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Database: UniProt
Entry: Q94HT9_ORYSJ
LinkDB: Q94HT9_ORYSJ
Original site: Q94HT9_ORYSJ 
ID   Q94HT9_ORYSJ            Unreviewed;      1714 AA.
AC   Q94HT9; Q7XG10;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 132.
DE   RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE            EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN   OrderedLocusNames=LOC_Os10g16720 {ECO:0000313|EMBL:AAP52863.1};
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:AAP52863.1};
RN   [1] {ECO:0000313|EMBL:AAP52863.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12791992; DOI=10.1126/science.1083523;
RG   Rice Chromosome 10 Sequencing Consortium;
RT   "In-depth view of structure, activity, and evolution of rice chromosome
RT   10.";
RL   Science 300:1566-1569(2003).
RN   [2] {ECO:0000313|EMBL:AAP52863.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Buell C.R., Wing R.A., McCombie W.R., Messing J., Yuan Q., Ouyang S.;
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:AAP52863.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Buell R.;
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; DP000086; AAP52863.1; -; Genomic_DNA.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; 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; IPR001969; Aspartic_peptidase_AS.
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; PF00665; rve; 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; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS50878; RT_POL; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          548..563
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          801..980
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   DOMAIN          1345..1508
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   REGION          117..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          450..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          89..116
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        140..164
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        474..516
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1714 AA;  194669 MW;  168C0139B37AF1E0 CRC64;
     MAVEASGGTA DHACQEAAYL MMARIRERHD YIFHDTAYRY HPRRAHGDGV SSFRPTAGEN
     DTTFGHMCAV IRGLDRMHSD LHKATKALND GKLMRIVALK DEIARLKKEN AQLKGLPAPG
     GVRIRTTPRK TTTAPVRIQL APRNPPPPAA PAAPSVPPAV PAAPAPAPAF TLSFAPASAA
     RGSASGTGGC LFGMVYTRNG SRATGEGSNG EERADGVHPN SDSGNGPPPL PENPTLAQVM
     AHQTQMIAAM MQQMQQQHQQ MHQRMMQHAE QQHQQFGPPP PQSKLPEFLR VRPPTFSSTT
     NPMEANDWLH AIEKKLNLLQ CNDQEKVAFA THQLQGPASA WWDNHMATRP PGTEVTWAEF
     CRSFRKAQVP DGVVAQKKRE FRALHQGNRT VTEYLHEFNR LARYAPEDVR TDAEKQEKFM
     AGLDDELTNQ LISGDYADFE RLVDKAIRQE DQRNKMDRKR KAAQFRAHQG SHQRPRFTPG
     QQGGPTTMIV RQHRPFNPSN FHQGTSGSQN HHGSQPNRGA APRPSVAPAQ SGQPAQAKKE
     TGAKPGSCFN CGELGHFADK CPKPRRAGPR FIQARVNHAS AEEAQAAPEV VLGTFPVNSI
     PATVLFDSGA THSFISKKFV GMHGLIREEL STPMRVHTPG NSSTSVQFSP SITIEIQRSP
     FLANLILLES KDLDVILGMD WLTKFKGVID CASRTVTLTN EKGETVVYKS LVSPKKGVSL
     NQIETEIPVD TVEKNLRKLE DIPIVCEYPE VFPEDLTTMP PKREIEFRID LAPGTAPIYK
     RPYRMAANEL AEVKKQVDEQ LQKGYIRPST SPWGAPVIFV EKKDKTKRMC VDYRALNEVT
     IKNKYPLPRI DDLFDQLKGA KVFSKIDLRS GYHQLRIREE DIPKTAFTTR YGLYECTVMS
     FGLTNAPAFF MNLMNKVFME FLDKFVVVFI DDILIYSKSE EEHEQHLRLV LEKLKEHQLY
     AKFSKCDFWL TEVKFLGHVI TAQGVAVDPS NVESVTKWTP PKTVSQIRSF LGLAGYYRRF
     IENFSRIARP MTQLLKKDEK FKWTAECDKS FEELKKKLVS APVLILPDPT KDFQVYCDAS
     RHGLGCVLMQ EGRVVAYASR QLRPHEGNYP THDLELAAVV HALKIWRHYL IGNRCEVYTD
     HKSLKYIFTQ PDLNLRQRRW LELIKDYDMS IHYHPGKANV VADALSRKSY CTALCVEGMC
     EELRQEFEHL NVGIVEHGFV AALEARPTLV DQVRAAQVND SEIAELKKNM RVGKARDFHE
     DEHGTIWMGE RLCVPNDKEL KDLILTEAHQ TQYSIHPGST KMYQDLKEKF WWVSMRREIA
     EFVALCDVCQ RVKAEHQRPA GLLQPLQIPE WKWEEIGMDF ITGLPRTSLG HDSIWVVVDR
     LTKVAHFIPV HTTYTGKRLA ELYLARIMCL HGVPKKIVSD RGSQFTSKFW QKLQEELGTR
     LNFSTAYHPQ TDGQTERVNQ ILEDMLRACA LDFGGAWDKS LPYAEFSYNN SYQASLQMAP
     FEALYGRKCR TPLFWDQTGE RQLFGTEVLA EAEEKVRIIR ERLRIAQSRQ KSYADNRRRE
     LTFEAGDYVY LRVTPLRGVH RFQTKGKLAP RFVGPYKILE RRGEVAYQLE LPSNMIGIHD
     VFHVSQLKKC LRVPEEQADS EHIDIQEDLT YVEKPVRILD TSERRTRNKV TRFCRVQWSH
     HSEEEATWER EDELKAAHPH LFTSSSESRG RDSV
//
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