ID   A0A6M5UPD0_9CALI        Unreviewed;      2275 AA.
AC   A0A6M5UPD0;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   02-OCT-2024, entry version 17.
DE   RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
DE   Flags: Fragment;
OS   Sapovirus GII.1.
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Picornavirales; Caliciviridae; Sapovirus; Sapporo virus.
OX   NCBI_TaxID=1398548 {ECO:0000313|EMBL:QJW39046.1};
RN   [1] {ECO:0000313|EMBL:QJW39046.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C86 {ECO:0000313|EMBL:QJW39046.1};
RX   PubMed=32392864;
RA   Tohma K., Kulka M., Coughlan S., Green K.Y., Parra G.I.;
RT   "Genomic Analyses of Human Sapoviruses Detected over a 40-Year Period
RT   Reveal Disparate Patterns of Evolution among Genotypes and Genome
RT   Regions.";
RL   Viruses 12:0-E516(2020).
CC   -!- FUNCTION: Displays NTPase activity, but no helicase activity (By
CC       similarity). Induces the formation of convoluted membranes derived from
CC       the host ER (By similarity). These remodeled membranes probably form
CC       the viral factories that contain the replication complex (By
CC       similarity). Together with NS2 and NS4, initiates the formation of the
CC       replication complex. {ECO:0000256|ARBA:ARBA00044732}.
CC   -!- FUNCTION: Probable key protein responsible for the formation of
CC       membrane alterations by the virus (By similarity). Induces the
CC       formation of convoluted membranes derived from the host ER (By
CC       similarity). These remodeled membranes probably form the viral
CC       factories that contain the replication complex (By similarity).
CC       Together with NS2 and NTPase, initiates the formation of the
CC       replication complex. {ECO:0000256|ARBA:ARBA00044736}.
CC   -!- FUNCTION: Together with NTPase and NS4, initiates the formation of the
CC       replication complex (By similarity). Induces the proliferation of the
CC       host smooth ER membranes forming long tubular structures (By
CC       similarity). These remodeled membranes probably form the viral
CC       factories that contain the replication complex.
CC       {ECO:0000256|ARBA:ARBA00044722}.
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   -!- 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; MN794211; QJW39046.1; -; Genomic_RNA.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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; -; 2.
DR   Gene3D; 6.10.250.3230; -; 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   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Covalent protein-RNA linkage {ECO:0000256|ARBA:ARBA00022520};
KW   Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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   Viral RNA replication {ECO:0000256|ARBA:ARBA00022953};
KW   Virion {ECO:0000256|ARBA:ARBA00022844}.
FT   DOMAIN          449..604
FT                   /note="SF3 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51218"
FT   DOMAIN          1051..1199
FT                   /note="Peptidase C24"
