ID B5RUQ6_DEBHA Unreviewed; 1488 AA.
AC B5RUQ6;
DT 04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=DEHA2G11297p {ECO:0000313|EMBL:CAR65950.1};
GN OrderedLocusNames=DEHA2G11297g {ECO:0000313|EMBL:CAR65950.1};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAR65950.1, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAR65950.1, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.49;
CC Evidence={ECO:0000256|ARBA:ARBA00024557};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000256|ARBA:ARBA00024632};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CR382139; CAR65950.1; -; Genomic_DNA.
DR RefSeq; XP_002770616.1; XM_002770570.1.
DR STRING; 284592.B5RUQ6; -.
DR GeneID; 8999178; -.
DR KEGG; dha:DEHA2G11297g; -.
DR VEuPathDB; FungiDB:DEHA2G11297g; -.
DR eggNOG; KOG0017; Eukaryota.
DR HOGENOM; CLU_001650_5_0_1; -.
DR InParanoid; B5RUQ6; -.
DR OMA; EPHAAWR; -.
DR OrthoDB; 2056154at2759; -.
DR Proteomes; UP000000599; Chromosome G.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR GO; GO:0032196; P:transposition; IEA:UniProtKB-KW.
DR CDD; cd09272; RNase_HI_RT_Ty1; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR035179; DUF5314.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR013103; RVT_2.
DR InterPro; IPR001878; Znf_CCHC.
DR PANTHER; PTHR42648:SF22; RETROVIRUS-RELATED POL POLYPROTEIN FROM TRANSPOSON TNT 1-94; 1.
DR PANTHER; PTHR42648; TRANSPOSASE, PUTATIVE-RELATED; 1.
DR Pfam; PF17241; Retrotran_gag_4; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF07727; RVT_2; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Transposable element {ECO:0000256|ARBA:ARBA00022464};
KW Transposition {ECO:0000256|ARBA:ARBA00022578};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 248..263
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 529..699
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT REGION 260..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1488 AA; 166424 MW; 64094651BE5213D3 CRC64;
MNALNMDLDN LLQQVMSRFI NFNVPESSKL KGAANYKKWN NLVMNKVKNM HCYLEFYLNN
NFESIPSVST FDEVSKSIFR SRYDDLVDML LEKYLPAEML ETYVGEQCLS GLPLWHELLK
DFGSISFKQT LEMQLSFFRK LKDPSVTLSE KLHLLEHADQ DILPIPIPYR IGLLYSFTEN
STVKATLLHM HDRIETMEGG SLTWASLKDG ISEILNDTRS PTSDLSNVAL TVQRQIPRPI
SIKSSVTCFK CGGIGHKSNV CPSKDENDDG KNKSSSVKPP AKPAYAVTAD TKAENNSSSS
PTFGMGYKDS SKNKAFSVSR FASSALVASD ASHRNTFFFD SGASVHLTHQ KELLHDFIPG
QFGSIAGLDP ATPFQVCGTG TLNFMLPDGS LLPVHDVQYV PSCGRNLISM CRAIFAGADI
RAVGDTMFDY HLGFQIATRT SPDKYALYKF TLPCIPAHGG TSGSALAAIP NAHSRLGHPS
HPVAHQVGTS FPSYADAVKS ESKNPICEAC VRGKATRSLP KFSTTSGSIV KAPLELVHSD
VCGPFSQASL TDDRYYAVFV DDYTHFMAVY PIQRKSDVYE CARSYFLQSE RFFYNRGGYK
PITFRTDNGG EYMSSQLQKF LTTQGITHQT TVPYNSHQNG VSERAIRTIT EKARVMMFDA
STPLNFWAEA VSCANYLLNR LPSSAINKNY PYQRWYQTMP DLDHLRPFGC SAYALIPQEV
RSSKLSPRSI RGIMVGYAQT QHAYRIFDLD SGKIAVSNNV KFDEFVFPFQ TITNIPRDIA
SKGSSSSSSS SSSSSFSSIS GIRATAELPG TLMSPPESAV SDIEMDDAES DFSAHDFKVP
QDLASTVDGT SPDITTTPRV VEPLSPLVTQ EVSRPRIEYI SDSEASVPGE DYATSFYERH
HDNFDNSDDE DYVDEPVRRR RKAITMPERS RRRSEVSSEG ETEPSKKSKY EASHTESDSS
LVVRGSAYFM SHAYVVSTKK DGVPVTYKQA MVSDEAEKWK FAMDSEMSAH YSNNTWDLVS
LPKDRKAIGN RWVFTKKDDG RYKARLVAQG FSQVPGEDYL DTFSPVIRYE SVKLLLAFSA
VDNRVVHQMD VDTAFLNGTV EETLYMKQPV DFINENEPEK VCKLNKSLYG LKQAPICWNT
TISDFLAEHR FNRIDTELGI YVRGNIIIGL YVDDILISGK DIKEIEDVKK MLASKFKMKD
LGVAKKFLGI NIAQDTNGIK ICLYDYIGKV LQDFDMSDAN TVATPTLAGE DLHKDDTEDC
DATRYRSLVG KLLFASTTVR TDIAYAVGIL SRHLAKPSEM HMKCAKHVLR YLKGTQDIGH
HYTGDSSLDI YCDSDWASDK SDRKSITGYI VRYGGAPISW KSKKQTTVAM STTEAEYLAL
GEATKEALWI IMLFDEMRVP LQLPISIHED NNSCILLAEH PVFHSRTKHI DIRHHFIREH
IIKKQIKLCP ISTHTQIADM LTKGLNKIKF QDLRSLAGMT RIRIKGKC
//
