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
//