ID A0A0N1P9V3_LEPSE Unreviewed; 1124 AA.
AC A0A0N1P9V3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU363044};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU363044};
GN ORFNames=ABL78_8138 {ECO:0000313|EMBL:KPI82848.1};
OS Leptomonas seymouri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI82848.1, ECO:0000313|Proteomes:UP000038009};
RN [1] {ECO:0000313|EMBL:KPI82848.1, ECO:0000313|Proteomes:UP000038009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI82848.1,
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|ARBA:ARBA00001665,
CC ECO:0000256|RuleBase:RU363044};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|RuleBase:RU363044};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the helicase family. PIF1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009781}.
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:KPI82848.1}.
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DR EMBL; LJSK01000512; KPI82848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1P9V3; -.
DR EnsemblProtists; KPI82848; KPI82848; ABL78_8138.
DR VEuPathDB; TriTrypDB:Lsey_0512_0010; -.
DR OMA; FLHPLEM; -.
DR OrthoDB; 164846at2759; -.
DR Proteomes; UP000038009; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR CDD; cd18037; DEXSc_Pif1_like; 1.
DR CDD; cd18809; SF1_C_RecD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47642; ATP-DEPENDENT DNA HELICASE; 1.
DR PANTHER; PTHR47642:SF5; ATP-DEPENDENT DNA HELICASE; 1.
DR Pfam; PF13245; AAA_19; 1.
DR Pfam; PF05970; PIF1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU363044};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU363044};
KW DNA recombination {ECO:0000256|RuleBase:RU363044};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU363044};
KW Helicase {ECO:0000256|RuleBase:RU363044, ECO:0000313|EMBL:KPI82848.1};
KW Hydrolase {ECO:0000256|RuleBase:RU363044};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU363044}.
FT REGION 276..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1124 AA; 122675 MW; DCA37E272FE45497 CRC64;
MHAIERFSIG WQSKSIPGSI VSNDRDYVML ANNRQAPPLC YPSSISFFRD NLSVLDAGAD
SSHVSDVGVM HRPEASAYAF EEAAGLLGVD TDGVLAYIRD PLRVPDGAPL QSLQTEADNE
AGKAAKDSGA AVTVCSEDDD ERAMLLSLFN DLPPTGGGEA AVKDVSAQAG ADSGLLPADQ
TSQDDQNFKE EHVRGITTPA PVLETAAPSA TTDAESELAL DMFQARAVDL ALRGHNLFIT
GGAGTGKSRT LHHIIAALRA REMEEIIALK RKAYAPPMPG SSGSTTEKWR GHSSSQRRAP
YAAVHTSDLT AKKSSSISAP SRRMQRASSV YVTATTGLAA VPLCGTTIHN FAGIISGKAH
PEALFRHLRK SRKVCQRWKR CRVLIIDEIS MMEAALFESL DYIARRLRRQ ASVPFGGIQI
IVCGDFHQLP PIVKRSEWYA IDHGTTATLW QQKQQQQQPH PSLCRAVAPH AAMPPPAQPF
SIPNLDAFFA SSVKDTKKNT AAIAAPQRSD EEACTHARRC LYAFQTLAWH RLQLWPVVLQ
IPHRQASDVL FQRTLDEVRR GELSPEGCRA LASRCVVEGV ANPDAMGKIA PPTLTFTRGN
SDPRRSGEQL PPSAAMAIRL CATNSAVDAR NAFFLSQLPP HHSHFGALPA DRDAAASCVY
YAVDSQVTAQ RPAHGLCQNG TEVEPRYGQR MVAAASADDH HLLGEITLKI GTRVLLVSNV
SLRYSLVNGS IGEVVGFLHP LEMVALVHWT MQQRFRRYRH LRQGNGDTAE SVAEEGSWRP
ASSSSWLDEL RRRGGFSDDD AAILRCIETS QGIRFSSLWW RMQHARKPSS FASSPSSGGY
RPPQRSRSSC VDVHADCIPY DAMFPSRHCI DLLRVTRPPS TTPPTSHNLR DYSVLSTHLR
YDFWKDDSSH HCAPDTLPSL HPHSSSRSPT DGVSAPPPWK RRLCDLTPEE RHREQLPIVR
FETVSSLPPS SYGRAAKYAM IAPSCYTYGD GDGSVTQREG EMPGLIGKGT ASRTQLPLRY
AWALTVHKSQ GLTLHPVQVD MESIRSAGQA YVALSRAPSL DQLYILNFDP SVISASPVVK
RFYESLVTSS NDGTESGVQS TSDSSSAASH SPVFTYEDSA RDTN
//
