POLG_RTSVT
ID POLG_RTSVT Reviewed; 3471 AA.
AC Q91PP5;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
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 Vt6) (RTSV) (Rice tungro spherical
OS waikavirus).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Picornavirales; Secoviridae; Waikavirus.
OX NCBI_TaxID=337080;
OH NCBI_TaxID=4530; Oryza sativa (Rice).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=10766310; DOI=10.1023/a:1008116408733;
RA Isogai M., Cabauatan P.Q., Masuta C., Uyeda I., Azzam O.;
RT "Complete nucleotide sequence of the rice tungro spherical virus genome of
RT the highly virulent strain Vt6.";
RL Virus Genes 20:79-85(2000).
RN [2]
RP PROTEOLYTIC PROCESSING OF PICORNAIN 3C-LIKE PROTEASE, AND MUTAGENESIS OF
RP CYS-2763.
RX PubMed=15503215; DOI=10.1007/s00705-004-0421-9;
RA Sekiguchi H., Isogai M., Masuta C., Uyeda I.;
RT "3C-like protease encoded by Rice tungro spherical virus is
RT autocatalytically processed.";
RL Arch. Virol. 150:595-601(2005).
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 (By similarity). Picornain 3C-like protease is
CC autocatalytically processed. {ECO:0000250,
CC ECO:0000269|PubMed:15503215}.
CC -!- MISCELLANEOUS: The Vt6 strain is a highly virulent strain.
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DR EMBL; AB064963; BAB61927.1; -; Genomic_RNA.
DR MEROPS; C03.024; -.
DR Proteomes; UP000007184; 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; Helicase; Host membrane;
KW Hydrolase; Membrane; Nucleotide-binding; Nucleotidyltransferase; Protease;
KW RNA-directed RNA polymerase; Thiol protease; Transferase; Transmembrane;
KW Transmembrane helix; Viral RNA replication; Virion.
FT CHAIN 1..641
FT /note="Putative leader protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041147"
FT CHAIN 642..849
FT /note="Capsid protein 1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041148"
FT CHAIN 850..1052
FT /note="Capsid protein 2"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041149"
FT CHAIN 1053..?1367
FT /note="Capsid protein 3"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041150"
FT CHAIN ?1368..2523
FT /note="Putative helicase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000041151"
FT CHAIN 2524..?2849
FT /note="Probable picornain 3C-like protease"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041152"
FT CHAIN ?2850..3471
FT /note="Probable RNA-directed RNA polymerase"
FT /evidence="ECO:0000250"
FT /id="PRO_0000041153"
FT TRANSMEM 1493..1513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1592..1612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 2360..2380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1748..1914
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT DOMAIN 2629..2847
FT /note="Peptidase C3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT DOMAIN 3152..3283
FT /note="RdRp catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00539"
FT REGION 603..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2391..2411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2435..2460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 513..603
FT /evidence="ECO:0000255"
FT COMPBIAS 608..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2435..2452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2677
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 2714
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT ACT_SITE 2808
FT /note="For picornain 3C-like protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01222"
FT BINDING 1774..1781
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT SITE 641..642
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 849..850
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 1052..1053
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT SITE 2523..2524
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT MUTAGEN 2763
FT /note="C->W: Complete loss of cleavage between 3C-like
FT protease and RNA-directed RNA polymerase."
