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-JUN-2021, entry version 5. DE RecName: Full=Calicivirin {ECO:0000256|PROSITE-ProRule:PRU01242}; DE EC=3.4.22.66 {ECO:0000256|PROSITE-ProRule:PRU01242}; DE Flags: Fragment; OS Sapovirus GII.1. OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes; OC Picornavirales; Caliciviridae; Sapovirus. 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: 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:ARBA00002567}. 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:0000256|PROSITE- CC ProRule:PRU01242}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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:0019012; C:virion; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0017111; F:nucleoside-triphosphatase 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-directed 5'-3' RNA polymerase activity; 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; -; 2. 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 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, ECO:0000256|PROSITE- KW ProRule:PRU01242}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE- KW ProRule:PRU01242}; KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484}; KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE- KW ProRule:PRU01242}; Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953}. 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 ACT_SITE 1081 FT /note="For 3CLpro activity" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01242" FT ACT_SITE 1102 FT /note="For 3CLpro activity" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01242" FT ACT_SITE 1166 FT /note="For 3CLpro activity" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01242" 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 //