ID S6A747_9CALI Unreviewed; 1701 AA.
AC S6A747;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 08-NOV-2023, entry version 48.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Norovirus Hu/GII.12/CGMH39/2010/TW.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Norovirus; Norwalk virus.
OX NCBI_TaxID=1380574 {ECO:0000313|EMBL:AGT39193.1, ECO:0000313|Proteomes:UP000161578};
RN [1] {ECO:0000313|EMBL:AGT39193.1, ECO:0000313|Proteomes:UP000161578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hu/GII.12/CGMH39/2010/TW {ECO:0000313|EMBL:AGT39193.1};
RX PubMed=24009100; DOI=10.1002/jmv.23728;
RA Tsai C.N., Lin C.Y., Lin C.W., Shih K.C., Chiu C.H., Chen S.Y.;
RT "Clinical relevance and genotypes of circulating noroviruses in northern
RT Taiwan, 2006-2011.";
RL J. Med. Virol. 86:335-346(2014).
CC -!- FUNCTION: 3C-like protease processes the polyprotein: 3CLpro-RdRp is
CC first released by autocleavage, then all other proteins are cleaved.
CC May cleave polyadenylate-binding protein thereby inhibiting cellular
CC translation. {ECO:0000256|PROSITE-ProRule:PRU00870}.
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=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:PRU00870};
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 -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. 3CLpro
CC is first autocatalytically cleaved, then processes the whole
CC polyprotein. {ECO:0000256|PROSITE-ProRule:PRU00870}.
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; KC464497; AGT39193.1; -; Genomic_RNA.
DR Proteomes; UP000161578; Genome.
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; cd23192; Caliciviridae_RdRp; 1.
DR Gene3D; 1.20.960.20; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 6.10.20.70; -; 1.
DR Gene3D; 6.10.250.3230; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR001665; Norovirus_pept_C37.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR013614; Viral_PP_Calicivir_N.
DR Pfam; PF08405; Calici_PP_N; 1.
DR Pfam; PF05416; Peptidase_C37; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR PRINTS; PR00917; SRSVCYSPTASE.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS51537; NV_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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00870}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU00870};
KW RNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022484};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW ProRule:PRU00870}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Viral RNA replication {ECO:0000256|ARBA:ARBA00022953}.
FT DOMAIN 467..634
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51218"
FT DOMAIN 1011..1191
FT /note="Peptidase C37"
FT /evidence="ECO:0000259|PROSITE:PS51537"
FT DOMAIN 1427..1548
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..78
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1040
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00870"
FT ACT_SITE 1064
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00870"
FT ACT_SITE 1149
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00870"
SQ SEQUENCE 1701 AA; 189391 MW; 4F9460E661C06738 CRC64;
MKMASNDASA AAAAISNNDI AKSSSDGVLS SMAVTFKRAL GARPKQPPPR ETTQKQKPPR
PPTPELIKKI PPPPPNGEDD IVVSYSAKEG VSGLPELSTV RQPDETNTAF SVPPLNQREN
RDAKEPLPGT ILEMWDGEIY HYGLYVERGL VLGVHKPPAA ISLAKVELTP LSLYWRPVYT
PQYLISPETL KKLHGETFPY TAFDNNCYAF CCWVLDLNDS WLSRRMIQRT TGFFRPYQDW
NRKPLPTMDD SKLKKVANIV LCALSSLFTR PIKDIIGKLR PLNILNILAS CDWTFAGVVE
SLILLAELFG VFWTPPDVSA MIAPLLGDYE LQGPEDLAVE LVPVVMGGIG LVLGFTKEKI
GKMLSSAAST LRACKDLGAY GLEILKLVMK WFFPKKDEAN ELAMVRSIED AVLDLEAIEN
NHMTTLLKDK DSLATYMKTL DLEKEKARKL STESASRDIG GTINSLLARI AAARSLVHRA
KEELSSRPRP VVVMISGKPG IGKTHLARDL AKKVAATLTG DQRVGLIPRN GVDHWDAYKG
ERVVLWDDYG MSNPIHDALR LQELVDTCPL TLNCDRIENK GKVFDSDAII ITTNLANPAP
LDYVNFEACS RRMDFIVYDD APDAEKAKRD FPGQPDMWKD AFRPDFSHIK LMLAPQGGFD
KNGNTPHGKG VMKTLTSGSL VARASGLLHE RLDEYELQGP TPTTFNFDQN KVFAFRQLAA
ENKYGLMDTM RVGSQLKNVK TVSELKQALK NIAIRRCQIV YSGLTYSLES DGKGNVRVEK
VQSPAVQTNN ELTGALHHLR CARIRYYVKC VQEALYSIIQ IAGAAFVTTR IAKRMNIQNL
WSRPQVEDEE ETTSKDGCPK PKDEEEFVIS SEDIKVEGKK GKNKSGRGKK HTAFSSKGLS
DEEYDEYKRI REERNGKYSI EEYLQDRDKY YEEVAIARAT EEDFCEEEEA KIRQRIFRPT
RKQRKEERAS LGLITGSEIR KRNPDDFKPK GKLWADDDRS VDYNEKLSFE APPSIWSRIV
NFGSGWGFWV SPSLFVTSTH VIPQGAQEFF GVSIKQIQIH KSGEFCRLRF PKPIRTDVTG
MILEEGAPEG TVATLLIKRP TGELMPLAAR MGTHATMRIQ GRTVGGQMGM LLTGSNAKSM
DLGTTPGDCG CPYIYKRGND YVVIGVHTAA ARGGNTVICA TQGSEGEAVL EGGDNKGTYC
GAPILGPGNA PKLSTKTKFW RSSTAPLPPG TYEPAYLGGK DPRVKGGPSL QQVMRDQLKP
FTEPRGKPPK PSVLEAAKKT IINVLEQTID PPQKWTFAQA CASLDKTTSS GYPHHVRKNE
HWNGESFTGK LADQASKANL MFEEGKHMTP VYTGALKDEL VKTDKIYGKI KKRLLWGSDL
ATMIRCARAF GGLMDELKAH CVTLPIRVGM NMNEDGPIIF EKHSRYTYHY DADYSRWDST
QQRAVLAAAL EIMVKFSPEP HLAQIVAEDL LSPSVMDVGD FKISITEGLP SGVPCTSQWN
SIAHWLLTLC ALSEVTDLSP DIIQANSLFS FYGDDEIVST DIKLDPEKLT AKLKEYGLKP
TRPDKTEGPL VISEDLDGLT FLRRTVTRDP AGWFGKLEQS SILRQMYWTR GPNHEDPAET
MIPHSQRPIQ LMSLLGEAAL HGPSFYSKIS KLVISELKEG GMDFYVPRQE PMFRWMRFSD
LSTWEGDRNL APSFVNEDGV E
//
