ID A0A0D3CKZ4_BRAOL Unreviewed; 972 AA.
AC A0A0D3CKZ4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN Name=106295229 {ECO:0000313|EnsemblPlants:Bo5g134810.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo5g134810.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo5g134810.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo5g134810.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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 RefSeq; XP_013586529.1; XM_013731075.1.
DR AlphaFoldDB; A0A0D3CKZ4; -.
DR STRING; 109376.A0A0D3CKZ4; -.
DR EnsemblPlants; Bo5g134810.1; Bo5g134810.1; Bo5g134810.
DR GeneID; 106295229; -.
DR Gramene; Bo5g134810.1; Bo5g134810.1; Bo5g134810.
DR KEGG; boe:106295229; -.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_004957_0_0_1; -.
DR OMA; NEKTTEC; -.
DR OrthoDB; 5476186at2759; -.
DR Proteomes; UP000032141; Chromosome C5.
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; cd01374; KISc_CENP_E; 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; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF9; KINESIN MOTOR DOMAIN-CONTAINING 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|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Reference proteome {ECO:0000313|Proteomes:UP000032141}.
FT DOMAIN 75..394
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 396..483
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 634..702
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 564..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..972
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 155..162
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 972 AA; 109290 MW; 37F9F9B76F7EF488 CRC64;
MMASSKQGSK SRKTGFSNFK GADSTASSTT SSSKLYQETS IDDGHSSPAS SSAQSKQHFF
SPDSVPQSAQ RSKENVTVTV RFRPLSPREI RQGEEVAWYA DGETIVRNEY NPTIAYAYDR
VFGPTTTTRN VYDVAAHHVV NGAMEGINGT IFAYGVTSSG KTHTMHGDQR SPGIIPLAVK
DAFSIIQETP NREFLLRISY MEIYNEVVND LLNPAGHNLR IREDKQGTFV EGIKEEVVLS
PAHALSLIAA GEEQRHVGST NYNLLSSRSH TIFTLTIESS PLGNKIKGEA VHLSQLNLVD
LAGSESSKVE TSGLRRKEGS YINKSLLTLG TVISKLTDVK ASHVPYRDSK LTRILQSSLS
GHDRVSLICT VTPASSSSEE THNTLKFAHR AKHIEIQAEQ NKIIDEKSLI KKYQHEIRQL
KEELEQIKQD IVPIPQLNDI GTDDIVLLKQ KLEDGQVKLQ SRLEEEEEAK AALLSRIQRL
TKLILVSTKT SQTSRLPHRF EPRRRHSFGE EELAYLPYKR RDLMDDEHLD LYVSPEGHHE
IRDIACREEK KTRKHGLLNW LKPKKRDNSS STSDQSSVVK SNSTPSTPQG GGNNLHAESR
FSEVSPLMEQ FSEPKEDREA LEDTSHEMDT PEASSKMIDE LDLLREQKKI LSEEAALQSS
LLKRLLDDAA KSPQNEEIKE EIKVLNDDIK AKNDQIATLE KQILDFVMTS HEALDKSDIV
QALAEMRDQL NEKSFELEVK AADNNIIQEQ LNQKTCECEA LQEEVANLKQ ELSNALELAQ
ETKIEELKQK AKELSESKEQ LEHRNRKLAE ESSYAKGLAS AAAVELKALS EEVAKLMNHN
ERLASELATL KSSVPQRGNK PGTTTATNVR NNGRRESLTK RQQEQESSSM ELKRELRMSK
ERERSYEAAL VDRDQREAEL ERIVEESKQR EAYLENELAS MWVLVSKLRR SQEGGSEISD
SVSETLQTDR SF
//
