ID   F5BXG7_RHDV             Unreviewed;      2344 AA.
AC   F5BXG7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 71.
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:AEB26305.1, ECO:0000313|Proteomes:UP000145249};
OH   NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
RN   [1] {ECO:0000313|EMBL:AEB26305.1, ECO:0000313|Proteomes:UP000145249}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HYD {ECO:0000313|EMBL:AEB26305.1};
RA   Liu J.S., Liu H.R., Guo D.C., Qu L.D.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007829|PDB:3J1P}
RP   STRUCTURE BY ELECTRON MICROSCOPY (6.50 ANGSTROMS) OF 1766-2344.
RX   PubMed=23341770; DOI=10.1371/journal.ppat.1003132;
RA   Wang X., Xu F., Liu J., Gao B., Liu Y., Zhai Y., Ma J., Zhang K.,
RA   Baker T.S., Schulten K., Zheng D., Pang H., Sun F.;
RT   "Atomic model of rabbit hemorrhagic disease virus by cryo-electron
RT   microscopy and crystallography.";
RL   PLoS Pathog. 9:e1003132-e1003132(2013).
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.
CC       {ECO:0000256|ARBA:ARBA00002279}.
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}.
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DR   EMBL; JF412629; AEB26305.1; -; Genomic_RNA.
DR   PDB; 3J1P; EM; 6.50 A; A/B/C=1766-2344.
DR   PDBsum; 3J1P; -.
DR   SMR; F5BXG7; -.
DR   MEROPS; C24.001; -.
DR   UniLectin; F5BXG7; -.
DR   Proteomes; UP000145249; 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:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-EC.
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; 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   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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3J1P};
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;  256610 MW;  AAA47274D6CC39F3 CRC64;
     MAVMSRPIGT TTAILPEKKP LSFFLDLRDK TPPCCIRATG KLAWPVFLGQ NENEGPLETC
     DICGKWLNGF GNFGLEDLGN VCLCSIAQQK HKFGPVCLCN RAYIHDCGRW RRRSRFLKHY
     KALNKVIPCA YRFDEGSSPP VFEGEVDDLF VELGAPTSMG FMDKKLLKKG KKLMDKFVDV
     DEPCLTSRDA GLLDSIASDN TIRAKLEEEY GVEMVQAARD RKDFMKNLRL ALDNRPANPV
     TWHTKLGNIT DKGKQWAKKV VYGACKVTEP LKTLASILLV GLHNVIAVDT TVMLSTFKPV
     NLLAILMDWT NDLAGFVTTL VRLLELYGVV QATVNLIIEG VKSFWDKVIC ATDRCYDLLK
     RLFDTFEDSV PTGPTAGCLI FMAFVFSTVV GYLPNNNVIT TFMKGAGKLT TFAGVIGAIR
     TLWITINQHM VAKDLTSIQQ KVMTVVKMAN EAATLGQLEI VSCLCSDLEN TLTNRCTLPS
     YNQHLGILNA SQKVVSDLHT MVLGKINMTK QRPQPVAVIF KGAPGIGKTY LVHRIARDLG
     CQHPSTINFG LDHFDSYTGE EVAIADEFNT CGDGESWVEL FIQMVNTNPC PLNCDKAENK
     NKVFNSKYLL CTTNSNMILN ATHPRAGAFY RRVLIVEARN KAVESWQATR HGAKPGKSCY
     NKDMSHLTFQ VYPHSMPAPG FVFVGDKLVK SQVAPREYKY SELLDLIKSE HPDVASFEGA
     NKFNFIYPDA QYEQALLMWK QYFVMYGCVA RLAKSFVDDI PYNQVHISKA SDPKIDGCVE
     YQCKFQHLWR MVPQFVLGCV NMTNQLGTPL TQQQLDRITN GVEGVTVTTV NNILPFHSQT
     TLINPSFIKL IWAVRKHLKG LSGVTKVAQF IWRVMTNPVD AYGSLVRTLI GAATFSDDPV
     STTIICSNCT IQIHSCGGLL VRYSRDPVPV ASDNVDRGDQ GVDVFTDPNL ISGFSWRQIA
     HLFVEVISHL CANHLVNLAT MAALGAVATK AFQGVKGKTK RGRGARVNLG NDEYDEWQAA
     RREFVNAHDM TAEEYLAMKN KAAMGSDDQD SVMFRSWWTR RQLRPDEDQV TIVGRGGVRN
     EVIRTRARQA PKGPKILDDG GFYDNDYEGL PGFMRHNGSG WMIHIGNGLY ISNTHTARSS
     CSEIVTCSPT TDLCLVKGET IRSVAQIAEG TPVCDWKKSP ISTYGIKKTL SDSTKIDVLA
     YDGCTQTTHG DCGLPLYDSS GKIVAIHTGK LLGFSKMCTL VDLTITKGVY ETSNFFCGEP
     IDYRGITAHR LVGAEPRPPV SGTRYARVPG VPDEYKTGYR PANLGRGDPD SDKSLMNIAV
     KNLQVYQQEP KLDKVDEFIE RAAADVLGYL RFLTKGERQA NLNFKAAFNT LDLSTSCGPF
     VPGKKIDHIK 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 FIDVCPLSKI SFLKRTFELT DIGWVSKLDK SSILRQLEWS
     KTTSRHMLIE 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
     RPSDDFEFVM IRAPSSKTVD SISPAGLITT PVLTGVGNDN RWDGQIVGLQ PVPGGFSTCN
     RHWNLNGSTY GWSSPRFADI DHRRGSASYS GNNSANALQF WYANAGSAID NPISQVAPDG
     FPDMSFVPFN SPNIPTAGWV GFGGIWNSNN GAPAATTVQA YELGFATGAP NNLQPTTNTS
     GAQTVAKSIY AVVTGTNQNP TGLFVMASGV ISTPNASAVT YTPQPDRIVT TPGTPAAAPV
     GKNTPIMFAS VVRRTGDVNA AAGSTNGTQY GTGSQPLPVT IGLSLNNYSS ALMPGQFFVW
     QLTFASGFME IGLSVDGYFY AGTGASTTLI DLTELIDVRP VGPRPSKSTL VFNLGGTTNG
     FSYV
//