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Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Protein VP2 (P1B) (Virion protein 2); Protein VP3 (P1C) (Virion protein 3); Protein VP1 (P1D) (Virion protein 1); Protein 2A (P2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Protein 3B (P3B) (VPg); Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]

 POLG_AEVVR              Reviewed;        2134 AA.
Q6R325;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 86.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Protein VP0;
AltName: Full=VP4-VP2;
Contains:
RecName: Full=Protein VP4;
AltName: Full=P1A;
AltName: Full=Virion protein 4;
Contains:
RecName: Full=Protein VP2;
AltName: Full=P1B;
AltName: Full=Virion protein 2;
Contains:
RecName: Full=Protein VP3;
AltName: Full=P1C;
AltName: Full=Virion protein 3;
Contains:
RecName: Full=Protein VP1;
AltName: Full=P1D;
AltName: Full=Virion protein 1;
Contains:
RecName: Full=Protein 2A;
Short=P2A;
Contains:
RecName: Full=Protein 2B;
Short=P2B;
Contains:
RecName: Full=Protein 2C;
Short=P2C;
EC=3.6.1.15;
Contains:
RecName: Full=Protein 3A;
Short=P3A;
Contains:
RecName: Full=Protein 3B;
Short=P3B;
AltName: Full=VPg;
Contains:
RecName: Full=Protease 3C;
Short=P3C;
EC=3.4.22.28;
AltName: Full=Picornain 3C;
Contains:
RecName: Full=RNA-directed RNA polymerase 3D-POL;
Short=P3D-POL;
EC=2.7.7.48;
Avian encephalomyelitis virus (strain Van Reokel) (AEV).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Tremovirus.
NCBI_TaxID=475779;
NCBI_TaxID=8835; Anas (ducks).
NCBI_TaxID=9031; Gallus gallus (Chicken).
NCBI_TaxID=9005; Phasianidae (turkeys).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Guan Y., Ge J., Chen H.;
"The complete genomic sequence of avian encephalomyelitis virus strain
van Roekel.";
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: 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).
{ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- FUNCTION: Protein 2B and 2BC precursor affect membrane integrity
and cause an increase in membrane permeability. {ECO:0000250}.
-!- FUNCTION: Protein 2C: Associates with and induces structural
rearrangements of intracellular membranes. It displays RNA-
binding, nucleotide binding and NTPase activities (By similarity).
{ECO:0000250}.
-!- FUNCTION: Protein 3A, via its hydrophobic domain, serves as
membrane anchor. {ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- FUNCTION: 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). {ECO:0000250}.
-!- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic
and antigenomic RNA by recognizing replications specific signals.
{ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: 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.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- SUBCELLULAR LOCATION: Protein VP2: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein VP3: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein VP1: Virion. Host cytoplasm
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein 2B: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. 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). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 2C: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. 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). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 3A: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. 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). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 3B: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protease 3C: Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: Host
cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane
protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
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). {ECO:0000250}.
-!- PTM: 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).
{ECO:0000250}.
-!- PTM: 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).
{ECO:0000250}.
-!- MISCELLANEOUS: Strain Van Reokel is an egg-adapted strain.
-!- SIMILARITY: Belongs to the picornaviridae polyprotein family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY517471; AAS01728.1; -; Genomic_RNA.
ProteinModelPortal; Q6R325; -.
SMR; Q6R325; -.
MEROPS; C03.005; -.
PRIDE; Q6R325; -.
OrthoDB; VOG0900028T; -.
Proteomes; UP000006887; Genome.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd00205; rhv_like; 2.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR024354; Hepatitis_A_VP1-2A.
InterPro; IPR007053; LRAT-like_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001676; Picornavirus_capsid.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
Pfam; PF12944; HAV_VP; 1.
Pfam; PF04970; LRAT; 1.
Pfam; PF00548; Peptidase_C3; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00073; Rhv; 2.
Pfam; PF00910; RNA_helicase; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
3: Inferred from homology;
ATP-binding; Capsid protein; Complete proteome;
Covalent protein-RNA linkage; Helicase; Host cytoplasm;
Host cytoplasmic vesicle; Host membrane; Host-virus interaction;
Hydrolase; Ion channel; Ion transport; Membrane; Nucleotide-binding;
Nucleotidyltransferase; Phosphoprotein; Protease; RNA-binding;
RNA-directed RNA polymerase; Thiol protease; Transferase; Transport;
Viral attachment to host cell; Viral ion channel;
Viral RNA replication; Virion; Virus entry into host cell.