FT /evidence="ECO:0000269|PubMed:15503215"
SQ SEQUENCE 3471 AA; 389212 MW; 82B008325F931FB3 CRC64;
MQSFLLSSKN QAKLLHAGLE FVGGVRCAHQ GWVSGKAVVF CNYCNFAHRL YRFYTKNHCV
LNKETIENLC GRSFVSLYRA GLLLDDFTID DLLGKGKYAK GSIDNLSIPF DDCALCPNAG
TRLSQTGVSH DHFVCNYVEH LFECASFSRE TGGKFIRACS KGWHWNATCT TCGASCRFAN
PRENVVIAIF MNFLRVMYDG NKYYVSLHCD TEWIPVHPLF ARLVLMVRGF APLDNSHVIE
EDEMDICGHP SEVTYDDPSN YAFSHQHVTR GVGMGHLAFC RDANGVDRGE HKFYLHGPFD
LKMTHAMFRV FMILLNCHGY VQSEFREEHP AVKDRSLCAL LSVAGLRGVN IACNEEFIHL
HSQFHNGSFR SQRPIPMVYA EPEMYPPLEY VRLTESWVPR GRVMIDDLPS LLSRVYAESS
QPHAGEIYEE IFDEDDLFEL GDDEGTSTRG LLDLGRRLGG LLLGATKCVK GLHAVIEWPV
DVLTKEAEDL GTWLADNKKY VSESTWSCQV CPEVQDALEK SMREQAKLNA QVIGGIKKLA
TTMDSATSKL KDSLKELERR ISVLEQGVDE TQQARITNLE NFCEDAAKAF DALRADIDAL
KKKPAQSVTP LPSPSGNSGT AGEQRPPPRR RPPVVEMSEA QAGETVIVGG DEEQEAHQDS
SVAAAGPTDE HNAMLQKIYL GSFKWKVSDG GGSILKTFSL PSDIWAANDR MKNFLSYFQY
YTCEGMTFTL TITSIGLHGG TLLVAWDALS SATRRGIVSM IQLSNLPSMT LHASGSSIGT
LTVTSPAIQH QICTSGSEGS IANLGSLVIS VANVLCADSA SAQELNVNAW VQFDKPKLSY
WTAQHTIAQS GGFEESQDLG DLQAIIATGK WSTTSDKNLM EIIVHPTACY VSEKLIYQTN
LSVVAHMFAK WSGSMKYTFV FGASMFDRGK IMVSAVPVQF RNSKLTLSQM AAFPSMVCDL
SVETREFTFE VPYISIGKMS LVCKDYLFDI SSYNADLVVS RLHVMILDPL VKTGNASNSI
GFYVVAGPGK DFKLHQMCGV KSQFAHDVLT AQDFGRSLSC SRLLGNGFKE WCSRESLLMR
IPLKNGKKRA FKYAVTPRMR TLPPEATSLS WLSQIFVEWR GSLTYTIHVQ SGSAIQHSYM
RIWYDPNGKT DEKEIKFLDS AHPPAGIKVY HWDLKIGDSF RFTVPYCART EKLQIPKAYA
STPYEWLTMY NGAVTIDLRS GADMELFVSI AGGDDFEMFE QTVPPKCGSV SDSYTVLSYA
DDIKSVTEVP NKTTYLADEQ PTTSAPRTST VDTEEDPPTE GEIARTSNGT LVQYRGGAWK
PMVERTPTMS KKQVGPELVA SDSHMYKCIK NMNKNVKILT DRQCTAKLAD IVDSTQGLVG
SNSTFVEDLA VGAKQIRKFG ESLEVFEGSM SAAKTAELID NTHAAFSGPA DGSPISNVVQ
LLLPMLSSIK GMSGKMESKM ASLTAMFQPC KKAITHLIER SFPYLACKGF KTDKWIWAAL
ASILVGAALL HYYRSDLKFV KKWSVMCMII WAPLLAEKAY HLGTWIKEKF LKSLPRTRTI
KDSCRKHSLA GAFECLASAS CAYIKDNWAK TMSSLLTILS VVASLVMWGK IPDDKEITSF
ADKFHSIGKK GRSITNIIGG FEKITSVCKK WSETLVGWIV SNVSGGIPKE DLAMTAYLGF
