UniProtKB - Q9YLS4 (POLG_AEVCA)
Protein
Genome polyprotein
Gene
N/A
Organism
Avian encephalomyelitis virus (strain Calnek vaccine) (AEV)
Status
Functioni
Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these 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).By similarity
VP0 precursor is a component of immature procapsids. The N-terminal domain of VP0, protein VP4, is needed for the assembly of 12 pentamers into the icosahedral structure. Unlike other picornaviruses, AEV VP4 may not be myristoylated (By similarity).By similarity
Protein 2B and 2BC precursor affect membrane integrity and cause an increase in membrane permeability.By similarity
Associates with and induces structural rearrangements of intracellular membranes. It displays RNA-binding, nucleotide binding and NTPase activities (By similarity).By similarity
Protein 3A, via its hydrophobic domain, serves as membrane anchor.By similarity
Protein 3B is covalently linked to the 5'-end of both the positive-strand and negative-strand genomic RNAs. It acts as a genome-linked replication primer (By similarity).By similarity
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 cooperatively to the protease (By similarity).By similarity
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals.PROSITE-ProRule annotation
Catalytic activityi
- 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.PROSITE-ProRule annotation EC:3.4.22.28
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 791 | PROSITE-ProRule annotation | 1 | |
Active sitei | 802 | PROSITE-ProRule annotation | 1 | |
Active sitei | 863 | Acyl-thioester intermediatePROSITE-ProRule annotation | 1 | |
Active sitei | 1477 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1515 | For protease 3C activityPROSITE-ProRule annotation | 1 | |
Active sitei | 1603 | For protease 3C activityPROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 1153 – 1160 | ATPPROSITE-ProRule annotation | 8 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- cysteine-type endopeptidase activity Source: UniProtKB-EC
- ion channel activity Source: UniProtKB-KW
- RNA binding Source: UniProtKB-KW
- RNA-directed 5'-3' RNA polymerase activity Source: UniProtKB-KW
- RNA helicase activity Source: InterPro
- structural molecule activity Source: InterPro
GO - Biological processi
- pore formation by virus in membrane of host cell Source: UniProtKB-KW
- protein complex oligomerization Source: UniProtKB-KW
- RNA-protein covalent cross-linking Source: UniProtKB-KW
- transcription, DNA-templated Source: InterPro
- viral entry into host cell Source: UniProtKB-KW
- viral RNA genome replication Source: InterPro
- virion attachment to host cell Source: UniProtKB-KW
Keywordsi
Molecular function | Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel |
Biological process | Host-virus interaction, Ion transport, Transport, Viral attachment to host cell, Viral RNA replication, Virus entry into host cell |
Ligand | ATP-binding, Nucleotide-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Genome polyproteinCleaved into the following 12 chains: Alternative name(s): VP4-VP2 Alternative name(s): P1A Virion protein 4 Alternative name(s): P1B Virion protein 2 Alternative name(s): P1C Virion protein 3 Alternative name(s): P1D Virion protein 1 Alternative name(s): VPg Alternative name(s): Picornain 3C |
Organismi | Avian encephalomyelitis virus (strain Calnek vaccine) (AEV) |
Taxonomic identifieri | 475778 [NCBI] |
Taxonomic lineagei | Viruses › Riboviria › Orthornavirae › Pisuviricota › Pisoniviricetes › Picornavirales › Picornaviridae › Tremovirus › |
