ID Q6C613_YARLI Unreviewed; 2621 AA.
AC Q6C613;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN ORFNames=YALI0_E13376g {ECO:0000313|EMBL:CAG79492.1};
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG79492.1, ECO:0000313|Proteomes:UP000001300};
RN [1] {ECO:0000313|EMBL:CAG79492.1, ECO:0000313|Proteomes:UP000001300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX PubMed=15229592; DOI=10.1038/nature02579;
RG Genolevures;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA Wincker P., Souciet J.L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR382131; CAG79492.1; -; Genomic_DNA.
DR RefSeq; XP_503899.1; XM_503899.1.
DR STRING; 284591.Q6C613; -.
DR EnsemblFungi; CAG79492; CAG79492; YALI0_E13376g.
DR GeneID; 2911838; -.
DR KEGG; yli:YALI0E13376g; -.
DR VEuPathDB; FungiDB:YALI0_E13376g; -.
DR HOGENOM; CLU_227760_0_0_1; -.
DR InParanoid; Q6C613; -.
DR OrthoDB; 1998016at2759; -.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
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; 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; 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; PTHR33064; POL PROTEIN; 1.
DR PANTHER; PTHR33064:SF36; RT_RNASEH_2 DOMAIN-CONTAINING PROTEIN-RELATED; 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; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 4: Predicted;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|ARBA:ARBA00022750};
KW Reference proteome {ECO:0000313|Proteomes:UP000001300};
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 1611..1807
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 2248..2418
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT REGION 80..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1276..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1500..1525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..779
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1297..1317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2621 AA; 288658 MW; 1A5B2672B06CB83B CRC64;
MSKVTKDEFQ ALTAKMDALT LSHQEITTTL ATAVNTKEFR SALDELKQSN ESFKTHQAGE
FEKLHQLVSA QHETIANLSK RVDSPPSTSS LEGISRIGKA DSEFEPDTPQ KGNSVLHGMD
FAASDTGSVD YRKESDALKS IIRNEVYPSL SSEEFRKQLY AYKSFDSRVA TFILLQDDIR
WSTRARAFHL WCGVNDKQPL FDQQYLQLRS TFEAETADES TKPGAHARLN TACERLLRDL
FRKRGFDHEP AVSFAEQEEE LRFRFKDYHT AFSIETLRAY LSALSTALTS SPLPVLSRCL
QLQKLAPTHL GTALGREIPR DNTRWLSLGM DSDPERDHQV ATELIQPLAK MITQHVQRLD
DLNDEALLRW RQHTVSFEDV WMWVEPSAPP EPSTPEPDKV VVHVAGRGRS TRKPADGPVS
