ID   Q6FVW6_CANGA            Unreviewed;       692 AA.
AC   Q6FVW6;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 140.
DE   SubName: Full=Candida glabrata strain CBS138 chromosome D complete sequence {ECO:0000313|EMBL:CAG58539.1};
GN   Name=KAR3 {ECO:0000313|CGD:CAL0128117};
GN   OrderedLocusNames=CAGL0D04994g {ECO:0000313|CGD:CAL0128117,
GN   ECO:0000313|EMBL:CAG58539.1};
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG58539.1, ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG58539.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
RN   [2] {ECO:0007829|PDB:4GKR}
RP   X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) OF 324-692 IN COMPLEX WITH ADP AND
RP   MG(2+).
RX   PubMed=23043140; DOI=10.1074/jbc.M112.416529;
RA   Duan D., Jia Z., Joshi M., Brunton J., Chan M., Drew D., Davis D.,
RA   Allingham J.S.;
RT   "Neck rotation and neck mimic docking in the noncatalytic Kar3-associated
RT   protein Vik1.";
RL   J. Biol. Chem. 287:40292-40301(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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR380950; CAG58539.1; -; Genomic_DNA.
DR   RefSeq; XP_445628.1; XM_445628.1.
DR   PDB; 4GKR; X-ray; 2.69 A; A/B=324-692.
DR   PDBsum; 4GKR; -.
DR   AlphaFoldDB; Q6FVW6; -.
DR   SMR; Q6FVW6; -.
DR   STRING; 284593.Q6FVW6; -.
DR   EnsemblFungi; CAGL0D04994g-T; CAGL0D04994g-T-p1; CAGL0D04994g.
DR   GeneID; 2887096; -.
DR   KEGG; cgr:CAGL0D04994g; -.
DR   CGD; CAL0128117; KAR3.
DR   VEuPathDB; FungiDB:CAGL0D04994g; -.
DR   eggNOG; KOG0239; Eukaryota.
DR   HOGENOM; CLU_001485_12_4_1; -.
DR   InParanoid; Q6FVW6; -.
DR   OMA; ETARDKW; -.
DR   Proteomes; UP000002428; Chromosome D.
DR   GO; GO:0005871; C:kinesin complex; IDA:CGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0008569; F:minus-end-directed microtubule motor activity; IDA:CGD.
DR   GO; GO:0031534; P:minus-end directed microtubule sliding; IDA:CGD.
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; 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; PS50067; KINESIN_MOTOR_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4GKR};
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:4GKR};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000002428}.
FT   DOMAIN          350..686
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          69..197
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          260..350
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        27..51
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         435..442
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
FT   BINDING         438
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4GKR"
FT   BINDING         439
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4GKR"
FT   BINDING         440
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4GKR"
FT   BINDING         441
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4GKR"
FT   BINDING         442
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4GKR"
FT   BINDING         442
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:4GKR"
FT   BINDING         443
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /evidence="ECO:0007829|PDB:4GKR"
SQ   SEQUENCE   692 AA;  80008 MW;  FEE397B31974A064 CRC64;
     MDEPATPAKQ TGIGGAGQKR RYTTTPPREI RQYQSRSSFG VNSSGNVDGK SIRSRTHLTS
     FYKENVMELN ELQDKLFQKK GVLDGLKDEY EDLKSRYTAL DLKWEQKKEE RKLKAQKLEL
     KEKELKKIKD DFANKKTFLE ESHKLKLEQL TANKNAELNK MNDEYRSKLE ALKYEKIKKF
     ENEKNELIEK IEEIRNKMIT NDVALQQRMK DIEADHLEEK EKWLKDYQKE WREVTEKNQE
     SIRKTKELKS EIETVLTPRI DTQNKRLEEL KSEIKKLDDT LQNKNEQVGE IRKNIDLERE
     KKDKLLAEKE EILAYIEKSK KEVEEIKKIL VKEESLRRAL HNELQELRGN IRVYCRIRPP
     LPHEDDNIEH IKVQPFDDDN GDQGMTINRG NSQVIPFKFD KIFDQQETND EIFKEVGQLI
     QSSLDGYNVC IFAYGQTGSG KTYTMLNPGD GIVPATINHI FSWIDKLAAR GWSYKVSCEF
     IEIYNENIVD LLRSGAPSQE NNDRNADSKH EIRHDQELKT TYITNITTCV LDSRDTVDKV
     LKRANKLRST ASTAANEHSS RSHSIFIIHL EGKNEGTGEK SQGILNLVDL AGSERLNSSM
     VVGERLRETQ SINKSLSCLG DVIHALNSPD GQKRHIPFRN SKLTYLLQYS LIGSSKTLMF
     VNISPAALHL NETINSLRFA SKVNNTKMIT RN
//