ID Q2QR60_ORYSJ Unreviewed; 1470 AA.
AC Q2QR60;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN OrderedLocusNames=LOC_Os12g28690 {ECO:0000313|EMBL:ABA98459.1};
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:ABA98459.1};
RN [1] {ECO:0000313|EMBL:ABA98459.1}
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:ABA98459.1}
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:ABA98459.1}
RP NUCLEOTIDE SEQUENCE.
RA Buell R.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DP000011; ABA98459.1; -; 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; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
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 Pfam; PF00098; zf-CCHC; 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; SSF57756; Retrovirus zinc finger-like domains; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50878; RT_POL; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 291..305
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 566..745
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 1106..1273
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT DOMAIN 1425..1470
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 327..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1470 AA; 168786 MW; 5D4DFB535F5D3C65 CRC64;
MASRRRATTS NDETQTPDLN TLAGIMATQT QLLQAIASNQ GNRGGSSFGE FMRTKPPTFA
TADEPMEAED WLRIIEKKLT LVRVREADKV IFAVNQLEGP AGDWWDTYKE AREDGAGEPT
WEEFTAAFRE NFVPTAVMRM KKNEFRRLRQ GNTTVQEYLN KFTQLARYAI GDLADEEEKI
DKFIEGLNDE LRGPMIGQDH ESFQSLINKV VRLENDQRTV EHNRKRRLAM SRPPQTMPQR
LKGATPSGWK PPVMVTNRPA ALSNFNRPVA LQNRTPTPTL AAPGAKKNVD CFNCGKYGHY
ANNCPHPRKT PVRTGANAMT VRGTTTPAVG RGLFKTPQPN RTTTGFGRGQ VNHVRAEEAQ
EDQGVLMGMF SLNSTPIKVL FDSGALHSFI SLKASQQHNL TRVKLRQPML VHSPGGEIAV
DTACIDVPIR LRDVVFPSNL MVLIPQTLDV ILGMDWLAKH RGVIDCRRRE VTLTTPWGSD
MRATMDQDPR LTERAGGIFT MLPLKGMPVV QRFPDVFPED LPGMPPDRDI EFIIDLIPGT
APISKRPYRM PVNELEELKK QIRELQEKGF VRPSSSPWGA PVLFVKKKDG SMRMCVDYRS
LNEVTIKNKY PLPRIDDLFD QLKGAKVFSK IDLRSGYHQL KIRTEDIPKT AFSTRYGLYE
FTVMSFGLTN APAYFMNLMN KVFMDYLDKF VVVFIDDILI YSKDEEEHAE HLRLVLQKLR
KHKLYAKFSK CEFWLKEVAF LGHVISAGGV AVDPAKVEAV TEWKAPKSVT EIRSFLGLAG
YYRRFIEGFS KIARPMTQLL KKEKKFAWSE QCQGSFEQLK EKLTSAPILV LPDIRKDFVV
YCDASRQGLG GVLMQEGKVV AYASRQLRPH EENYPTHDLE LAAVVHALKI WRHYLIGNHC
DIYTDHKSLK YIFTQSDLNL RQRRWLELIK DYDLEVHYHP GKANVVADAL SRKSHCNHLR
TEGMVPELRE EMAQLNLHIV PHGQINTLDI QPLLRTQIEE AQKDNEEVRE VKERLAAGRA
KEFSTDEKDV LWYKKRIYVP EQGGLRGLIL KEAHESAYSL HPGSTKMYQD LKEGYWWPNM
KRDVAEYVAL CDVCQKVKAE HQRPAGLLQP LRIPEWKWDE IGMDFIVGLP KTATGYDSIW
VIVDRLTKTA RFIPVKTNYS SAKLAELYMT RIVCLHGIPK KIISDRGTQF TSHFWEKVHE
ALGSYLAFST AYHPQTDGQT ERTNQVLEDM LRACALDFSK DWERCLPYAE FSYNNSFQAS
LKMSPNEALF GRRCRTPLMW SETGERAVFG PDIIQEAEEK VRLIRDRLKV AQSRQKSYAD
TRRRNLEFKE GDYVYLKVSP MRGTKRFKVK GKLAPRYVGP FQIIARRGEV AYQLQLPEYI
ADVHPVFHVS QLKKCLRVPE EQAPLEEIHI SNDLTYPEHP IRILDEAEKR TRSKVWRMYK
VQWSNHTEDE ATWEGEEFLR TEYPHLFGNW
//