POLG_LORDV
ID POLG_LORDV Reviewed; 1699 AA.
AC P54634;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Protein p37;
DE Contains:
DE RecName: Full=NTPase;
DE EC=3.6.1.15;
DE AltName: Full=p40;
DE Contains:
DE RecName: Full=Protein p20;
DE Contains:
DE RecName: Full=Viral genome-linked protein;
DE AltName: Full=VPG;
DE Contains:
DE RecName: Full=3C-like protease;
DE Short=3CLpro;
DE EC=3.4.22.66;
DE AltName: Full=Calicivirin;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE Short=RdRp;
DE EC=2.7.7.48;
GN ORFNames=ORF1;
OS Lordsdale virus (strain GII/Human/United Kingdom/Lordsdale/1993) (Human
OS enteric calicivirus) (Hu/NV/LD/1993/UK).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Caliciviridae; Norovirus.
OX NCBI_TaxID=82658;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=7561776; DOI=10.1099/0022-1317-76-9-2349;
RA Dingle K.E., Lambden P.R., Caul E.O., Clarke I.N.;
RT "Human enteric Caliciviridae: the complete genome sequence and expression
RT of virus-like particles from a genetic group II small round structured
RT virus.";
RL J. Gen. Virol. 76:2349-2355(1995).
CC -!- FUNCTION: Protein p37 may play a role in viral replication by
CC interacting with host VAPA, a vesicle-associated membrane protein that
CC plays a role in SNARE-mediated vesicle fusion. This interaction may
CC target replication complex to intracellular membranes (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: NTPase presumably plays a role in replication. Despite having
CC similarities with helicases, does not seem to display any helicase
CC activity (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Protein P20 may play a role in targeting replication complex
CC to intracellular membranes. {ECO:0000250}.
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 (By
CC similarity). {ECO:0000250}.
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:0000255|PROSITE-ProRule:PRU00870}.
CC -!- FUNCTION: RNA-directed RNA polymerase replicates genomic and
CC antigenomic RNA by recognizing replications specific signals.
CC Transcribes also a subgenomic mRNA by initiating RNA synthesis
CC internally on antigenomic RNA. This sgRNA codes for structural
CC proteins. Catalyzes the covalent attachment VPg with viral RNAs (By
CC similarity). {ECO:0000255|PROSITE-ProRule:PRU00539}.
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 -!- 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:0000255|PROSITE-
CC ProRule:PRU00870};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
CC -!- SUBUNIT: [Protein p37]: Interacts with human VAPA.
CC {ECO:0000250|UniProtKB:Q83883}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins. 3CLpro
CC is first autocatalytically cleaved, then processes the whole
CC polyprotein. {ECO:0000255|PROSITE-ProRule:PRU00870}.
CC -!- PTM: VPg is uridylylated by the polymerase and is covalently attached
CC to the 5'-end of the polyadenylated genomic and subgenomic RNAs. This
CC uridylylated form acts as a nucleotide-peptide primer for the
CC polymerase (By similarity). {ECO:0000250}.
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DR EMBL; X86557; CAA60254.1; -; Genomic_RNA.
DR SMR; P54634; -.
DR MEROPS; C37.001; -.
DR PRIDE; P54634; -.
DR Proteomes; UP000007767; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0017111; F:nucleoside-triphosphatase 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-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 3.40.50.300; -; 1.
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; SSF50494; SSF50494; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51537; NV_3CL_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Covalent protein-RNA linkage; Host-virus interaction;
KW Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW Protease; RNA-directed RNA polymerase; Thiol protease; Transferase;
KW Viral RNA replication.
