	550 – 784	235	Protein VP1 Potential		PRO_0000039742
	Chain	785 – 931	147	Picornain 2A Potential		PRO_0000039743
	Chain	932 – 1053	122	Protein 2B Potential		PRO_0000039744
	Chain	1054 – 1382	329	Protein 2C Potential		PRO_0000039745
	Chain	1383 – 1499	117	Protein 3A Potential		PRO_0000039747
	Chain	1500 – 1519	20	Protein 3B By similarity		PRO_0000311174
	Chain	1520 – 1719	200	Picornain 3C Potential		PRO_0000039748
	Chain	1720 – 2188	469	RNA-directed RNA polymerase 3D-POL Potential		PRO_0000039749
Regions
	Domain	1165 – 1326	162	SF3 helicase
	Domain	1953 – 2067	115	RdRp catalytic
	Nucleotide binding	1193 – 1200	8	ATP Potential
	Motif	772 – 774	3	Cell attachment site Potential
Sites
	Active site	1558	1	For picornain 3C activity Potential
	Active site	1589	1	For picornain 3C activity Potential
	Active site	1678	1	For picornain 3C activity Potential
	Site	784 – 785	2	Cleavage; by picornain 2A Potential
Amino acid modifications
	Modified residue	1502	1	O-(5'-phospho-RNA)-tyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9YID8 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 02CC77D0A5ED3D93	FASTA	2,188	246,604
	10 20 30 40 50 60 METIKSIADM ATGFTNTIDS TVNAVTEGVS KIGNDSGGEI LTKVADDASN LLGPNCVAST 70 80 90 100 110 120 SQPENKDVVQ ATTTVNTLTN LTQHPSAPTM PFTPDFSNVD VFHSMAYDIT TGDKNPSKLI 130 140 150 160 170 180 RLDTTTWQHT WPRQHLINDV ELPKAFWDKN SKPAYGQSRY FAAVRCGFHF QVQINVNQGT 190 200 210 220 230 240 AGCALVVYEP KPIVTHGGHL EFGSYTNLPH VLMNLAETTQ ADLCIPYVSD TNYVKTDSSD 250 260 270 280 290 300 LGRLRVYVWT PLTIPSSATN DVDVTVLGSL LQLDFQNPRT YDTDVNIYDN SPLDTKTKYG 310 320 330 340 350 360 KLRFSKKILS MSTKYKWTRN KIDIAEGPGS MNMANVLSTT GAQSIALVGE RAFYDPRTAG 370 380 390 400 410 420 SKSRFGDMIH IAQLFSVMSD TTTPSTSSGI DDLGYLDWSA TYVPQQVIHR NVVKLNQFSN 430 440 450 460 470 480 LKPFVNAYTY FRGSLVLRMS VYASTFNRGR LRMGFFPNFT TNTTSEMDNA IYTICDIGSD 490 500 510 520 530 540 NSFEITIPYT FSTWMRKTNG RPIGLFQVEV LNRLTYNSSC PNKVHCIVQG RLGNDARFYC 550 560 570 580 590 600 PTGSLVEFQN SWGSQMDLTD PLCVEDDEAE DCKQTISPDE LGLTSAQDDG PLGVEKPNYF 610 620 630 640 650 660 LNFRAINVDI FTVSHTKVDN IFGRAWLALE HTFADDGTWR ADLNFPTQGH GTLTRLFTYY 670 680 690 700 710 720 SGELNVHVLY LSDNGFLRVT HAYDHDNDRS NFLSSNGVIT VPAGEQMTLS VPFYSSKPLR 730 740 750 760 770 780 TIRETGALGK LICKPLLSGT HSGKIEVYLS LRCPNLFFPS PAPKEKTSRA LRGDLANFID 790 800 810 820 830 840 QSPYGQQQQT QMMKLAYLDR GFYKHYGIIV GGYVYQLDSD DIFKTALTGK ARFTKTRLTP 850 860 870 880 890 900 DWIVEEECEL DYFRVKYLES SVNSEHIFSV DSNCETIAKD IFGTHTLSQH QAIGLVGAIL 910 920 930 940 950 960 LTAGLMSTIK TPVNATTIKE FFNHAIDGDE QGLSLLVQKC TTFFSSAATE ILDNDLVKFI 970 980 990 1000 1010 1020 VKILVRILCY MVLYCHKPNI LTTACLSTLL IMDVTSSSVL SPSCKALMQC LMDGDVKKLA 1030 1040 1050 1060 1070 1080 EVVAESMSNT DDDEIKEQIC DTVKYTKTIL SNQGPFKGFN EVSTAFRHVD WWIHTLLKIK 1090 1100 1110 1120 1130 1140 DMVLSVFKPS IESKAIQWLE RNKEHVCSIL DYASDIIVES KDQTKMKTQE FYQRYSDCLA 1150 1160 1170 1180 1190 1200 KFKPIMAICF RSCHNSISNT VYRLFQELAR IPNRISTQND LIRVEPIGVW IQGEPGQGKS 1210 1220 1230 1240 1250 1260 FLTHTLSRQL QKSCKLNGVY TNPTASEFMD GYDNQDIHLI DDLGQTRKEK DIEMLCNCIS 1270 1280 1290 1300 1310 1320 SVPFIVPMAH LEEKGKFYTS KLVIATTNKS DFSSTVLQDS GALKRRFPYI MHIRAAKAYS 1330 1340 1350 1360 1370 1380 KSGKLNVSQA MSTMSTGECW EVSKNGRDWE TLKLKDLVQK ITEDYQERQK NYNAWKQQLE 1390 1400 1410 1420 1430 1440 NQTLDDLDDA VSYIKHNFPD AIPYIDEYLN IEMSTLIEQM EAFIEPRPSV FKCFAVKLPH 1450 1460 1470 1480 1490 1500 KPGKQPRKLW AGSAGKIKSM LSFIERNKAW LTVVSAVTSA ISILLLVTKI FKKEESKDER 1510 1520 1530 1540 1550 1560 AYNPTLPITK PKGTFPVSQR EFKNEAPYDG QLEHIISQMA YITGSTTGHL THCAGYQHDE 1570 1580 1590 1600 1610 1620 IILHGHSIKY LEQEEDLTLH YKNKVFPIEN PSVTQVTLGG KPMDLAILKC KLPFRFKKNS 1630 1640 1650 1660 1670 1680 KYYTNKIGTE SMLIWMTEQG IITKEVQRVH HSGGIKTREG TESTKTISYT VKSCKGMCGG 1690 1700 1710 1720 1730 1740 LLISKVEGNF KILGMHIAGN GEMGVAIPFN FLKNDMSDQG IITEVTPIQP MYINTKSQIH 1750 1760 1770 1780 1790 1800 KSPVYGAVEV KMGPAVLSKS DTRLEEPVDC LIKKSASKYR VNKFQVNNEL WQGVKACVKS 1810 1820 1830 1840 1850 1860 KFREIFGVNG IVDMKTAILG TSHVNSMDLS TSAGYSLVKS GYKKKDLICL EPFSVSPMLE 1870 1880 1890 1900 1910 1920 KLVQDKFHNL LKGNQITTIF NTCLKDELRK LDKIAAGKTR CIEACEVDYC IVYRMIMMEI 1930 1940 1950 1960 1970 1980 YDKIYQTPCY YSGLAVGINP YKDWHFMINA LNDYNYEMDY SQYDGSLSSM LLWEAVEVLA 1990 2000 2010 2020 2030 2040 YCHDSPDLVM QLHKPVIDSD HVVFNERWLI HGGMPSGSPC TTVLNSLCNL MMCIYTTNLI 2050 2060 2070 2080 2090 2100 SPGVDCLPIV YGDDVILSLD REIEPERLQS IMADSFGAEV TGSRKDEPPS LKPRMEVEFL 2110 2120 2130 2140 2150 2160 KRKPGYFPES TFIVGKLDTE NMIQHLMWMK NFSTFKQQLQ SYLMELCLHG KDIYQRYIKI 2170 2180 LDPYLKEWNI VVDDYDVVIA KLMPMVFD

