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Database: UniProt
Entry: I1BZU2_RHIO9
LinkDB: I1BZU2_RHIO9
Original site: I1BZU2_RHIO9 
ID   I1BZU2_RHIO9            Unreviewed;      1671 AA.
AC   I1BZU2;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE            EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN   ORFNames=RO3G_06427 {ECO:0000313|EMBL:EIE81722.1};
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:EIE81722.1, ECO:0000313|Proteomes:UP000009138};
RN   [1] {ECO:0000313|EMBL:EIE81722.1, 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; CH476735; EIE81722.1; -; Genomic_DNA.
DR   STRING; 246409.I1BZU2; -.
DR   VEuPathDB; FungiDB:RO3G_06427; -.
DR   eggNOG; KOG0017; Eukaryota.
DR   InParanoid; I1BZU2; -.
DR   OrthoDB; 1367639at2759; -.
DR   Proteomes; UP000009138; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
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; 2.40.50.40; -; 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   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
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; 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   PANTHER; PTHR33064; POL PROTEIN; 1.
DR   PANTHER; PTHR33064:SF35; RIBONUCLEASE H; 1.
DR   Pfam; PF13650; Asp_protease_2; 1.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF17921; Integrase_H2C2; 1.
DR   Pfam; PF17917; RT_RNaseH; 1.
DR   Pfam; PF00665; rve; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS50013; CHROMO_2; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS50878; RT_POL; 1.
PE   4: Predicted;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Protease {ECO:0000256|ARBA:ARBA00022750};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009138};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transposable element {ECO:0000256|ARBA:ARBA00022464}.
FT   DOMAIN          484..500
FT                   /note="Peptidase A2"
FT                   /evidence="ECO:0000259|PROSITE:PS50175"
FT   DOMAIN          672..856
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   DOMAIN          1207..1366
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   DOMAIN          1500..1549
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1561..1650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1562..1577
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1581..1604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1633..1649
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1671 AA;  192342 MW;  5402228ED66326D7 CRC64;
     MEDAPLNNAR HAISGEKKNA SRSSKSVSKS KSSIPEKLKR FNRKYDETAD LLDKLVEKRD
     LEEDESKRKA LKIQIREYRE DLDYYEEHIT KLEVSANEIS QKINEVGNNT NNTRESEPTV
     PIKVIPPFRL LVSAAYNPKY YSSSKVSPDD VKNDNAFKTL QLSIENGQDD RSINWLQHKL
     TVADFKNNNW EGAKTALIGK FGESFTYLQY RQKLMRIKQP NGEYLNMYVD RYIDLLTKAK
     FADSPLAVMH FLGTLLPPVK DCLERRLAEI RAKKNADFIL EDDTLSKIQT IIENNKMHFI
     EECKKIFPGL KNQERSQFKP ADKKAPRQIE TKRKFHGDEQ RYFPENKNRE RNFHKRPAHS
     TPKCRYCGEK YTPGHLDKCR EMEKRRDHYL NKDTGFRARK DAPKNYTGNF SQRRRSFEEK
     IHNANDSRIT VHNIEKVEKQ TATEPEIMQT HPADEVMNDL LNDDEIISPF QKALKQIREK
     KKHKQALVDT GADVSFISKN VVSKLKLRII PVHGSLLLAD KEKTVKRLGV TDKLNVGYKG
     QTVAHEFEVL NMHDKVDAIF GRDILPSLGI HLVGVATNWD DNKVKFDDSI EDSEYIPNVS
     NAGTPDEHEA LLKALQSHID KNQQIDVHSL CNLPEAVVKL DTSHGKHAHV RQYPIANKMM
     PIFDEAVKTW LENGVIVRAP PSPWNSPITF APKKDANGNP TDYRPCIDPR KINALLESDN
     YPLPLIDDIF HDLAGSTIFT SLDLKSAFHR LPIRKSDQVK TTFTHRNKQY MFRSAPFGLK
     HVSSHFMRIM NLILSDLSNV HVYVDDIVIG TTGDSMEKHY QAVSAVIDRL TQHNMILNPQ
     KCHFGKRSVH LLGFCISEKG KSLDPRKLTN IADWPRPKTG REMMQWLGTV NYFRAHIPCA
     ATLTAPLDAL RNVAFIDDIN WTRELQVHFQ SIKDILCSNV VLSPYDPTKS LYVATDASNT
     GVGAVLFQKF DEKQSDGLTV TTIKYLGFMA RSLSQSERNY SVTRRELLAI VFALKKFHKF
     LYGHHFTLYS DHRALTYLFT SDELNPMMVG WMDTLLSYDF DIAHIPGVQN VLPDALSRLF
     PPEKELAGSD SNSSTVKHQN LAYKPNLKKE HELKMKKENR KVFYVQSPTK FSDKDYITPP
     YEDRQEILDG VHKFGHFGAD HIVKSIHNQN LHWPNLLADA VNYVSKCNTC QKYNIAKKGY
     NPHRPVYAYV PGDAYAFDLI GPFQSSSNMY TYVLILVDIC TRFCVLKPLV DKKAKTVAGA
     MVDTFSLLGY PRHFVCSDNG SEFKNEILEN LFNAMGIDKR YTTPYHPSAN GAAERYVQSA
     KKILAKFLEG ATEDWHHYIP SVQLMINNKI STRLQTTPFS LMFARNINDF IEYRDDAGEL
     KKKEYMPHDE LLKRIDYMSQ VVFPAIQDRT DLYTKRQKEK ADSKNRQSTF PEGSYVMVRD
     REQYNSLSPV YKGPYRVVRQ VQGGAYILRD VDETLMSRNY SPEELKLISQ DEIIPKDELY
     EIEAIINHRG EPGNREYLVR WKNYSKDDDS WLTAEAFTDP ESINIYWRKL GKSINQNGEV
     VKKKNNEAEK NKKQKLPSDY APSKLLTTTI MNEQSKSGTM SHNRQSHNTK EKKKAQPKHN
     GNALSRYPKR RLQQSQEGFD RKTDHHESSV TQKFITVQTL PIQLPNVDTN W
//
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