POL_RTBVP
ID POL_RTBVP Reviewed; 1675 AA.
AC P27502; P27528;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Polyprotein P3;
DE AltName: Full=P194 protein;
DE Contains:
DE RecName: Full=Putative movement protein;
DE Short=MP;
DE Contains:
DE RecName: Full=Capsid protein;
DE AltName: Full=Coat protein;
DE Short=CP;
DE Contains:
DE RecName: Full=Protease;
DE Short=PR;
DE EC=3.4.23.-;
DE Contains:
DE RecName: Full=Reverse transcriptase/Ribonuclease H;
DE Short=RT;
DE EC=2.7.7.49;
DE EC=3.1.26.4;
DE AltName: Full=p55;
DE Flags: Precursor;
OS Rice tungro bacilliform virus (isolate Philippines) (RTBV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Caulimoviridae; Tungrovirus.
OX NCBI_TaxID=10655;
OH NCBI_TaxID=4530; Oryza sativa (Rice).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2041739; DOI=10.1093/nar/19.10.2615;
RA Hay J.M., Jones M.C., Blakebrough M.L., Dasgupta I., Davies J.W., Hull R.;
RT "An analysis of the sequence of an infectious clone of rice tungro
RT bacilliform virus, a plant pararetrovirus.";
RL Nucleic Acids Res. 19:2615-2621(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 503-526.
RX PubMed=1926781; DOI=10.1016/0042-6822(91)90783-8;
RA Qu R.D., Bhattacharyya M., Laco G.S., de Kochko A., Rao B.L.S.,
RA Kaniewska M.B., Elmer J.S., Rochester D.E., Smith C.E., Beachy R.N.;
RT "Characterization of the genome of rice tungro bacilliform virus:
RT comparison with Commelina yellow mottle virus and caulimoviruses.";
RL Virology 185:354-364(1991).
RN [3]
RP FUNCTION OF CAPSID PROTEIN, NUCLEAR LOCALIZATION SIGNAL, AND INTERACTION
RP WITH ORYZA SATIVA IMPORTIN ALPHA-1A.
RX PubMed=15914861; DOI=10.1099/vir.0.80920-0;
RA Guerra-Peraza O., Kirk D., Seltzer V., Veluthambi K., Schmit A.C., Hohn T.,
RA Herzog E.;
RT "Coat proteins of Rice tungro bacilliform virus and Mungbean yellow mosaic
RT virus contain multiple nuclear-localization signals and interact with
RT importin alpha.";
RL J. Gen. Virol. 86:1815-1826(2005).
RN [4]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=15831103; DOI=10.1186/1743-422x-2-33;
RA Marmey P., Rojas-Mendoza A., de Kochko A., Beachy R.N., Fauquet C.M.;
RT "Characterization of the protease domain of Rice tungro bacilliform virus
RT responsible for the processing of the capsid protein from the
RT polyprotein.";
RL Virol. J. 2:33-33(2005).
CC -!- FUNCTION: Capsid protein self assembles to form a bacilliform capsid
CC about 130 nm in length. The capsid encapsulates the genomic dsDNA.
CC Following virus entry into host cell, provides nuclear import of the
CC viral genome. Virus particles do not enter the nucleus, but are
CC targeted to the nuclear membrane through the interaction with host
CC importins (By similarity). {ECO:0000250, ECO:0000269|PubMed:15914861}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- SUBUNIT: Interacts (via nuclear localization signal) with host importin
CC alpha-1a. {ECO:0000269|PubMed:15914861}.
CC -!- SUBCELLULAR LOCATION: [Capsid protein]: Virion. Host nucleus.
CC -!- PTM: Polyprotein P3 is proteolytically cleaved into several chains by
CC viral protease. {ECO:0000269|PubMed:15831103}.
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DR EMBL; X57924; CAA40997.1; -; Genomic_DNA.
DR EMBL; M65026; AAB03094.1; -; Genomic_DNA.
DR PIR; S70770; S70770.
DR RefSeq; NP_056762.1; NC_001914.1.
DR SMR; P27502; -.
DR MEROPS; A03.002; -.
DR GeneID; 1489557; -.
DR KEGG; vg:1489557; -.
DR Proteomes; UP000002246; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046740; P:transport of virus in host, cell to cell; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR034728; Peptidase_A3B.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR041373; RT_RNaseH.
DR InterPro; IPR028919; Viral_movement.
DR Pfam; PF01107; MP; 1.
DR Pfam; PF17917; RT_RNaseH; 1.
DR Pfam; PF00078; RVT_1; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51817; PEPTIDASE_A3B; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Capsid protein; Direct protein sequencing; Endonuclease;
KW Host nucleus; Host-virus interaction; Hydrolase; Metal-binding; Nuclease;
KW Nucleotidyltransferase; Protease; Reference proteome;
KW RNA-directed DNA polymerase; Transferase; Transport;
KW Viral movement protein; Viral penetration into host nucleus; Virion;
KW Virus entry into host cell; Zinc; Zinc-finger.
FT CHAIN 1..?
