ID A8HC73_RHDV Unreviewed; 2344 AA.
AC A8HC73;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE AltName: Full=p254 {ECO:0000256|ARBA:ARBA00032539};
OS Rabbit hemorrhagic disease virus (RHDV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Lagovirus.
OX NCBI_TaxID=11976 {ECO:0000313|EMBL:ABV56616.1, ECO:0000313|Proteomes:UP000161977};
OH NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
RN [1] {ECO:0000313|EMBL:ABV56616.1, ECO:0000313|Proteomes:UP000161977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NY-01 {ECO:0000313|EMBL:ABV56616.1};
RX PubMed=17910765;
RA McIntosh M.T., Behan S.C., Mohamed F.M., Lu Z., Moran K.E., Burrage T.G.,
RA Neilan J.G., Ward G.B., Botti G., Capucci L., Metwally S.A.;
RT "A pandemic strain of calicivirus threatens rabbit industries in the
RT Americas.";
RL Virol. J. 4:96-96(2007).
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:0000256|ARBA:ARBA00003176}.
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.
CC {ECO:0000256|ARBA:ARBA00024666}.
CC -!- FUNCTION: NTPase presumably plays a role in replication. Despite having
CC similarities with helicases, does not seem to display any helicase
CC activity. {ECO:0000256|ARBA:ARBA00025124}.
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.
CC {ECO:0000256|ARBA:ARBA00025359}.
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 Evidence={ECO:0000256|ARBA:ARBA00001491};
CC -!- SUBUNIT: Binds to histo-blood group antigens at surface of target
CC cells. {ECO:0000256|ARBA:ARBA00011868}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Host
CC cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Virion
CC {ECO:0000256|ARBA:ARBA00004328}.
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DR EMBL; EU003581; ABV56616.1; -; Genomic_RNA.
DR MEROPS; C24.001; -.
DR Proteomes; UP000161977; Genome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
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-dependent RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd23192; Caliciviridae_RdRp; 1.
DR CDD; cd00205; rhv_like; 1.
DR Gene3D; 1.10.260.110; -; 1.
DR Gene3D; 1.20.960.20; -; 1.
DR Gene3D; 2.60.120.20; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 4.10.8.20; DNA/RNA polymerases; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
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 InterPro; IPR049434; VPg.
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 Pfam; PF20915; VPg; 1.
DR PRINTS; PR00916; 2CENDOPTASE.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88633; Positive stranded ssRNA viruses; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51894; CV_3CL_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Capsid protein {ECO:0000256|ARBA:ARBA00022561};
KW Covalent protein-RNA linkage {ECO:0000256|ARBA:ARBA00022520};
KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW Virion {ECO:0000256|ARBA:ARBA00022561}.
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 405..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 492..653
