POLN_CRPVC
ID POLN_CRPVC Reviewed; 1771 AA.
AC Q9IJX4;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Replicase polyprotein;
DE Contains:
DE RecName: Full=Protein 1A;
DE AltName: Full=CrPV-1A;
DE Contains:
DE RecName: Full=Protein 2A;
DE Contains:
DE RecName: Full=Protein 2B;
DE Contains:
DE RecName: Full=Protein 2C;
DE Contains:
DE RecName: Full=Protein 3A;
DE Contains:
DE RecName: Full=Protein 3B;
DE Contains:
DE RecName: Full=3C-like protease;
DE EC=3.4.22.-;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase 3D-POL;
DE EC=2.7.7.48;
GN ORFNames=ORF1;
OS Cricket paralysis virus (isolate Teleogryllus
OS commodus/Australia/CrPVVIC/1968) (CrPV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Dicistroviridae; Cripavirus.
OX NCBI_TaxID=928300;
OH NCBI_TaxID=128161; Teleogryllus oceanicus (black field cricket).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10866656; DOI=10.1128/mcb.20.14.4990-4999.2000;
RA Wilson J.E., Powell M.J., Hoover S.E., Sarnow P.;
RT "Naturally occurring dicistronic cricket paralysis virus RNA is regulated
RT by two internal ribosome entry sites.";
RL Mol. Cell. Biol. 20:4990-4999(2000).
RN [2]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=18810573; DOI=10.1007/s00705-008-0208-5;
RA Nakashima N., Nakamura Y.;
RT "Cleavage sites of the 'P3 region' in the nonstructural polyprotein
RT precursor of a dicistrovirus.";
RL Arch. Virol. 153:1955-1960(2008).
RN [3]
RP FUNCTION OF PROTEIN 1A, AND INTERACTION WITH HOST AGO2.
RX PubMed=20400949; DOI=10.1038/nsmb.1810;
RA Nayak A., Berry B., Tassetto M., Kunitomi M., Acevedo A., Deng C.,
RA Krutchinsky A., Gross J., Antoniewski C., Andino R.;
RT "Cricket paralysis virus antagonizes Argonaute 2 to modulate antiviral
RT defense in Drosophila.";
RL Nat. Struct. Mol. Biol. 17:547-554(2010).
CC -!- FUNCTION: Protein 1A functions as a suppressor of RNA-mediated gene
CC silencing, an antiviral defense mechanism of insect cells. Inhibits
CC siRNA function, but does not interfere with miRNA pathway. Does not
CC bind to dsRNA or siRNA. {ECO:0000269|PubMed:20400949}.
CC -!- FUNCTION: RNA-directed RNA polymerase replicates genomic and
CC antigenomic RNA. {ECO:0000255|PROSITE-ProRule:PRU00539,
CC ECO:0000269|PubMed:20400949}.
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 1A]: Interacts with host AGO2; this interaction may
CC block the RNA-induced silencing complexes (RISC) activity.
CC {ECO:0000269|PubMed:20400949}.
CC -!- INTERACTION:
CC Q9IJX4; Q9VUQ5: AGO2; Xeno; NbExp=3; IntAct=EBI-15848754, EBI-442476;
CC -!- PTM: Protein 1A might be expressed through a ribosomal skip from one
CC codon to the next without formation of a peptide bond.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF218039; AAF80998.1; -; Genomic_RNA.
DR RefSeq; NP_647481.1; NC_003924.1.
DR PDB; 6C3R; X-ray; 2.60 A; A/B=14-154.
DR PDBsum; 6C3R; -.
DR SMR; Q9IJX4; -.
DR DIP; DIP-59000N; -.
DR IntAct; Q9IJX4; 1.
DR MEROPS; C03.015; -.
DR GeneID; 944541; -.
DR KEGG; vg:944541; -.
