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Database: UniProt
Entry: A0A0N0P8H3_LEPSE
LinkDB: A0A0N0P8H3_LEPSE
Original site: A0A0N0P8H3_LEPSE 
ID   A0A0N0P8H3_LEPSE        Unreviewed;      1104 AA.
AC   A0A0N0P8H3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=Putative transcription activator DNA-dependent ATPase {ECO:0000313|EMBL:KPI89527.1};
GN   ORFNames=ABL78_1403 {ECO:0000313|EMBL:KPI89527.1};
OS   Leptomonas seymouri.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX   NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI89527.1, ECO:0000313|Proteomes:UP000038009};
RN   [1] {ECO:0000313|EMBL:KPI89527.1, ECO:0000313|Proteomes:UP000038009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI89527.1,
RC   ECO:0000313|Proteomes:UP000038009};
RX   PubMed=26317207;
RA   Kraeva N., Butenko A., Hlavacova J., Kostygov A., Myskova J., Grybchuk D.,
RA   Lestinova T., Votypka J., Volf P., Opperdoes F., Flegontov P., Lukes J.,
RA   Yurchenko V.;
RT   "Leptomonas seymouri: Adaptations to the Dixenous Life Cycle Analyzed by
RT   Genome Sequencing, Transcriptome Profiling and Co-infection with Leishmania
RT   donovani.";
RL   PLoS Pathog. 11:E1005127-E1005127(2015).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPI89527.1}.
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DR   EMBL; LJSK01000022; KPI89527.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0P8H3; -.
DR   EnsemblProtists; KPI89527; KPI89527; ABL78_1403.
DR   VEuPathDB; TriTrypDB:Lsey_0022_0480; -.
DR   OMA; KEIYVSC; -.
DR   OrthoDB; 5482994at2759; -.
DR   Proteomes; UP000038009; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.10.1040.30; ISWI, HAND domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR015194; ISWI_HAND-dom.
DR   InterPro; IPR036306; ISWI_HAND-dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015195; SLIDE.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   PANTHER; PTHR45623:SF49; ISW-1; 1.
DR   Pfam; PF09110; HAND; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF09111; SLIDE; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          179..347
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          476..630
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          876..901
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1085..1104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        876..891
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1104 AA;  125779 MW;  EC71758848F37742 CRC64;
     MASTMTRAIR RRQDLHSTLV FEREINDITA DELYEQLLLG NIRNGTDPNA KAVIEVYEDY
     VEPSYDPVKG AQVAAAHKEV IHEIYKERDV IIRTLRSSDE HQQLSPFDRL LRETEFYTGV
     REWKADAARS GRRSHLYRHI SNDNDEDPTG FAMMHLTETP SYIRGKLRPY QVEGVNWLLG
     LFSRGVNGIL ADEMGLGKTF QTIATIAYLK FTVGMPGPHL VVCPKSVMGN WYREFKHWCP
     SLSVFKFHAS SDLRSSLVKA HLHPVDHIKY DVIVTTFEMV LDEINTFKRV AWQYLIVDEA
     HKLKNEEGRA HTALDSLQTS HRLIITGTPL QNNLKELWAL LHFLAPRLFS DSESFDTWFD
     TTSGHQDASV MSNLHKILAP LMIRRLKADV NTGIPPKKEI YVACQLSKKQ REWYMNVLAK
     DAEVLNKASG SAASLTSVMM NLRKVINHPY LMDGGEEGPP FITDEKLVRT SGKMIILDKL
     LNRLRSDVVG KHKVLIFSQF TSMLNILEDY CNMRGFRYCR IDGNTSGYDR DSQMASFNSP
     SSDYFIFLLS TRAGGLGINL QAANHVVIYD SDWNPQMDLQ AQDRAHRIGQ KRSVRVYRFV
     TDGTVEEKIY RRALKKLYLD AVVVQQGRLQ AKAASSASKE ELLSMIKFGA EEIFKTRHQD
     VTEADIDRLL DEGETISNQL TNEAKQQVQM SLASFQLGAE EANIYDFEGV SFKTGAETRI
     LHIKLGAPVS QTDLQAQCSQ HGEVIKTVLH PNMREALVYF RSISGAIEAK VRLPYESTFA
     SRDSQTVVSN DMIAECIGVG EKLGRGHRVR EPVQFFSAAD VESMQKKASK APPLKLPKPP
     KFYPHQLYNM KRLTELHNTE VALMVRNWKR KFEEVKEAPT TNDAEGGEEG EATKGEAEDE
     DELLTEVEQE ERERLLSEGF PNWTFSEYRA VVSSLTSGNV DLTDYPAIAA IVGDTKTVGE
     VRDYVVALLE RGEQCIKRFA NVEARIRKSK AKREAKENIL KAARWKVETC EDPEKELTFK
     TRGNAALDRE IFLIAYDTGF KQDNTSELVR NKPQHRFNVW YQSRPENFFE KRLHTLMKAV
     KRECERSTDA DVGMPESSRR RLEV
//
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