ID D9U2H4_9CALI Unreviewed; 1699 AA.
AC D9U2H4;
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/Pune/PC15/2006/India.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Norovirus; Norwalk virus.
OX NCBI_TaxID=585766 {ECO:0000313|EMBL:ADK94749.1, ECO:0000313|Proteomes:UP000158972};
RN [1] {ECO:0000313|EMBL:ADK94749.1, ECO:0000313|Proteomes:UP000158972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC15 {ECO:0000313|EMBL:ADK94749.1};
RX PubMed=19319938; DOI=10.1002/jmv.21458;
RA Chhabra P., Dhongade R.K., Kalrao V.R., Bavdekar A.R., Chitambar S.D.;
RT "Epidemiological, clinical, and molecular features of norovirus infections
RT in western India.";
RL J. Med. Virol. 81:922-932(2009).
RN [2] {ECO:0000313|EMBL:ADK94749.1, ECO:0000313|Proteomes:UP000158972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC15 {ECO:0000313|EMBL:ADK94749.1};
RX PubMed=20633703; DOI=10.1016/j.meegid.2010.07.007;
RA Chhabra P., Walimbe A.M., Chitambar S.D.;
RT "Complete genome characterization of Genogroup II norovirus strains from
RT India: Evidence of recombination in ORF2/3 overlap.";
RL Infect. Genet. Evol. 10:1101-1109(2010).
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; EU921344; ADK94749.1; -; Genomic_RNA.
DR MEROPS; C37.001; -.
DR Proteomes; UP000158972; 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..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..862
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; 188956 MW; D89DD26E302812BF CRC64;
MKMASNDASA AAVANSNNDT AKSSSDGVLS SMAVTFKRAL GARPKQPPPR EIPQRPPRPP
TPELVKNVPP PPPNGEDEIV VSYSVKDGVS GLPDLSTVRQ PEESNTAFSV PPLNQRENRD
AKEPLTGTIL EMWDGEIYHY GLYVERGLVL GVHKPPAAIS LARVELTPLS LFWRPVYTPQ
YLISPDALKK LHGETFPYTA FDNNCYAFCC WVLDLNDSWL SRRMIQRTTG FFRPYQDWNR
KPLPTMDDSK LKKVANIFLC ALSSLFTRPI KDIIGKLRPL NILNILASCD WTFAGIVESL
ILLADLFGVF WTPPDVSAMI APLLGDYELQ GPEDLAVELV PVVMGGIGLV LGFTKEKIGK
MLSSAASTLR ACKDLGAYGL EILKLAMKWF FPKKEEANEL AIVRSIEDAV LDLEGIENNH
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
KYGLMDTMRV GRQLKDVRTM PELKQALKNI SIKKCQIVHN GCTYTLESDG KGNVKVDRVQ
SASVQTNNEL TGALHHLRCA RIRYYVRCVQ EALYSIIQIA GAAFVTTRIV KRMNIQDLWS
KPQVENTEET TSKGGCPKPK DDEEFVISSD DIKTEGKKGK NKTGRGKKHT AFSSKGLSDE
EYDEYKRIRE ERNGKYSIEE YLQDRDKYYE EVAIARATEE DFCEEEEAKI RQRIFRPTRK
QRKEERASLG LVTGSEIRKR NPDDFKPKGK LWADDDRSVD YNEKLSFEAP PSIWSRIVNF
GSGWGFWVSP SLFITSTHVI PQGAKEFFGV PIKQIQVHKT GEFCRLRFPK PIRTDVTGMI
LEEGAPEGTV VTLLIKRSTG ELMPLAARMG THATMKIQGR TVGGQMGMLL TGSNAKSMDL
GTTPGDCGCP YIYKRGNDYV VIGVHTAAAR GGNTVICATQ GSEGEATLEG GDNKGTYCGA
PILGPGSAPK LSTKTKFWRS STAPLPPGTY EPAYLGGKDP RVKGGPSLQQ VMRDQLKPFT
EPRGKPPKPS VLEAAKQTII NVLEQTIDPP EKWSFAQACA SLDKTTSSGH PHHMRKNDCW
NGESFTGKLA DQASKANLMF EEGKNMTPVY TAALKDELVK TDKIYGKIKK RLLWGSDLAT
MIRCARAFGG LMDELKTHCV TLPIRVGMNM NEDGPVIFEK HSRYTYHYDA DYSRWDSTQQ
RAVLAAALEI MVKFSPEPHL AQVVAEDLLS PSVVDVGDFT ISINEGLPSG VPCTSQWNSI
AHWLLTLCAL SEVTNLSPDT IQANSLFSFY GDDEIVSTDI KLDPEKLTAK LREYGLKPTR
PDKTEGPLVI SEDLNGLTFL RRTVTRDPAG WFGKLEQSSI LRQMYWTRGS NHEDPSETMI
PHSQRPIQLM SLLGEAALHG PAFYSKISKL VIAELKEGGM DFYVPRQEPM FRWMRFSDLS
TWEGDRNLAP SFVNEDGVE
//
