ID I1CL79_RHIO9 Unreviewed; 1807 AA.
AC I1CL79;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN ORFNames=RO3G_13920 {ECO:0000313|EMBL:EIE89209.1};
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:EIE89209.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE89209.1, 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; CH476744; EIE89209.1; -; Genomic_DNA.
DR STRING; 246409.I1CL79; -.
DR VEuPathDB; FungiDB:RO3G_13920; -.
DR eggNOG; KOG0017; Eukaryota.
DR InParanoid; I1CL79; -.
DR OMA; ETRTDEN; -.
DR OrthoDB; 1409741at2759; -.
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: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 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; PTHR37984:SF7; INTEGRASE CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR37984; PROTEIN CBG26694; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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 620..636
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 808..992
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 1343..1502
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT DOMAIN 1636..1685
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 32..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1701..1720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1729..1786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 148..212
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 58..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1769..1785
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1807 AA; 206780 MW; CFC130C1782C31D6 CRC64;
MAVITRNNRP TRTSRASISS VSSLSSVVSE VASSCPASPV APGLDNFSDR PGSPSYVEMV
TGSRSRSPSP ADSVSGAIGE RLNSLSIKKD ESSLVRGDAI SLSTAEDDVV MEDAPLNNAR
HAISGEKKNA SRSSKSVSKS KSSIPEKLKR FNRKYDETAD LLDKLVEKRD LEEDESKRKA
LKIQIREYRE DLDYYEERIT KLEVSANEIS QKINEVGNNT NNTRESEPTV PIKVIPPFRL
LVSAAYNPKY YSSSKVSPDD VKNDNAFKTV KDFIRKFEAI VKHYGVNIDK NWLGYLQLSI
ENGQDDRSIN WLQHKLTVAD FKNSNWEGAK TALIGKFGES FTYLQYRQKL MRIKQPNGEY
LNMYVDRYID LLTKAKFADS PLAVMHFLGT LLPPVKDCLE RRLAEIRAKK NADFILEDDT
LSKIQTIIEN NKMHFIEECK KIFPGLKNQE RSQFKPADKK APRQIETKRK FHGDEQRYFP
ENKNRERNFH KRPAHSTPKC RYCGEKYTPG HLDKCREMEK RRDHYLNKDT GFRARKDAPK
NYTGNFSQRR RSFEEKIHNA NDSRITVHNI EKVEKQTATE PEIMQTHPAD EVMNDLLNDD
EIISPFQKAL KQIREKKKHK QALVDTGADV SFISKNVVNK LKLRIIPVHG SLLLADKEKT
VKRLGVADKL NVGYKGQTVA HEFEVLNMHD KVDAIFGRDI LPSLGIHLVG VATNWDDNKV
KFDDSIEDSE YIPNVSNAGT PDEHEALLKA LQSHIDKNQQ IDVHSLCNLP EAVVKLDTSH
GKHAHVRQYP IANKMMPIFD EAVKTWLENG VIVRAPPSPW NSPITFAPKK DANGNPTDYR
PCIDPRKINA LLESDNYPLP LIDDIFHDLA GSTIFTSLDL KSAFHRLPIR KSDQVKTTFT
HRNKQYMFRS APFGLKHVSS HFMRIMNLIL SDLSNVHVYV DDIVIGTTGD SMEKHYQAVS
AVIDRLTQHN MILNPQKCHF GKRSVHLLGF CISEKGKSLD PRKLTNIADW PRPKTGREMM
QWLGTVNYFR AHIPCAATLT APLDALRNVA FIDDINWTRE LQVHFQSIKD ILCSNVVLSP
YDPTKSLYVA TDASNTGVGA VLFQKFDEKQ SDGLTVTTIK YLGFMARSLS QSERNYSVTR
RELLAIVFAL KKFHKFLYGH HFTLYSDHRA LTYLFTSDEL NPMMVGWMDT LLSYDFDIVH
ISGVQNVLPD ALSRLFPPEK ELAGSDSNSS TVKHQNLAYK PNLKKEHELK MKKENRKVFY
VQSPTKFSDK DYITPPYEDR QEILDGVHKF GHFGADHIVK SIHNQNLHWP NLLADAVNYV
SKCNTCQKYN IAKKGYNPHR PVYAYVPGDA YAFDLIGPFQ SSSNMYTYVL ILVDICTRFC
VLKPLVDKKA KTVAGAMVDT FSLLGYPRHF VCSDNGSEFK NEILENLFNA MGIDKRYTTP
YHPSANGAAE RYVQSAKKIL AKFLEGATED WHHYIPSVQL MINNKISTRL QTTPFSLMFA
RNINDFIEYR DDAGELKKKE YMPHDELLKR IDYMSQVVFP AIQDRTDLYT KRQKEKADSK
NRQSTFPEGS YVMVRDREQY NSLSPVYKGP YRVVRQVQGG AYILRDVDET LMSRNYSPEE
LKLISQDEII PKDELYEIEA IINHRGEPGN REYLVRWKNY SKDDDSWLTA EAFTDPESIN
IYWHKLGKSI NQNGEVVKKK NNEAEKNKKQ KLPSDYAPSK LLTTTIMNEQ SKSGTMSHNR
QSHNTKEKKK AQPKRNGNAL SRYPKRRLQQ SQEGFDRKTD HHESSVTQKF ITVQTLPIQL
PNVDTNW
//