Virus hosti | Anas (ducks) [TaxID: 8835] Gallus gallus (Chicken) [TaxID: 9031] Phasianidae (turkeys) [TaxID: 9005] |
Proteomesi |
|
Subcellular locationi
- Virion
- Host cytoplasm Curated
- Virion
- Host cytoplasm Curated
- Virion
- Host cytoplasm Curated
- Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated 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).By similarity
- Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated 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. May associate with membranes through a N-terminal amphipathic helix (By similarity).By similarity
- Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated 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).By similarity
- Virion Curated
- Host cytoplasm Curated
- Host cytoplasmic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated Note: Interacts with membranes in a complex with viral protein 3AB. 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).By similarity
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 1 – 1377 | CytoplasmicSequence analysisAdd BLAST | 1377 | |
Intramembranei | 1378 – 1392 | Sequence analysisAdd BLAST | 15 | |
Topological domaini | 1393 – 2134 | CytoplasmicSequence analysisAdd BLAST | 742 |
GO - Cellular componenti
- host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
- integral to membrane of host cell Source: UniProtKB-KW
- membrane Source: UniProtKB-KW
- viral capsid Source: UniProtKB-KW
Keywords - Cellular componenti
Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Membrane, VirionPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000310495 | 1 – 2134 | Genome polyproteinAdd BLAST | 2134 | |
ChainiPRO_0000310496 | 1 – 242 | Protein VP0Sequence analysisAdd BLAST | 242 | |
ChainiPRO_0000310497 | 1 – 19 | Protein VP4Sequence analysisAdd BLAST | 19 | |
ChainiPRO_0000310498 | 20 – 242 | Protein VP2Sequence analysisAdd BLAST | 223 | |
ChainiPRO_0000310499 | 243 – 487 | Protein VP3Sequence analysisAdd BLAST | 245 | |
ChainiPRO_0000310500 | 488 – 757 | Protein VP1Sequence analysisAdd BLAST | 270 | |
ChainiPRO_0000310501 | 758 – 806 | Protein 2ASequence analysisAdd BLAST | 49 | |
ChainiPRO_0000310502 | 807 – 1021 | Protein 2BSequence analysisAdd BLAST | 215 | |
ChainiPRO_0000310503 | 1022 – 1347 | Protein 2CSequence analysisAdd BLAST | 326 | |
ChainiPRO_0000310504 | 1348 – 1412 | Protein 3ASequence analysisAdd BLAST | 65 | |
ChainiPRO_0000310505 | 1413 – 1433 | Protein 3BSequence analysisAdd BLAST | 21 | |
ChainiPRO_0000310506 | 1434 – 1648 | Protease 3CSequence analysisAdd BLAST | 215 | |
ChainiPRO_0000310507 | 1649 – 2134 | RNA-directed RNA polymerase 3D-POLSequence analysisAdd BLAST | 486 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1415 | O-(5'-phospho-RNA)-tyrosineBy similarity | 1 |
Post-translational modificationi
Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins. 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).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).By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 19 – 20 | CleavageSequence analysis | 2 | |
Sitei | 242 – 243 | Cleavage; by protease 3CSequence analysis | 2 | |
Sitei | 487 – 488 | Cleavage; by protease 3CSequence analysis | 2 | |
Sitei | 757 – 758 | Cleavage; by hostSequence analysis | 2 | |
Sitei | 806 – 807 | Cleavage; by protease 3CBy similarity | 2 | |
Sitei | 1021 – 1022 | Cleavage; by protease 3CSequence analysis | 2 | |
Sitei | 1347 – 1348 | Cleavage; by protease 3CSequence analysis | 2 | |
Sitei | 1412 – 1413 | Cleavage; by protease 3CSequence analysis | 2 | |
