ID Q7XNK8_ORYSJ Unreviewed; 1680 AA.
AC Q7XNK8;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2004, sequence version 2.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN Name=OSJNBb0062B06.9 {ECO:0000313|EMBL:CAE04051.2};
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:CAE04051.2, ECO:0000313|Proteomes:UP000000763};
RN [1] {ECO:0000313|Proteomes:UP000000763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763};
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RA Matsumoto T., Wu J., Kanamori H., Katayose Y., Fujisawa M., Namiki N.,
RA Mizuno H., Yamamoto K., Antonio B.A., Baba T., Sakata K., Nagamura Y.,
RA Aoki H., Arikawa K., Arita K., Bito T., Chiden Y., Fujitsuka N.,
RA Fukunaka R., Hamada M., Harada C., Hayashi A., Hijishita S., Honda M.,
RA Hosokawa S., Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M.,
RA Ito K., Ito S., Ito T., Ito Y., Ito Y., Iwabuchi A., Kamiya K.,
RA Karasawa W., Kurita K., Katagiri S., Kikuta A., Kobayashi H., Kobayashi N.,
RA Machita K., Maehara T., Masukawa M., Mizubayashi T., Mukai Y., Nagasaki H.,
RA Nagata Y., Naito S., Nakashima M., Nakama Y., Nakamichi Y., Nakamura M.,
RA Meguro A., Negishi M., Ohta I., Ohta T., Okamoto M., Ono N., Saji S.,
RA Sakaguchi M., Sakai K., Shibata M., Shimokawa T., Song J., Takazaki Y.,
RA Terasawa K., Tsugane M., Tsuji K., Ueda S., Waki K., Yamagata H.,
RA Yamamoto M., Yamamoto S., Yamane H., Yoshiki S., Yoshihara R., Yukawa K.,
RA Zhong H., Yano M., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Bera J., Fadrosh D., Jin S., Johri S., Kim M.,
RA Overton L., Reardon M., Tsitrin T., Vuong H., Weaver B., Ciecko A.,
RA Tallon L., Jackson J., Pai G., Aken S.V., Utterback T., Reidmuller S.,
RA Feldblyum T., Hsiao J., Zismann V., Iobst S., de Vazeille A.R., Buell C.R.,
RA Ying K., Li Y., Lu T., Huang Y., Zhao Q., Feng Q., Zhang L., Zhu J.,
RA Weng Q., Mu J., Lu Y., Fan D., Liu Y., Guan J., Zhang Y., Yu S., Liu X.,
RA Zhang Y., Hong G., Han B., Choisne N., Demange N., Orjeda G., Samain S.,
RA Cattolico L., Pelletier E., Couloux A., Segurens B., Wincker P., D'Hont A.,
RA Scarpelli C., Weissenbach J., Salanoubat M., Quetier F., Yu Y., Kim H.R.,
RA Rambo T., Currie J., Collura K., Luo M., Yang T., Ammiraju J.S.S.,
RA Engler F., Soderlund C., Wing R.A., Palmer L.E., de la Bastide M.,
RA Spiegel L., Nascimento L., Zutavern T., O'Shaughnessy A., Dike S.,
RA Dedhia N., Preston R., Balija V., McCombie W.R., Chow T., Chen H.,
RA Chung M., Chen C., Shaw J., Wu H., Hsiao K., Chao Y., Chu M., Cheng C.,
RA Hour A., Lee P., Lin S., Lin Y., Liou J., Liu S., Hsing Y., Raghuvanshi S.,
RA Mohanty A., Bharti A.K., Gaur A., Gupta V., Kumar D., Ravi V., Vij S.,
RA Kapur A., Khurana P., Khurana P., Khurana J.P., Tyagi A.K., Gaikwad K.,
RA Singh A., Dalal V., Srivastava S., Dixit A., Pal A.K., Ghazi I.A.,
RA Yadav M., Pandit A., Bhargava A., Sureshbabu K., Batra K., Sharma T.R.,
RA Mohapatra T., Singh N.K., Messing J., Nelson A.B., Fuks G., Kavchok S.,
RA Keizer G., Linton E., Llaca V., Song R., Tanyolac B., Young S., Ho-Il K.,
RA Hahn J.H., Sangsakoo G., Vanavichit A., de Mattos Luiz.A.T., Zimmer P.D.,
RA Malone G., Dellagostin O., de Oliveira A.C., Bevan M., Bancroft I.,
RA Minx P., Cordum H., Wilson R., Cheng Z., Jin W., Jiang J., Leong S.A.,
RA Iwama H., Gojobori T., Itoh T., Niimura Y., Fujii Y., Habara T., Sakai H.,
RA Sato Y., Wilson G., Kumar K., McCouch S., Juretic N., Hoen D., Wright S.,
RA Bruskiewich R., Bureau T., Miyao A., Hirochika H., Nishikawa T.,
RA Kadowaki K., Sugiura M., Burr B., Sasaki T.;
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2] {ECO:0000313|Proteomes:UP000000763}
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare {ECO:0000313|Proteomes:UP000000763};
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL606729; CAE04051.2; -; Genomic_DNA.
