ID A4K7J1_9CALI Unreviewed; 1699 AA.
AC A4K7J1;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 08-NOV-2023, entry version 83.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Norovirus Hu/MK04/2004/JP.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Norovirus; Norwalk virus.
OX NCBI_TaxID=379081 {ECO:0000313|EMBL:ABE41640.1, ECO:0000313|Proteomes:UP000148483};
RN [1] {ECO:0000313|EMBL:ABE41640.1, ECO:0000313|Proteomes:UP000148483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hu/MK04/2004/JP {ECO:0000313|EMBL:ABE41640.1};
RA Hansman G.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; DQ456824; ABE41640.1; -; Genomic_RNA.
DR MEROPS; C37.001; -.
DR Proteomes; UP000148483; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 465..632
FT /note="SF3 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51218"
FT DOMAIN 1009..1189
FT /note="Peptidase C37"
FT /evidence="ECO:0000259|PROSITE:PS51537"
FT DOMAIN 1425..1546
FT /note="RdRp catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50507"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 431..481
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..77
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..879
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1038
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00870"
FT ACT_SITE 1062
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00870"
FT ACT_SITE 1147
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00870"
SQ SEQUENCE 1699 AA; 189262 MW; EA87A62E763FF792 CRC64;
MKMASNDASA AAAVNSNNDN TKSSSDGMFN NVAVTLKRAL GARSKQPAPR EKPPRPPRPP
TPELIKRIPP PPPNDGDEPT VMFSTVGGVS GLPELTTVGQ PPEANTAFSV PPLSQRENRD
AKEPLTGTIL EMWDGEIYHY GLYVERGLVL GVHKPPAAIS IAKVELTPLS LYWRPVYTPQ
YLISPDTLRK LHGELFPYTA FENNCYAFCC WVLDLNDSWL SRRMISRTTG FFRPYQEWNR
KPLPTMDDSK LKKVANIVLC ALSSLFTRPI KDIIGKLKPL NILNILASCD WTFAGIVESL
ILLAELFDVF WTPPDVSAMI APLLGDYELQ GPEDIAVELV PVVMGGIGLV LGFTKEKIGK
MLSSAASTLR ACKDLGAYGL EILKLVMKWF FPKKDEANEL AMVRAIEDAV LDLEAIENNH
MTTLLKDKNS LAAYMKTLDM EEEKARKLST KSASPDIVGT INALLARIAA ARSLVHRAKE
ELSSRPRPVV LMISGKPGIG KTHLARELAK KIASTLTGDQ RVGLIPRNGV DHWDAYKGER
VVLWDDYGMS NPIHDALRLQ ELADTCPLTL NCDRIENKGK VFDSDAIIIT TNLVNPAPLD
YVNFEACSRR IDFLVYADAP EVEKAKRDFP GQPDMWKDAY RSDFSHIKLQ LAPQGGFDKN
GNTPHGKGVM KTLTASSLVA RASGLLHERL DEYELQGPPL STFNFDRNKI AAFRQLAAEN
KYGLVDTMRV GNQLRNVTTM DELKKAIKNI IIRKCQIVYG GNTYTLESDG KGKVVVERVQ
SASVQINNEI AGAVHHLRCA RIRYYVKCVQ EAIYSLLQIA GTVFVTSRII SRMNIQNLWS
RPLTEDADEA TMKEGCPKPR EEEEFVVSSD DIKPEGKKGK NKSGRGKKHT AFSSKGLSDE
EYEEYKRIRE ERNGKYSIEE YLQDRDKYYE EVAIARATEE DFCEEEEVKI RQRIFRPTRK
QRKEERANLG LVTGSEIRKR NPDDFKPKGK LWADDDRSVD YNERISFEAP PSIWSRIVNF
GSGWGFWVSP SLFITSTHVI PQGITEAFGV PIRQVQIHKS GEFCRLRFPK PIRTDVSGMI
LEEGAPEGTV ATILIKRTTG ELMPLAARMG THATMRIQGR TVGGQMGMLL TGSNAKSMDL
GTTPGDCGCP YIYKRGNDYI VIGVHTAAAR GGNTVICATQ GSEGEATLEG GDNKGTYCGA
PILGPGNAPK LSTKTKFWRS STTPLPPGTY EPAYLGGKDP RVKGGPSLQQ VMRDQLKPFT
EPRGKPPKPS VLEAAKKTII NVLEQTIDPP QKWSYAQACA SLDKTTSSGY PHHVRKNEHW
NGESFTGKLA DQASKANLMF EEGKHMTPVY TAALKDELVK TEKVYGKIKK RLLWGSDLAT
MVRCARSFGG LMDELKAHCV TLPIRVGMNM NEDGPIVFEK HSRYRYHYDA DYSRWDSTQQ
RAVLAAAMEI MVKFSAEPQL AQIVAEDLLS PSVVDVGDFK ISINEGLPSG VPCTSQWNSI
AHWLLTLCAL SEVTDLSPDI VQANSLFSFY GDDEIVSTDI KLDPEKLTGK LREYGLKPTR
PDKTEGPLII SEDLNGLTFL RRTVTRDPAG WFGKLDQSSI LRQLYWTKGP NHEDPFESMI
PHSQRPIQLM SLLGEAALHE PSFYSKISKL VISELKESGM DFYVPRQEPM FRWMRFSDLS
TWEGDRNLAP SLVNEDGVE
//
