POLG_RTSVA
ID POLG_RTSVA Reviewed; 3473 AA.
AC Q83034;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Genome polyprotein;
DE Contains:
DE RecName: Full=Putative leader protein;
DE Contains:
DE RecName: Full=Capsid protein 1;
DE Short=CP-1;
DE AltName: Full=22.5 kDa protein;
DE AltName: Full=Coat protein 1;
DE Contains:
DE RecName: Full=Capsid protein 2;
DE Short=CP-2;
DE AltName: Full=26 kDa protein;
DE AltName: Full=Coat protein 2;
DE Contains:
DE RecName: Full=Capsid protein 3;
DE Short=CP-3;
DE AltName: Full=31 kDa protein;
DE AltName: Full=Coat protein 3;
DE Contains:
DE RecName: Full=Putative helicase;
DE EC=3.6.4.-;
DE AltName: Full=Putative NTP-binding protein;
DE Contains:
DE RecName: Full=Probable picornain 3C-like protease;
DE Short=3C-like protease;
DE EC=3.4.22.-;
DE Contains:
DE RecName: Full=Probable RNA-directed RNA polymerase;
DE EC=2.7.7.48;
OS Rice tungro spherical virus (strain A) (RTSV) (Rice tungro spherical
OS waikavirus).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Secoviridae; Waikavirus.
OX NCBI_TaxID=337081;
OH NCBI_TaxID=4530; Oryza sativa (Rice).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], PROTEIN SEQUENCE OF 645-659; 853-867 AND
RP 1056-1073, AND PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=8460478; DOI=10.1006/viro.1993.1170;
RA Shen P., Kaniewska M., Smith C., Beachy R.N.;
RT "Nucleotide sequence and genomic organization of rice tungro spherical
RT virus.";
RL Virology 193:621-630(1993).
RN [2]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND MUTAGENESIS OF GLN-2509;
RP GLN-2526; GLN-2526; GLN-2852 AND GLN-2885.
RX PubMed=9683576; DOI=10.1006/viro.1998.9225;
RA Thole V., Hull R.;
RT "Rice tungro spherical virus polyprotein processing: identification of a
RT virus-encoded protease and mutational analysis of putative cleavage
RT sites.";
RL Virology 247:106-114(1998).
RN [3]
RP CHARACTERIZATION OF PICORNAIN 3C-LIKE PROTEASE, AND MUTAGENESIS OF
RP HIS-2680; GLU-2717; ASP-2735; CYS-2811 AND HIS-2830.
RX PubMed=12466496; DOI=10.1099/0022-1317-83-12-3179;
RA Thole V., Hull R.;
RT "Characterization of a protein from Rice tungro spherical virus with serine
RT proteinase-like activity.";
RL J. Gen. Virol. 83:3179-3186(2002).
CC -!- FUNCTION: Picornain 3C-like protease is a thiol protease that probably
CC cleaves the polyprotein. {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: [Capsid protein 1]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein 2]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein 3]: Virion {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Putative helicase]: Host membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
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}.
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DR EMBL; M95497; AAA66056.1; -; Genomic_RNA.
DR PIR; A46112; A46112.
DR PIR; S27927; S27927.
DR RefSeq; NP_042507.1; NC_001632.1.
DR MEROPS; C03.024; -.
DR PRIDE; Q83034; -.
DR GeneID; 1497257; -.
DR KEGG; vg:1497257; -.
DR Proteomes; UP000007086; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; 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: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:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; 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 CDD; cd00205; rhv_like; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 2.60.120.20; -; 3.
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; IPR024387; Pept_C3G_Picornavir.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001676; Picornavirus_capsid.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR033703; Rhv-like.
DR InterPro; IPR001205; RNA-dir_pol_C.
DR InterPro; IPR007094; RNA-dir_pol_PSvirus.
DR InterPro; IPR029053; Viral_coat.
DR InterPro; IPR024379; Waikavirus_capsid-1.
DR Pfam; PF12381; Peptidase_C3G; 1.
DR Pfam; PF00680; RdRP_1; 1.