DR Proteomes; UP000000763; Chromosome 4.
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; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR041588; Integrase_H2C2.
DR InterPro; IPR001995; Peptidase_A2_cat.
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; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 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 669..684
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 757..836
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 916..1095
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 1458..1638
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT REGION 187..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..228
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1680 AA; 190287 MW; B194BB11BB88989E CRC64;
MAVNASFSSH SFGEGHHVAQ LRELAHFLRF SCPEYTVYSV DRVPPRCELS VYLYPRGGIH
GAGLRPYHFT VARPTLQIAY QDLSWTALRR LAHDYSHRLG GSAFRQLPRL PSGHADARYP
CPYSESQPVL TRMVEFSEAQ ATQHDLLLEA YRSLACRYAA LEARLAEEGV TSVDTVSWDS
GRLCHASHLS SHSSRGSART PSGPRSPSSR APYSPVYSPY PHPVSPSYTP GHTPVASSRR
GPRFIRTARK RVVGSSTVFR FDYPAPPPPA ARATAGPRQM ASRPRRAARF DFEGGRVEPE
ANHESANEQS HHSNRSHHTA SRNAEIEQPH RSNRLHHTTS YNAEVEQSHR SHRTASHNSG
EERIPSPPQV ENNMQHLMVV QTQILQGLAA AIAGFQHNAH GNGHPHMGNN RSKLTDFLRS
RPPEFSQTVE PVEADDWLKD VDRKLNIVQC TPVEKTLYAS HQLRGPAADW WENYCNAHPE
PTNIAWDEFA TAFRAAHVPE STIDMKKEEF NRLKQGNNSV NEYLSQFNKL ARYAPEEVDT
DKKKIRKFLK GIAVGMRLQL LAHDFPTFQH MINKALLLED ARKEATEEYR KRKSNHQGNS
SRGAPRPRYG QPMQYHQSVT QANRQPGYAP RPQMNRPTPQ PQQRAPSGNT APNSVTSFKS
PLGPSAVQCF RCNQMGHYAR QCPQNSTNTN SEHANGSTAR TPTPAAAQSR PSSQASGQGS
RASNNFGRGR VNHIQAETAQ DAPDVVMGMF SVNSVPAIVL FDSGASHSFI SQAFVKRNGW
KTQNLRVPMI VHSLGRNIRA TQICPEVNLK IEEVDFLAKP IVLDSQSLDI ILGMDWLAKH
KGQLDCAEKS ITLQGPGGKL VRFTSNTPTA SRSILTCLQV TSLESVPIVC EYPDVFPEEL
TTNELAEVKR QIEELESKGY VRPSSSPWGA PVLLVKKEDG SERMVIDYRV LNEVTMKNKY
PLPRINDLFD QLKGARVFSK IDLRSGYHQL KIRSEDIPKT AFSTRYGLYE FTVMSFGLTN
APAFFMNLMN KIFMEYLDQF VVVFIDDILI YSKNEEEHAE HLRLIMEKLR DHQLFAKFSK
CEFWLDRVAF LGHVISSNGV EVDPSKVEAV LAWNPPKNVS EIRSFLGLAG YYRRFIEGLS
KLARPMIELL KKEKKFEWSA ACEDGFQEMK KRLTTAPVLT LPDIRKDFEI FCDASRQGLE
CVLMQERKVV AYASRQLRPH EVNYPTHDLE LAAVVHALKI WRHYLIGNRC EVYTDHKSLK
YIFTQTELNM RQRRWLELIK DYDLGIHYHS GKANVVADAL SRKTYCNVAQ TWPDQDHLCR
ELEKLRLAVV QSGVPASLTV QPTLESQIRE AQKDDEGIKG LIKRIQEKKG TDFSIDDQGT
VWCGPRICVP AKKELRDLIL KEAHESAYSI HPGSTKMYQD IKAYFWWAGM KRDVTEYVAL
CDICQRVKAE YQRPAGLPQP LPIPEWKWEE IGMDLITGLP RTPSGYDSIW VIVDRLTKSA
HFVPVKTTFD GKKLAELYMT HVVCRFGCPK KIVSDRGTQF TSRFWKQLHE ALGTDLNFST
AYHPQTDGQI ERVGEALVFG PDMLKAAEEQ VKVIRERLKT AQNSQKNYAD NRRRDLEFEK
GDHVYLRVSP LRGMRRFGMS GKLAPRYIGP YLITARRGEV AYQLELPEGL ADVHNVFHVS
//
