ID   Q3HNQ2_RHDV             Unreviewed;      2344 AA.
AC   Q3HNQ2;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE   AltName: Full=p254 {ECO:0000256|ARBA:ARBA00032539};
GN   Name=RHDV {ECO:0000313|EMBL:ABA46865.1};
OS   Rabbit hemorrhagic disease virus (RHDV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Caliciviridae; Lagovirus.
OX   NCBI_TaxID=11976 {ECO:0000313|EMBL:ABA46865.1, ECO:0000313|Proteomes:UP000171525};
OH   NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
RN   [1] {ECO:0000313|EMBL:ABA46865.1, ECO:0000313|Proteomes:UP000171525}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JX/CHA/97 {ECO:0000313|EMBL:ABA46865.1};
RA   Liu G., Ni Z., Zhang Y., Yun T.;
RT   "Sequencing and analyzing the complete nucleotide sequence of Rabbit
RT   haemorrhagic disease virus JX/CHA/97 strain isolated from China.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007829|PDB:4EGT, ECO:0007829|PDB:4EJR}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1993-2344.
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. 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; DQ205345; ABA46865.1; -; mRNA.
DR   PDB; 4EGT; X-ray; 2.00 A; A/B=1993-2344.
DR   PDB; 4EJR; X-ray; 2.00 A; A/B=1766-1995.
DR   PDBsum; 4EGT; -.
DR   PDBsum; 4EJR; -.
DR   SMR; Q3HNQ2; -.
DR   MEROPS; C24.001; -.
DR   UniLectin; Q3HNQ2; -.
DR   Proteomes; UP000171525; 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; 6.10.140.320; -; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4EGT, ECO:0007829|PDB:4EJR};
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          1769..1793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1776..1791
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2344 AA;  257035 MW;  B5E2D9F0570D50EE CRC64;
     MPPMSRLIGM TTAILPEKKP LSFFLDLRDK TPPCCIRATG ELAWPVFLGQ NENEGLLETC
     DKCGKWLNGF GNFGLEDLGN VCLCSIAQQK HKFGPVCLCN RAYIHDCGRW RRRSRFLKHY
     KALNKVIPCA YQFDEGSSPS VFEGEVDDLF VELGAPTSMG FMDKKLLKKG KKLMDKFVDV
     DEPCLTSRDA GLLDSIASDN TIRAKLEEEY GIEMVQAARD RKDFMKNLRL ALDNRPANPV
     TWYTKLGNIT DKGKQWAKKV VYGACKATEP LKTLASILLV GLHNVIAVDT TVMLSTFKPV
     NLLAILMDWT NDLTGFVTTL VRLLELYGVV QVTVNLIIEG VKSFWDKVIC ATDRCFDLLK
     RLFDTFEDSV PTGPTAGCLI FMAFVFSTVV GYLPNNNVIT TFMKGAGKLT TFAGVIGAIR
     TLWITINQHM VAKDLTSIQQ KVMTVVKMAN EAATLDQLEI VSCLCSDLEN TLTNRCTLPS
     YNQHLGILNA SQKVVSDLHT MVLGKINMTK QRPQPVAVIF KGAPGIGKTH LVHRIARDLG
     CQHPSTINFG LDHFDSYTGE EVAIADEFNT CGDGESWVEL FIQMVNTNPC PLNCDKVENK
     NKVFNSKYLL CTTNSNTILN ATHPRAGAFY RRVLIVEARN KAVESWQATR HGSRPGKSCY
     SKDMSHLTFQ VYPHNMPAPG FVFVGDKLVR SQVAPREYKY SELLDLIKSE HPDVASFEGA
     NKFNFIYPDA QYEQALLMWK QYFVMYGCVA RLAKNFVDDI PYNQVHISKA SDPKIDGCVE
     YQCKFQHLWR MVPQFVLGCV NMTNQLGTPL TQQQLDRITN GVEGVTVTTV NNILPFHSQT
     TLINPSFIKL IWAVRKHLKG LSGVTKVAQF IWRVMTNPVD AYGSLVRTLT GAATFSDNPV
     STTIICSNCT IQIHSCGGLL VRYSRDPVPV ASDNADRGDQ GVDVFTDPNL ISGFSWRRIA
     HLFVEVISHL CANHLVNLAT MAALGAVATK AFQGVKGKTK RGRGARVNLG NDEYDEWQAA
     RREFVNAHDM TAEEYLAMKN KAAMGSDDQD SVMFRSWWTR RQLRPDEDQV TIVGRGGVRN
     EVIRTRARQA PKGPKTLDDG GFYDNDYEGL PGFMRHNGSG WMIHIGNGLY ISNTHTARSS
     CSEIVTCSPT TDLCLVKGEI IRSVAQIAEG TPVCDWKKSP ISTYGIKKTL SDSTKIDVLA
     YDGCTQTTHG DCGLPLYDSS GKIVAIHTGK LLGFSKMCTL VDLTITKGVY ETSNFFCGEP
     IDYRGITAHR LVGAEPRPPV SGTRYARVPG VPDEYRTGYR PANLGRGDPD SDKSLMNIAV
     KSLQVYQQEP KLDKVDEFIE RAAADVLGYL RFLTKGERQV NLNFKAAFNT LDLSTSCGPF
     VPGKKIDHIK DGVMDQVLAK HLYKCWSVAN SGKALHHIYA CGLKDELRPL DKVKEGKKRL
     LWGCDVGVAV CAAAVFHNIC YKLKMVARFG PIAVGVDMTS RDFDVIINNL TVKASDFLCL
     DYSKWDSTMS PCVVRLAIDI LADCCEQTEL TKSVVLTLKS HPMTILDAMI VQTKRGLPSG
     MPFTSVINSI CHWLLWSAAV YKSCAEIGLH CSNLYEDAPF YTYGDDGVYA MTPMMVSLLP
     AIIENLRDYG LSPTAADKTE FIDVCPLNKI SFLKRTFELT DIGWVSKLDK SSILRQLEWS
     KTTSRHMVIE ETYDLAKEER GVQLEELQVA AAAHGQEFFN FVRKELERQQ AYTQFSVYSY
     DAARKVLADR KRVVSVVPDD EFVNVMEGKT RTAPQGEAAG TATTASVPGT TTDGMDPGVV
     AATSVVTAEN SSASVATAGI GGPPQQVDQQ ETWRTNFYYN DVFTWSVADA PGSILYTVQH
     SPQNNPFTAV LSQMYAGWAG GMQFRFIVAG SGVFGGRLVA AVIPPGIEIG PGLEVRQFPH
     VVIDARSLEP VTITMPDLRP NMYHPTGDPG LVPTLVLSVY NNLINPFGGS TNAIQVTVET
     RPSDDFEFVM IRAPSSKTVD SISPAGLLTT PVLTGVGNDN RWNGQIVGLQ PVPGGFSTCN
     RHWNLNGSTY GWSSPRFADI DHRRGSASYS GNSSTNVLQF 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
//