DR Proteomes; UP000008590; Genome.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IPI:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0060698; F:endoribonuclease inhibitor activity; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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:0060702; P:negative regulation of endoribonuclease activity; IDA:FlyBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR GO; GO:0016567; P:protein ubiquitination; IDA:FlyBase.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0140533; P:suppression of host RNAi-mediated antiviral immune response; IGI:FlyBase.
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; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR024387; Pept_C3G_Picornavir.
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 Pfam; PF12381; Peptidase_C3G; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR PRINTS; PR00918; CALICVIRUSNS.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS51874; PCV_3C_PRO; 1.
DR PROSITE; PS50507; RDRP_SSRNA_POS; 1.
DR PROSITE; PS51218; SF3_HELICASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coiled coil; Helicase; Host-virus interaction;
KW Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Protease;
KW Reference proteome; RNA-binding; RNA-directed RNA polymerase;
KW Suppressor of RNA silencing; Thiol protease; Transferase;
KW Viral RNA replication.
FT CHAIN 1..1771
FT /note="Replicase polyprotein"
FT /id="PRO_0000398372"
FT CHAIN 1..190
FT /note="Protein 2A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000398373"
FT CHAIN 1..166
FT /note="Protein 1A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000398374"
FT CHAIN 191..328
FT /note="Protein 2B"
FT /evidence="ECO:0000255"
FT /id="PRO_0000398375"
FT CHAIN 329..739
FT /note="Protein 2C"
FT /evidence="ECO:0000255"
FT /id="PRO_0000398376"
FT CHAIN 740..?
FT /note="Protein 3A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000398377"
FT CHAIN ?..908
FT /note="Protein 3B"
FT /evidence="ECO:0000255"
FT /id="PRO_0000398378"
FT CHAIN 909..1220
FT /note="3C-like protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000398379"
FT CHAIN 1221..1771
FT /note="RNA-directed RNA polymerase 3D-POL"
FT /evidence="ECO:0000255"
FT /id="PRO_0000398380"
FT DOMAIN 482..656
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 954..1201
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1495..1634
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 919..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..29
FT /evidence="ECO:0000255"
FT COILED 1385..1413
FT /evidence="ECO:0000255"
FT ACT_SITE 1003
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1063
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1162
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 510..517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 166..167
FT /note="Cleavage; by ribosomal skip"
FT /evidence="ECO:0000255"
FT SITE 190..191
FT /note="Cleavage; by 3C-like protease"
FT /evidence="ECO:0000255"
FT SITE 328..329
