ID   A0A1G4KEK9_9SACH        Unreviewed;       705 AA.
AC   A0A1G4KEK9;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=LAMI_0H04412G {ECO:0000313|EMBL:SCV02965.1};
OS   Lachancea mirantina.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=1230905 {ECO:0000313|EMBL:SCV02965.1, ECO:0000313|Proteomes:UP000191024};
RN   [1] {ECO:0000313|Proteomes:UP000191024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Devillers H.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; LT598468; SCV02965.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4KEK9; -.
DR   STRING; 1230905.A0A1G4KEK9; -.
DR   OrthoDB; 5476186at2759; -.
DR   Proteomes; UP000191024; Chromosome h.
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:0007018; P:microtubule-based movement; IEA:InterPro.
DR   CDD; cd01366; KISc_C_terminal; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
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   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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 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}; Reference proteome {ECO:0000313|Proteomes:UP000191024}.
FT   DOMAIN          365..698
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          84..212
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          253..365
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         449..456
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   705 AA;  81102 MW;  A97DD915D448F9C9 CRC64;
     MSTDEQPIPK TPPWQLSNAA EEPTSQIPSP TVSNSPKYKK RATSPAIPFS LEERRSNSAK
     SSFQAGNGSS SRMTAFYKEN LRELNDLQEE MFRKKVKLDV AKDELSDHRD QLKALELKID
     RLKEDRYVKS QQINLKDNEL KKLKEEQETR ETFMNKGHEL ELQQLHAKNA AELNSLSSDY
     ELKIAELNHE RHQKLIQRRD MLITEVKAAE RNIANNGSIL RDMLNECTSK DRQLREDWLR
     EHQTSWKKKV NQNETLKTEV QRLESRVTNE LEKTLKKKCS ALTEKKGVLK GLEERLNEAE
     KVHSAIEKQM DDLKCEAASL TSRKTELETY ITTSSSELVQ VNEILLKEET IRRKLHNELQ
     ELRGNIRVFC RVRPPLANEE KDLSHFRVED FDDNAGTQSM EVKRDSKVHQ FNFDRIFDVH
     ESNEEVFQEI GQLVQSCLDG YNVCIFAYGQ TGSGKTFTML HPKDGIIPLT LNHIFGWIER
     LEELGWKYEI TSEFVEIYNE TIRDLLKDID CDSDDNTENF KHDIRHDPET HTTQITNITN
     CLLTNRSMVD DILKRASRLR STAATAANER SSRSHSIFVI KLKGSNEQTG EISVGTLNLV
     DLAGSERVSA EQHSPARMRE TQNINRSLSC LGDVIHSLGG RDANKRHIPF RNSKLTYLLK
     YSLIGESKTL MFVNVSPALK NMNETLNSLR FASKVNSTKI NRKIT
//