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Database: UniProt
Entry: A0A0N1PFB3_LEPSE
LinkDB: A0A0N1PFB3_LEPSE
Original site: A0A0N1PFB3_LEPSE 
ID   A0A0N1PFB3_LEPSE        Unreviewed;      2136 AA.
AC   A0A0N1PFB3;
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 RNA helicase {ECO:0000313|EMBL:KPI90208.1};
GN   ORFNames=ABL78_0726 {ECO:0000313|EMBL:KPI90208.1};
OS   Leptomonas seymouri.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX   NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI90208.1, ECO:0000313|Proteomes:UP000038009};
RN   [1] {ECO:0000313|EMBL:KPI90208.1, ECO:0000313|Proteomes:UP000038009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI90208.1,
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:KPI90208.1}.
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DR   EMBL; LJSK01000009; KPI90208.1; -; Genomic_DNA.
DR   EnsemblProtists; KPI90208; KPI90208; ABL78_0726.
DR   VEuPathDB; TriTrypDB:Lsey_0009_0570; -.
DR   OMA; MCSATEF; -.
DR   OrthoDB; 57056at2759; -.
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:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:UniProt.
DR   CDD; cd18795; SF2_C_Ski2; 2.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004179; Sec63-dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR   PANTHER; PTHR47961:SF13; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00270; DEAD; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF02889; Sec63; 2.
DR   PIRSF; PIRSF039073; BRR2; 1.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM00487; DEXDc; 2.
DR   SMART; SM00490; HELICc; 2.
DR   SMART; SM00973; Sec63; 2.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR   PROSITE; PS51194; HELICASE_CTER; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:KPI90208.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          447..629
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          667..868
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          1316..1490
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1521..1732
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2136 AA;  239790 MW;  CF4E3FF171777B5E CRC64;
     MQSTGPSDPG PGGNGQEKVN LNANAAPYQG KFSGRGRGGN NRIYCSPTNN NSSSANDAER
     DSATQGAGMT SGSPEFKAPD VQAANAGSFY GNEKAASASR AQLGNRGRRN RGGAGSSDAA
     SVGTSAAVTA AMSRLQSLLA ASQRSSAKQG LSDPQGSGLH CSLAEDMFSG GASASSFVTE
     CMQTQRPVAL LTHSGEPLSP RGDRVGGAGR SAYQLQRKVP LDMLLSSVDD IVSQVYVNFD
     EDLTKVLLNA LDRVTACDTA DQRERAKVRV IDEMLEVLGD KHYDLLQCIM YRPREVFLRL
     LEEFCTLDDD GDTGASQSSG GPQGLTVRFV KNAAQRSQAQ DVVIGSTGKI TDQKWLSQMN
     KRYRILMQES DLDALFKRDF SVTGSIMPAG ATVTKKPGHV RIHIPPPRQE IMPAEKRVCV
     ATSLPEWTHP AFLSITHLNT IQTTIFQTAF HTSQNMLVCA PTGAGKTVCA LLVMLRCISE
     HFDDGILDRD FKIIFVAPMK ALAQEMVENF SRRLAPFMMK VRELTGDMQL TKRELAETQV
     IVTTPEKWDV ITRKSSNEEL ISQVRLIIMD EIHLLNEERG PVLEAIVART LRHGELNPEL
     RVRLVGLSAT LPNYKDVANF LQADLREGLK VFGPEYRPVP LEQTFIGVQS SGSQQKHNKE
     YELDRLAYEE VVRNMREGHQ VMVFVHSRKQ TVQLAKYFVE EAKRRGEEHL FQFKGVMPPA
     IEKKGRTLQG RDLSALFASG FGAHHAGLIR YDRTSTEGFF RDGYLRVLCC TSTLAWGVNL
     PAHTVVIRGT QMYDPKRGGL VSISVLDVMQ IFGRAGRPQF DTSGHGIIIS DDKEVSHFLR
     LIAHALPIES QMQGKLCDHL NAEVNAGTVS SVMEASSWLE YTYMWQRIRV NPLTYGLKVN
     NVRKDPELKM VRYEMINTSF TDLAIAGMVR YNPETGSVES TDLGRLASHY YITYESISIF
     NEKMRRPDDT WIDSLDMGTA MNIAASAKEF SQLKVRQEEL DELQKLHQML PKQVREYRVS
     GESTDETSTQ WKVTTLLKAY ISRLAVEAHS LSSDMVYVLQ NMPRICRALF EIELERGHPL
     TTYTYLTLCK CMEHRCWDFE HPLMQFANWG RRVNITDAVW VNLNKRNPSM QLLQEMSAKE
     VGQMVHNVRV GRDIADLVAK FPSVNIDIDV QPITRSILRV KVTIVADFAW SRDISGNSEL
     FWLLVEDQDN HFIFHHESVM ITRKEVEAGI PHVVNLAVPI VPQYDMYSVR LYSDRWMGCK
     EDYTFSIGHL HLPEDSQMTT KLLPLSPLRL HVIPEEYHVL YKRYNQFNAV QTQIFHAMFH
     TDQNVFLGAP TGSGKTIAAE MAVLRVFERY PGKKVVYIAP LKALVKERLR DWRTRMRLIG
     RSVVELSGDA TPDISALAKA DILCTTPEKW DGISRNWQVR SYVTAVKLVV FDEVHMLGTD
     RGPILEVIVS RMRYIGWNLK APIRLVGLST AVSNPGDLGS WLGVEKKWAI FNFDPSVRPV
     PMTVHISGYH GKNYCPRMAT MNKPTYNAIC EKSPTQPVIV FVSSRRQTRL TAMALIGFLL
     MEGNTAKWVH MDVGQVQKYT SQLDDPYVKH CLQFGVGIHH AGLLEGDRTI VEDAFLSGRI
     QVLVATSTLA WGVNFPAHMV VVKGTEYYDA KTSSYVDFPI TDVLQMIGRA GRPQYDTEGV
     AQVLCHEPKK GFYRKFLYDP FPVESALHRQ LHVHINAEIV SGTINTRQDA VNYLTWTYLF
     RRIARNPSYY GLEDGSPKAV TIFLSSLVKN VLADLERCGC IEPPEAMDDD ADPDAIQYTV
     LGKLCSYYYI SHLTVDLFNR SIEPDQTCAE LLRLLCDAEE FNELPVRHNE DKLNMELARQ
     LPLPIRDAES DSPHAKAYLL FQALFDRAPM PITDYLTDQK SAMDNAVRVI QAMTDVAANN
     GHLYAALRCM TLMQCMVQAR WWDDNSLMQI PNVVKAMLPV IEKECGVRHA AELANSPLSV
     LQQFQRVLEM PVFGLQKRDV NESMEAVRGL PLIQVDLTVA QQPTQPEDED AGATYELGVH
     LQRLSFGQNS VVAPHFSKTK DEQYWVVVGH EPTGELVALK RVNRLRQSHT AVLRIDWDED
     WVQYSSDGTV ELNVYLVCDS YIGMDQQYSF TLPKPC
//
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