FT CHAIN 1..1699
FT /note="Genome polyprotein"
FT /id="PRO_0000341998"
FT CHAIN 1..330
FT /note="Protein p37"
FT /id="PRO_0000036914"
FT CHAIN 331..696
FT /note="NTPase"
FT /id="PRO_0000036915"
FT CHAIN 697..875
FT /note="Protein p20"
FT /id="PRO_0000036916"
FT CHAIN 876..1007
FT /note="Viral genome-linked protein"
FT /id="PRO_0000036917"
FT CHAIN 1008..1189
FT /note="3C-like protease"
FT /id="PRO_0000036918"
FT CHAIN 1190..1699
FT /note="RNA-directed RNA polymerase"
FT /id="PRO_0000036919"
FT DOMAIN 465..632
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1009..1189
FT /note="Peptidase C37"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00870"
FT DOMAIN 1425..1546
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..894
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 49..76
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 843..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:0000255|PROSITE-ProRule:PRU00870"
FT ACT_SITE 1062
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00870"
FT ACT_SITE 1147
FT /note="For 3CLpro activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00870"
FT BINDING 495..502
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 330..331
FT /note="Cleavage; by 3CLpro"
FT /evidence="ECO:0000250"
FT SITE 696..697
FT /note="Cleavage; by 3CLpro"
FT /evidence="ECO:0000250"
FT SITE 875..876
FT /note="Cleavage; by 3CLpro"
FT /evidence="ECO:0000250"
FT SITE 1008..1009
FT /note="Cleavage; by 3CLpro"
FT /evidence="ECO:0000250"
FT SITE 1189..1190
FT /note="Cleavage; by 3CLpro"
FT /evidence="ECO:0000250"
FT MOD_RES 902
FT /note="O-(5'-phospho-RNA)-tyrosine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1699 AA; 189201 MW; FA00B3B67FF3A0B6 CRC64;
MKMASNDASA AAVVNSNNDT AKSSSDGVLS SMAVTFKRAL GGRAKQPPPR ETPQRPPRPP
TPELVKKIPP PPPNGEDELV VSYSVKDGVS GLPELSTVRQ PDEANTAFSV PPLNQRENRD
AKEPLTGTIL EMWDGEIYHY GLYVERGLVL GVHKPPAAIS LAKVELTPLS LFWRPVYTPQ
YLISPDTLKR LHGESFPYTA FDNNCYAFCC WVLDLNDSWL SRRMIQRTTG FFRPYQDWNR
KPLPTMDDSK LKKVANVFLC ALSSLFTRPI KDIIGKLRPL NILNILASCD WTFAGIVESL
ILLAELFGVF WTPPDVSAMI APLLGDYELQ GPEDLAVELV PIVMGGIGLV LGFTKEKIGK
MLSSAASTLR ACKDLGAYGL EILKLVMKWF FPKKEEANEL AMVRSIEDAV LDLEAIENNH
MTTLLKDKDS LATYMRTLDL EEEKARKLST KSASPDIVGT INALLARIAA ARSLVHRAKE
ELSSRLRPVV VMISGKPGIG KTHLARELAK RIAASLTGDQ RVGLIPRNGV DHWDAYKGER
VVLWDDYGMS NPIHDALRLQ ELADTCPLTL NCDRIENKGK VFDSDAIIIT TNLANPAPLD
YVNFEACSRR IDFLVYAEAP EVEKAKRDFP GQPDMWKNAF SPDFSHIKLA LAPQGGFDKN
GNTPHGKGVM KTLTTGSLIA RASGLLHERL DEYELQGPAL TTFNFDRNKV LAFRQLAAEN
KYGLMDTMKV GRQLKDVRTM PELKQALKNI SIKRCQIVYS GCTYTLESDG KGNVKVDRVQ
SATVQTNHEL AGALHHLRCA RIRYYVKCVQ EALYSIIQIA GAAFVTTRIV KRMNIQDLWS
KPQVEDTEDT ANKDGCPKPK DDEEFVVSSD DIKTEGKKGK NKTGRGKKHT AFSSKGLSDE
EYDEYKRIRE ERNGKYSIEE YLQDRDKYYE EVAIARATEE DFCEEEEAKI RQRIFRPTRK
QRKEERASLG LVTGSEIRKR NPDDFKPKGK LWADDDRSVD YNEKLDFEAP PSIWSRIVNF
GSGWGFWVSP SLFITSTHVI PQGAQEFFGV PVKQIQIHKS GEFCRLRFPK PIRTDVTGMI
LEEGAPEGTV VTLLIKRSTG ELMPLAARMG THATMKIQGR TVGGQMGMLL TGSNAKSMDL
GTTPGDCGCP YIYKRENDYV VIGVHTAAAR GGNTVICATQ GSEGEATLEG GDNKGTYCGA
PILGPGSAPK LSTKTKFWRS STAPLPPGTY EPAYLGGKDP RVKGGPSLQQ VMRDQLKPFT
EPRGKPPKPS VLEAAKRTII NVLEQTIDPP QKWSFTQACA SLDKTTSSGH PHHMRKNDCW
NGESFTGKLA DQASKANLMF EEGKNMTPVY TGALKDELVK TDKIYGKIKK RLLWGSDLAT
MIRCARAFGG LMDELKAHCV TLPIRVGMNM NEDGPIIFER HSRYKYHYDA DYSRWDSTQQ
RAVLAAALEI MVKFSPEPHL AQIVAEDLLS PSVMDVGDFK ISINEGLPSG VPCTSQWNSI
AHWLLTLCAL SEVTNLSPDI IQANSLFSFY GDDEIVSTDI NLNPEKLTAK LKEYGLKPTR
PDKTEGPLII SEDLNGLTFL RRTVTRDPAG WFGKLDQSSI LRQMYWTRGP NHEDPSETMI
PHSQRPIQLM SLLGEAALHG PAFYSKISKL VIAELKEGGM DFYVPRQEPM FRWMRFSDLS
TWEGDRNLAP SFVNEDGVE
