ID A0A0N1IM03_LEPSE Unreviewed; 662 AA.
AC A0A0N1IM03;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Putative DNA repair protein {ECO:0000313|EMBL:KPI89124.1};
GN ORFNames=ABL78_1768 {ECO:0000313|EMBL:KPI89124.1};
OS Leptomonas seymouri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI89124.1, ECO:0000313|Proteomes:UP000038009};
RN [1] {ECO:0000313|EMBL:KPI89124.1, ECO:0000313|Proteomes:UP000038009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI89124.1,
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 -!- 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:KPI89124.1}.
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DR EMBL; LJSK01000031; KPI89124.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1IM03; -.
DR EnsemblProtists; KPI89124; KPI89124; ABL78_1768.
DR VEuPathDB; TriTrypDB:Lsey_0031_0250; -.
DR OMA; VHIHHGK; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000038009; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd18793; SF2_C_SNF; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF22; DNA REPAIR PROTEIN RAD5; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 75..228
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 349..396
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 429..606
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 610..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 74592 MW; 78570B8D2B78A96E CRC64;
MQRISVIANC SRINRPGGDL NSLISATNEL MRSRKGDFKA IFCEIDKWLH FAGKFHPSFE
GRARDFLNDT ERKDFQLIAS KELRTLVVVP ASLMLQWKSE IESKVNASRK ITIYLYHGES
KWVSSTELET YDFVITTYET LTNSAAQAFI PGDDPRTYAF SRKEAGPLFH VYWKRIILDE
AHMVRHSRTQ RWRAVQELQG LHRWAVTATP LHNSIDDLQN LLHFVGLPRL PILPGTNSEE
LLGDPILQRS IARSLQPAFL RRGPVMFRNG VKEVLVQLPP KTEVVVKQPF TVKESHMYNG
VLARSKSALA SSEGKEGAVF HIFAMMTRLR QACCHPWISQ GRAVQISVCG ICQSEASSAV
VTKCGHVFCH ECLLLRFREA VDGDEVATRI QCPSCSQVVT YASAFKKQIL SSSDRIAQYK
RNEFELSTKL RMVLRAIHEM QQKYPNDKMI IFSQFTSFMD VVTVALERYK IDSLRIDGTM
TLSARNAVIR QFQSSERVKI VLASKTATGV GLNLTAANHV IVVDPWWNPA IEEQAVHRCY
RIGQKKPVYV TRFIISDTIE QYCYEICQRK KEFGDAVLRA ATAGDSGAKM AASRLHELMS
RLKYVGDGAH GPANTKSIDD SGCTTEDGEK TSTPRQKDGS EKNTTGQKTT LKRNAMVTTT
IV
//