DR Pfam; PF00073; Rhv; 1.
DR Pfam; PF00910; RNA_helicase; 1.
DR Pfam; PF12264; Waikav_capsid_1; 1.
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 ATP-binding; Capsid protein; Coiled coil; Direct protein sequencing;
KW Helicase; Host membrane; Hydrolase; Membrane; Nucleotide-binding;
KW Nucleotidyltransferase; Protease; Reference proteome;
KW RNA-directed RNA polymerase; Thiol protease; Transferase; Transmembrane;
KW Transmembrane helix; Viral RNA replication; Virion.
FT CHAIN 1..644
FT /note="Putative leader protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041140"
FT CHAIN 645..852
FT /note="Capsid protein 1"
FT /id="PRO_0000041141"
FT CHAIN 853..1055
FT /note="Capsid protein 2"
FT /id="PRO_0000041142"
FT CHAIN 1056..?1366
FT /note="Capsid protein 3"
FT /id="PRO_0000041143"
FT CHAIN ?1367..2526
FT /note="Putative helicase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041144"
FT CHAIN 2527..2852
FT /note="Probable picornain 3C-like protease"
FT /evidence="ECO:0000305"
FT /id="PRO_0000041145"
FT CHAIN 2853..3473
FT /note="Probable RNA-directed RNA polymerase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041146"
FT TRANSMEM 1496..1516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1595..1615
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2363..2383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1751..1917
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 2632..2850
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 3155..3286
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 602..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1278..1306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2394..2415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2438..2465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 514..604
FT /evidence="ECO:0000255"
FT COMPBIAS 609..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1278..1298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2438..2455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2680
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 2717
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 2811
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 1777..1784
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 644..645
FT /note="Cleavage"
FT SITE 852..853
FT /note="Cleavage"
FT SITE 1055..1056
FT /note="Cleavage"
FT SITE 2526..2527
FT /note="Cleavage"
FT /evidence="ECO:0000305"
FT SITE 2852..2853
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT MUTAGEN 2509
FT /note="Q->R: No effect on processing."
FT /evidence="ECO:0000269|PubMed:9683576"
FT MUTAGEN 2526
FT /note="Q->P: Complete loss of processing between putative
FT helicase and picornain 3C-like protease."
FT /evidence="ECO:0000269|PubMed:9683576"
FT MUTAGEN 2680
FT /note="H->G: Severe loss of polyprotein processing."
FT /evidence="ECO:0000269|PubMed:12466496"
FT MUTAGEN 2717
FT /note="E->Q: Complete loss of polyprotein processing."
FT /evidence="ECO:0000269|PubMed:12466496"
FT MUTAGEN 2735
FT /note="D->E: No effect on polyprotein processing."
FT /evidence="ECO:0000269|PubMed:12466496"
FT MUTAGEN 2811
FT /note="C->A: Complete loss of polyprotein processing."
FT /evidence="ECO:0000269|PubMed:12466496"
FT MUTAGEN 2830
FT /note="H->E: Complete loss of polyprotein processing."
FT /evidence="ECO:0000269|PubMed:12466496"
FT MUTAGEN 2852
FT /note="Q->P: Delayed and partial processing between
FT picornain 3C-like protease and RNA-directed RNA
FT polymerase."
FT /evidence="ECO:0000269|PubMed:9683576"
FT MUTAGEN 2885
FT /note="Q->L: No effect on processing."
