ID A0A0N0P8X9_LEPSE Unreviewed; 845 AA.
AC A0A0N0P8X9;
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=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=ABL78_0800 {ECO:0000313|EMBL:KPI90047.1};
OS Leptomonas seymouri.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leptomonas.
OX NCBI_TaxID=5684 {ECO:0000313|EMBL:KPI90047.1, ECO:0000313|Proteomes:UP000038009};
RN [1] {ECO:0000313|EMBL:KPI90047.1, ECO:0000313|Proteomes:UP000038009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30220 {ECO:0000313|EMBL:KPI90047.1,
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: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283,
CC ECO:0000256|RuleBase:RU000394}.
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:KPI90047.1}.
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DR EMBL; LJSK01000011; KPI90047.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0P8X9; -.
DR EnsemblProtists; KPI90047; KPI90047; ABL78_0800.
DR VEuPathDB; TriTrypDB:Lsey_0011_0040; -.
DR OMA; SVLEIYC; -.
DR OrthoDB; 453489at2759; -.
DR Proteomes; UP000038009; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR Gene3D; 1.25.40.90; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002014; VHS_dom.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR PANTHER; PTHR47972:SF28; PROTEIN CLARET SEGREGATIONAL; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50179; VHS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW Microtubule {ECO:0000256|RuleBase:RU000394};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}.
FT DOMAIN 23..133
FT /note="VHS"
FT /evidence="ECO:0000259|PROSITE:PS50179"
FT DOMAIN 507..830
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT COILED 332..373
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 588..595
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 845 AA; 94108 MW; BF94C749AA05F5E3 CRC64;
MYQQLARVSP TTTGPPAGGV EADVAELIRR EIASKHPEGD PEATARLVEH IRRGSGAIVL
EEIRQHFKYN PPATQIRMLT VMDQCLINSG PQFAVMLSSE KWTDRLFKVA KTTTSPEVRD
KIVQTTISWY QRYHTNGHQR LLHRFQQSHT LGEPFHSIAS KTVKNQQMQR SAEQHHQRNF
ANLDAANRND ILDTEDTFLL QCQGDLASLE YALEHPHILP DTEIATDCKA HKLACMRMLE
SGEHERIAAE LMGLIERFSE VLDLFEAMTG VDIGEGAASK MRALESDDLG EADSDDDDQQ
KRLRRMRAGG AGRHVDAAAV MMQAQQQTES LMNRERTETE HLRQQLEELR QKHEELQNKY
KDAKVKNKEA VGMLEQYAER VEILEKGKGG ATAGLGPLPV LGAVSVGTGG AAGRAAVPAS
VVAQMRSNVS AVRKGLREIR DMRCADLVKE ISYHSAQISN AMAAMVQASE TDRQADRKAL
QWTQELYKRE MKLRKQYYNT IQELKGNIRV YCRVRPMLRK ELEGGHTDVM SFPSEDEVKF
VDASGRPKLF EFDEVYSPMD SQSKVFEDTA PLIDSVVDGF NVCIFAYGQT GSGKTFTMGG
GEGEQRGINT RALERLFQII EDRKETEVST VSVSVLEIYC EQIRDLLVSK KDAANTVYEV
KQGGPYGTYV TNLKELPVTS PRDIDGIMST AQTHRSESMT NMNEHSSRSH MLLYIIVRTT
NKQTNMQSYG KLSLIDLAGS ERLDKSGAEG QRMKEAVSIN KSLSALGDVI AGLAQSAKHV
PFRNSVLTFL LQDSMTGQAK VLMFVCVSPA SYNASESSSS LLFASRARGV AFGQIKKNAV
TEKKD
//
