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Database: UniProt
Entry: Q8SQY6_ENCCU
LinkDB: Q8SQY6_ENCCU
Original site: Q8SQY6_ENCCU 
ID   Q8SQY6_ENCCU            Unreviewed;       581 AA.
AC   Q8SQY6;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   OrderedLocusNames=ECU11_0470 {ECO:0000313|EMBL:CAD25957.1};
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813 {ECO:0000313|EMBL:CAD25957.1, ECO:0000313|Proteomes:UP000000819};
RN   [1] {ECO:0000313|EMBL:CAD25957.1, ECO:0000313|Proteomes:UP000000819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1 {ECO:0000313|EMBL:CAD25957.1,
RC   ECO:0000313|Proteomes:UP000000819};
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
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; AL590450; CAD25957.1; -; Genomic_DNA.
DR   RefSeq; NP_586353.1; NM_001042186.1.
DR   AlphaFoldDB; Q8SQY6; -.
DR   STRING; 284813.Q8SQY6; -.
DR   GeneID; 860006; -.
DR   KEGG; ecu:ECU11_0470; -.
DR   VEuPathDB; MicrosporidiaDB:ECU11_0470; -.
DR   HOGENOM; CLU_430888_0_0_1; -.
DR   InParanoid; Q8SQY6; -.
DR   OMA; LCIEMED; -.
DR   OrthoDB; 239968at2759; -.
DR   Proteomes; UP000000819; Chromosome XI.
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; cd01367; KISc_KIF2_like; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 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   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   PANTHER; PTHR47971:SF8; KINESIN-LIKE PROTEIN KIF24; 1.
DR   PANTHER; PTHR47971; KINESIN-RELATED PROTEIN 6; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Microtubule {ECO:0000256|RuleBase:RU000394};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000819}.
FT   DOMAIN          1..63
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          174..485
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          489..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..527
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         258..265
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   581 AA;  65177 MW;  74C109E689994662 CRC64;
     MKDLRTYLAE NKVEHLYKIF KGLGIDESQL LAKLKYSDLE KIGIENLIER RKVFDIINEI
     NQDIYNEDIE MNKNDSYEDS LLSSDFVCKG TDRPGYRIFP GSLAEKSGAM FGSGETISQK
     LSLCSMPRKN SPRKSLIGLD GLDIDGSKLN THGACNESLL TSSDTGGLGV KEEKIVVCVR
     KKPCSNPKMD VVDIEGRSVV VNEEKFRVDL RPYVEQYRFE FDYSFDGSQK NMDVYRGCVK
     SIVNHVISGG LGTILAYGQT GTGKTYTMLE RDTGMMYLAI KDLMAFKSHG AVTFCEIYMG
     QVYDLLDNGK RVQLREVNGI VHLSNSREEK FEGYEEALEI IEKGMSLRKT GVTGANSKSS
     RSHAVILVNF SEHRAGNEGF QASGSIVFVD LAGSERGSDR KEMGSDVKNE GAEINKSLLA
     LKECIRGMEK DKRHLPFRQS KLTQILKNSF IGTSKTCLIA TISPTPENVE HTLNTLRYAA
     RIKESVVPKG RRARDSLGGN GIIDQARPPP TTSRKEPEEE SFEHPRLELS RSRDVLVREI
     QKALSRIESK IPLLRGSEEL ERMLSLCIEM EDIVDHRTNK Y
//
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