ID I1BSB1_RHIO9 Unreviewed; 1298 AA.
AC I1BSB1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN ORFNames=RO3G_03796 {ECO:0000313|EMBL:EIE79091.1};
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:EIE79091.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE79091.1, 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; CH476733; EIE79091.1; -; Genomic_DNA.
DR STRING; 246409.I1BSB1; -.
DR VEuPathDB; FungiDB:RO3G_03796; -.
DR eggNOG; KOG0017; Eukaryota.
DR InParanoid; I1BSB1; -.
DR OrthoDB; 3616499at2759; -.
DR Proteomes; UP000009138; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0004519; F:endonuclease 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 CDD; cd00024; CD_CSD; 1.
DR CDD; cd09274; RNase_HI_RT_Ty3; 1.
DR CDD; cd01647; RT_LTR; 1.
DR Gene3D; 2.40.50.40; -; 1.
DR Gene3D; 3.10.20.370; -; 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; 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; 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; PTHR37984:SF7; INTEGRASE CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR37984; PROTEIN CBG26694; 1.
DR Pfam; PF00385; Chromo; 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; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000009138};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transposable element {ECO:0000256|ARBA:ARBA00022464}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1298
FT /note="RNA-directed DNA polymerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003638265"
FT DOMAIN 919..1079
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT DOMAIN 1177..1235
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 72..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1242..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1244..1258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1259..1298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1298 AA; 149356 MW; B2AC21559A3C9F3E CRC64;
MLPRIRPFLV SLTLSVQTLI IVTVARVGKS KADTNEKWTV EYITQVGRDI LGDDNKLYAE
ATALIPGANK SDTVKSRYNE NGSRGDGSLS GHRRHQFKRR SHNMTKVNKN YFCTHHGKNG
THDTVDCFTT KRVEKVNTNK KCFKCGQPWS KEHKCKNNDK KVFAVTSHKN DNNPDDDVVK
DKTALLDQAT SEVNTMMEGL SYDCKYQNKE RTLDKKEIKA NAFNLLTPII IENEKLMGLV
DTGSDTSFID INAFTKKLKL NKINKISGSY NFLSHNNDVS RIGITDPLKF KYSNGIMFEH
SLEIMKFNTG FDFDVLLGTD ILPKMNIGLT GVAFRLSSEH SHSDTATDEI QILENINIDQ
VNEFEPDNSP AGTAEQRANF FDTIKDVLKR NQSIPVTSSC PMPESIIHLP TKEGATAYRR
QYPIPHALRP FLDKQIEEWL KTGTIIKSKV NTSFNSPLLL VPKRNKAGEI VNHRVCLDVR
LLNNILPPTF NYPVPLIRDI FDNLSGKKVF STIGLSNAYH RFKVAPEDVH KLTFTHDNAQ
YSFIKGCFGV KMLTSQFQKC LAILFDGIPC VQNFVDDCIV ASDSFEQHAE DVKLVLEKLT
SVNLIVNPDK CVWFQHSVRL LSFVVNTTGT KVDRNKLTNV QNWPIPNQSH KHVQQFMGLI
NYFRDYVPMI SRVAEPITRL SNAVNIRELW TDEQTNSFNA LKAILQSNLV LHYPDLNKKF
FVATDASLYG VAAVLYQKDE LQRDKYISFV SSSLTPSQRR WSTTKRELYA IILALKEYRK
FLWGKHFTIY SDHKALVYLH TQKIANPMMI GWMETLLDFD FDVVHIPGVL NKLPDQLSRL
YPPLEDDNKL VEDSVYKKNK NNLKIKKVVV KRKKYCRDKS INVLATRLIE NKNELTDYLT
PPEEERDAIL RETHSYGHYG YQAIVRDIHS RDLAGPLPAT GDDYIYLLVL TDICTKYIVI
RPLKNKQSDT VAKELISIFG DYGFPRIIQS DNGTEFRNSL MSHISKNLGI DRRYSTAYHP
QGNGSAEASV KIAMNTLRKM IQSNGRDWNH YLPIVQLCIN RYIKNKTLSS PFSLMYARRV
NMPDDYANKK YPIPNDLMTV EELEERIKHM EEIVFPAILE RTQKIIEEYS SYTVVRKNRG
GSYELKDEQN ELLHRNYTPS ELKVVNMDES NIENEYYEVE DICDHRGPIG HREFLVKWAG
YGERANTWQK ASDFTDPTII EKYWDKQDEL KKLEHERAEH IVNKASSNSK YNESNRNSAP
KLSDEKKVYS VETKKRTLPT KLSREERLLK RRLNKEKK
//