FT /note="Cleavage; by 3C-like protease"
FT /evidence="ECO:0000255"
FT SITE 739..740
FT /note="Cleavage; by 3C-like protease"
FT /evidence="ECO:0000255"
FT SITE 884..885
FT /note="Cleavage; by 3C-like protease"
FT /evidence="ECO:0000255"
FT SITE 908..909
FT /note="Cleavage; by 3C-like protease"
FT /evidence="ECO:0000255"
FT SITE 1220..1221
FT /note="Cleavage; by 3C-like protease"
FT /evidence="ECO:0000255"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:6C3R"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:6C3R"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:6C3R"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:6C3R"
FT HELIX 66..83
FT /evidence="ECO:0007829|PDB:6C3R"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:6C3R"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:6C3R"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:6C3R"
FT HELIX 123..127
FT /evidence="ECO:0007829|PDB:6C3R"
FT HELIX 130..136
FT /evidence="ECO:0007829|PDB:6C3R"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:6C3R"
SQ SEQUENCE 1771 AA; 203830 MW; 78C5969469EAA716 CRC64;
MSFQQTNNNA TNNINSLEEL AAQELIAAQF EGNLDGFFCT FYVQSKPQLL DLESECYCMD
DFDCGCDRIK REEELRKLIF LTSDVYGYNF EEWKGLVWKF VQNYCPEHRY GSTFGNGLLI
VSPRFFMDHL DWFQQWKLVS SNDECRAFLR KRTQLLMSGD VESNPGPVQS RPVYACDNDP
RAIRLEKALQ RRDEKISTLI KKLRQEIKNN RIYTQGFFDD LKGAKGEVGQ LNGNLTRICD
FLENSLPTLT AQIQTTVLTT TDKYVNLKED LLKVAILLVL VRLLMVWKKY RAALIVIILF
VMHFYGFDKQ ILDIVLDLKD KILQTTTQAG TETLEEVVYH PWFDTCGKLI FAVLAFFAIK
KIPGKQDWDN YISRLDRIPK AIEGSKKIVD YCSEYFNLSV DEVKKVVLGK ELKGTQGLYD
EIHVWAKEIR HYLDLDERNK ITLDTETAAK VEDLYKRGLK YSEEKIPDRD IARFITTMLF
PAKSLYEQVL LSPVKGGGPK MRPITVWLTG ESGIGKTQMI YPLCIDILRE MGIVKPDAYK
HQAYARQVET EYWDGYNGQK IVIYDDAFQL KDDKTKPNPE IFEVIRTCNT FPQHLHMAAL
QDKNMYSQAE VLLYTTNQFQ VQLESITFPD AFYNRMKTHA YRVQIKQEKS IWVRNARGEE
YNALDVTKLN KDEAIDLSVY EFQKMRFDDE SATKWIDDGE PISYDEFART ICKAWKEEKE
KTFHQLQWLE AYASRTVAQG GSETSEYYDV WDETYFSNLL SQGFMAGKSL IEMEAEFASD
AETFNAYIEY KKNIPKETKW SKWMTILDEQ ISALSTKIRE LKNKAYKFIS EHPYLTALGF
IGVMISAFAM YSFFERTLTD DTITSEVGSS GDNKTQKISK RVVEVGGSGD VKTTKPAKTA
VEVGSSGDSK TMKNKITKVE VGSSGDSKTQ KQRNTKVEVG KELEKEAETQ GCSDPAAHAL
VLDVLQKNTY CLYYERMVKG EMKRYRLATA TFLRGWVCMM PYHFIETLYA RKVAPSTNIY
FSQPNCDDVI VVPVSHFIAP NAERVELTTA CTRIHYKDET PRDCVLVNLH RRMCHPHRDI
LKHFVKKSDQ GNLRGVFQGT LATFHQSANE LCRAYQWLQA IRPLDQEITI YHEDTDMFDY
ESESYTQRDC YEYNAPTQTG NCGSIVGLYN KRMERKLIGM HIPGNVSECH GYACPLTQEA
IMDGLNRLEK LDPVNNITVQ CCFEPPSDIK DTMSGETPEG KFCAIGKSNI KVGQAVKTTL
LKSCIYGMLS KPITKPAHLT RTRLPNGEIV DPLMKGLKKC GVDTAVLDAE IVESAALDVK
QVVLTQYNSM LDVNKYRRFL TYEEATQGTG DDDFMKGIAR QTSPGYRYFQ MPRKLPGKQD
WMGSGEQYDF TSQRAQELRR DVEELIDNCA KGIIKDVVFV DTLKDERRPI EKVDAGKTRV
FSAGPQHFVV AFRKYFLPFA AYLMNNRIDN EIAVGTNVYS TDWERIAKRL KKHGNKVIAG
DFGNFDGSLV AQFFGQSCGK SFYPWFKTFN DVNTEDGKRN LMICIGLWTH IVHSVHSYGD
NVYMWTHSQP SGNPFTVIIN CLYNSMIMRI VWILLARKLA PEMQSMKKFR ENVSMISYGD
DNCLNISDRV VEWFNQITIS EQMKEIKHEY TDEGKTGDMV KFPSLSEIHF LKKRFVFSHQ
LQRTVAPLQK DVIYEMLNWT RNTIDPNEIL MMNINTAFRE IVYHGKSEYQ KLRSGIEDLA
MKGILPQQPQ ILTFKAYLWD ATMLADEVYD F