FT /note="Putative movement protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000316099"
FT CHAIN 477..791
FT /note="Capsid protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026137"
FT PROPEP 792..964
FT /evidence="ECO:0000255"
FT /id="PRO_0000316100"
FT CHAIN 965..1085
FT /note="Protease"
FT /id="PRO_0000316101"
FT PROPEP 1086..1138
FT /evidence="ECO:0000255"
FT /id="PRO_0000316102"
FT CHAIN 1139..1619
FT /note="Reverse transcriptase/Ribonuclease H"
FT /id="PRO_0000316103"
FT PROPEP 1620..1675
FT /evidence="ECO:0000255"
FT /id="PRO_0000316104"
FT DOMAIN 970..1077
FT /note="Peptidase A3B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01160"
FT DOMAIN 1208..1390
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT ZN_FING 772..789
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 479..499
FT /note="Bipartite nuclear localization signal 1"
FT /evidence="ECO:0000255"
FT MOTIF 744..760
FT /note="Bipartite nuclear localization signal 2"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 987
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01160"
FT CONFLICT 1292
FT /note="D -> E (in Ref. 2; AAB03094)"
FT /evidence="ECO:0000305"
FT CONFLICT 1630
FT /note="Y -> H (in Ref. 2; AAB03094)"
FT /evidence="ECO:0000305"
FT CONFLICT 1635
FT /note="S -> P (in Ref. 2; AAB03094)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1675 AA; 194082 MW; B24D7181463E466F CRC64;
MSLRPFTGTS RTITQDSTSE SNIKKGKNST KRELIEEVDV NQEVENFDWK KLSGIKPNKL
YEKNWQEKVK LKQQSIVSAY KEEAISVTHN AYTTTLFPQE VIKNVKNQGK LYYHIGMMAI
GVKGLHRRKI GTKVMIMFYD DSFGKAREAS IGSIEMDMNA GCGVFYSCPD FAKYIKDLSH
LKIGIQTLGY ENYEGKNLSV AIKTIGRLTT NIQSKYKINV KDIVEQISSQ GIIMVAPMEI
DSSHLDGNEW DLSKFLNHEN TSRVPTKALI YQNLQGGESL RFSNYKQTRM HDPTENNSDE
DEDLKILGEQ LNIKMARFYT MQTPEEELRE VIQQLEREKQ AMIAKLEAKM KESSKMAIVE
DNFNPNNEYL EDTYSEYEDL EFEKLGLTGW EDLDQDSIET EEITEWENPN QVLHREIRAY
KSVSEQIEDI FGELLKEHGN YDMALKNLEE KYDLDKIEKA KSIEEIAKSS TSSEIRPTKR
PKEEQTAYED DMRDDWKRKE LTVNPIEASK DRNFERIGSS YKKNFYPSRS EILNLDNVPP
QFYYDQLVTW EGIVKNEWEA RKKDGMDMWS WMDGRITGLV LYLVQDWISK NQAAYNDIKS
RGDRPENFVK MVKDRFLIED PTDERRTALQ RLAQRELEAL NCEDPTKIQP FMAEYLKKAS
EAKKGFDVVY VERLFDRLPE AVGKVVKADF VKDGNSYEAG IGIAVSYIST WMRAKCIKET
EAKTQKKASL AFCRSIYTIG DYKKRKILKR VTNYNKNRRK NYVRRPSIKK KCRCYICQDE
NHLANRCPRR YTNQARASLI DGLDEDIVSI ASDDEDIENF LEIIELDEFI AHSSQEHEHT
WEIGGKKDKV CEICSYFTDY NKTVSCKTCE TQYCKTCSDQ LALEVTEVKK PTKEETMIDD
LKLNVKNLEF RVTILEHKVE MQNLQDKFET MQIRNKSEIT EIPTTSLAMR ANESNYIKTS
INKTAGCYVE TKISFNNENR IITALIDSGS THNIICPTLI PASWINNTHR EIIMFAVDNS
KYNLNQELID DIKLQFQEVD ETFGIKYKLG QTYVAPKPTK TFIIGHRFLT NENGSVTIHK
DYITIQKTTG IYPTARHELK SEFARKHGGR PPLFSNIPET YNKIPHLHSY QPQPILGYKN
EIGNQSLITM VKELEALGFI GDDITKNRTT WVCDFKIINP DINITCATIP YTPADKEVFE
KQIKELLDNK LIKKADPTCR HRTAAFIVRN HSEEVAQKPR IVYNYKRLND NMHTDPFNIP
HKISMINLIQ KANIFSKFDL KAGFHHMKLK DDFKDWTTFT CSEGLYTWNV CPFGIANAPC
AFQRFMQESF GDLKFALLYI DDILIASNNE KEHIEHLKIF FNRVKEVGCV LSKKKSKMFL
KEVEYLGVEI KEGKISLQPH IVDKIKKFDK NKLNTLKGLQ AYLGLLNYAR GYIKDLSKLV
GPLYKKTGKN GQRIFNKEDW NIIFKIEREV SKIKPLERPK ETDYIIIETD ASEEGWGAVL
VCKPDKYSGK DTEKIAGYAS GNFGEKKTWT SLDYEIEAIN EALNKFQIYL DKDFTIRTDC
EAIVKGIKTE DYKKRSKTRW IKLRDNLLKD GYKPTFEHIK GNKNFLPNFL SREGDFILKC
LQNPDSTESY SIDSSESIPL YIDSKESHSI ESDDSIPLYR DKLLPLVERL KEKSA
