ID B5RSU2_DEBHA Unreviewed; 926 AA.
AC B5RSU2;
DT 04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 04-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN OrderedLocusNames=DEHA2A09812g {ECO:0000313|EMBL:CAR65398.1};
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592 {ECO:0000313|EMBL:CAR65398.1, ECO:0000313|Proteomes:UP000000599};
RN [1] {ECO:0000313|EMBL:CAR65398.1, ECO:0000313|Proteomes:UP000000599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC 2968 {ECO:0000313|Proteomes:UP000000599};
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).
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; CR382133; CAR65398.1; -; Genomic_DNA.
DR RefSeq; XP_002770021.1; XM_002769975.1.
DR AlphaFoldDB; B5RSU2; -.
DR STRING; 284592.B5RSU2; -.
DR GeneID; 8998068; -.
DR KEGG; dha:DEHA2A09812g; -.
DR VEuPathDB; FungiDB:DEHA2A09812g; -.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_001485_21_2_1; -.
DR InParanoid; B5RSU2; -.
DR OMA; MQRNAFP; -.
DR OrthoDB; 5476186at2759; -.
DR Proteomes; UP000000599; Chromosome A.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005819; C:spindle; IEA:UniProt.
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 GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR CDD; cd01370; KISc_KIP3_like; 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; PTHR24115:SF372; KINESIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR24115; KINESIN-RELATED; 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|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:UP000000599}.
FT DOMAIN 20..401
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 685..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 157..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 926 AA; 104382 MW; B9BBA85E63593AC1 CRC64;
MNATGTVASS SGLNSSRESS ITVAVRVRPF TPGEENNLIK LNNEEFFLGD GSLSTNNAAT
DTPSKKSNLM PRGIRKIINV VDDRMLIFDP PETNPLIQMQ RNAFPNTKAT SRIREHRFVF
DKLFDIQATQ EDVYNNTTRP LLDSVLDGFN ATVFAYGATG CGKTHTISGT PLDPGVIFLT
MKELYEKIEG LADTKLFDVS MSFLEIYNET IRDLLNPETN FKRLVLREDA NKKISVSNLS
SHKPKSVQEV MDLILVGNQN RTSSPTEANA TSSRSHAVLQ INVVQRNRTA DISEEHTYAT
LSIIDLAGSE RAAATKNRGA RLNEGANINK SLLALGNCIN ALCDPRRRNH VPYRDSKLTR
LLKFSLGGNC KTVMIVCVSP SSQHYDETLN TLKYADRAKE IKTKLIRNQH NLDRHVGSYL
KMITQQKQEI EDLRAREQKV VESTIAKQNT LSQKCLNVTM DNISNLKASL SKQHQEKWKK
YFFLAKRKLL LLQKLEMESL VKYLHKLSKS GNINGFQNIV NLSEQLISKI TTGISDLESQ
YSRPNEIDYI FNESTLQMLK KLKEQEGWSD HNTVVFDSLV ACLRDSLERE ILFNSSILFD
HLVHEIRGFD FFPKSFIDML ATYSHSEKEN MHEYTTASLS NAINGLTKTL EEILDGEYDT
AIENVTSSFM QRKLKEQEMQ ANKVNNHSID PSIVIPKPRD CKRGSNSPLK SSPPRDFKKS
ITKKNGSSIS PAMLQKQGKK VRWDVPNQDS TLAESDVSID EQNTILKSDY EDDSPIGNNI
IDKTNMIDDL DLKFDPTLDS PPLAQLLKDS MNRSLMADLS KGRNKHRKFQ PLTNRKLSTN
ENSEPLTKLP LLNKQASTKI TNSMQPTTPN EVPESSPNYL PGTQTNTKFK MNTLGAPSRV
INRYNTYVED DEDSRDIESN GSEKVE
//