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Database: UniProt
Entry: A0A0N1I7T1_LEPSE
LinkDB: A0A0N1I7T1_LEPSE
Original site: A0A0N1I7T1_LEPSE 
ID   A0A0N1I7T1_LEPSE        Unreviewed;      1597 AA.
AC   A0A0N1I7T1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Putative kinesin {ECO:0000313|EMBL:KPI88644.1};
GN   ORFNames=ABL78_2248 {ECO:0000313|EMBL:KPI88644.1};
OS   Leptomonas seymouri.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX   NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI88644.1, ECO:0000313|Proteomes:UP000038009};
RN   [1] {ECO:0000313|EMBL:KPI88644.1, ECO:0000313|Proteomes:UP000038009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI88644.1,
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   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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:KPI88644.1}.
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DR   EMBL; LJSK01000044; KPI88644.1; -; Genomic_DNA.
DR   EnsemblProtists; KPI88644; KPI88644; ABL78_2248.
DR   VEuPathDB; TriTrypDB:Lsey_0044_0150; -.
DR   OrthoDB; 47485at2759; -.
DR   Proteomes; UP000038009; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   Gene3D; 1.20.58.1980; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR24115:SF1004; KINESIN-LIKE PROTEIN KIFC2; 1.
DR   PANTHER; PTHR24115; KINESIN-RELATED; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283}.
FT   DOMAIN          767..1548
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          404..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          898..986
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1008..1036
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1093..1141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1153..1176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          612..639
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        15..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..218
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..239
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..301
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        494..520
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..564
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        916..930
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1016..1035
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1160..1176
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         889..896
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1597 AA;  168979 MW;  F9BFE8D7B15F7E3B CRC64;
     MASHPSIKRG GEQALCTAEQ SSSSTPPKLS STAGPAGLPT VAPHRQSLTS SADSRSACEG
     DIYVVDAANS KRFHLAVALQ GPFHPLTCVT HASIQRTVRH TLLPPSSTAT AEPQLKLLFE
     GMPLDESTTE TLPNNAVVIV HREAPVQDSP HPHCCSHALS QPAGDGFTVV EMLSDSLLHS
     QAVPLQPFCQ PGVRSAMQAN PLSTGVPQSC SRSSREAKFT ANGVRAAGST RNSSAMPAPT
     QRLPLRCAYG SEGGGSTSSA VKPSSRTPST PAPSSLQPLS KCARPNNGTP RTLTLATASN
     IPSPGPHDDV MPNATAPPSP TKHLFPSPRE RAGNRACAVS KPVLAARAEP FDAFESIGIS
     AAMASSPSSI ESMPALQSVN GMRSPVDGAS SVEPPLPIHK GSVASSLSPF RSSQRPTAAG
     HAVASPLHFS DTSSTVDSLR DRRRLPPAAL LLSSSSSRQP TAFTSPAFSQ VPPPSVLSRS
     VPDSLHLTSV SDAEVGDGNW TSALSTTPPR RTVPASTAPT GAVASSALFH TPERTPDGLR
     KAVTTRGATA DVGTRDTSTA TGAAPGFSVK PAASLPAHEG PTTIRSPQLH CSVDVRQAAY
     DAQRDAIVNA AAAEQQRLLT RLQQHCDALQ KEKRELLTKQ LNGCRAQEVA SRLRALRAAQ
     EAAAAREIDA VRARLGQCRD QILDRWLSVL HTHSGQHDTM SQELLKELET EGEQLSLNCL
     SLIASYHSEK ARLQALHQQR LLKEAEVARL KWESHVRRCT TEELRGCLRV VARVRPPLRQ
     AWLPDWMLTS TEAGRFDRGY AVQVPPAAVT FPTSNNTRDK NAAAAAPFPC VEVVDPSRNV
     CRRYAISAAY GSADGSDDNS QQRLFTEQLQ PLLEHMCRTG QHVAVLAFGT VGSGKTYTLI
     GPPVEPPPQW GHGRQSEDET SAKPRASSHH HYGDGTLTFS SEESDEEGEA RVGTDGLLQH
     RLGNGATLSS GNAQPRGVTA VGVPPRRGIT RCLDPADKEM EARVLQSMAQ AEAGGRRQRS
     SERHTREESR WRAQAGIDGR DGMLPRAVAW LTAHLRANAT ARTEAVGEPI VESVVFSMFE
     VYNDHIYDLL RAPPAEASPT KKEQEGGEKQ GRRCRGSGPS PRPRWNAGSL PASRAKDSNP
     EGLTELQMEL LPPTGWDSKD AAATLSQQPQ STSQPQWRVK ACEVEVRSAE EALEAIQLGM
     QRRRAAATLR NTQSSRSHLF LRFRVEVQRP AMPERASAAA ANASSAAIRS ALDVMQGGVL
     TGDAAAGVVS AGNADNGVAQ DASTPKGYNF LCAALVPSSS SASSGADAAT PTNPAAAAAA
     PAPTCVTELL FTDFAGSERA DLVGAAGDSL KEAQYISGSL SAVKDVLIAL ARANPCRDAV
     AGCDGAFAAT KKVGENATGG PGAAAAASAT VPLAERWGAL VGRPGVTLSR STPVFLQPRF
     SQLVGDRFRV PSSEKDSSAE HGLPLRRRTL ALVDAYVAGQ SVAQWWRSWR ASSTYIPFRA
     CKTTQLLQSA LGAPCKTLVL ACVRPCTLAE VALPASMRHT KGKRVRELAL ALFDRQAPLM
     MAEVHSTLMF ADRINAATHE SDAAATLPSS NTAAARV
//
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