ID   C4YKK8_CANAW            Unreviewed;       694 AA.
AC   C4YKK8;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=CAWG_06014 {ECO:0000313|EMBL:EEQ47437.1};
OS   Candida albicans (strain WO-1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294748 {ECO:0000313|EMBL:EEQ47437.1, ECO:0000313|Proteomes:UP000001429};
RN   [1] {ECO:0000313|EMBL:EEQ47437.1, ECO:0000313|Proteomes:UP000001429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WO-1 {ECO:0000313|EMBL:EEQ47437.1,
RC   ECO:0000313|Proteomes:UP000001429};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
RN   [2] {ECO:0007829|PDB:4H1G}
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 352-694 IN COMPLEX WITH ADP.
RX   PubMed=23137538; DOI=10.1016/j.bbrc.2012.10.101;
RA   Delorme C., Joshi M., Allingham J.S.;
RT   "Crystal structure of the Candida albicans Kar3 kinesin motor domain fused
RT   to maltose-binding protein.";
RL   Biochem. Biophys. Res. Commun. 428:427-432(2012).
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; CH672354; EEQ47437.1; -; Genomic_DNA.
DR   PDB; 4H1G; X-ray; 2.15 A; A=346-346, A=352-694.
DR   PDBsum; 4H1G; -.
DR   AlphaFoldDB; C4YKK8; -.
DR   SMR; C4YKK8; -.
DR   PaxDb; 5476-C4YKK8; -.
DR   VEuPathDB; FungiDB:CAWG_06014; -.
DR   HOGENOM; CLU_001485_12_4_1; -.
DR   OMA; QDERHAM; -.
DR   Proteomes; UP000001429; Chromosome 2, Supercontig 1.9.
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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4H1G};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0007829|PDB:4H1G};
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          354..690
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   COILED          80..208
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          235..305
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         363
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4H1G"
FT   BINDING         449..456
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
FT   BINDING         452
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4H1G"
FT   BINDING         454
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4H1G"
FT   BINDING         455
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4H1G"
FT   BINDING         456
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4H1G"
FT   BINDING         456
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:4H1G"
FT   BINDING         457
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4H1G"
SQ   SEQUENCE   694 AA;  78925 MW;  561113221D874A8E CRC64;
     MANRAQVMSD ENTKHKFLNV SQPSNLLGGS SSSNSLRRPL NDNTVSVSNK MRKTTSQIPV
     AKDTVPTLTI SESNRFRQLV NEKKIDLEQL KLNATTLRNE LEKQTYENFT IQSNYQNLER
     ILNDLNLKIG ELNSYKQSSL DALIKNFELN NHQLKMNHQE KLNNLKEDIT KQVDKILTEK
     QHKYEVEISN LNKEINKIKS DRKNTESDLN RRLIQLKEDQ HKQELMMVGR VNDDINNMKK
     EIADINSLLE SKTKQIELIK SVEIEGASNK VDKFTLLLDQ LTSKNKSKQE DIQALEKKVA
     TTKESVKAIF EKSTARTSEV HRLQFEVGRM KTELVDQETK RRKLHAQLQD LKGNIRVFCR
     IRNVSSSSSS SSSSSSEDII QYEAPQDIND ESKQELVITR NINNNFSNLR FSFDKIFERE
     QSNDLVFEEL SQLIQCSLDG TNVCVFAYGQ TGSGKTFTMS HPTNGMIPLS LKKIFNDIEE
     LKEKGWSYTV RGKFIEIYNE AIVDLLNPKI DPNTKYEIKH DDIAGKTTVT NVSTIDIKSP
     EQAITILNQA NKKRSTAATK SNDHSSRSHS IFIIDLQGYN SLTKESSYGT LNLIDLAGSE
     RLNNSRAEGD RLKETQAINK SLSCLGDVIH SLNLKDGSHV PYRNSKLTYL LKHSLGGNSK
     TLMFVNISPL TKDLNETINS LRFATKVNNA RINK
//