ID D9N2M0_9CALI Unreviewed; 1699 AA.
AC D9N2M0;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 08-NOV-2023, entry version 61.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Norovirus Hu/GII-4/Sakai2/2007/JP.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Norovirus; Norwalk virus.
OX NCBI_TaxID=707524 {ECO:0000313|EMBL:BAJ13953.1, ECO:0000313|Proteomes:UP000161631};
RN [1] {ECO:0000313|Proteomes:UP000161631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Vidal-Mas J., Besumbes O., Manresa M., Busquets M.;
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000161631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Norovirus Surveillance Group of Japan;
RA Motomura K., Yokoyama M., Ode H., Nakamura H., Mori H., Kanda T., Oka T.,
RA Katayama K., Noda M., Tanaka T., Takeda N., Sato H.;
RT "Genome Recombination for Independent and Concurrent Evolution of Non-
RT structural and Capsid Proteins of Norovirus GII/4 in Humans.";
RL Submitted (AUG-2010) 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; AB541341; BAJ13953.1; -; Genomic_RNA.
DR MEROPS; C37.001; -.
DR Proteomes; UP000161631; 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 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..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..76
FT /note="Pro 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; 189248 MW; 70B6F022E231D60F CRC64;
MKMASNDASA AAVANSNNDT AKSSSDKMFS NMAVTFKRAL GARPKQPPPR EIPQRPPRPP
TPELVKKIPP PPPNGEDEVV VSYSAKDGVS GLPELSTVRQ PEETNTAFSV PPFNQRENRD
AKEPLTGTIL EMWDGEIYHY GLYVERGLVL GVHKPPAAIS LAKVELTPLS LFWRPVYTPQ
YLISPDTLTK LHGETFPYTA FDNNCYAFCC WVLDLNDSWL SRRMIQRTTG FFRPYQDWNR
KPLPTMDDSK LKKVANIFLC TLSSLFTRPI KDIIGKLRPL NIINILASCD WTFAGIVESL
ILLAELFGVF WTPPDVSAMI APLLGDFELQ GPEDLVVELV PVVMGGIGLV LGFTKEKIGK
MLSSAASTLR ACKDLGAYGL EILKLVMKWF FPKKEEANEL AMVRSIEDAV LDLEAIENNH
MTTLLKDKDS LATYMRTLDL EEEKARKLST KSASPDIVGT INALLARIAA ARSLVHRAKE
ELSSRPRPVV LMISGRPGIG KTHLAREVAK RIAASLTGDQ RVGLIPRNGV DHWDAYKGER
VVLWDDYGMS NPIHDALRLQ ELADTCPLTL NCDRIENKGK VFDSDVIIIT TNLANPAPLD
YVNFEACSRR IDFLVYAEAP EVEKAKRDFP GQPDMWKNAF SSDFSHIKLA LAPQGGFDKN
GNTPHGKGVM KTLTTGSLIA RASGLLHERL DEFELQGPAL TTFNFDRNKV LAFRQLAAEN
KYGLMDTMKV GRQLKDVKTM PELKQALKNI SIKKCQIVYS GCTYTLESDG KGNVKVDRVQ
STSVQTNNEL AGALHHLRCA RIRYYVKCVQ EALYSIIQIA GAAFVTTRII KRVNIQDLWS
KPQVENTEEA TNKDGCPKPK DNEEFVISSD DIKTEGKKGK NKTGRGKKHT AFSSKGLSDE
EYDEYKRIRE ERNGKYSIEE YLQDRDKYYE EVAIARATEE DFCEEEEAKI RQRIFRPTRK
QRKEERASLG LVTGSEIRKR NPEDFKPKGK LWADDDRSVD YNEKLSFEAP PSIWSRIVNF
GSGWGFWVSP SLFITSTHVI PQGAKEFFGV PIKQIQVHKS GEFCRLRFPK PIRTDVTGMI
LEEGAPEGTV VTLLIKRSTG ELMPLAARMG THATMRIQGR TVGGQMGMLL TGSNAKSMDL
GTTPGDCGCP YIYKRGNDYV VIGVHTAAAR GGNTVICATQ GGEGEATLEG GDSKGTYCGA
PILGPGSAPK LSTKTKFWRS STAPLPPGTY EPAYLGGKDP RVKDGPSLQQ VMRDQLKPFT
EPRGKPPKPS VLEAAKKTII NVLEQTIDPP EKWSFAQACA SLDKTTSSGH PHHMRKNDCW
NGESFTGKLA DQASKANLMF EEGKNMTPVY TGALKDELVK TDKIYGRIKK RLLWGSDLAT
MIRCARAFGG LMDELKAHCV TLPIRVGMNM NEDGPIIFEK HSRYRYHYDA DYSRWDSTQQ
RAVLAAALEI MVKFSSEPHL AQVVAEDLLS PSVVDVGDFT ISINEGLPSG VPCTSQWNSI
AHWLLTLCAL SEVTNLSPDI IQANSLFSFY GDDEIVSTDI KLDPEKLTAK LKEYGLKPTR
PDKTEGPLVI SEDLDGLTFL RRTVTRDPAG WFGKLEQSSI LRQMYWTRGP NHEDPSESMI
PHSQRPIQLM SLLGEAALHG PTFYSKISKL VIAELKEGGM DFYVPRQEPM FRWMRFSDLS
TWEGDRNLAP SFVNEDGVE
//