TETVQKPTIR ASDASTSWAA DKAPCVFCGS TAHALVNCDD SEGSPLVKAK YLGSFKSFTR
LGYQGFEKYL SPVDADFPLK QSALYTSWKQ KEWSNPLMEP RLRTFNAQWR PALAGRVNAV
EFVHVEDPGG PLDNSYDSDS SASGYDFQDL LQPGTFSVCL GGVPRDLLSD TFSSYDEPRT
IIDSTDSQLE LTKEAIHQHI LQMEKQPTPL PVTYAIDAPV SGSYSGNMKR LVAHPAFMQL
VARLTAPPGT FKASTLEAGF VGAVMAPSSP VAGRVYFVDA VQRLLNKYNV VLPTKLYECF
ATVRNDLMEP AYATEGDPRR QSLKTNINAL KTVVDSKHPD RPVAPLPRRS PRRDVREDMP
PPALPQATKR GAASSTVSSA APPTAKRTKA VANPSSVGPT DSASSTGAVV DVPSSRVAVH
PPRLGDNHYV SPGTRVTNHI HDASAVAENA PLKDYKDALD RLPSDLEDSK ALFTRDHPRY
DNALLKAGRL PLFKLEAIHA LPESEKADLF ERILKASDVD GLVLFELLQV CPDLTKYIWK
NFRHQRHRLA GPDIQAIALE LGDDLMECAM DLALNVISST PYELNSGTFG RLQEVFTTID
RQLYDDKVGR PLSPHFTDNI ALFDQQTSAL FDSGSSNNVI DTDFFALVLA KAGVTPDRVI
VFSDGQSHAT VANGAKVKVD FWALLPVTFL GVVTLETFCV MKCSMKCILG TGYISKLRIS
FDHDRYRVAS VENPGNPGVR CYPSDRPSAG LVAHLGLLDR LVRPGRRPVP AFPAAKLSRQ
NVMAHVRPTP SLCGDVDEAT NLLDASSLGG PQPGSYSHRS ETAAGCFAIS FADDCESAGP
PSSAATAILK ALASSSGPDP LGIPPRDDPD ESYSSSPGHH GDVSGEPNSS SPGHTSAPVD
GTLGPLLPTD ASSVDDSNEL CSSSSGSEAP SEAPSGVSAA LSDVGTVFQE SYTSYRFHDN
LADNALHARP PDAHALSGFI SSADLDSVFQ YPPPASPCSC CQQPVRECRV LGNTVFIMAD
IGDSATIVQV QPDTDLSMRQ QLYLAEVLSD AQEITPEDSL HSLSVSVNAM YKPLHKRSLP
LNKLRPDGSF PVGDGSKPSP RHRNFSGDES CQFDAKLAPV LFPAELALCR HRMSDTEGVW
AFNEDQEGVL SHHIEEPTKI YVEEGGVINS KHFPLRGAMV GAAKDIIMKG LANGQMEPSS
SPHRNAWFLV SKKSSGYRFI LDCQGLNKIT LRDAFHPPNA DLLAESFCGR AVTSLLDIKN
GYGQKEIAPE SRDLTAFNTD FGSYRLTRLP QGWCNSPAVF HRAMLRVLGP LFPDQAVVFL
DDIGVLGPKT DYGGAMHDDF PGCRRYIVEH MDNLMAVLQN LYEAGLTVSF DKAELFVSEA
EFLGFLTTSE GRFPSPGSSE KIESFEFPTT VRGVRSFLGA VVYFRMWIPH FSSIAAPLYD
CISAAQKAGK LKITKTEATE SAFMALKKAM VSPAVLHRYD PTLPIVITTD ASSLGWGAVM
SHIVSVGPPA ARRPVRFESG LWNPTERTYA STKTECLAVK RALEKCRHYV TGVHFVIETD
NQALVFLLQQ SRVELPNAMF TRWFAYIKQF DYEVRFVKGR DNPVADWLSR EKFSDFRPVD
FRPPVADTAR QADELAPLVP PTWSPVASIT VLSIGPEPVF IHKGISLDLI FTTIASGDLD
RDGVDIPPRL RQICSEFFIF DDILLLISSP GLHRRVLFTE KEVSEVLRAT HEQYGHRGAA
AILHALRRLY YWPGMADHVK SHRASCGTCA KATNHGLLKA SLHFVVPRLI WETVQLDILY
LPAVHGPTKE YPDLADPAKA LAAQTTLTDF LPTAPQFTDV SSAPRGRLNV TIAPYQYVLV
ARDEFSGWPE AVPLRSINSL STAAFFYDFI IARFGVPRRV YTDGGSEFKG DFKHLCEDFH
IKQVFTTPAH GQSTGIVERG HQNLLHCLRK YGRQWILYLH TALWADRCTR RSSTGKSPFE
LMYGVSGVLP VESRFLTWNY LSGKTDLAHN DPAHAAFLRT LQLAASTFEV GSARDHLTLQ
RQRQKAFYDK HHNTADTDPL AVNDFVFVHD LRPHNKLTPR WTGPSIVTAC HPETSTYTVN
DVDGENPRRI HRNRLKVFHP ASIVEFQDRM KEHQSRESAL PAIPGRFSAC SPHVLPPASV
ATRSVRSAAT TASTRVTSRS KLARVDSGLA QGSFLAQGLY S
//
