O41174 (POLG_PEV9U) 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	Porcine enterovirus 9 (strain UKG/410/73) [Complete proteome]
Taxonomic identifier	64141 [NCBI]
Taxonomic lineage	Viruses › ssRNA viruses › ssRNA positive-strand viruses, no DNA stage › Picornavirales › Picornaviridae › Enterovirus › Enterovirus G
Virus host	Sus scrofa (Pig) [TaxID: 9823]

Protein attributes

Sequence length	2168 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	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. 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. It also inhibits endoplasmic reticulum-to-Golgi transport 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 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 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 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 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 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 – 315	314	Protein VP0 Potential		PRO_0000311077
	Chain	2 – 69	68	Protein VP4 Potential		PRO_0000040058
	Chain	70 – 315	246	Protein VP2 Potential		PRO_0000040059
	Chain	316 – 553	238	Protein VP3 Potential		PRO_0000040060
	Chain	554 – 835	282	Protein VP1 Potential		PRO_0000040061
	Chain	836 – 985	150	Picornain 2A Potential		PRO_0000040062
	Chain	986 – 1084	99	Protein 2B Potential		PRO_0000040063
	Chain	1085 – 1413	329	Protein 2C Potential		PRO_0000040064
	Chain	1414 – 1502	89	Protein 3A Potential		PRO_0000040065
	Chain	1503 – 1524	22	Protein 3B Potential		PRO_0000040066
	Chain	1525 – 1707	183	Picornain 3C Potential		PRO_0000040067
	Chain	1708 – 2168	461	RNA-directed RNA polymerase 3D-POL Potential		PRO_0000040068
Regions
	Topological domain	2 – 1479	1478	Cytoplasmic Potential
	Intramembrane	1480 – 1495	16	Potential
	Topological domain	1496 – 2168	673	Cytoplasmic Potential
	Domain	1189 – 1347	159	SF3 helicase
	Domain	1934 – 2048	115	RdRp catalytic
	Nucleotide binding	1213 – 1220	8	ATP Potential
Sites
	Active site	856	1	For picornain 2A activity By similarity
	Active site	874	1	For picornain 2A activity By similarity
	Active site	945	1	For picornain 2A activity By similarity
	Active site	1564	1	For picornain 3C activity Potential
	Active site	1595	1	For picornain 3C activity Potential
	Active site	1671	1	For picornain 3C activity By similarity
	Site	69 – 70	2	Cleavage Potential
	Site	315 – 316	2	Cleavage; by picornain 3C Potential
	Site	835 – 836	2	Cleavage; by picornain 2A Potential
	Site	985 – 986	2	Cleavage; by picornain 3C Potential
	Site	1084 – 1085	2	Cleavage; by picornain 3C Potential
	Site	1413 – 1414	2	Cleavage; by picornain 3C Potential
	Site	1502 – 1503	2	Cleavage; by picornain 3C Potential
	Site	1524 – 1525	2	Cleavage; by picornain 3C Potential
	Site	1707 – 1708	2	Cleavage; by picornain 3C Potential
Amino acid modifications
	Modified residue	1505	1	O-(5'-phospho-RNA)-tyrosine By similarity
	Lipidation	2	1	N-myristoyl glycine; by host By similarity