References

[1]	"Complete sequence of echovirus 23 and its relationship to echovirus 22 and other human enteroviruses." Oberste M.S., Maher K., Pallansch M.A. Virus Res. 56:217-223(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF055846 Genomic RNA. Translation: AAC79756.1.
3D structure databases
ProteinModelPortal	Q9YID8.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR004004. Helic/Pol/Pept_Calicivir-typ. IPR000605. Helicase_SF3_ssDNA/RNA_vir. IPR014759. Helicase_SF3_ssRNA_vir. IPR027417. P-loop_NTPase. IPR000199. Peptidase_C3A/C3B_picornavir. IPR001676. Picornavirus_capsid. IPR001205. RNA-dir_pol_C. IPR007094. RNA-dir_pol_PSvirus. IPR009003. Trypsin-like_Pept_dom. IPR009419. VPP_parechovir_P3A. IPR009407. VPP_parechovir_P3B. [Graphical view]
Pfam	PF06344. Parecho_VpG. 1 hit. PF00548. Peptidase_C3. 1 hit. PF06363. Picorna_P3A. 1 hit. PF00680. RdRP_1. 1 hit. PF00073. Rhv. 2 hits. PF00910. RNA_helicase. 1 hit. [Graphical view]
PRINTS	PR00918. CALICVIRUSNS.
SUPFAM	SSF50494. Pept_Ser_Cys. 1 hit. SSF52540. SSF52540. 1 hit.
PROSITE	PS50507. RDRP_SSRNA_POS. 1 hit. PS51218. SF3_HELICASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

POLG_HPE23

Accession

Primary (citable) accession number: Q9YID8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 1999
Last modified:	May 29, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program