POL1_CNSV
ID POL1_CNSV Reviewed; 2336 AA.
AC Q8QVV0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=RNA1 polyprotein;
DE AltName: Full=P1;
DE Contains:
DE RecName: Full=P1A protein;
DE Short=1A;
DE AltName: Full=Protease cofactor;
DE Contains:
DE RecName: Full=Putative ATP-dependent helicase;
DE EC=3.6.4.-;
DE AltName: Full=1B;
DE AltName: Full=Membrane-binding protein;
DE AltName: Full=NTP-binding protein;
DE Short=NTB;
DE Contains:
DE RecName: Full=Viral genome-linked protein;
DE AltName: Full=1C-VPg;
DE Contains:
DE RecName: Full=Picornain 3C-like protease;
DE Short=3C-like protease;
DE EC=3.4.22.-;
DE AltName: Full=1D-PRO;
DE Contains:
DE RecName: Full=RNA-directed RNA polymerase;
DE EC=2.7.7.48;
DE AltName: Full=1E-POL;
OS Cycas necrotic stunt virus (CNSV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Secoviridae; Comovirinae; Nepovirus.
OX NCBI_TaxID=173976;
OH NCBI_TaxID=16901; Aucuba japonica (Japanese laurel) (Spotted laurel).
OH NCBI_TaxID=3396; Cycas revoluta (Sago palm).
OH NCBI_TaxID=49747; Gladiolus.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12417954; DOI=10.1007/s00705-002-0876-5;
RA Han S.S., Karasev A.V., Ieki H., Iwanami T.;
RT "Nucleotide sequence and taxonomy of Cycas necrotic stunt virus.";
RL Arch. Virol. 147:2207-2214(2002).
CC -!- FUNCTION: Picornain 3C-like protease is a thiol protease that cleaves
CC the P1 and P2 polyproteins. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: [Viral genome-linked protein]: Host endoplasmic
CC reticulum lumen {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Putative ATP-dependent helicase]: Host
CC endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: Specific enzymatic cleavages by picornain 3C-like protease in vivo
CC yield mature proteins. Picornain 3C-like protease is autocatalytically
CC processed (By similarity). {ECO:0000250}.
CC -!- PTM: VPg is uridylylated by the polymerase and is covalently linked to
CC the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-
CC peptide primer for the polymerase (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nepoviruses RNA1 polyprotein family.
CC {ECO:0000305}.
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DR EMBL; AB073147; BAB89369.1; -; Genomic_RNA.
DR RefSeq; NP_620619.1; NC_003791.1.
DR SMR; Q8QVV0; -.
DR MEROPS; C03.025; -.
DR PRIDE; Q8QVV0; -.
DR GeneID; 988023; -.
DR KEGG; vg:988023; -.
DR Proteomes; UP000008564; Genome.
DR GO; GO:0044166; C:host cell endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
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: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; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
DR InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
DR InterPro; IPR044067; PCV_3C_PRO.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00910; RNA_helicase; 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 3: Inferred from homology;
KW ATP-binding; Covalent protein-RNA linkage; Helicase;
KW Host endoplasmic reticulum; Host membrane; Hydrolase; Membrane;
KW Nucleotide-binding; Nucleotidyltransferase; Protease; RNA-binding;
KW RNA-directed RNA polymerase; Thiol protease; Transferase; Transmembrane;
KW Transmembrane helix; Viral RNA replication.
FT CHAIN 1..598
FT /note="P1A protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037065"
FT CHAIN 599..1253
FT /note="Putative ATP-dependent helicase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037066"
FT CHAIN 1254..1280
FT /note="Viral genome-linked protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000037067"