Sitei | 1433 – 1434 | Cleavage; by protease 3CSequence analysis | 2 | |
Sitei | 1648 – 1649 | Cleavage; by protease 3CBy similarity | 2 |
Keywords - PTMi
Covalent protein-RNA linkage, PhosphoproteinProteomic databases
PRIDEi | Q9YLS4 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 781 – 882 | LRATPROSITE-ProRule annotationAdd BLAST | 102 | |
Domaini | 1127 – 1289 | SF3 helicasePROSITE-ProRule annotationAdd BLAST | 163 | |
Domaini | 1431 – 1643 | Peptidase C3PROSITE-ProRule annotationAdd BLAST | 213 | |
Domaini | 1880 – 2001 | RdRp catalyticPROSITE-ProRule annotationAdd BLAST | 122 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 251 – 254 | Poly-Ser | 4 |
Sequence similaritiesi
Belongs to the picornaviridae polyprotein family.Curated
Family and domain databases
CDDi | cd00205, rhv_like, 2 hits |
Gene3Di | 2.40.10.10, 2 hits 2.60.120.20, 3 hits 3.30.70.270, 1 hit |
InterProi | View protein in InterPro IPR043502, DNA/RNA_pol_sf IPR000605, Helicase_SF3_ssDNA/RNA_vir IPR014759, Helicase_SF3_ssRNA_vir IPR024354, Hepatitis_A_VP1-2A IPR007053, LRAT_dom IPR027417, P-loop_NTPase IPR044067, PCV_3C_PRO IPR000199, Peptidase_C3A/C3B_picornavir IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR001676, Picornavirus_capsid IPR043128, Rev_trsase/Diguanyl_cyclase IPR033703, Rhv-like IPR001205, RNA-dir_pol_C IPR007094, RNA-dir_pol_PSvirus IPR029053, Viral_coat |
Pfami | View protein in Pfam PF12944, HAV_VP, 1 hit PF04970, LRAT, 1 hit PF00548, Peptidase_C3, 1 hit PF00680, RdRP_1, 1 hit PF00073, Rhv, 2 hits PF00910, RNA_helicase, 1 hit |
SUPFAMi | SSF50494, SSF50494, 1 hit SSF52540, SSF52540, 1 hit SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS51934, LRAT, 1 hit PS51874, PCV_3C_PRO, 1 hit PS50507, RDRP_SSRNA_POS, 1 hit PS51218, SF3_HELICASE_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q9YLS4-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSKLFSTVGK TVDEVLSVLN DENTESYAGP DRTAVVGGGF LTTVDQSSVS
60 70 80 90 100
TATMGSLQDV QYRTAVDIPG SRVTQGERFF LIDQREWNST QSEWQLLGKI
110 120 130 140 150
DIVKELLDQS YAVDGLLKYH SYARFGLDVI VQINPTSFQA GGLIAALVPY
160 170 180 190 200
DQVDIESIAA MTTYCHGKLN CNINNVVRMK VPYIYSRGCY NLRNSAYSIW
210 220 230 240 250
MLVIRVWSQL QLGSGTSTQI TVTTLARFVD LELHGLSPLV AQMMRNEFRL
260 270 280 290 300
SSSSNIVNLA NYEDARAKVS LALGQEEFSR DSSSTGGELL HHFSQWTSIP
310 320 330 340 350
CLAFTFTFPG TVGPGTQIWS TTVDPFSCNL RASSTVHPTN LSSIAGMFCF
360 370 380 390 400
WRGDIVFEFQ VFCTKYHSGR LMFVYVPGDE NTKISTLTAK QASSGLTAVF
410 420 430 440 450
DINGVNSTLV FRCPFISDTP YRVNPTTHKS LWPYATGKLV CYVYNRLNAP
460 470 480 490 500
ASVSPSVSIN VYKSAVDLEL YAPVYGVSPT NTSVFAQGKE DEGGFSSVPE
510 520 530 540 550
VEQHVVEDKE PQGPLHVTPF GAVKAMEDPQ LARKTPGTFP ELAPGKPRHT
560 570 580 590 600
VDHMDLYKFM GRAHYLWGHK FTKTDMQYTF QIPLSPIKEG FVTGTLRWFL
610 620 630 640 650
SLFQLYRGSL DITMTFAGKT NVDGIVYFVP EGVAIETERE EQTPLLTLNY
660 670 680 690 700
KTSVGAIRFN TGQTTNVQFR IPFYTPLEHI ATHSKNAMDS VLGAITTQIT
710 720 730 740 750
NYSAQDEYLQ VTYYISFNED SQFSVPRAVP VVSSFTDTSS KTVMNTYWLD
760 770 780 790 800
DDELVEESSH SSFDEIEEAQ CSKCKMDLGD IVSCSGEKAK HFGVYVGDGV
810 820 830 840 850
VHVDPEGNAT NWFMKRKATV KKSKNLDKWC FALSPRIDRT LICETANLMV
860 870 880 890 900
GREVEYDIFV KNCETYARGI ASGDYGTKEG EKWKTLLSAV GVAAMTTTMM
910 920 930 940 950
AMRHELLDTS LTKLPQKVGE VTNEVRKILE DTSAGVREFK EKVSSILRKT
960 970 980 990 1000
WPGKTSIKIM KWTCRIVKMC VGVGLCYAHG WDSKTVTAVV TMFSMDFLDL
1010 1020 1030 1040 1050
VIDGIEIGRM IIDELTTPKA QGLSEINQVL SIAKNAKDVI KMLIEIFCKV
1060 1070 1080 1090 1100
IERITGEHGK KIQWAQDKKE EIMNVLERAE KWITTSDDHS EGIECLKLVR
1110 1120 1130 1140 1150