KIHDWVRETR DMALMENRFQ GFGGDEHLVR VRRLYGHSLK IDNALMEKQI VPDMQLSLII
KECRQKCLEL MNESYTYKGM KQSRIDPLHV CMLGAPGVGK STIAHVVINN LLDHRGEPEV
DRIYTRCCAD AYWSNYHQEP VILYDDLGAI KSNLRLSDYA EIMGIKTNDP FSVPMAAVED
KGKHCTSKYV FSCTNVLNLD DTGDVVTKMA YYRRRNVLVK VERDPDVPKN EANPTEGLVF
TVLGHDQNCQ GDPQFVVKEN WDEPFLREVD TEGWRFERVE YRTFLRFLCM YTDAYMYSQE
QVLQGIKTFK MNPFAPEPEF AQAQSGEAAE CEIVEETQEI PGEAPQEVKE LAKIETAPNM
DELVEAFNKL RVTPGHLNEI LRDGSGCYID EWAIAGPRWL SFHELLPFTC GCHHTRVCDF
NIVYNNMCKA VRSQSVHFKY RANQAIKYAY THKLHSQCRY SIDFEKLREC NPLDVFVCVL
SKYTADDHSF ERRCPKKMNV VRMQRPPVFE LKMRPPSDSV VVEDDQGQRA FEWPHLYTFL
RYRAIEFKDD KGSLTVREDA SADVCPWNEF LKLPWLDGDQ LKSVLPAHLH RMVQARLEQV
EIMEENGNYS GEMRNAIAEI KEYLDQDHQW VAALVLVACA VKERRKMTHD KLHRKSFNAL
DRLDKWYTTT APKTSKKMKI LLAIGASVAV AGVAVGAVIL LQKTNLFGSK EDEEIEGEEG
ETQASGAHES DGIVTQHLKR DIRPKMRVTY TDHHVAEAHE EKSTEKPRKP GNPTRKNFLG
LSPGFAERGM GVTYEEHTPL KDALLDESNK VFRRKIVASV ESAVKQGGKA SKDSVLSQIS
EWQDKVRATG VIAARQLEAS GSLKKIHNLN SRRTSSHVMP GLVVHDGTFE RSDEVDAELH
RITIDEVKSC PKMIKEGVST LSVKKASVGV LALQKAESQL SFPFTSRAGV DRDLSMTNLI
DTHMAGMSCI IISELGNVFR TFGVLRLCGT YVCMPAHYLD EITSEHTLYF VCPSKITQIQ
LERHRVCLVN GFQETVVWDL GPSVPPSRNY IDFTAKADDW KNYKATSGAL VMSKYLVDSM
LQCVHFLDSI ELTEANVSVP TSYYEANGGI HTIISGLRYR VHCMPGFCGA AIMRADATCY
RKIIGMHVSG LRNKCMGYAE TLTQEHLMRA IETLKETGLL KHIPRGAIGA GEEKLPEHSK
KQSLSLEGKG NLGIVGQLPA QLVPTSVTKT TICKSMIHGL IGEIKTEPSV LSAWDRRLPF
PPGEWDPMKD AVKKYGSYIL PFPTEEIQEV ENFLIKKFRR KENSRRTRNV NSLEVGINGI
DGSDFWSPIE MKTSPGYPYI LKRPSGAQGK KYLFEELEPY PSGRPKYAMK DPELIENYER
IKEEVTSGVK PSIMTMECLK DERRKLAKIY EKPATRTFTI LSPEVNILFR QYFGDFAAMV
MSTRREHFSQ VGINPESMEW SDLINSLLRV NTKGFAGDYS KFDGIGSPAI YHSIVNVVNA
WYDDGEVNAR ARHSLISSIV HRDGICGDLI LRYSQGMPSG FAMTVIFNSF VNYYFMALAW
MSTVGSSLLS PQGSCKDFDT YCKIVAYGDD NVVSVHEEFL DVYNLQTVAA YLSHFGVTYT
DGDKNPIHMS KPYEDITKMS FLKRGFERVE SSGFLWKAPL DKTSIEERLN WIRDCPTPVE
ALEQNIESAL HEAAIHGRDY FDDLVQRLNS ALKRVMLPPT DISFEECQAR WWASVTGDAL
RAADYSSLVR RASSGHVEFN KKYRDMFRQQ DLPLKEILMK SKPVALLDLE V