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51218"
FT DOMAIN 1109..1244
FT /note="Peptidase C24"
FT /evidence="ECO:0000259|PROSITE:PS51894"
FT DOMAIN 1495..1619
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 1771..1793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1777..1791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2344 AA; 256786 MW; 9D075293BFBD4229 CRC64;
MAVMSRLIGM TTAIIPEKKP LSFFLDLRDK TPPCCIRATG ELAWPVFLGQ NENEGLLEIC
EKCGKWLNGF GNFGLEDLGN VCLCSIAQQK HKFGPVCLCN RAYIHDCGRW RRRSRFLKHY
KALNKVIPCA YRFDEGSSPP VFEGEVDDLF VELGAPTSMG FMDKKLLKKG KKLMDKFVDV
DEPCLTSRDA GLLDSIASDN TIRAKLEEEY GVEMVQAARD RKDFMKNLRL ALDNRPANPV
TWHTKLGNIT DKGKQWAKKV VYGACKVTEP LKTLASILLV GLHNVIAVDT TVMLSTFKPV
NLLAILMDWT NDLTGFVTTL VRLLELYGVV QATVNLIIEG VKSFWDKVIC ATDRCFDLLK
RLFDTFEDSV PTGPTAGCLI FMAFVFSTVV GYLPNNNVIT TFMKGAGKLT TFAGVIGAIR
TLWISINQHM VAKDLTSIQQ KVMTVVIMAN EAATLDQLEI VSCLCSDLEK TLTNRCTQPS
YNQHLGILNA SQKVVSDLHT MVLGKINMTK QRPQPVAVIF KGAPGIGKTH LVHKIARDLG
CQHPSTINFG LDHFDSYTGE EVAIADEFNT CGDGESWVEL FIQMVNTNPC PLNCDKVENK
NKVFNSKYLL CTTNSNTILN ATHPRAGAFY RRVLIVEARN KAVESWQATR HGSRPGKSCY
SKDMSHLTFQ VYPHNMPAPG FVFVGDRLVK SQVAPREYKY SELLDLIKSE HRDVASLEGA
NKFNFIYPDA QYEQALLMCK QYFVMYGCVA RLAKNFVDDI PYNQVHISKA SDPKIDGCVE
YQCKFQHLWR MVPQFVLGCV NMTNQLGTPL TQQQLDRITN GVEGVTVTTV NNILPFHSQT
TLINPSFIKL IWAVRKHLKG LSGVTKVAQF IWRVMTNPVD AYGSLVRTLT GAATFSDDPV
STTIICSNCT IQIHSCGGLL VRYSRDPVPV ASDNVDRGDQ GVDVFTDPNL ISGYSWRQIA
HLFVEVISHL CANHLVNLAT MAAIGAVATK AFQGVKGKTK RGRGARVNLG NDEYDEWQAA
RREFVNAHDM TAEEYLAMKN KAAMGSDDQD SVMFRSWWTR RQLRPDEDQV TIVGRGGVRN
EVIRTRARQA PKGPKTLDDG GFYDNDYEGL PGFMRHNGSG WMIHIGNGLY ISNTHTARSS
CSEIVTCSPT TDLCLVKGET IRSVAQIAEG TPVCDWKKSP ISTYGIKKTL SDSTKIDVLA
YDGCTQTTHG DCGLPLYDSS GKVVAIHTGK LLGFSKMCTL VDLTITKGVY ETSNFFCGEP
IDYRGITAHR LVGAEPRPPV SGTRYARVPG VPDEYRTGYR PANLGRGDPD SDKSLMNIAV
KSLQVYQQEP KLDKVDEFIE RAAADVLGYL RFLTKGERQV NLNFKAAFNT LDLSTSCGPF
VPGKKIDHVK DGVMDQVLAK HLYKCWSVAN SGKALHHIYA CGLKDELRPL DKVKEGKKRL
LWGCDVGVAV CAAAVFHNIC YKLKMVARFG PIAVGVDMTS RDVDVIINNL TAKASDFLCL
DYSKWDSTMS PCVVRLAIDI LADCCEQTEL TKSVVLTLKS HPMTILDAMI VQTKRGLPSG
MPFTSVINSI CHWLLWSAAV YKSCAEIGLH CSNLYEDAPF YTYGDDGVYA MTPMMVSLLP
AIIENLRDYG LSPTAADKTE FIDVCPLNKI SFLKRTFELT DIGWVSKLDK SSILRQLEWS
KTTSRHMVIE ETYDLAKEER GVQLEELQVA AAAHGQEFFS FVRKELERQQ AYTQFSVYSY
DAARKILADR KRVVSVVPDD EFVNVMEGKA RTAPQGEAAG TATTASVPGT TTDGMDPGVV
AATSVVTAEN SSASVATAGI GGPPQQVDQQ ETWRTNFYYN DVFTWSVADA PGSILYTVQH
SPQNNPFTAV LSQMYAGWAG GMQFRFIVAG SGVFGGRLVA AVIPPGIEIG PGLEVRQFPH
VVIDARSLEP VTITMPDLRP NMYHPTGDPG LVPTLVLSVY NNLINPFGGS TNAIQVTVET
RPSEDFEFVM IRAPSSKTVD SISPAGLLTT PVLTGVGNDN RWNGQIVGLQ PVPGGFSTCN
RHWNLNGSTY GWSSPRFADI DHRRGSASFA GNNSTNVLQF WYANAGSAID NPISQVAPDG
FPDMSFVPFN SPNIPTAGWV GFGGIWNSNS GAPAATTVQA YELGFATGAP NNLQPTTNTS
GAQTVAKSIY AVVTGTNQNP TGLFVMASGV ISTPNANAVT YTPQPDRIVT TPGTPAAAPV
GKNTPIMFAS VVRRTGDVNA AAGSANGTQY GTGSQPLPVT IGLSLNNYSS ALMPGQFFVW
QLTFASGFME IGLSVDGYFY AGTGASTTLI DLTELIDVRP VGPRPSKSTL VFNLGGTTNG
FSYV
//
