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Q6R325

- POLG_AEVVR

UniProt

Q6R325 - POLG_AEVVR

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Protein
Genome polyprotein
Gene
N/A
Organism
Avian encephalomyelitis virus (strain Van Reokel) (AEV)
Status
Reviewed - Annotation score: 5 out of 5 - Protein inferred from homologyi

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.
Protein VP0: 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.
Protein 2B and 2BC precursor affect 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 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.
Protease 3C: 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.
RNA-directed RNA polymerase 3D-POL replicates genomic and antigenomic RNA by recognizing replications specific signals By similarity.

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei19 – 202Cleavage Reviewed prediction
Sitei242 – 2432Cleavage; by protease 3C Reviewed prediction
Sitei487 – 4882Cleavage; by protease 3C Reviewed prediction
Sitei757 – 7582Cleavage; by host Reviewed prediction
Sitei806 – 8072Cleavage; by protease 3C By similarity
Sitei1021 – 10222Cleavage; by protease 3C Reviewed prediction
Sitei1347 – 13482Cleavage; by protease 3C Reviewed prediction
Sitei1412 – 14132Cleavage; by protease 3C Reviewed prediction
Sitei1433 – 14342Cleavage; by protease 3C Reviewed prediction
Active sitei1477 – 14771For protease 3C activity By similarity
Active sitei1515 – 15151For protease 3C activity By similarity
Active sitei1603 – 16031For protease 3C activity By similarity
Sitei1648 – 16492Cleavage; by protease 3C By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1153 – 11608ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. RNA binding Source: UniProtKB-KW
  3. RNA helicase activity Source: InterPro
  4. RNA-directed RNA polymerase activity Source: UniProtKB-KW
  5. cysteine-type endopeptidase activity Source: InterPro
  6. ion channel activity Source: UniProtKB-KW
  7. structural molecule activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. RNA-protein covalent cross-linking Source: UniProtKB-KW
  2. pore formation by virus in membrane of host cell Source: UniProtKB-KW
  3. protein oligomerization Source: UniProtKB-KW
  4. suppression by virus of host RIG-I activity by RIG-I proteolysis Source: UniProtKB
  5. transcription, DNA-templated Source: InterPro
  6. viral RNA genome replication Source: InterPro
  7. viral entry into host cell Source: UniProtKB-KW
  8. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase, Ion channel, Nucleotidyltransferase, Protease, RNA-directed RNA polymerase, Thiol protease, Transferase, Viral ion channel

Keywords - Biological processi

Host-virus interaction, Ion transport, Transport, Viral attachment to host cell, Viral RNA replication, Virus entry into host cell

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Protein family/group databases

MEROPSiC03.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Genome polyprotein
Cleaved 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
Protein 2A
Short name:
P2A
Protein 2B
Short name:
P2B
Protein 2C (EC:3.6.1.15)
Short name:
P2C
Protein 3A
Short name:
P3A
Protein 3B
Short name:
P3B
Alternative name(s):
VPg
Protease 3C (EC:3.4.22.28)
Short name:
P3C
Alternative name(s):
Picornain 3C
OrganismiAvian encephalomyelitis virus (strain Van Reokel) (AEV)
Taxonomic identifieri475779 [NCBI]
Taxonomic lineageiVirusesssRNA positive-strand viruses, no DNA stagePicornaviralesPicornaviridaeTremovirus
Virus hostiAnas (ducks) [TaxID: 8835]
Gallus gallus (Chicken) [TaxID: 9031]
Phasianidae [TaxID: 9005]
ProteomesiUP000006887: Genome

