ID G0SUD9_RHOT2 Unreviewed; 951 AA.
AC G0SUD9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=RTG_00046 {ECO:0000313|EMBL:EGU13609.1};
OS Rhodosporidium toruloides (strain ATCC 204091 / IIP 30 / MTCC 1151) (Yeast)
OS (Rhodotorula glutinis (strain ATCC 204091)).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1001064 {ECO:0000313|EMBL:EGU13609.1, ECO:0000313|Proteomes:UP000006141};
RN [1] {ECO:0000313|EMBL:EGU13609.1, ECO:0000313|Proteomes:UP000006141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204091 / IIP 30 / MTCC 1151
RC {ECO:0000313|Proteomes:UP000006141};
RX PubMed=24526636; DOI=10.1128/genomeA.00046-14;
RA Paul D., Magbanua Z., Arick M.II., French T., Bridges S.M., Burgess S.C.,
RA Lawrence M.L.;
RT "Genome sequence of the oleaginous yeast Rhodotorula glutinis ATCC
RT 204091.";
RL Genome Announc. 2:E0004614-E0004614(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGU13609.1}.
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DR EMBL; AEVR02000026; EGU13609.1; -; Genomic_DNA.
DR AlphaFoldDB; G0SUD9; -.
DR HOGENOM; CLU_001485_3_0_1; -.
DR InParanoid; G0SUD9; -.
DR Proteomes; UP000006141; 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; 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; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR PANTHER; PTHR47969:SF29; KINESIN-LIKE PROTEIN; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006141}.
FT DOMAIN 6..336
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 406..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..573
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 852..904
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 453..468
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..494
FT /note="Basic and acidic 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; 105721 MW; 4FE9CF82523239FE CRC64;
MSASNNIKVV CRFRPPNKIE LANNGGGSIV QIDEEGTTVK LQSQEAMKGP DAQGFTFDRV
FQMDTKQEEV FEYGVKGIVD DVMNGYNGTV FAYGQTGSGK SHTMMGPDID NPEMKGIIPR
ITEQIFASII ASPANIEYLV KVSYMEIYME KIRDLLQPEN 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 LDRVSEGDVS RPDTPMSGSL GADEREDLLR RQNEMEDQLA KTESQLSSQE
KIIRDLREEL SSMKESESSA LSESKAMSGE VADLRLQLER LRYDSKEAAI TSDSLKEQNA
ELERELEELR KTLADAKTSQ KSAEQEGKDK KKAERMAAMM AGFSAGGLSE RESEIRASLA
RLDDAVNSDK PLSPDDIATL RRQLEDTTVS LREQQDKSKQ VHEENDLLTR RRDELEQRLG
TLEQEYEELL DKTVADEERA NADHVQDIRN KLEAQYAMKL DAALNDANDL KQQIELKSQE
VKSVNAKLEQ ARAANLELER AFKITTASIE GGKNLEEAAK DLERQHKAVA QQLADFDAMK
KSLMRDLQDR CEKVVELEIS LDEARENYRN LAKNSNSKAQ QRKMDFLTRN LDQLTVVQKQ
LVDQNTILKR DVALAERKLI ARNERIQNLE ALLQDANDKL NQQNAKFEAR LQAVRERLDQ
ARAQNQPAIA SSLNFGRIAK PLRGGGAEAE SNPSQDRRTS GFFSRFGSAA R
//
