ID I1CF37_RHIO9 Unreviewed; 1825 AA.
AC I1CF37;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN ORFNames=RO3G_11778 {ECO:0000313|EMBL:EIE87067.1};
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:EIE87067.1, ECO:0000313|Proteomes:UP000009138};
RN [1] {ECO:0000313|EMBL:EIE87067.1, 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; CH476740; EIE87067.1; -; Genomic_DNA.
DR STRING; 246409.I1CF37; -.
DR VEuPathDB; FungiDB:RO3G_11778; -.
DR eggNOG; KOG0017; Eukaryota.
DR InParanoid; I1CF37; -.
DR OrthoDB; 1367639at2759; -.
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; 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; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR041588; Integrase_H2C2.
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; 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; PS50013; CHROMO_2; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000009138};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Transposable element {ECO:0000256|ARBA:ARBA00022464}.
FT DOMAIN 795..979
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 1376..1535
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT DOMAIN 1678..1736
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..429
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 REGION 1733..1825
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 395..426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1738..1769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1777..1792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1799..1817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1825 AA; 208702 MW; 48E290AF9E22038F CRC64;
MNSSINQSPA KNIEKDSADE VAKSLDRMDL ETLESRASNP SIHPRDDASI ETDVEMGEVT
DSSPAVPSSD PPNYLERLMV QKTMFFDLIE KLNNNKASFI LENKLTLLEE NEKQLSYALS
ALNDVNALIA SQFELRNHEL KGNGSKNSSP KDRLIPSREI PRFNVNPTAS ALYQLTLREG
DKNVNPSNEP SLDMFIRDFQ RKFLDYDVSI EDHWLHYLEV SFEKSDSDID HDWFERFIKR
RCMDKKTALN WNQAKEVLKQ RFDLASQTTP EMWFKNLINF KQERCETLTQ AMDRYRLFSL
GAKVNMHDNT FLIGHFISRL HTVKFQEMVQ ATITRNLPSL VPASSNTTGE SVYSTRNLPI
PLPKEWNVLE SILIKEMANL ESALLNILKD KKKEENTKKY GEHDDNANTK KRKMVHQSEH
KNQKASKSSV EFQQEIADLK KQGICTFCKT VKYSPGHYSS CSVRLEYVKR KHGKQIVSNS
SKGNDKTVSN LELSNSITSI SQTNKSPKNR VTDLSLSPSN NESTSQSYEL NESSDDEFEF
LYKHYDRNII CSNKNINASF DEEYNKNVFA IRNNKVGEDD SLFASDNVAY SPVTPITLNN
VNTYGIIDTG ARVSVMNKKF AIDNNIKFHS VPGNLVLANG DQIPRMRSVD YVNVEYDNID
YIIKHKFDII NDHASSYNCK ILIGTDLLPK LSIHLMNVAV KHKSTEKELD DSILDKAYEP
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 YSDYLTPPLA EHQQLLIDAH
NKIGHYGAEQ MVKRLHNDGI HWPNLIGDCI KFIKQCKDCM KHNIEKRGFH PLRSIYSYYP
GDHYAIDLGG PMHTTSVYNN NYFMVIIDVC TRFCILRALP DKRSDTILRS LIDVFSTMGF
PTKLQSDNGT EFKNSLSKDL ADAMGYDHRF ITPLHPSANG ISERTVQSVK KLLAKATHGV
GNDWDLYLPS IQLAMNNRIS KRLNSTPFSL MFARKMNEPY GFRSDKDKLK EVKDKPPMSH
EELMKRIDYM TDIVFPAIVN KTKAQIELEQ AKFNDSHRLV DYAPGSHVMV RIPNKSGQLA
PAYEGPYTVV RKNKGNAYIL RDETGVLMPR AYTSVELKLI SNEEVIELDD EGNEIINFEI
EAVINHRGPP KNREYLVRWK NYSSEWDEWL SADKFNDPNT LRNYWKNLGK KYIPPKNAPI
TNSPSSSELL KSTPSGTIST AMKHFSSDDE NNSNLVDKKS TIKSNVGSSA RPVKRTRRNK
PPTNNACDTP STATRSSKRL KSLHK
//