CHAIN 1 2134 Genome polyprotein. {ECO:0000250}.
/FTId=PRO_0000310508.
CHAIN 1 242 Protein VP0. {ECO:0000255}.
/FTId=PRO_0000310509.
CHAIN 1 19 Protein VP4. {ECO:0000255}.
/FTId=PRO_0000310510.
CHAIN 20 242 Protein VP2. {ECO:0000255}.
/FTId=PRO_0000310511.
CHAIN 243 487 Protein VP3. {ECO:0000255}.
/FTId=PRO_0000310512.
CHAIN 488 757 Protein VP1. {ECO:0000255}.
/FTId=PRO_0000310513.
CHAIN 758 806 Protein 2A. {ECO:0000255}.
/FTId=PRO_0000310514.
CHAIN 807 1021 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000310515.
CHAIN 1022 1347 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000310516.
CHAIN 1348 1412 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000310517.
CHAIN 1413 1433 Protein 3B. {ECO:0000255}.
/FTId=PRO_0000310518.
CHAIN 1434 1648 Protease 3C. {ECO:0000255}.
/FTId=PRO_0000310519.
CHAIN 1649 2134 RNA-directed RNA polymerase 3D-POL.
{ECO:0000255}.
/FTId=PRO_0000310520.
TOPO_DOM 1 1377 Cytoplasmic. {ECO:0000255}.
INTRAMEM 1378 1392 {ECO:0000255}.
TOPO_DOM 1393 2134 Cytoplasmic. {ECO:0000255}.
DOMAIN 1127 1289 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1433 1627 Peptidase C3.
DOMAIN 1880 2001 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1153 1160 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
COMPBIAS 251 254 Poly-Ser.
ACT_SITE 1477 1477 For protease 3C activity. {ECO:0000250}.
ACT_SITE 1515 1515 For protease 3C activity. {ECO:0000250}.
ACT_SITE 1603 1603 For protease 3C activity. {ECO:0000250}.
SITE 19 20 Cleavage. {ECO:0000255}.
SITE 242 243 Cleavage; by protease 3C. {ECO:0000255}.
SITE 487 488 Cleavage; by protease 3C. {ECO:0000255}.
SITE 757 758 Cleavage; by host. {ECO:0000255}.
SITE 806 807 Cleavage; by protease 3C. {ECO:0000250}.
SITE 1021 1022 Cleavage; by protease 3C. {ECO:0000255}.
SITE 1347 1348 Cleavage; by protease 3C. {ECO:0000255}.
SITE 1412 1413 Cleavage; by protease 3C. {ECO:0000255}.
SITE 1433 1434 Cleavage; by protease 3C. {ECO:0000255}.
SITE 1648 1649 Cleavage; by protease 3C. {ECO:0000250}.
