ID A9YYE3_9CALI Unreviewed; 1699 AA.
AC A9YYE3;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 08-NOV-2023, entry version 80.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
OS Norovirus Hu/Houston/TCH186/2002/US.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Norovirus; Norwalk virus.
OX NCBI_TaxID=489822 {ECO:0000313|EMBL:ABY27559.1, ECO:0000313|Proteomes:UP000144333};
RN [1] {ECO:0000313|EMBL:ABY27559.1, ECO:0000313|Proteomes:UP000144333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hu/Houston/TCH186/2002/US {ECO:0000313|EMBL:ABY27559.1};
RX PubMed=17054072; DOI=10.1086/508430;
RA Larsson M.M., Rydell G.E., Grahn A., Rodriguez-Diaz J., Akerlind B.,
RA Hutson A.M., Estes M.K., Larson G., Svensson L.;
RT "Antibody prevalence and titer to norovirus (genogroup II) correlate with
RT secretor (FUT2) but not with ABO phenotype or Lewis (FUT3) genotype.";
RL J. Infect. Dis. 194:1422-1427(2006).
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; EU310927; ABY27559.1; -; Genomic_RNA.
DR MEROPS; C37.001; -.
DR Proteomes; UP000144333; 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..76
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; 189120 MW; F0B666623A9AB77E CRC64;
MKMASNDASA AAVANSNNDT AKSSSDGVLS SMAVTFKRAL GARPKQPPPR EIPQRPPRPP
TPELVKKIPP PPPNGEDEIV VSYSVKDGVS GLPELSTVRQ PEEANTAFSV PPLNQRENRD
AKEPLTGTIL EMWDGEIYHY GLYVERGLVL GVHKPPAAIS LAKVELTPLS LFWRPVYTPQ
YLISPDTLKK LHGETFPYTA FDNNCYAFCC WVLDLNDSWL SRRMIQRTTG FFRPYQDWNR
KPLPTMDDSK LKKVANIFLC ALSSLFTRPI KDIIGKLRPL NILNILASCD WTFAGIVESL
ILLAELFGVF WTPPDVSAMI APLLGDYELQ GPEDLAVELV PVVMGGIGLV LGFTKEKIGK
MLSSAASTLR ACKDLGAYGL EILKLVMKWF FPKKEEANEL AMVRSIEDAV LDLEAIENNH
MTTLLKDKDS LATYMRTLDL EEEKARKLST KSASPDIVGT INALLARIAA ARSLVHRAKE
ELSSRPRPVV LMISGRPGIG KTHLAREVAK RIAASLTGDQ RVGLVPRNGV DHWDAYKGER
VVLWDDYGMS NPIHDALRLQ ELADTCPLTL NCDRIENKGK VFDSDVIIIT TNLANPAPLD
YVNFEACSRR IDFLVYAEAP EVEKAKRDFP GQPDMWKNAF SSDFSHIKLT LAPQGGFDKN
GNTPHGKGVM KTLTTGSLIA RASGLLHERL DEFELQGPTL TTFNFDRNKV LAFRQLAAEN
KYGLMDTMKV GRQLKDVRTM PELKQALKNI SIKKCQIVYS GCTYTLESDG KGNVKVDRVQ
SASVQTNNEL TGALHHLRCA RIRYYVRCVQ EALYSIIQIA GAAFVTTRIV KRMNIQDLWS
KPQVENTEEA TNKDGCPKPR DDEEFVISSD DIKTEGKKGK NKTGRGKKHT AFSSKGLSDE
EYDEYKRIRE ERNGKYSIEE YLQDRDKYYE EVAIARATEE DFCEEEEAKI RQRIFRPTKK
QRKEERASLG LVTGSEIRKR NPDDFKPKGK LWADDDRSVD YNEKLSFEAP PSIWSRIVNF
GSGWGFWVSP SLFITSTHVI PQGAKEFFGV PIKQIQVHKS GEFCRLRFPK PIRTDVTGMI
LEEGAPEGTV VTLLIKRSTG ELMPLAARMG THATMKIQGR TVGGQMGMLL TGSNAKSMDL
GTTPGDCGCP YIYKRGNDYV VIGVHTAAAR GGNTVICATQ GSEGEATLEG GDSKGTYCGA
PILGPGSAPK LSTKTKFWRS STAPLPPGTY EPAYLGGKDP RVKGGPSLQQ VMRDQLKPFT
EPRGKPPKPS VLEAAKKTII NVLEQTIDPP EKWSFAQACA SLDKTTSSGH PHHMRKNDCW
NGESFTGKLA DQASKANLMF EEGKNMTPVY TGALKDELVK TDKIYGKIKK RLLWGSDLAT
MIRCARAFGG LMDELKAHCV TLPIRVGMNM NEDGPIIFER HSRYRYHYDA DYSRWDSTQQ
RAVLAAALEV MVKFSSEPHL AQVVAEDLLS PSVVDVGDFT ISINEGLPSG VPCTSQWNSI
AHWLLTLCAL SEVTNLSPDI IQANSHFSFY GDDEIVSTDI KLDPEKLTAK LKEYGLKPTR
PDKTEGPLVI SEDLNGLTFL RRTVTRDPAG WFGKLEQSSI LRQMYWTRGP NHEDPSETMI
PHSQRPIQLM SLLGEAALHG PTFYSKISKL VIAELKEGGM DFYVPRQEPM FRWMRFSDLS
TWEGDRNLAP SFVNEDGVE
//