FT /evidence="ECO:0000269|PubMed:9683576"
SQ SEQUENCE 3473 AA; 390264 MW; F560A352130E7E96 CRC64;
MQSFLLSSKN QAKLLHAGLE FVGGVRCAHQ GWVSGKAVVF CNYCNFAHRL YRFYTKNHCV
LNKELLKISV EGLLCHCIEQ AFLFRRFYDR RFAWQRKYAK GFLFDNLSIP FDDCALCPNA
GTRLSQTGVS HDHFVCNYVE HLFECASFSR ETGGKFFRAC SEGWHWNATC TTCGASCRFA
NPRENIVIAI FMNFLRVMYD GNKYYVSLHC DTEWIPVHPL FARLVLMVRG FAPLDNSHVI
EEDEMDICGH SSEVTYEDPS KFAFTHQHVT RGVGMGHLAF CRDANGVDRG EHKFYLHGPF
DLKMTHAMFR VFMILLNCHG YVQSEFRDEF PDIKDRSLCG LLSVAGLRGV NVSCNEEFIH
LHSQFHNGSF RSQRPIPMVY AEPEMYPPLG YVHLTESWVP RGRLLIDDLP SLMSRVYAES
SQAQAGEIYE ETFDEDDLFE LDGEEGTSTR GLLDLGRRLG GLLLGATKCV KGLHSVIEWP
VDVLTKEAED LGTWLADNKK YVSESTWSCQ VCPEVQDALE KSMREQAKLN AQMISGIKKL
ATTMDSATLK LRDNLKELEQ RISVLEQGAD DTQQVRITNL ENFCEDAAKA FEALRNDIEA
LKKKPAQSVT PLPSPSGNSG TAGEQRPPPR RRRRPPVVEM SEAQAGETVI VGGDEEQEAH
QDSSVAAAGP ADEHNAMLQK IYLGSFKWKV SDGGGSILKT FSLPSDIWAA NDRMKNFLSY
FQYYTCEGMT FTLTITSIGL HGGTLLVAWD ALSSATRRGI VSMIQLSNLP SMTLHASGSS
IGTLTVTSPA IQHQICTSGS EGSLANLGSL VISVANVLCA DSASAQELNV NAWVQFNKPK
LSYWTAQHSI AQSGGFEESQ DLGDLQAIIA TGKWSTTSDK NLMEIIVHPT ACYVSEKLIY
QTNLSVVAHM FAKWSGSMRY TFVFGASMFD RGKIMVSAVP VQFRNSKLTL SQMAAFPSMV
CDLSMETREF TFEVPYISIG KMSLVCKDYL FDISSYNADL VVSRLHVMIL DPLVKTGNAS
NSIGFYVVAG PGKGFKLHQM CGVKSQFAHD VLTAQDFGRS LSCSRLLGNG FKEWCSRESL
LMRVPLKSGK KRAFKYAVTP RMRTLPPEAT SLSWLSQIFV EWRGSLTYTI HVQSGSAIQH
SYMRIWYDPN GKTDEKEVKF LDSAHPPAGI KVYHWDLKIG DSFRFTVPYC ARTEKLQIPK
AYASTPYEWL TMYNGAVTFD LRSGADMELF VSIAGGDDFE MFEQTVPPKC GSVSDSYTVL
SYADDVKSVT EVPNKTTYLA DEQPTTSAPR TSIVNTEDDP PTEGEIARTT NGTLVQYRGG
AWKPMVERTP TMSKKQVGPE LTVSDPQMYK CIKNMNKNVK ILTDRQCTAK LANIVDSAQE
LVGSNSTFVE DLAVGAKQIR KFGESLDVFE GSMSAAKTAE LIDNTHAAFS GPADGSPISN
VVQLLLPMLS SIKGMSGKME SKMASLTAMF QPCKKAITHL IERSFPYLAC KGFKTDKWIW
AALASILVGA ALLHYYRSDL KFVKKWSVMC MIIWAPLLAE KAYHLGTWIK EKFLKSLPRT
RTIKDSCRKH SLAGAFECLA SASCAYIKDN WAKTMSSLLT ILSVVASLVM WGKIPDDKEI
TSFADKFHSI GKKGRSITNI IGGFEKITSV CKKWSETLVS WIVSNVSGGI PKEDLAMTAY
