ID   I1CHK9_RHIO9            Unreviewed;      1310 AA.
AC   I1CHK9;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE            EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN   ORFNames=RO3G_12650 {ECO:0000313|EMBL:EIE87939.1};
OS   Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL
OS   43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX   NCBI_TaxID=246409 {ECO:0000313|EMBL:EIE87939.1, ECO:0000313|Proteomes:UP000009138};
RN   [1] {ECO:0000313|EMBL:EIE87939.1, ECO:0000313|Proteomes:UP000009138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880
RC   {ECO:0000313|Proteomes:UP000009138};
RX   PubMed=19578406; DOI=10.1371/journal.pgen.1000549;
RA   Ma L.-J., Ibrahim A.S., Skory C., Grabherr M.G., Burger G., Butler M.,
RA   Elias M., Idnurm A., Lang B.F., Sone T., Abe A., Calvo S.E.,
RA   Corrochano L.M., Engels R., Fu J., Hansberg W., Kim J.-M., Kodira C.D.,
RA   Koehrsen M.J., Liu B., Miranda-Saavedra D., O'Leary S.,
RA   Ortiz-Castellanos L., Poulter R., Rodriguez-Romero J., Ruiz-Herrera J.,
RA   Shen Y.-Q., Zeng Q., Galagan J., Birren B.W., Cuomo C.A., Wickes B.L.;
RT   "Genomic analysis of the basal lineage fungus Rhizopus oryzae reveals a
RT   whole-genome duplication.";
RL   PLoS Genet. 5:E1000549-E1000549(2009).
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DR   EMBL; CH476741; EIE87939.1; -; Genomic_DNA.
DR   STRING; 246409.I1CHK9; -.
DR   VEuPathDB; FungiDB:RO3G_12650; -.
DR   eggNOG; KOG0017; Eukaryota.
DR   InParanoid; I1CHK9; -.
DR   OrthoDB; 1367639at2759; -.
DR   Proteomes; UP000009138; Unassembled WGS sequence.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   CDD; cd00303; retropepsin_like; 1.
DR   CDD; cd09274; RNase_HI_RT_Ty3; 1.
DR   CDD; cd01647; RT_LTR; 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   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR000477; RT_dom.
DR   InterPro; IPR041373; RT_RNaseH.
DR   PANTHER; PTHR37984:SF7; INTEGRASE CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR37984; PROTEIN CBG26694; 1.
DR   Pfam; PF17917; RT_RNaseH; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   PROSITE; PS50878; RT_POL; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000009138}.
FT   DOMAIN          795..979
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   REGION          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          396..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          499..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..420
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1310 AA;  150004 MW;  AFCE56EDCB1D3D95 CRC64;
     MNSSINQSPS KNVEKDSADE VAKSLDRMDL ETLESRASNS SIHPRDDPSI ETDVEMDEAT
     NSSPAVPSSD PPNYLERLMV QKTMFFDLIE KLNNNKASFI LENKLTLLEE NEKQLSYAVS
     ALNDVNALIA SQFELRNHEL KGSGSKNSSP KDRLIPSREI PRFNVNPTAS ALYQLTLREG
     DKNVNPSNEP SLDMFIRDFQ RKFLDYDVSI EDHWLHYLEV SFEKSDSDTD HDWFERFIKR
     RCMDKKTALN WDQAKEVLKQ RFDLASQTTP EMWFKNLINF RQERCETLTQ AMDRYRLFSL
     GAKVNMHDNT FLIGHFVSRL HTVKFQEMVQ ATITRNLPSL VSASSNTNGE SVYSTRNLPI
     PLPKEWNVLE SILIKEMANL ESALLNILKD KKKEENTKKL GEHDDNANTK KRKMVHQSEH
     INQKVSKSSV EFQQEIADLK KQGVCTFCKT AKYSPGHYSS CSVRLEYVKR KHGKQIVSNS
     SKGNDKTVSN LELSNSITSI SQTNKSPKNR VTDLSLSPSN NESTSQSYEL NESSDDEFEF
     LYKHYDRNII CSNKNINANF DEEYNKNVFA IRNNKVGEDD SLFESDNVAY SPVTPITLNN
     VNTYGIIDTG ARVSVMNKKF AIDNNIKFHS VPGNLVLANG DQIPRMRSVD YVNVEYDNID
     YIIKHKFDII DDHASSYNCK ILIGTDLLPK LSIHLMNVAV KHKSTEKELD DSILDKAYKP
     NISRAGTEKE QKVFDMAIKP YIEANKKLNK NSLCNIKEAV LHLPTPKDYV ANIKQYPIAY
     TLQPKVMDII NSWLDEGIII PATPSGWNLP MTVTHKKNLD GTKTDKIRLV LDPRMLNKVL
     PVDNHQLPLI NDIFNSMSGA VIFSTLDLKS AFNQFPVNKD DQIKTTFTAP NNLQYMYRGA
     PFGISTISQL FSRIMLTLFK DLPYVKCFVD DICIFSSSIH AHFLHVKKVL QILTDANLKI
     NFEKTYLAKS AVYLLGYSIS ASGKQIDARK LTNIFDWPRP TTQKQVQSFL GFVNYFRQHT
     PNAALLMAPL DALRCHDEKV KGPFEWTKEH QMHFDSIKHI LSSELMLSHP DLSKPFCIAT
     DSSDYSTGCC LYQEFEVTKP NGEISKIKRY IGFMSRSLSR SEKRYSVTMR ELLGVVYALT
     QFHKFIWGTR FTLYTDHKAL CYIHSQKNAN SMLIKWLDVI LDYNFSVIHV PGLENVLPDK
     LSRLYPPKDT FEHESDIKKG KRLSSYRQNH AISETINTKK KHRAYSKYNA AINIISVIQE
     TTTSDAQKDI IQVKENTDIR DIDYNINDQY LFYVQSAQPL YSDYLTPPLG
//