ID J7SBP5_NAUDC Unreviewed; 1255 AA.
AC J7SBP5;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN Name=NDAI0G04700 {ECO:0000313|EMBL:CCK73455.1};
GN OrderedLocusNames=NDAI_0G04700 {ECO:0000313|EMBL:CCK73455.1};
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:CCK73455.1, ECO:0000313|Proteomes:UP000000689};
RN [1] {ECO:0000313|EMBL:CCK73455.1, 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; HE580273; CCK73455.1; -; Genomic_DNA.
DR RefSeq; XP_003980131.1; XM_003980082.1.
DR AlphaFoldDB; J7SBP5; -.
DR GeneID; 13926934; -.
DR KEGG; ndi:NDAI_0G04700; -.
DR eggNOG; KOG0017; Eukaryota.
DR HOGENOM; CLU_000384_38_1_1; -.
DR OMA; AYTENCE; -.
DR OrthoDB; 2726298at2759; -.
DR Proteomes; UP000000689; Chromosome 7.
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; 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 SUPFAM; SSF50630; Acid proteases; 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:UP000000689};
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 274..452
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 887..1046
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT REGION 1209..1255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1209..1244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1255 AA; 144588 MW; BF1FB03DB0611B5B CRC64;
MYTVSNKRNY NLNNTTVYSQ DLSTTNQTIY HIRARHQWKT LPMATIWIDK RQVQALLDSG
SEINLIQEDI AKMLEHQKNV SRINNNNPVR IECGGKISMS EYLLLGSCFK LKERSYTALF
HVVNISTNVP KMILGIPWLR EHGIILNFEQ NAYSIMDQGG KIIDQVNNDT GYKSNFQQVT
DNSSYLTQEH ANSNLEDEGH DKVDNSEITL PPELSDLAIY FAKPDYKGKL KESDFKTFIE
FEKTKPNRMG TPGYPIPQAW LTQAKKQMQV MVDQGVVEEV NGYCNYVSPG FFIRKRDTEE
LRLVINYRTA NQYVIGMESQ LPSIYDSIVT LPDSVFTVLD ITSAFYTVKL DKLSQDFLCF
KVGNQTYRPL RAPMGYKNSA QLFAAFINHI LPSSLKPHLT IYVDDLLIIG KPNTIVSLTR
EVIQHLGGYG IRFSAKKIQF NQRSIEYLGY KIVPGGIKPL ERHIEAIVNL PPPQTVRDVR
SLIGMANFIR NWIPNISESL KHMYQTIKDY GDKGKKGRIS ISEELILEYQ NFKETLQRLP
TIGRFIPGYP ILIFTDASRY STGAVVIQLS DKADSRKPIQ IIIDEIKERN GKVQGKISGF
SSHKLTPAEQ NYSVYDLELL AIDKVLEQYE QWLIGSPVTV ITDHANLSRL TTKVRLTPRI
SRTMEFLMQF DVRIGFMEGD SNTMADGLSR YPIHKSSEPS KIEVELFRRS KLRPEILEPS
IPYEDTEIPN QVKRLFITTA KINESDNVFL RVPEMTLEIV EKYQEDQIHD ITGLPITLHD
KLKEAVSNIK VNSKLHFLTI QGDKLLTKEH KWWIPQEQYE IILWIIWNTH INNDMHRGIQ
ETLRCIRKRY NFDDLYKLTQ VVVNSCKICQ SNKPTNFSIS NYRYIPTPSR PHMIMSADHI
TDLDTSKDGY NEILVIVDLF TRYTYLIAAK KQDTAEETFQ RLEERLCLHG GLPITMLTDN
GTKYKGEFNK NLSWRGINHW NTSIYRAKSN GANERMNGII KQCLRTHGAL MRPHWPQHLS
ATEFFINSRT HSATRRSPNE LKFGYEPEWI DTNKRLEMLN TDTRIQVMSD EEWYNYIQEK
VKPIQALLVK SKDRNKQKIT KTGKPVVFKV GEMVWISRHA YVAKGLKALK AVFIGPAVIK
EAVRETSYKV NILNSSIVLH VNAEFLSKFI KPIDTVRQLR IAMDEYFETI VTTDNTPKQT
KLNGIMKASQ ENGHPNQEDF QSTNKRGAPS ELNEKNAIND ANTTTRKKIC RRSKH
//
