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Database: UniProt
Entry: G0W8A2_NAUDC
LinkDB: G0W8A2_NAUDC
Original site: G0W8A2_NAUDC 
ID   G0W8A2_NAUDC            Unreviewed;      1263 AA.
AC   G0W8A2;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, 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   Name=NDAI0C03530 {ECO:0000313|EMBL:CCD24013.1};
GN   OrderedLocusNames=NDAI_0C03530 {ECO:0000313|EMBL:CCD24013.1};
OS   Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC
OS   0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD24013.1, ECO:0000313|Proteomes:UP000000689};
RN   [1] {ECO:0000313|EMBL:CCD24013.1, ECO:0000313|Proteomes:UP000000689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639
RC   {ECO:0000313|Proteomes:UP000000689};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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; HE580269; CCD24013.1; -; Genomic_DNA.
DR   RefSeq; XP_003669256.1; XM_003669208.1.
DR   AlphaFoldDB; G0W8A2; -.
DR   STRING; 1071378.G0W8A2; -.
DR   GeneID; 11494758; -.
DR   KEGG; ndi:NDAI_0C03530; -.
DR   eggNOG; KOG0017; Eukaryota.
DR   HOGENOM; CLU_000384_38_1_1; -.
DR   OMA; GHNTIWA; -.
DR   OrthoDB; 2038104at2759; -.
DR   Proteomes; UP000000689; Chromosome 3.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; 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; IPR024650; Peptidase_A2B.
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; PF12384; Peptidase_A2B; 1.
DR   Pfam; PF17917; RT_RNaseH; 1.
DR   Pfam; PF00665; rve; 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   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000689};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Transposable element {ECO:0000256|ARBA:ARBA00022464}.
FT   DOMAIN          324..501
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   DOMAIN          882..1054
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
SQ   SEQUENCE   1263 AA;  146773 MW;  236AB971706D8F47 CRC64;
     MTFVETVMNM VIIRNNARNP MRGLCKANEE LEATVAIPEC SSNDDLLVCN LESHTREDPL
     LTCNLESHEK EDPRVTTTKI NPPVEDVCIV NIGTKSRTLE ALIDTGSPTH FIRSDVVTKL
     DLKTSQVPFR RVKGLVSDAI TTCNTACRLD FRLENREFDI CAYVTDIIKN DVLIGYPFVK
     RHPSLMESIH KNIDNVKFNN RPVSDPGRMN YEDVTYGKDP IDDICNIETD ENWIDIQRDA
     SDVIIVEVTE VTNKDESKFD TIPEELQVKY RGIVRNDLPP RQRDHKHVSH SIELKEGSRL
     PRRSPYRLTP KKQKEVDEII KDLLDKGFIV PSKSSYSSPI VLVTKHDGSY RLCVDYRELN
     KVTVKDPFPL PHVDELLGKV GSASVFTTLD LHSGYHQIPM NPTDMDKTAF VTPTGKYEYT
     VMPFGLVNAP STFARYMADL FRDLEFVNVY LDDILIFSND LESHWKHIDV VLSRLDQEKL
     IAKKKKCHFA QSEVQFLGYI IGRNKIKPVQ EKCEAINRFP VPKTIKEAQR FVGMINYYRK
     FIKDCSRKVR PLVDFISRNV PWGDLQDDAF ATLKRDLMSE PLLVPFKRDA EYRLTTDASM
     DGLGAVLEEV ADNKVLGVVS YYSKSLNETQ RRYPPGELEL MAIIEGLEHF KYMLHGKHFV
     LRTDHISLLS IQNQKEPARR VQRWLDTLSE FDFSLAYLPG PKNVVADAIS RAKLENKEVS
     NEPVNDYKEI LTVATADTLH TLDPESWTTD WRTDPWGAAV LKSLDDKFDH EIPTEQVNEF
     TRYLKKFERT PEYLKHFKWT NDVLYYEDRI CVPHIRRPLV METYHDHKWF GGHFGEHDTF
     KKISEIYFWP NCYKTVQDYV KSCIQCQVMK AHRPRSQGLH KPLSVPSGRW LDISMDFLTG
     IPTTLAGWDM IMVVIDRFTK RAHFVACKKV NGSTGVFDAL FRFVFSLHGF PRTIVSDRDI
     RFTSNAYREL TDRLGIKLLM STSNHPQTDG QTERVNRTLN QLLRMYCSND QSCWDKLLPH
     VEYVYNSTYQ RVLCMSPFEA DLGYKPNEPR MNRDYIINAR HLTSAEYARD IDALTLRIKD
     QLEENQLRQE YDANKNRTPV NYKIGDYVLL HRDAYFTGGQ YRKIQAIYLG PFQVVGVGTN
     CCELDLPSMR KLHRMINVTW LKPYVERTNM YPKWKPRAKI ERLQRLEEIT SIIGYSLNDK
     IYYCKMKDVD PRLTVEYPEE ELRNLSKPRL DSLLRNFNQL ETEEEKPVEW ARVGCLKVWG
     RRM
//
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