ID   M7WMV8_RHOT1            Unreviewed;       951 AA.
AC   M7WMV8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=RHTO_04402 {ECO:0000313|EMBL:EMS19401.1};
OS   Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS19401.1, ECO:0000313|Proteomes:UP000016926};
RN   [1] {ECO:0000313|EMBL:EMS19401.1, ECO:0000313|Proteomes:UP000016926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NP11 {ECO:0000313|EMBL:EMS19401.1,
RC   ECO:0000313|Proteomes:UP000016926};
RX   PubMed=23047670; DOI=10.1038/ncomms2112;
RA   Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA   Ye M., Zou H., Zou H., Zhao Z.K.;
RT   "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL   Nat. Commun. 3:1112-1112(2012).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283,
CC       ECO:0000256|RuleBase:RU000394}.
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; KB722669; EMS19401.1; -; Genomic_DNA.
DR   RefSeq; XP_016270520.1; XM_016418068.1.
DR   AlphaFoldDB; M7WMV8; -.
DR   GeneID; 27368415; -.
DR   eggNOG; KOG0240; Eukaryota.
DR   HOGENOM; CLU_001485_3_0_1; -.
DR   OrthoDB; 5476186at2759; -.
DR   Proteomes; UP000016926; Unassembled WGS sequence.
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; cd01369; KISc_KHC_KIF5; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR047149; KIF11-like.
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; PTHR47970; KINESIN-LIKE PROTEIN KIF11; 1.
DR   PANTHER; PTHR47970:SF12; KINESIN-LIKE PROTEIN KIF11; 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}; 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|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394}.
FT   DOMAIN          6..336
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          406..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          629..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          921..951
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          455..496
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          525..566
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          852..904
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        928..942
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         94..101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   951 AA;  105914 MW;  29A7A844DF9D9356 CRC64;
     MSASNNIKVV CRFRPPNKIE LANNGGESIV QIDEEGTTVK LQSQEAMKGP DAQGFTFDRV
     FQMDTKQEEV FEYGVKGIVD DVMNGYNGTV FAYGQTGSGK SHTMMGPDID SPEMKGIIPR
     ITEQIFASII ASPANIEYLV KVSYMEIYME KIRDLLSPEN DNLPVHEDKQ RGVYVKNLSE
     FYVGNSAEVY EVMRQGGSAR AVSATNMNAE SSRSHSIFVI TIQARNTETG TQKTGSLYLV
     DLAGSEKIGK TGATGQTLEE AKKINKSLSA LGMVINALTD GKSSHIPYRD SKLTRILQES
     LGGNSRTTLI INCSPSPYNE TETLSTLRFG MRAKSIKNKA RVNAELSPAE LKALLKKAQR
     DYSNAGAYIG LLEQEVNVWR EGGKVEKEQW ASMEKALGLG EGELEKLVGG PAKSPTPGSA
     PGRTTPRPPA LDRISEGDVS RPDTPMSGSL GADEREDLLR RQNEMEDQLA KTESQLSSQE
     KLIRDLREEL SSLKESESFA LSESKAMSGE VADLRLQLER LRYDSKEAAI TSDSLKEQNA
     ELERELEELR RTLADAKTTQ KSAEQEGKDK KKAERMAAMM AGFSAGGLSE RESEIRASLA
     RLDDAVNADK PLSPDDIATL RRQLEDTTVS LREQQDKSKQ VHEENDLLTR RRDELEQRLG
     TLEQEYEELL DKTVADEERA NADHVQDIRN KLEAQYAMKL DAALNDANDL KQQIELKSQE
     VKSVNAKLEQ ARAANLELER AFKITRASIE GGKNLEEAAK DLERQHKAVA QQLADFDTMK
     KSLMRDLQDR CEKVVELEIS LDEARENYRN LAKNSNSKAQ QRKMDFLTRN LDQLTIVQKQ
     LVDQNTILKR DVALAERKLI ARNERIQNLE ALLQDANDKL NQQNAKFEAR LQAVRERLDQ
     ARAQNQPAMA SSLNFGRIAK PLRGGGAEAE SNSSQDRRTS GFFSRFGSAA R
//