LGFKIHDWVR ETRDMALMEN RFRGFGGDEH LVKVRRLYGH SLKIDNALME KQIVPDMQLS
LIIKECRQKC LELMNESYTY KGMKQSRIDP LHVCMLGAPG VGKSTIAHVV INHLLDHRGE
PEVDRIYTRS CADAYWSNYH QEPVILYDDL GAIKSNLRLS DYAEIMGIKT NDPFSVPMAA
VEDKGKHCTS KYVFSCTNVL NLDDTGDVVT KMAYYRRRNV LVKVERDPDV PKNEANPTEG
LVFTVLGHDQ NCQGDPQFVV KENWDEPFLR EVDTEGWRFE RVEYRTFLRF LCMYTDAYMY
SQEQVLQGIK TFKMNPFAPE PEFAQAQNGE AAECEIVEEM QEVPGEAPQE AKELVKIETA
PNMDELVEAF NKLRVTPGHL NDILRDGSGC YIDEWAIAGP RWLSFHELLP FTCGCHHTRV
CDFNIVYNNM CKAVRSQSVH FKYRANQAIK YAYTHKLHSQ CRYSIDFEKL RECNPLDVFV
CVLSKYTADD HSFERRCPKK MNVVRMQRPP VFELKMRPPS DSVVVEDEQG QRIFEWPHLY
IFLRYRAIEF KDDKGSLTVR EDAGADVCPW NEFLKLPWLD GDQLKSVLPA HLHRMVQARL
EQVEIMEENG NYSGEMRNAI AEIKEYLDQD HQWVAALVLV ACAVKERRRM THDKLHRKSF
NALDKLDAWY TTTAPKTSKK MKILLAIGAS VAVAGVAVGA VILLQKTNLF GSKEDEEIEG
EEGETQASGA HESDGIVTQH LKRDIRPKMR VTYTDHHVAE AHEEKDAEKP RKSGNPTRKS
YLGLSPGFAE RGMGVTYEEH TPLKDALLDE SNKVFRRKIV ASVESAVKQG GKASKDTVLS
QIGDWQDKVK ATGVIAARQL EASGSLKKIH NLNSRRTSSH VMPGLVVHDG AFERSDEVDA
ELHRITIDEV KSCPKMIKEG VSTLSVKKAS VGMLALQKAE SQLSFPFTSR AGVDRDLSMT
NLIDTHMAGM SCIIISELGN VFRTFGVLRL CGTYVCMPAH YLDEITSEHT LYFVCPSKIT
QIQLERHRVC LVNGFQETVV WDLGPSVPPS RNYIDFIANA DDWKNYKATS GALVMSKYSV
DSMLQCVHFL DSIELTEANV SVPTSYYEAN GGIHTIISGL RYRVHCMPGF CGRAIMRADA
TCFRKIIGMH VSGLRNKCMG YAETLTQEHL MQAIETLKET GLLKHIPKGA IGAGEEKLPE
HSKKQSLSLE GKGNLGIVGQ LTAQLVPTSV TKTTICKSMI HGLIGEIKTE PSVLSAWDRR
LPFPPGEWDP MKDAVKKYGS YILPFPTEEI QEVENFLIKK FRRKENSRRT RNVNSLEVGI
NGIDGSDFWS PIEMKTSPGY PYILKRPSGA QGKKYLFEEL EPYPSGRPKY AMKDPELIEN
YERIKEEVTS GVKPSIMTME CLKDERRKLA KIYEKPATRT FTILSPEVNI LFRQYFGDFA
AMVMSTRREH FSQVGINPES MEWSDLINSL LRVNTKGFAG DYSKFDGIGS PAIYHSIVNV
VNAWYNDGEV NARARHSLIS SIVHRDGICG DLILRYSQGM PSGFAMTVIF NSFVNYYFMA
LAWMSTVGSS LLSPQGSCKD FDTYCKIVAY GDDNVVSVHE EFLDVYNLQT VAAYLSHFGV
TYTDGDKNPI HMSKPYEDIT KMSFLKRGFE RVESSGFLWK APLDKTSIEE RLNWIRDCPT
PVEALEQNIE SALHEAAIHG RDYFDDLVRR LNSALTRVML PPTDISFEEC QARWWASVTG
ALRAADYTSL VRRASSGHVE FNKKYRDMFR QQDLPLKEIL MKSKPVALLD LEV
