ID K7XSK3_9CALI Unreviewed; 1699 AA.
AC K7XSK3;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 08-NOV-2023, entry version 52.
DE RecName: Full=Genome polyprotein {ECO:0000256|ARBA:ARBA00020107};
GN Name=POL {ECO:0000313|EMBL:AFX81144.1};
OS Norovirus Hu/Norwalk/10110/2009/VNM.
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Norovirus; Norwalk virus.
OX NCBI_TaxID=1261203 {ECO:0000313|EMBL:AFX81144.1, ECO:0000313|Proteomes:UP000131891};
RN [1] {ECO:0000313|EMBL:AFX81144.1, ECO:0000313|Proteomes:UP000131891}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hu/Norwalk/10110/2009/VNM {ECO:0000313|EMBL:AFX81144.1};
RA Madupu R., Halpin R.A., Ransier A., Fedorova N., Tsitrin T., McLellan M.,
RA Stockwell T., Amedeo P., Appalla L., Bishop B., Edworthy P., Gupta N.,
RA Hoover J., Katzel D., Li K., Schobel S., Shrivastava S., Thovarai V.,
RA Wang S., My P.V., Campbell J., Farrar J., Vinh H., Hoang N.V.,
RA Wentworth D.E., Baker S.;
RL Submitted (OCT-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; KC175350; AFX81144.1; -; Genomic_RNA.
DR Proteomes; UP000131891; 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..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..120
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 COMPBIAS 97..113
FT /note="Polar 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; 189108 MW; 9EA7985BA8FDE6FA CRC64;
MKMASNDASA AAVANSNNDT AKSSSDKMFS NMAVTFKRAL GARPKQPPPR EIPQRPPRPP
TPELVKKIPP PPPNGEDEAV VSYSAKDGVS GLPELSTVRQ PEETNTAFSV PPLNQRENRD
AKEPLTGTIL EMWDGEIYHY GLYVERGLVL GVHKPPAAIS LAKVELTPLS LFWRPVYTPQ
YLISPDTLKK LHGETFPYTA FDNNCYAFCC WVLDLNDSWL SRRMIQRTTG FFRPYQDWNR
KPLPTMDDSK LKKVANIFLC ALSSLFTRPI 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 GQPDMWKNVF SSDFSHIKLA LAPQGGFDKN
GNTPHGKGVM KTLTTGSLIA RASGLLHERL DEFELQGPAL TTFNFDRNKV LAFRQLAAEN
KYGLIDTMKV GRQLKDVKTM PELKQALKNI SIKKCQIVYS GCTYTLESDG KGNVKVDRIQ
STSVQTNNEL AGALHHLRCA RIRYYVKCVQ EALYSIIQIA GAAFVTTRII KRVNIQDLWS
KPQVENTEEA TNKDGCPKPK DDEEFVISSD DIKTEGKKGK NKTGRGKKHT AFSSKGLSDE
EYDEYKRIRE ERNGRYSIEE YLQDRDKYYE EVAIARATEE DFCEEEEAKI RQRIFRPTRK
QRKEERASLG LVTGSEIRKR NPDDFKPKGK LWADDDRSVD YNEKLSFEAP PSIWSRIVNF
GSGWGFWVSP SLFITSTHVI PQGAKEFFGV PIKQIQVHKS GEFCRLRFPK PIRTDVTGMI
LEEGAPEGTV VTLLIKRSTG ELMPLAARMG THATMKIQGR TVGGQMGMLL TGSNAKSMDL
GTTPGDCGCP YIYKRGNDYV VIGVHTAAAR GGNTVICATQ GGEGEATLEG GDSKGTYCGA
PILGPGSAPK LSTKTKFWRS STAPLPPGTY EPAYLGGKDP RVKGGPSLQQ VMRDQLKPFT
EPRGKPPKPS VLEAAKKTII NVLEQTIDPP EKWSFAQACA SLDKTTSSGH PHHMRKNDCW
NGESFTGKLA DQASKANLMF EEGKNMTPVY TGALKDELVK TDKIYGKIKK 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
//