ID A5E405_LODEL Unreviewed; 1676 AA.
AC A5E405;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN ORFNames=LELG_04344 {ECO:0000313|EMBL:EDK46163.1};
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK46163.1, ECO:0000313|Proteomes:UP000001996};
RN [1] {ECO:0000313|EMBL:EDK46163.1, ECO:0000313|Proteomes:UP000001996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
CC -!- FUNCTION: Integrase (IN) targets the VLP to the nucleus, where a
CC subparticle preintegration complex (PIC) containing at least integrase
CC and the newly synthesized dsDNA copy of the retrotransposon must
CC transit the nuclear membrane. Once in the nucleus, integrase performs
CC the integration of the dsDNA into the host genome.
CC {ECO:0000256|ARBA:ARBA00025615}.
CC -!- FUNCTION: Reverse transcriptase/ribonuclease H (RT) is a
CC multifunctional enzyme that catalyzes the conversion of the retro-
CC elements RNA genome into dsDNA within the VLP. The enzyme displays a
CC DNA polymerase activity that can copy either DNA or RNA templates, and
CC a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-
CC DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA
CC primers. The conversion leads to a linear dsDNA copy of the
CC retrotransposon that includes long terminal repeats (LTRs) at both
CC ends. {ECO:0000256|ARBA:ARBA00025590}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000077};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CH981529; EDK46163.1; -; Genomic_DNA.
DR RefSeq; XP_001524372.1; XM_001524322.1.
DR KEGG; lel:LELG_04344; -.
DR VEuPathDB; FungiDB:LELG_04344; -.
DR eggNOG; KOG0017; Eukaryota.
DR HOGENOM; CLU_241641_0_0_1; -.
DR InParanoid; A5E405; -.
DR OMA; NGATAMI; -.
DR OrthoDB; 2007226at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
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; 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; 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; PF00078; RVT_1; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001996};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transposable element {ECO:0000256|ARBA:ARBA00022464}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 738..915
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 1278..1446
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
SQ SEQUENCE 1676 AA; 192008 MW; 86F50BF5D0F37980 CRC64;
MSHGGPNQMV KTRATQVAIR FQRNVAFTAF IATLSGLVGS LLYQHDPEHF AVVRQWSLFI
FTTLQIWKQQ LIVPDWWYNS TYTTQAVVTS LRLPWYRTHY TTITYQYTTR SFQEFHLDDL
LGTELDTFIK SVKLDPAAPH WLITAFNIIK ITITYCSLLF HILSGWALPI ITFILLTTSI
TFFRMVWSIL TWPIRASQPK RVTNHNTTPT ANTPVTSIRT EITHGSNSPT RIVIETLPEL
VAQIHGRAQI PAGRQPWHAR LITFCWMLIR WIFLFPFQLT RWLRESRARA LTRDYRDYQL
VDLDFISREA LANSLFPQIR LVRFDPKRLY GAIIRASENR NWNDRNTFTS RRSKFLRMTT
LWQFQTEFIK MGLSNDVYNT LSEQARQTAL EFKTPVLDYQ ETLDLLRELD QIPYLHKHFN
SVMPALLRTA FSKPAIHNVI LTLYDTTQSY WTLMSLLDSN WYDLAVNVPE RPSTRPYNKH
HLRNGRPRLV TPNIVSTTTE TTTPSSIIPK MHSTNYSQTG YVAAALANQA KHSFFVPILL
QSADVPETMG YLDQGSTFSF ISPALVSSLG LVTSPRAQRI NLAAFGQGAR TVTAPTVDVD
FNIKDHDTPF SFTFVVHETR IAPILLGADW WEKYELLCVV GKRLEINGQT IPTIQGEEHQ
LIFSTDDLDP PPDPTPPLFA HLIQQYKSKA PTLTLPPARS TDYVINIRKD AIIKPNRPHP
KYAVNAEQAI INNTRELLQQ GLIIPSKARH YSIPSAVPKK NGTYRIVYDF RAVNALTIPI
NSTWNNFREL LPGITGATCF STIDLSSAYH QLRIAPLTQP WTAFWTPIGV FEFLVLPFGL
TDAPEVFGRY MKQLFMDMPF VRTYLDDILV FSENEKVHYS HLKKIFERLV QHQHTINWEK
SVFAQPEIQW VGHLLTKDGV LPTDTTKGQI QLIAIPRDKD EVRQFLGHVG YIQDHIANYS
HRAAPLTDLL TKHTQFNWSQ KCQSAFNDLK AAVLETTSLQ FFDPKQPIAV FTDASHIAMA
AILMQPDQAG GGNWRPIEYR SRKFTGGEVN WDIFLKEFAA VKMAFEKFRL YLEGTHFSLF
VDQLPIKQVF EAFGRGKIHG DARIQRWMSK LLCYNFDVFH INGNENFIAD HMSRNPAHFQ
SSTAISIIGA VNVLLVPDEW FHQFPPAYAD DPFFANVYDL LQQGQTNNEA TQNYSLDTTT
TLLYYHDKLC IPHALLQQFL MTQHDSLEGG HCGITNFFNK VDPYYYFPKM RLVIRQYVDL
CLQCQRHKPP NRAPNGLLQS FPDPKGRWTD INVDIISGYP EVEFNGRLVN AILTIVCRFS
RRVHFYPIST KFSTLDFIHV FQHLYMPLHG IPTIITTDRG TQFTSELFQN YMSSLKITSN
IAVTSHQQSN GLAETKNKQI ERYLRLYIDQ NPEWPQLLLI GEYVMNSTPK SALDHKSPFE
MDLSYIPRSP ATILFPTHAG AQDNAAIDIT EKLERLTTAA RHAHKATFQR LKDNYDRHHR
DIEFNVGDAV LVRTPLLKSH PDAANHGQRR KFLSEFTGPF TIAAKSDNGV NYTLEMPQSY
KGHSDFHVSQ LRLLKSLPPD AITAPQPEVG FKVYKDGSQL VEIDAIVDHK PRKTGFLLLC
RHTPTSKHPD GECVYYSASS LRQTARDLLL AYACEKSLPA LVAPKDRHLV TPPQTT
//