SIQSVIRGEE SLKELAGELR AVGTHVLNKL GRLDKPNAPI LVRAEPTVLY
1160 1170 1180 1190 1200
LYGNRGGGKS LASMAIAVKL CKELGISHVE GIYTKPIMSD FWDGYAGQPV
1210 1220 1230 1240 1250
VIMDDLGQST SDEDWTNFCQ LVSSCPLRLN MANLEKKGTQ FNSPFIIASS
1260 1270 1280 1290 1300
NLSHPCPKTV YCTDAIARRL HIKVKVSPKE EFSTHAMLDV AKAKKAGAYC
1310 1320 1330 1340 1350
NLDCLDFQKI SDLASTPVSV QDIVLEMLHT NVDKQTLMGD IIQYWAQSNP
1360 1370 1380 1390 1400
REVFDTMAEG KNSGKYLWLF EKIKTSKWYI LGCVGAVLSV SVLGVFAYHM
1410 1420 1430 1440 1450
IKNHFRDQQH DQSAYSAAIK PLRVVRLEQS DAQSVVDISN VVHGNLVRVG
1460 1470 1480 1490 1500
VGPNEARIHW LYNGLGVYDT YILMPYHGIK DADVDDDLYI ERAGTIYSTN
1510 1520 1530 1540 1550
MKMVQVLFLE SREGDLVLIN VPRLPKFRDI RNHFSTEENI RRAEGMPGTL
1560 1570 1580 1590 1600
CTLDHERFTL VTESDLKMVE AATYVCEDDK GVRTDISVGR SWKAKACTVA
1610 1620 1630 1640 1650
GMCGGALVTS NNKMQNAIVG IHVAGGAHAI SRVITKEMIE EMLKTRAQCS
1660 1670 1680 1690 1700
RIWKTEFVEE KISVGSKTKY HKSPLYDFCP QEVIKCPTKL FYQGEIDVMQ
1710 1720 1730 1740 1750
VMLAKYSSPI VSEPLGYATV VEAYTNRMVS FFSEPRQLTY DECINGIEGL
1760 1770 1780 1790 1800
DAIDLKTSAG FPYNTLGLRK SDLIINGKMA QRLQQDVEKM EEDLHMNRSI
1810 1820 1830 1840 1850
QVVFTTCAKD ELRPLSKVML GKTRAIEACP VSFTILFRRY LGYALAQIQS
1860 1870 1880 1890 1900
HPGFHTGIAV GVDPDQDWHC MWYSIVTQCD LVVGLDFSNY DASLSPFMIY
1910 1920 1930 1940 1950
HAGRVLGQIC GLDPRLVDRI MEPIVNSVHQ LGSMRYYVHG SMPSGTPATS
1960 1970 1980 1990 2000
VLNSIINVVN ICHVLCALEK ISVFEVFKLF KILTYGDDVL LCIKKEYLDQ
2010 2020 2030 2040 2050
KSFPLSSFVQ GLEELGLSPT GADKMEVKVT PVHKMSFLKR TFYVDEWSIC
2060 2070 2080 2090 2100
HPRISEETVY SMLAWKSDNA SMKDLIETSI WFMFHHGPRK YVRFCTWLRG
2110 2120 2130
VLCRVGIGLY IPTYKELEVR YDRLVKYRFI DDSF
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ225173 mRNA Translation: CAA12416.1 |
RefSeqi | NP_653151.1, NC_003990.1 |
Genome annotation databases
GeneIDi | 944582 |
KEGGi | vg:944582 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ225173 mRNA Translation: CAA12416.1 |
RefSeqi | NP_653151.1, NC_003990.1 |
3D structure databases
SMRi | Q9YLS4 |
ModBasei | Search... |
Proteomic databases
PRIDEi | Q9YLS4 |
Genome annotation databases
GeneIDi | 944582 |
KEGGi | vg:944582 |
Family and domain databases
CDDi | cd00205, rhv_like, 2 hits |
Gene3Di | 2.40.10.10, 2 hits 2.60.120.20, 3 hits 3.30.70.270, 1 hit |
InterProi | View protein in InterPro IPR043502, DNA/RNA_pol_sf IPR000605, Helicase_SF3_ssDNA/RNA_vir IPR014759, Helicase_SF3_ssRNA_vir IPR024354, Hepatitis_A_VP1-2A IPR007053, LRAT_dom IPR027417, P-loop_NTPase IPR044067, PCV_3C_PRO IPR000199, Peptidase_C3A/C3B_picornavir IPR009003, Peptidase_S1_PA IPR043504, Peptidase_S1_PA_chymotrypsin IPR001676, Picornavirus_capsid IPR043128, Rev_trsase/Diguanyl_cyclase IPR033703, Rhv-like IPR001205, RNA-dir_pol_C IPR007094, RNA-dir_pol_PSvirus IPR029053, Viral_coat |
Pfami | View protein in Pfam PF12944, HAV_VP, 1 hit PF04970, LRAT, 1 hit PF00548, Peptidase_C3, 1 hit PF00680, RdRP_1, 1 hit PF00073, Rhv, 2 hits PF00910, RNA_helicase, 1 hit |
SUPFAMi | SSF50494, SSF50494, 1 hit SSF52540, SSF52540, 1 hit SSF56672, SSF56672, 1 hit |
PROSITEi | View protein in PROSITE PS51934, LRAT, 1 hit PS51874, PCV_3C_PRO, 1 hit PS50507, RDRP_SSRNA_POS, 1 hit PS51218, SF3_HELICASE_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | POLG_AEVCA | |
Accessioni | Q9YLS4Primary (citable) accession number: Q9YLS4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 13, 2007 |
Last sequence update: | May 1, 1999 | |
Last modified: | December 2, 2020 | |
This is version 117 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Viral Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families