FT                   /evidence="ECO:0000259|PROSITE:PS51894"
FT   DOMAIN          1438..1563
FT                   /note="RdRp catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50507"
FT   REGION          930..953
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:QJW39046.1"
SQ   SEQUENCE   2275 AA;  250587 MW;  94561E73D1143AAA CRC64;
     FYPIEFNHKV ETTVLFSAHL RVSGREEIFE TKQDMYAHVC QVITGVRREI LRRTPVVGPS
     FSAEGLLDAF ASKPPVDINP DTTFRELFGI DPHEQFPLSI TDLAKLQGEL VDAAHNPGHI
     LRRHYSTDSL TKLINKITKY IPVQATLTEM QARRAHERER ADLFKELPLV DPEITQQQKS
     YFYAMWRQVV KKGKEFFIPL VKCTSWRKKF SEPAEIVRQL LVHFCEGMRT QFNTNANYIN
     LSLLAKLRPT VLTMIFQQHK NTYRGWLATI TALVEVYSNL FQDMRETAVS AVSAITLLFE
     SLKQFVEGVI DLVRGTFQAQ GPTNCGWAAI AAGVILILLK ISGCPSVMGY WQRLLKVCAG
     VTTIAAAARA FTWVRDIIVE AERKARLKKY MARTAALLEL AASRDVTGTE ELKRLLECFT
     QLIEEGTELI QEFGTSPMAG LARSYVSELE TAANGIRSTI LLDTPRKVPV AIILTGPPGI
     GKTHLAQHLA AGFGKTSNFS VTLDHHDSYT GNDVAIWDEF DVDAQGKFVE TMIGVVNTAP
     YPLNCDRVEN KGKVFTSNYI ICTSNYPTSV LPENPRAGAF YRRVTTVDVS SPVIDDWKKK
     NPGKKPPLDL YKKDFSHLRL SVRPYLGYNP EGDTLEGVRV KPILTSVDGL SRLMETKFKE
     QGNELRNLWI TCPRDLVTPA ASGLKSYMAA NRALAQVFAE PSSNEIAETC TSRIFVSANN
     PPPTFVGRHV KITAINPWDA SLANSMLSMF ETNTHIPAVT QREIMYRVWT PLIHMQTREP
     NTQMLPYINR VVPVTSSFDF VRGLRHHLGL CSIKGMWKAY QGWHSSATIL EFLSKHMEDV
     TFPSNPECTV FRAADGDVIF YTFGSYACFV SPARVPFVGD PPKTVHSNIT RNMTWIETLR
     LLVETITESL AHFGPLLLMV HNVTYLTTRS QRDEEAKGKT KHGRGARHAR RGGVSLSDDE
     YDEWRDLVRD WRQDMTVGEF VELRERYALG MDSEDVQRYR AWLQLRAMRL GAGAYQHATI
     IGRGRVEDTI IRTQPMRAPR APRSTGYDEE APTPIVTFTS NGDHVGYGCH IGNGVVVTVT
     HVAAAADVVE GLEFTVRKTE GETTWVNTPL SHLPHYQLGD GAPVYYSTRL HPVTTIAEGT
     YETPNITVHG FHLRIINGYP TKRGDCGTPY FDSCRRLVGL HAATSTNGET KLAQKVSRVS
     KVENAFAWKG LPVLRGPDCG GMPTGTRYHR SPAWPEQLSN ETHAPAPFGA GDSRYNFSQV
     EMLVTGLKPY SEPTPGIPPA LLQRAATHTR TYLESIVGTH RSPNLTYNEA CALLDRSTSC
     GPFIAGQKGD YWDEDRQCYT GVLAEHLGKA WDAANRGVAP QNAYKLALKD ELRPIEKNQQ
     GKRRLLWGCD AGATLVATAA FKGIATRLQA VAPMTPVGVG INMDSYQVEV LNESLKGGVV
     YCLDYSKWDS TQHPAVTAAS LAILERLSEA TPITTSAVEL LSSPARGHLN DIIFVTKSGL
     PSGMPFTSVV NSLNHMTYFA AAVLKAYEQH GAPYTGNVFQ VETVHTYGDD CIYSLCPATA
     SIFETVLANL SAFGLRPTAA DKTDKIAPTH TPIFLKRTLT CTPRGIRGLL DITSIRRQFF
     WIKANRTTDI SSPPAYDREA RSVQLENALA YASQHGHAIF EEIAEIAKKT AQAEGLVLTN
     VNYDQALATY EAWFIGGTGT GQDSPSEETT KLVFEMEGLG QSQSQRDQQV MDQVVTPQDT
     IGPTSALLLP TQVETPNASA QRVELAMATG AVTSNVPNCI RECFAAVTTI PWTTRQAANT
     FLGAIHLGPR INPYTAHLSA MFAGWGGGFQ VRVTISGSGL FAGRAITAIL PPGVNPAAVQ
     NPGVFPHAFI DARTTDPILI NLPDIRPIDF HRVDGDDATA SVGLWVAQPL INPFQTGSVS
     TCWLSFETRP GPDFDFCLLK APEQEMDNGI SPANLLPRRL GRSRGNRLGG RVVGLVVVAA
     AEQVNHHFGA NSTTLGWSTL PIEPIAGAVS WYDDNNEHTK IRGLLSAQGK GIIFPNIVNH
     WTDVSLSAKT SGQTTIPIAA DNLNNSPGAA GPVVMFENNG DVNESTANHG ILTAASHDFT
     SLSQTFDAAG LWVWMPWTRN KPDGRTNTNV YITPTWINGN PARPIHEKCT NMVGTNFQFG
     GTGTNNIMLW QEQHFTSFPG AAEVYCSQLE STAEMFQNNV VNIPANQMAV FNVETAGNTF
     QIGILPNGYS VTNAAIGTHQ LLDYETSFRF VGLFPQSTSL QGPNGNAGRA VRFLE
//