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Database: UniProt
Entry: Q2QST6_ORYSJ
LinkDB: Q2QST6_ORYSJ
Original site: Q2QST6_ORYSJ 
ID   Q2QST6_ORYSJ            Unreviewed;      1753 AA.
AC   Q2QST6;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE            EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN   OrderedLocusNames=LOC_Os12g22990 {ECO:0000313|EMBL:ABA97603.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947 {ECO:0000313|EMBL:ABA97603.1};
RN   [1] {ECO:0000313|EMBL:ABA97603.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
RN   [2] {ECO:0000313|EMBL:ABA97603.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Buell C.R., Wing R.A., McCombie W.A., Ouyang S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ABA97603.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Buell R.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; DP000011; ABA97603.1; -; Genomic_DNA.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR   CDD; cd00303; retropepsin_like; 1.
DR   CDD; cd09274; RNase_HI_RT_Ty3; 1.
DR   CDD; cd01647; RT_LTR; 1.
DR   Gene3D; 1.10.340.70; -; 1.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR041588; Integrase_H2C2.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR005162; Retrotrans_gag_dom.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR000477; RT_dom.
DR   InterPro; IPR041373; RT_RNaseH.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR45835:SF87; RNA-DIRECTED DNA POLYMERASE; 1.
DR   PANTHER; PTHR45835; YALI0A06105P; 1.
DR   Pfam; PF17921; Integrase_H2C2; 1.
DR   Pfam; PF03732; Retrotrans_gag; 1.
DR   Pfam; PF17917; RT_RNaseH; 1.
DR   Pfam; PF08284; RVP_2; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS50878; RT_POL; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..1753
FT                   /note="RNA-directed DNA polymerase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004214401"
FT   DOMAIN          590..605
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          840..1019
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   DOMAIN          1380..1547
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   REGION          248..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..584
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          601..624
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          216..243
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        249..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..289
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..544
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..568
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1753 AA;  198953 MW;  85B07F01C7097BA4 CRC64;
     MSWHRAGVLL LGAQSCLPVP GVLAVGGIGS VLLSMARMGW KLCHVFRLYT VVMAGSVTRR
     GLDMTGFVLE LRGMCVVLGY PHGVDYQGRP LPEQEGDDAE PHAAWEVTAV ILVGSPERTS
     LAVTAGGDSF PAACQSAALL AIGTLHQRYP DELQHSPYRY HPRRGGARDY ATFRDASSED
     DATIVHLARM VEAYDAARID FHQMVRRGMV ENNMKILELR QENLQLKKDL DAVEAQLHQL
     KIAQGEMVTT RRNAATGDGN QPEGSNHNNH QGNPPPPPPP PPPPPPDTNA ILTQILAQQA
     NMMTAFLHHL QNPPQHNAPP PPPQHSKLAE FLRIRPPTFS SSNNPVDALD WLHAVGKKLD
     TVQCSDEEKV IFAAHQLQGP ASLWWDHFQA TQPEGQPITW ARFTAAFQRT HVPAGVVALK
     KREFRELKQG NCSVMEYLHE FNNLARYAPE DVREDEEKQE KFLAGMDPEL SVRLVSGDYP
     DFQRLVDKSI RLEAKHKELE SHKRRLANFR NQQGANQRVR YTNPYPGGSS SQQQQQQQQP
     RSAPRPQFVV RVPQPQQQQN QQGTRAPRPP TPAVQPGQGR RDAQGQQRLC FNCFEPGHFA
     DKCPKPRRQQ GQAPPRSNNG GKDVIRGRVN HVTAEDVLTT PDVIVGTFLI HSIPATILFN
     SGASHSFISV PFVGRNQLGV ERLRNPLLIT TPGGVMTAKY YSPAVPIEIQ GIPFPSDLIL
     LDTKNLNVIL GMNWLAQFQG VVDCARRTVT LYRGPEQPVV FFAPPTSVSS SELHQIGLSE
     IPIVREFGDV FPEELPGMPP KREIEFWIDL APGTTPLYKR PYRMAANELA EVKKQLEELK
     EKGYIRPSTS PWGAPVIFVE KKDKTKRMCV DYRALNEVTI KNKYPLPRID DLFDQLKGAT
     VFSKIDLRSG YHQLRIREED IPKTAFTTRY GLYEFTVMSF GLTNAPAFFM NLMNKVFMEY
     LDKFVVVFID DILIYSQSEE DHQHHLRLVL GKLREHQLYA KLSKCEFWLS EVKFLGHVIS
     AKGVAVDPET VTAVTDWKQP KTVTQVRSFL GLAGYYRRFI ENFSKIARPM TQLLKKEEKF
     VWSPQCEKAF KTLKEKLVAS PVLILPDTRK DFMVYCDASR QGLGCVLMQD GHVVAYASRQ
     LRPHEGNYPT HDLELAAVVH ALKIWRHYLI GNRCEIYTDH KSLKYIFTQS DLNLRQRRWL
     ELIKDHDVGI HYHPGKANVV ADALSRKSHC NTLNVRGIPP ELSQQMAALN LSIVSRGFLA
     ALEAKPTLLD QIREAQKNDP DMHGLLKNMK QGKAAGFTED EHGTLWNGNR VCVPDNRELK
     QLILQEAHES PYSIHPGSTK MYLDLKEKYW WVSMKREIAE FVALCDVCQR VKAEHQRPAG
     LLQPLQVPEW KWDEIGMDFI TGLPKTQGGY DSIWVVVDRL TKVARFIPVK TTYGGNKLAE
     LYFARIVSLH GVPKKIVSDR GSQFTSHFWK KLQEELGTRL NFSTAYHPQT DGQTERLNQI
     LEDMLRACVL DFGKTWDKSL PYAEFSYNNS YQASIQMAPY EALYGRKCRT PLLWDQVGES
     QVFGTDILRE AEAKVRTIRD NLKVAQSRQK SYADNRRRDL EFAVDDFVYL RVTPLRGVHR
     FQTKGKLAPR YVGPFRIVAR RGEVAYQLEL PASLGNVHDV FHVSQLKKCL RVPSEQADSK
     QIEVREDLTY VERPVKILDT MERRTRNRVI RFCKVQWSNH AEEEATWERE DELKAAHPDL
     FASSSESRGR DSV
//
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