MOD_RES 1415 1415 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
SEQUENCE 2134 AA; 239104 MW; 121FDDD3360D7C02 CRC64;
MSKLFSTVGR TVDEVLSVLN DEDTESYAGP DRTAVVGGGF LTTVDQSSVS TATMGSLQDV
QYRTAVDIPG SRVTQGERFF LIDQREWNST QSEWQLLGKI DIVKELLDQS YAVDGLLKYH
SYARFGLDVI VQINPTSFQA GGLIAALVPY DQVDIESIAA MTTYCHGKLN CNINNVVRMK
VPYIYSRGCY NLRNSAYSIW MLVIRVWSRL QLGSGTSTQI TITTLARFVD LELHGLSPLV
AQMMRNEFRL SSSSNIVNLA NYEDARAKVS LALGQEGFSR DSSSTGGGML YHFSQWTSIP
CLAFIFTFPG TVGPGTRIWS TTVDPFSCNL RAFSTVHPTN LSSIAGMFCF WRGDIVFEFQ
VFRTKYHSGR LMFVYVPGDE NTKISTLTAT QASSGLTAVF DINGVNSTLV FRCPFISDTP
YRVNPTTHKS PWPYATGKLV CYVYNRLNAP ASVSPSVSIN VYKSAVDLEL YAPVYGVSPT
NTSVFAQGKG DEGGFSSVPE VEQHVVEDKE PQGPLHVTPF GAVKAMEDPQ LARKTPGTFP
ELAPGKPRHT VDHMDLYKFM GRAHYLWGHK FTKTDMQYTF QIPLSPIKEG FVTGTLRWFL
SLFQLYRGSL DITMTFAGKT NVDGIVYFVP EGVAIETERK EQTPLLTLNY KTSVGAIRFN
TGQTTNVQFR IPFYTPLEHI ATHSKNAMDS VLGAITTQIT NYSAQDEYLQ VTYYISFNED
SQFSVPRAVP VVSSFTDTSS KTVMNTYWLD DDELVEESSH FSFDEIEEAQ CSKCKIDLGD
IVSCSGEKAK HFGVYVGDGV VHVDPEGNAT SWFMKRKATV KKSKNLDKWC FALSPRIDRT
LICETANLMV GREVEYDIFV KNCETYARGI ASGDYGTKEG EKWKTLLSAV GVAAMTTTMM
AMRHELLDTS LTKLPQKVGE VTDEVRKILE DTSAGVREFK EKVSSILRKT WPGKTSIKIM
KWTCRIVKMC VGVGLCYMHG WDSKTVTAVV TMFSMDFLDL VIDGIEIGRM IIDELTTPKA
QGLSEINQVL SIAKNAKDVI KMLIEIFCKV IERITGEHGK KIQWAQDKKE EIMNVLERAE
KWITTSDDHS EGIECLKLVR SIQSVIRGEE SLKELAGELR AVGTHVLNKL GRLDKPNAPI
LVRAEPTVLY LYGNRGGGKS LASMAIAVKL CKELGISHVE GIYTKPIMSD FWDGYAGQPV
VIMDDLGQST SDEDWTNFCQ LVSSCPLRLN MANLEKKGTQ FNSPFIIASS NLSHPCPKTV
YCTDAIARRL HIKVKVSPKE EFSTHAMLDV AKAKKVGAYC NLDCLDLQKI SDLASTPVSV
QDIVLEMLHT NVDKQTLMGD IIQYWAQSNP REVFDTMAEG KNSGKYLWLF ERLKTSKWYI
LGCVGAVLAV SALGVFAYHM IKNHFRDQQH DQSAYSVAIK PLRVVRLEQS DAQSVVDISN
VVHGNLVRVG VGPNEARIHW LYNGLGVYDT YILMPYHGIK DADVDDDLYI ERAGTIYSTN
MKMVQVLFLE SREGDLVLIN VPRLPKFRDI RNHFSTEENI RRAEGMPGTL CTLDHERFTL
VTESDLKMVE AATYVCEDDK GVRTDISVGR SWKAKACTVA GMCGGALVTS NNKMQNAIVG
IHVAGGAHAI SRVITKEMIE EMLKTRAQCS RIWKTEFVEE KISVGSKTKY HKSPLYDFCP
QEVVKCPTKL FYQGEIDVMQ VMLAKYSSPI VSEPSGYATV VEAYTNRMVS FFPEPRQLTY
DECINGIEGL DAIDLKTSAG FPYNTLGLRK SDLIINGKMA HRLQQDVEKM EEDLHMNRSI
QVVFTTCAKD ELRPLSKVML GKTRAIEACP VSFTILFRRY LGYALAQIQS HPGFHTGIAV
GVDPDQDWHC MWYSIVTQCD LVVGLDFSNY DASLSPFMIY HAGRVLGQIC GLDPRLVDRI
MEPIVNSVHQ LGSMRYYVHG SMPSGTPATS VLNSIINVVN ICYVLCALEE ISVFEVFKLF
KILTYGDDVL LCIKKEYLDQ KSFPLSSFVQ GLEELGLSPT GADKMEVKVT PVHKMSFLKR
TFYVDEWSIC HPRISEETVY SMLAWKSDNA SMKDLIETSI WFMFHHGPRK YVRFCTWLRG
VLCRVGIGLY IPTYKELEVR YDRLVKYRFI DDNF


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