Subcellular locationi

Chain Protein VP2 : Virion. Host cytoplasm Reviewed prediction
Chain Protein VP3 : Virion. Host cytoplasm Reviewed prediction
Chain Protein VP1 : Virion. Host cytoplasm Reviewed prediction
Chain Protein 2B : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 2C : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 3A : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.
Chain Protein 3B : Virion Reviewed prediction
Chain Protease 3C : Host cytoplasm Reviewed prediction
Chain RNA-directed RNA polymerase 3D-POL : Host cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side Reviewed prediction
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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 13771377Cytoplasmic Reviewed prediction
Add
BLAST
Intramembranei1378 – 139215 Reviewed prediction
Add
BLAST
Topological domaini1393 – 2134742Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. host cell cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  2. integral to membrane of host cell Source: UniProtKB-KW
  3. membrane Source: UniProtKB-KW
  4. viral capsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host cytoplasm, Host cytoplasmic vesicle, Host membrane, Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21342134Genome polyprotein By similarity
PRO_0000310508Add
BLAST
Chaini1 – 242242Protein VP0 Reviewed prediction
PRO_0000310509Add
BLAST
Chaini1 – 1919Protein VP4 Reviewed prediction
PRO_0000310510Add
BLAST
Chaini20 – 242223Protein VP2 Reviewed prediction
PRO_0000310511Add
BLAST
Chaini243 – 487245Protein VP3 Reviewed prediction
PRO_0000310512Add
BLAST
Chaini488 – 757270Protein VP1 Reviewed prediction
PRO_0000310513Add
BLAST
Chaini758 – 80649Protein 2A Reviewed prediction
PRO_0000310514Add
BLAST
Chaini807 – 1021215Protein 2B Reviewed prediction
PRO_0000310515Add
BLAST
Chaini1022 – 1347326Protein 2C Reviewed prediction
PRO_0000310516Add
BLAST
Chaini1348 – 141265Protein 3A Reviewed prediction
PRO_0000310517Add
BLAST
Chaini1413 – 143321Protein 3B Reviewed prediction
PRO_0000310518Add
BLAST
Chaini1434 – 1648215Protease 3C Reviewed prediction
PRO_0000310519Add
BLAST
Chaini1649 – 2134486RNA-directed RNA polymerase 3D-POL Reviewed prediction
PRO_0000310520Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1415 – 14151O-(5'-phospho-RNA)-tyrosine By similarity

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.
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.

Keywords - PTMi

Covalent protein-RNA linkage, Phosphoprotein

Proteomic databases

PRIDEiQ6R325.

Structurei

3D structure databases

ProteinModelPortaliQ6R325.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1127 – 1289163SF3 helicase
Add
BLAST
Domaini1433 – 1627195Peptidase C3
Add
BLAST
Domaini1880 – 2001122RdRp catalytic
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi251 – 2544Poly-Ser

Sequence similaritiesi

Family and domain databases

Gene3Di2.60.120.20. 3 hits.
InterProiIPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR007053. LRAT-like_dom.
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.
IPR029053. Viral_coat.
[Graphical view]
PfamiPF04970. LRAT. 1 hit.
PF00548. Peptidase_C3. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 2 hits.
PF00910. RNA_helicase. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6R325-1 [UniParc]FASTAAdd to Basket

