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Database: UniProt
Entry: C5NNT6_ORYSI
LinkDB: C5NNT6_ORYSI
Original site: C5NNT6_ORYSI 
ID   C5NNT6_ORYSI            Unreviewed;      1727 AA.
AC   C5NNT6;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE            EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN   Name=OsPupK36-1 {ECO:0000313|EMBL:BAH80025.1};
OS   Oryza sativa subsp. indica (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=39946 {ECO:0000313|EMBL:BAH80025.1};
RN   [1] {ECO:0000313|EMBL:BAH80025.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=19422603; DOI=10.1111/j.1467-7652.2009.00415.x;
RA   Heuer S., Lu X., Chin J.H., Pariasca-Tanaka J., Kanamori H., Matsumoto T.,
RA   De Leon T., Ulat V.J., Ismail A.M., Yano M., Wissuwa M.;
RT   "Comparative sequence analyses of the major quantitative trait locus
RT   phosphorus uptake 1 (Pup1) reveal a complex genetic structure.";
RL   Plant Biotechnol. J. 7:456-457(2009).
RN   [2] {ECO:0000313|EMBL:BAH80025.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21602323; DOI=10.1104/pp.111.175471;
RA   Chin J.H., Gamuyao R., Dalid C., Bustamam M., Prasetiyono J.,
RA   Moeljopawiro S., Wissuwa M., Heuer S.;
RT   "Developing rice with high yield under phosphorus deficiency: Pup1 sequence
RT   to application.";
RL   Plant Physiol. 156:1202-1216(2011).
RN   [3] {ECO:0000313|EMBL:BAH80025.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22914168; DOI=10.1038/nature11346;
RA   Gamuyao R., Chin J.H., Pariasca-Tanaka J., Pesaresi P., Catausan S.,
RA   Dalid C., Slamet-Loedin I., Tecson-Mendoza E.M., Wissuwa M., Heuer S.;
RT   "The protein kinase Pstol1 from traditional rice confers tolerance of
RT   phosphorus deficiency.";
RL   Nature 488:535-539(2012).
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DR   EMBL; AB458444; BAH80025.1; -; 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; 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   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          566..581
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          814..993
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   DOMAIN          1358..1521
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   REGION          478..540
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1696..1727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..540
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1696..1711
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1712..1727
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1727 AA;  197239 MW;  94050DB296ECE6AB CRC64;
     MGVAGESMPL VVEGVIMIQE RCTVMPPHSP RNLIEVLGFV RELRLMAFEV GYEVAPEYRQ
     IPHDPDEEKC RVRVTLASDS EDLPSFKFEA GGRSYCHACQ EVALVAIGEL RQHFEEELDS
     SAFRYHPHKP HGQDYGSYTC PDGEESATLM HVVHMLNAMD TVGVEREKAA HDRENWNRGQ
     ICKLKSKVHR LQKELAELKG EAPPPTSKLR LTARKRTYPP PRLQLASNIR VMGEVVPDRA
     EPVIDIMVNT RTGTGSGSGS GANNNEGEPT LAQILAQQTQ LINLLVQQAQ NQQGNNQNQN
     PPPPPQNKLA DFLRVRPPTF SSTTNPVEAG DWLHAVEKKL DLIQCTEQEK VSFASHQLHG
     PAAEWWDHFR QGRAGGEPIT WQEFTAAFKK THIPTGVVAL KKREFRALSQ GSRSVTEYLH
     DFNRLARYAP EDVRTDEERQ EKFLEGLNDE LSYTLMSTEF RDFQQLVDKA IRQEDKYNRM
     EQKKRRAAQF KAQQGSNQRP RLITGPQVPS YPQGGSSSVV RPQRQFYNNN TGNRGNDNRN
     VVARPAATST QNQSVRKDQG SKPVICFNCG DPGHYADKCP KPRRVKNAPV PNNSNASAPK
     ARVNHVAAAE AQNAPDVVLG TFPVNSIPAT VLFDSGATHS FLSKSFATKH GMEVVSLGRP
     LLVNTPGNQV SSTRYCPSVT IEIEEVLFPS SLILLESKDL DVILGMDWLS RHRGVIDCAN
     RKVTLTNSNG ETVSFFASSP KSHGVVLNQV ALQEIPIVQD YPDVFPEDLP GMPPKRDIEF
     RIDLVPGTNP IHKRPYRMAA NELAEVKKQV DDLLQKGYIR PSTSPWGAPV IFVEKKDHTQ
     RMCVDYRALN EVTIKNKYPL PRIDDLFDQL EGATVFSKID LRSGYHQLRI REEDIPKTAF
     TTRYGLFECT VMSFGLTNAP AFFMNLMNKV FMEYLDKFVV VFIDDILIYS KTKEEHEEHL
     RLALEKLREH QLYAKFSKCE FWLSEVKFLG HVISSGGVAV DPSNVESVLS WKQPKTVSEV
     RSFLGLAGYY RRFIENFSKI ARPMTRLLQK DGKYKWTEDC ERSFQELKKR LVSAPVLILP
     DSRKDFQVYC DASRHGLGCV LMQEGKVVAY ASRQLRPHEN NYPTHDLELA AVVHALKIWR
     HYLYGNRTEI YTDHKSLKYI FTQPDLNMRQ RRWLELIKDY DMEIHYHPGK ANVVADALSR
     KSYCNMSEGR CLPWELCQEF EKLNLGIVSK GFVATLEAKP TLFDQIREAQ VNDPDIQEIK
     KNMRRGKAIG FVEDERGTVW LGERICVPEN KELKDTIMKE AHETLYSIHP GSTKMYQDLK
     QQFWWASMRR EIAEYVALCD VCQRVKAEHQ RPAGLLQPLK IPEWKWEEIG MDFITGLPRT
     SAGHDSIWVV VDRLTKVAHF IPVKTTYTGH KLAELYMARV VCLHGVPKKI VSDRGSQFTS
     KFWQKLQSEL GTRLNFSTAY HPQTDGQTER VNQILEDMLR ACVLDFGGSW DKNLPYPEFS
     YNNSYQASLQ MSPNEALYGR KCRTPLLWDQ IGERQVFGTD ILREAEEKVK IIQQRLRVAQ
     SRQKSYADNR RRDLTFEEGD YVYLRVTPLR GVHRFQTKGK LAPRFVGPFK IVSRRGEVAY
     QLELPPSMAG IHDVFHVSQL KKCLRVPTEE ADPDRIELQE DLTYVEKPVR ILEVSERKTR
     NRVIRFCKVQ WSNHSEEEAT WEREDELKSA HPHLFSSSSE SRGRDSV
//
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