FT CHAIN 1281..1490
FT /note="Picornain 3C-like protease"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037068"
FT CHAIN 1491..2336
FT /note="RNA-directed RNA polymerase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000037069"
FT TOPO_DOM 599..1210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1211..1231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1232..1253
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 797..964
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 1278..1486
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 1771..1899
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT ACT_SITE 1320
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1358
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 1450
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 827..834
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
SQ SEQUENCE 2336 AA; 261655 MW; 0A87B95930F2A963 CRC64;
MGWICPNVSC LGHTSVLSNK EISREGRCER AMCGSLLVKV AVPQQPAKKK KQATPAPRPT
YPPCVVEKTA ATPVTVEKVF VEVIPTVPSC LAPKWMLGIQ RVEGAPSKAP KQAVPKWVWQ
MRQLLKAALT GANSFGPRYV RAHFSRARIS WIYAQLCEGC PLPLWNRGRA LKKSSLALLA
RIEDTKQQKR AAWEKKEAAP LKSKREYEQK RALLIPLIEK LRARLLQDEA RELREQLFPS
GNGGTDTTKV AAASKAEIKA AAQLKAYQDV CAKVWRVKRQ EKKAQQAKLV EDLITSANCG
KQDVSEPAIE KAARPKRRIE IGDFVPQKTL WGLYPCVGLG ANMADPVCRV LSACVSIAGK
RPDLVSTIYA FITGEAQVWL SAPRVCMLAK RIIELSDWYP HELLAEELKK ISDEENCKEA
EREINLKYLE ISKATENMRA NGLFNKLKGK AQDLWSGIVD FASHPFRKYL ATAAEFVEGF
SHRVVDAVMS RVNAAIAQFA AQLDIAKTLV DQLVIHVKRW YTSLCTSFDD SLKLLGKWAG
YALGLIVGVG VCHLVEVICA HMGLPLGGVI TGVFTTAYMG WLFVKTPVGS ELVMNLRMQV
ARIARNIFDV QRTGIPPDLP ANPNVGFSVP YEAFGGIDNQ PFSMGADVPN ARAIPVVSPI
INAMAGFGAS MLSMKAMGLI EMGKLGAACH SLRMGKDALC EFVSTVLYYF GRLADKVTGR
ETEFFDELSI LVQIDVKDWI TRSRGVLLDS CYTSLNNMIC SDVVNKLVTD GEQIASNIAG
TPRRLSLDFG QLVSSIMKDL LDLQQRIVRH GVTVGRRKEP TWIYIFGPSH CGKSNMMDHL
TSEVCRYFDL PYTYIARNGQ DNFFTTGYKR QTVLQIDDLS CVENVPPIER ELINLVSCSE
YPLKMADLSD KSISFQSPFI ISTSNQRTCL PTCGITHCEA FNNRRAVVVE MRRKPGVVFD
PMDCHAAMQG RFLDKRDHTP LFGVQGQPET FWKDVPEMTT ILLNICVAHR QEQDILQEQH
IRKHAVNDPL ILASERFLKQ ESRKALCYMP RVEMEICGVQ SQAAGCYYLC VDQKLYTCED
DGNLVETPCL NPSYAQWERN SSENFVGGVQ ALDALECRSI LVSGILRNLV QGQCCVLSID
EMSRLPLCTQ RLFKALQLQE RVYLRLIQKK ISHILSVDES NVYSKNAWMR CLEFAAASRD
YLKEHGLEVL LLLAAMMILC VALYYFVGAF IGVMGGALSM GAAMAGLKEV DMKAQYSSGA
QEGRYRSRNI PIRQRYRYAR GELDEEVPLG GQLAVALYGS QGRFISALQY KGKSVMLTRH
QMLMFAEKER VTCIYLATGE SVVLTFNRDD VQEFPNHETC MWQAAGMLQL PAKFKDCFLE
KGETELAPAF ELEGYVLRPD STAFIMTILK TWARVQYEPF VVRGSLAKEK YVNELPTSIW
FQYQSRNNDC GMVCLAQVGG KKKIVGLLVA GVDQQTWADN LPNPCMAEMK SQIEYEFKLG
AHTEGYTKLG YLTKDKTPHL PKKNNAVLVK PEYRIDSPVP IKEPSIISAE DPRCPKDAEG
KPIDPIVKAF EKKFTTPMDL LEDDILESIA QEMVDEWQDC ESEPLCDVPL EVAINGIPGT
QIDDDDEFED AVECLKMRTS PGYPYVLHKE PGMKGKEAYF ELAPDGTRAL KEGSLAAELY
ENIVQYSKSA IPELVVIECP KDELLKTEKV NKACRPFEIM PLHYNLFLRE KTLAFSLFQQ
RNRHKLACQV GTKAYSHDWT HMYQRLVAKS DRAINCDYSS FDGLLNSQVV SCIANMINSM
YHSPEETVVS KRQRYNMINA LFGRLAITGQ EVMRVRAGLP SGFALTVVIN SVFNEILMRY
CFKVLVLGPQ RNSFSTYVTL LVYGDDNLMS CTDKIAIYFN GETIKETLKK KNVTITDGSD
KTAPDIKWKT LGELDFLKRR FLKLETGVVQ APLDLTAIFS CLHWVTPHPQ KMPKGGAQLQ
VENVDTLYEL ALNVQVALTE LYLHGNKEEF QRVRNFYTKK MNILPAGYYT WADREAFHMS
KQTGMEAYQP AKEIDLDVGQ EFARFMHTSD IGNQVHFTRQ CLVVAGPFYK PTPDQLLVST
TPLKQGESGY WVPVETGMGI GNLPTIAWVH RFMRPTQLVD AYGYKIWGNV RSHIESGKSL
VFRSEAPYVA GNAALMAFGQ AAKLLEIKTA LNLYRNVIPE STYGLEQYFD AAIPQASLPG
TFYLANAESE SLLQEHKTGT VIGLTTEKFN LNGARDLIMQ GQKLGKLPVM AATQAPNKFY
VGLCCQKNFC PGHATSSDSI AKAFSQCWAM RCAPNSSSRK VTFEPEWRKN KFLGIS