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MSKLFSTVGR TVDEVLSVLN DEDTESYAGP DRTAVVGGGF LTTVDQSSVS     50
TATMGSLQDV QYRTAVDIPG SRVTQGERFF LIDQREWNST QSEWQLLGKI 100
DIVKELLDQS YAVDGLLKYH SYARFGLDVI VQINPTSFQA GGLIAALVPY 150
DQVDIESIAA MTTYCHGKLN CNINNVVRMK VPYIYSRGCY NLRNSAYSIW 200
MLVIRVWSRL QLGSGTSTQI TITTLARFVD LELHGLSPLV AQMMRNEFRL 250
SSSSNIVNLA NYEDARAKVS LALGQEGFSR DSSSTGGGML YHFSQWTSIP 300
CLAFIFTFPG TVGPGTRIWS TTVDPFSCNL RAFSTVHPTN LSSIAGMFCF 350
WRGDIVFEFQ VFRTKYHSGR LMFVYVPGDE NTKISTLTAT QASSGLTAVF 400
DINGVNSTLV FRCPFISDTP YRVNPTTHKS PWPYATGKLV CYVYNRLNAP 450
ASVSPSVSIN VYKSAVDLEL YAPVYGVSPT NTSVFAQGKG DEGGFSSVPE 500
VEQHVVEDKE PQGPLHVTPF GAVKAMEDPQ LARKTPGTFP ELAPGKPRHT 550
VDHMDLYKFM GRAHYLWGHK FTKTDMQYTF QIPLSPIKEG FVTGTLRWFL 600
SLFQLYRGSL DITMTFAGKT NVDGIVYFVP EGVAIETERK EQTPLLTLNY 650
KTSVGAIRFN TGQTTNVQFR IPFYTPLEHI ATHSKNAMDS VLGAITTQIT 700
NYSAQDEYLQ VTYYISFNED SQFSVPRAVP VVSSFTDTSS KTVMNTYWLD 750
DDELVEESSH FSFDEIEEAQ CSKCKIDLGD IVSCSGEKAK HFGVYVGDGV 800
VHVDPEGNAT SWFMKRKATV KKSKNLDKWC FALSPRIDRT LICETANLMV 850
GREVEYDIFV KNCETYARGI ASGDYGTKEG EKWKTLLSAV GVAAMTTTMM 900
AMRHELLDTS LTKLPQKVGE VTDEVRKILE DTSAGVREFK EKVSSILRKT 950
WPGKTSIKIM KWTCRIVKMC VGVGLCYMHG WDSKTVTAVV TMFSMDFLDL 1000
VIDGIEIGRM IIDELTTPKA QGLSEINQVL SIAKNAKDVI KMLIEIFCKV 1050
IERITGEHGK KIQWAQDKKE EIMNVLERAE KWITTSDDHS EGIECLKLVR 1100
SIQSVIRGEE SLKELAGELR AVGTHVLNKL GRLDKPNAPI LVRAEPTVLY 1150
LYGNRGGGKS LASMAIAVKL CKELGISHVE GIYTKPIMSD FWDGYAGQPV 1200
VIMDDLGQST SDEDWTNFCQ LVSSCPLRLN MANLEKKGTQ FNSPFIIASS 1250
NLSHPCPKTV YCTDAIARRL HIKVKVSPKE EFSTHAMLDV AKAKKVGAYC 1300
NLDCLDLQKI SDLASTPVSV QDIVLEMLHT NVDKQTLMGD IIQYWAQSNP 1350
REVFDTMAEG KNSGKYLWLF ERLKTSKWYI LGCVGAVLAV SALGVFAYHM 1400
IKNHFRDQQH DQSAYSVAIK PLRVVRLEQS DAQSVVDISN VVHGNLVRVG 1450
VGPNEARIHW LYNGLGVYDT YILMPYHGIK DADVDDDLYI ERAGTIYSTN 1500
MKMVQVLFLE SREGDLVLIN VPRLPKFRDI RNHFSTEENI RRAEGMPGTL 1550
CTLDHERFTL VTESDLKMVE AATYVCEDDK GVRTDISVGR SWKAKACTVA 1600
GMCGGALVTS NNKMQNAIVG IHVAGGAHAI SRVITKEMIE EMLKTRAQCS 1650
RIWKTEFVEE KISVGSKTKY HKSPLYDFCP QEVVKCPTKL FYQGEIDVMQ 1700
VMLAKYSSPI VSEPSGYATV VEAYTNRMVS FFPEPRQLTY DECINGIEGL 1750
DAIDLKTSAG FPYNTLGLRK SDLIINGKMA HRLQQDVEKM EEDLHMNRSI 1800
QVVFTTCAKD ELRPLSKVML GKTRAIEACP VSFTILFRRY LGYALAQIQS 1850
HPGFHTGIAV GVDPDQDWHC MWYSIVTQCD LVVGLDFSNY DASLSPFMIY 1900
HAGRVLGQIC GLDPRLVDRI MEPIVNSVHQ LGSMRYYVHG SMPSGTPATS 1950
VLNSIINVVN ICYVLCALEE ISVFEVFKLF KILTYGDDVL LCIKKEYLDQ 2000
KSFPLSSFVQ GLEELGLSPT GADKMEVKVT PVHKMSFLKR TFYVDEWSIC 2050
HPRISEETVY SMLAWKSDNA SMKDLIETSI WFMFHHGPRK YVRFCTWLRG 2100
VLCRVGIGLY IPTYKELEVR YDRLVKYRFI DDNF 2134
Length:2,134
Mass (Da):239,104
Last modified:July 5, 2004 - v1
Checksum:i121FDDD3360D7C02
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY517471 Genomic RNA. Translation: AAS01728.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY517471 Genomic RNA. Translation: AAS01728.1 .

3D structure databases

ProteinModelPortali Q6R325.
ModBasei Search...

Protein family/group databases

MEROPSi C03.005.

Proteomic databases

PRIDEi Q6R325.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.60.120.20. 3 hits.
InterProi IPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR014759. Helicase_SF3_ssRNA_vir.
IPR007053. LRAT-like_dom.
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.
IPR029053. Viral_coat.
[Graphical view ]
Pfami PF04970. LRAT. 1 hit.
PF00548. Peptidase_C3. 1 hit.
PF00680. RdRP_1. 1 hit.
PF00073. Rhv. 2 hits.
PF00910. RNA_helicase. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEi PS50507. RDRP_SSRNA_POS. 1 hit.
PS51218. SF3_HELICASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The complete genomic sequence of avian encephalomyelitis virus strain van Roekel."
    Guan Y., Ge J., Chen H.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].

Entry informationi

Entry nameiPOLG_AEVVR
AccessioniPrimary (citable) accession number: Q6R325
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

Strain Van Reokel is an egg-adapted strain.

Keywords - Technical termi

Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi