POLG_EBHSG
ID POLG_EBHSG Reviewed; 2334 AA.
AC Q96725;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Genome polyprotein;
DE AltName: Full=p254;
DE Contains:
DE RecName: Full=Protein p16;
DE Contains:
DE RecName: Full=Protein p23;
DE Contains:
DE RecName: Full=NTPase;
DE EC=3.6.1.15;
DE AltName: Full=2C-like protein;
DE AltName: Full=P2C;
DE AltName: Full=p37;
DE Contains:
DE RecName: Full=Precursor p41;
DE Contains:
DE RecName: Full=Protein p29;
DE Contains:
DE RecName: Full=Protein p23/2;
DE Contains:
DE RecName: Full=Protein p18;
DE Contains:
DE RecName: Full=Viral genome-linked protein;
DE AltName: Full=VPg;
DE AltName: Full=p13;
DE Contains:
DE RecName: Full=3C-like protease;
DE Short=3CLpro;
DE EC=3.4.22.66;
DE AltName: Full=Calicivirin;
DE AltName: Full=Thiol protease P3C;
DE AltName: Full=p15;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE AltName: Full=3Dpol;
DE AltName: Full=p58;
DE Contains:
DE RecName: Full=Capsid protein VP60;
GN ORFNames=ORF1;
OS European brown hare syndrome virus (strain GD) (Ha/LV/EBHSV/GD/1989/FR)
OS (EBHSV-GD).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Lagovirus.
OX NCBI_TaxID=316979;
OH NCBI_TaxID=9983; Lepus europaeus (European hare).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8760416; DOI=10.1099/0022-1317-77-8-1693;
RA Le Gall G., Huguet S., Vende P., Vautherot J.-F., Rasschaert D.;
RT "European brown hare syndrome virus: molecular cloning and sequencing of
RT the genome.";
RL J. Gen. Virol. 77:1693-1697(1996).
CC -!- FUNCTION: NTPase presumably plays a role in replication. {ECO:0000250}.
CC -!- FUNCTION: Viral genome-linked protein is covalently linked to the 5'-
CC end of the positive-strand, negative-strand genomic RNAs and subgenomic
CC RNA. Acts as a genome-linked replication primer. May recruit ribosome
CC to viral RNA thereby promoting viral proteins translation (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: 3C-like protease processes the polyprotein: 3CLpro-RdRp (p72)
CC is first released by autocleavage, then all other proteins are cleaved.
CC {ECO:0000250}.
CC -!- FUNCTION: RNA-directed RNA polymerase replicates genomic and
CC antigenomic RNA by recognizing replications specific signals.
CC Transcribes also a subgenomic mRNA by initiating RNA synthesis
CC internally on antigenomic RNA. This sgRNA codes for structural
CC proteins. Catalyzes the covalent attachment VPg with viral RNAs (By
CC similarity). {ECO:0000255|PROSITE-ProRule:PRU00539}.
CC -!- FUNCTION: Capsid protein VP60 self assembles to form an icosahedral
CC capsid with a T=3 symmetry, about 35 nm in diameter, and consisting of
CC 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm
CC might be capsid proteins assembled as icosahedron with T=1 symmetry.
CC The capsid encapsulate VP2 proteins and genomic or subgenomic RNA.
CC Attaches virion to target cells by binding histo-blood group antigens,
CC inducing endocytosis of the viral particle. Acidification of the
CC endosome induces conformational change of capsid protein thereby
CC injecting virus genomic RNA into host cytoplasm (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endopeptidase with a preference for cleavage when the P1
CC position is occupied by Glu-|-Xaa and the P1' position is occupied by
CC Gly-|-Yaa.; EC=3.4.22.66; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU01242};
CC -!- SUBUNIT: Binds to histo-blood group antigens at surface of target
CC cells. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein VP60]: Virion. Host cytoplasm
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=Genome polyprotein;
CC IsoId=Q96725-1; Sequence=Displayed;
CC Name=Subgenomic capsid protein VP60; Synonyms=VP1;
CC IsoId=Q96725-2; Sequence=VSP_034377;
CC -!- PTM: Specific enzymatic cleavages by its own cysteine protease yield
CC mature proteins. The protease cleaves itself from the nascent
CC polyprotein autocatalytically. Precursor p41 can be cleaved by viral
CC 3CLpro into protein p19 and VPg, or cleaved by host protease into
CC protein p23/2 and protein p18 (By similarity). {ECO:0000250}.
CC -!- PTM: VPg is uridylylated by the polymerase and is covalently attached
CC to the 5'-end of the polyadenylated genomic and subgenomic RNAs. This
CC uridylylated form acts as a nucleotide-peptide primer for the
CC polymerase (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Two different RNAs lead the expression of the capsid
CC protein. One arises from the cleavage of the polyprotein translated
CC from the genomic RNA and the other from the translation of a subgenomic
CC RNA derived from the (-)RNA template. Capsid protein expressed from the
CC subgenomic mRNA is produced in much larger amounts than the cleaved one
CC (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform Genome polyprotein]: Produced from the genomic
CC RNA.
CC -!- MISCELLANEOUS: [Isoform Subgenomic capsid protein VP60]: Produced from
CC the subgenomic RNA. {ECO:0000305}.
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DR EMBL; Z69620; CAA93445.1; -; Genomic_RNA.
DR EMBL; Z32526; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR RefSeq; NP_068828.1; NC_002615.1.
DR SMR; Q96725; -.
DR MEROPS; C24.001; -.
DR PRIDE; Q96725; -.
DR GeneID; 912265; -.
DR KEGG; vg:912265; -.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR CDD; cd00205; rhv_like; 1.
DR Gene3D; 2.60.120.20; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004005; Calicivirus_coat.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000317; Peptidase_C24.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR033703; Rhv-like.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF00915; Calici_coat; 1.
DR Pfam; PF03510; Peptidase_C24; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR PRINTS; PR00916; 2CENDOPTASE.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51894; CV_3CL_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 3: Inferred from homology;
KW Alternative promoter usage; ATP-binding; Capsid protein;
KW Covalent protein-RNA linkage; Disulfide bond; Helicase; Host cytoplasm;
KW Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW Protease; RNA-directed RNA polymerase; Thiol protease; Transferase;
KW Viral RNA replication; Virion.
FT CHAIN 1..2334
FT /note="Genome polyprotein"
FT /id="PRO_0000341986"
FT CHAIN 1..138
FT /note="Protein p16"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036986"
FT CHAIN 139..334
FT /note="Protein p23"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036987"
FT CHAIN 335..711
FT /note="NTPase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036988"
FT CHAIN 712..1108
FT /note="Precursor p41"
FT /id="PRO_0000341987"
FT CHAIN 712..986
FT /note="Protein p29"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036989"
FT CHAIN 712..929
FT /note="Protein p23/2"
FT /id="PRO_0000341988"
FT CHAIN 930..1101
FT /note="Protein p18"
FT /id="PRO_0000341989"
FT CHAIN 987..1101
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036990"
FT CHAIN 1102..1244
FT /note="3C-like protease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036991"
FT CHAIN 1245..1760
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036992"
FT CHAIN 1761..2334
FT /note="Capsid protein VP60"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036994"
FT DOMAIN 487..647
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1102..1237
FT /note="Peptidase C24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT DOMAIN 1488..1612
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 1760..1784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1128
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT ACT_SITE 1145
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT ACT_SITE 1205
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01242"
FT SITE 138..139
FT /note="Cleavage; by 3CLpro"
FT /evidence="ECO:0000250"
FT SITE 334..335
FT /note="Cleavage; by 3CLpro"
FT /evidence="ECO:0000250"
FT SITE 711..712
FT /note="Cleavage; by 3CLpro"
FT /evidence="ECO:0000250"
FT SITE 929..930
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 986..987
FT /note="Cleavage; by 3CLpro"
FT /evidence="ECO:0000250"
FT SITE 1101..1102
FT /note="Cleavage; by 3CLpro"
FT /evidence="ECO:0000250"
FT SITE 1244..1245
FT /note="Cleavage; by 3CLpro"
FT /evidence="ECO:0000250"
FT SITE 1760..1761
FT /note="Cleavage; by 3CLpro"
FT /evidence="ECO:0000250"
FT MOD_RES 1007
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250"
FT DISULFID 1577..1584
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..1758
FT /note="Missing (in isoform Subgenomic capsid protein VP60)"
FT /evidence="ECO:0000305"
FT /id="VSP_034377"
SQ SEQUENCE 2334 AA; 255925 MW; 3865CFA2457C0FB6 CRC64;
MAVASRPCGV ATSVLPAKKP LSFFTDLVGK TPPRCIRAPH TLAWPVFADL DNEEESPEIC
RKCGKYANGF GVFDLTDLGD VCLCSIRPQR HVGGPCCLCN KQYIRACGRY CARVLKHYKA
FNKVIPCLHS RQVKPVFEGE VEDLFVELGA PTRMNFTEAE LASQGASIMD RFVDLVEPCL
STEDSNFLDN ICSDASIRKR LEDEYDVDMI AAARARKDFA KTLKLALQDR ERKPDKWYSK
LGCITTKGRQ WAKKVVHGAK KLSDPLKTLA AILLVALHNC VAVDTTTMLS HFKPVNLLAI
LLDWTNDLPG FLTTLIRFME LYGVVQSTVN LVVDAIKSFW DRVMCATERC CDLLKRLFDK
FEDSVPTGPT AGCLIFMSFV FSVIVGYLPN NSVISTFMKG AGKLTTFAGV IGAIRTLWIT
INQHMVAKDI TSIQEKVMAV VKMANEAATL NQLEIVSVLC SELESTLTNR CTLPSYNQHM
GVLNAAQKVV ADIHTLVLGK INMTKQRPQP VAVVFKGAPG IGKTYLVHRL AKDLGCPHPS
NINFGLDHFD SYTGEDVAIA DEFNTSGDER WVELFIQMVN TNPCPLNCDK VENKNKVFSS
KYLLCTTNSS MVLNATHPRA TAFYRRVIIV DVRNKAVEGW QSTRHGSKPG KHCYTKDMSH
LTFQVYPHNM PAPGFVFVGE KLVKSQVAPR ELKYNELLDM IKNEHPDANF EGATKHEFVY
PDVQYEQALL MWKQYFLMYG CTARLAKVFV DDIPYNQVHV ARKSDPRSPG AVHHECELKY
IWRMVPHFAL GCVNMTNQLG TDLTQSQLDR ITCGVEGITV TTVDNILPFH SQNTLINPSF
LKLIWALRRH LRGLRGITQV ATFIWKVMCN PVCAYDTLIR TLTGAATFSE DPVTTTIVCP
NCTIQIHTCG GLLVRYSGDP APVASDNVDR GNQGIDCLTN PNLIAGFSWR QIADLFSTVM
TSLCNNHLVN LATMAAIGAV ATKALQGVKG KTKRGRGARI NLGNDEYDEW QQMRREFNNA
HDMTAEEFLE LRNRAAMGSD DADAIKFRSW WTNRQLRQDE AHVTVVGKGG VRNEVIRTRV
RNAPKGPRTL DDGGFYDNDY EGLPGYLRFN GSGWMIHIGN GMYLSNTHTA RSSCSEIVTC
SPTTDLCLVK AEPIRSVAQI AEGTPVRDWK RASITTYGLK KTFSDSTKID VLAYDGPTQT
THGDCGLPLF DEAGKVVAIH TGKLLGFSKM CTLIDCTITK GVYENTDLFC GDPIDYRGLV
AFRVAGVEPR PPVSGTRYAK VPGVPEEYHT GYRPANLGRG DPDSHCTLMN IAVKNLQVYQ
QEPKLTKVDT FIERAAADVL GFLRFLTKGE RQMNLNFSAA FNVLDLSTSC GPFVPGKKID
HVKDGKLDEV LSKHLYKCWS VANSGKALHH VYACGLKDEL RPLDKVKEGK KRLLWGCNVG
VALCAAAVFH NLCFKLKTVA RFGPIAVGID MTSRDVDVMI TQLTSKAGDF LCLDYSKWDS
TMSPCVVRLA IDILADCCEQ TELTKSVVLT LKSLPMTVLD AMIVPTKRGL PSGMPFTSVI
NSICHWLLWS AAVYKACDEI GLFCSNLYED APFFVYGDDG VYAMTPMMVS LLPAILDNLR
DYGLSPTAAD KTEFIDVCPL KDISFLKRKF VMSELGWLSQ LDRSSILRQL EWTKTAKRHM
CIEECSELDK DERGVQLEEL QIHAAAHGEE FFELVKKELR RQQAFTRFSV FDYQTARKTL
GDRKRIVSVV PDDSFVNVME GKPRADAPGT ATTASVPGTT TDGMDPGVVA STDVVTADNV
AASVATAGIG GPPQQASPQE SWRVNFFYND VFTWSVTDAP GSILYTVQHS PQNNPFTQVL
SQMYAGWAGG MQFRFIVAGS GIFGGRLVCA IIPPGIQIQP GLEVRQFPHV VIDARSLEPV
TITMPDLRPE MYHPTGNPGL VPTLVVSVYN NLINPFGGTT SAIQVTVETR PSEDFEFVLI
RAPSSKTVDS VNPSWLLTTP VLTGAGSDNR WGAPIVGLQP VPGGFSTSNR HWNMNGETYG
WSSPRFDDID HPSGNVSYPS GSATNTIETW YANAGTATTN PISNIAPDGF PDMGAIPFSG
TTIPTGAWVG FGQVWNASNG TPYVGTVQAY ELGFANGAPS SIRPVTTTTG AQLVAKSIYG
VAIAQNQTSA GIIFLSKGMV STPGVAATTY TPQPSAIVTT PGTPVAAPIG KNTPIMFSAV
VRRTGDVNAG PGSANGTQYG VGSQPLSVTL GLSLTNYSSA LQPGQFFVWQ LNFASGFMEV
GMNTDGYFYA GTGAYSGMID LTDLIDVRPV GVRPNTSTLV FNLAGVATTG YSYV