Sequences

	Sequence		Length	Mass (Da)
	O41174 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 028E839E665E3180	FASTA	2,168	241,238
	10 20 30 40 50 60 MGMQMSKNTA GSHTTVTQAS GGSHINYTNI NYYSHSASAS QNKQDITQDP SKFTQPMVDI 70 80 90 100 110 120 MKESAVPLKS PSAEACGYSD RVAQLTLGNS TITTQEAANI TVAYGEWPSY LSDLDATAVD 130 140 150 160 170 180 KTTKPGVSCD RFYTLPGKKW EATTKGWEWK LPDALTELGV FGQNCQFHFL YRCGWSIHVQ 190 200 210 220 230 240 CNATKFHQGT LLVVAVPDHQ LGTTYQPEFD NVMPGKAGRE VKYPYNFEDG TSLANSLIYP 250 260 270 280 290 300 HQWINLRTNN SATLVLPYAN AIPMDSPIRH SSWSLLVIPV VPLACATGTT PFVGITITLA 310 320 330 340 350 360 PMFSEFSGLR RAIAQGIPTT NTPGSYQFLT TDEDSSACIL PDFTPTQEIH IPGEVKNLQA 370 380 390 400 410 420 LCQVESLLEI NNVDGKTGIE RLRLEVSTQS ELDRQLFALK VSFTEGEIMS KTLCGVMCSY 430 440 450 460 470 480 YTQWSGSLEI TFMFTGSFMT TGKLLLAYTP PGGSAPASRE DAMLGTHVIW DFGLQSSITL 490 500 510 520 530 540 VVPWICGGYY RDVNRANNYY AAGYVTGWFQ TNMVIPPDFP STAYILCFLA AQPNFSLRIL 550 560 570 580 590 600 KDRPDITQTA ALQAPVETAL NSAISSVIAG ITAQDTQPSS HNISTSETPA LQAAETGASS 610 620 630 640 650 660 NASDEGMMET RHVVNTNTVS ETSIESFYGR CGLVSIKEIA DNKQVEKWLV NFNEFVQLRA 670 680 690 700 710 720 KIELFTYMRF DIEFTLVATF TKGNSASQHP VQVQVMYLPP EQLLQLQQDS YAWQSAANPS 730 740 750 760 770 780 AIFSANTVPA RFSVPFVGTA NAYTIMYDGY NVFGSNRPSA DYGMINSSHM GSMAFRAISQ 790 800 810 820 830 840 LQATEKVKFM DLCQVKDVRA WCPRAPRMAP YKYIRNPVFE TQDRIVPNRN NITTTGAFGQ 850 860 870 880 890 900 QSGAIYVGNY KIMNRHLATH EDWENVEWED YNRDILVART TAHGADKLAR CHCNTGVYYC 910 920 930 940 950 960 KSRNKHYPVT SRVQASIGSR LVSTTQLDTR PICSLPSGIS EPGDCGGILR CQHGVIGIVT 970 980 990 1000 1010 1020 AGGQGVVGFA DVRDLFWVEH EAMEQGLTDY IQQLGNSFGQ GFTAEITNYA SQLSEMLIGA 1030 1040 1050 1060 1070 1080 DGMVERCLQT FVKVISAVVI ATRSQGDVPT ILATLALIGC DGSPWRWLKR QFCGIFKIPY 1090 1100 1110 1120 1130 1140 VEKQGDDWLK KFTSYVNAFK GLDWVAEKIM KFIDWMKNKL IPQARERQEF TTNLKTLPLL 1150 1160 1170 1180 1190 1200 EAQVATLEHS CPTTEQQETI FGNIQYLAHH CRRYAPLYAA EARRVYALEK RILGYIQFKS 1210 1220 1230 1240 1250 1260 KQRIEPVCLL IHGTAGTGKS LATSIIGRKL AEYEHSEVYA IPPDSDHFDG YQQQAVVVMD 1270 1280 1290 1300 1310 1320 DLNQNPDGKD MVAFCQMVST VPYHVPMAAI EEKGMLFTSS YVLASTNSGS IHPPTVSNSK 1330 1340 1350 1360 1370 1380 ALSRRFAFDV DIEVSEHYKT HNGTLDVVNA TQRCEDCCPA NFKTCMPLIC GEAYQLVDRR 1390 1400 1410 1420 1430 1440 NGMRYSIDTM ISAMRAEWKR RNQVGLCYVR LFQGPPQFKP LKISVDPEIP APPAIADLLA 1450 1460 1470 1480 1490 1500 SVDSEEVREY CKKKGWIVEV PVTATTLERN VSIATTILSS LVLLTSVITL VYLVYRLFAG 1510 1520 1530 1540 1550 1560 YQGPYTGLPN AKPKPPVLRE VRAQGPLMDF GVGMMKKNIV TVRTGAGEFT GLGVHDHVLV 1570 1580 1590 1600 1610 1620 LPKHSHPAEI VVVDGKETPV EDAYNLTDEQ GVSLELTLVT LKRNEKFRDI RAMIPENPCG 1630 1640 1650 1660 1670 1680 TNEAVVCVNT SNFPNAFLPV GKVEYYGYLN LAGSPTHRTM MYNFPTKAGQ CGGVVLSTGK 1690 1700 1710 1720 1730 1740 VLGIHIGGNG AQGFCAALKR SYFTKPQGKI DWVEPSKKHG FPVINAPSKT KLEPSVFFDV 1750 1760 1770 1780 1790 1800 FEGVKEPAAL HPKDPRLEVN LEEALFSKYT GNVDIEMPEE MKEAVDHYAN QLLALDIPTE 1810 1820 1830 1840 1850 1860 PLSMEEAIYG TEGLEALDLT TSAGYPYVTM GIKKRDILNK ETRDVKKMQE CIDKYGLNLP 1870 1880 1890 1900 1910 1920 MVTYIKDELR SKEKVKKGKS RLIEASSLND SVAMRCYFGN LYKAFHQNPG TLTGCAVGCD 1930 1940 1950 1960 1970 1980 PDTFWSKIPV MMDGELFGFD YTAYDASLSP LMFQALQMVL EKIGFGEGKH FIDNLCYSHH 1990 2000 2010 2020 2030 2040 LFRDKYYFVK GGMPSGCSGT SIFNSMINNI IIRTVVLQTY KGIELDQLKI IAYGDDVIAS 2050 2060 2070 2080 2090 2100 YPYRIDPAEL AKAGAKLGLH MTPPDKSETY VDLDWTNVTF LKRNFVPDEK YPFLVHPVMP 2110 2120 2130 2140 2150 2160 MKEIYESIRW TRDARNTQDH VRSLCLLAWH NGRKEYEEFC RKIRSVPVGR ALHLPSYSSL LREWYEKF

References

[1]	"Nucleotide sequence of porcine enterovirus serotype 9 and its relationship to other members of the family Picornaviridae, genus Enterovirus." Peng J.H., McCauley J.W., Kitching R.P., Knowles N.J. Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y14459 Genomic RNA. Translation: CAA74807.1.
3D structure databases
ProteinModelPortal	O41174.
SMR	O41174. Positions 23-62, 74-314, 316-553, 1525-2168.
ModBase	Search...
Protein family/group databases
MEROPS	C03.014.
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. 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...

Entry information

Entry name

POLG_PEV9U

Accession

Primary (citable) accession number: O41174

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 116 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program