ID A0A0D3E3X6_BRAOL Unreviewed; 1070 AA.
AC A0A0D3E3X6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=106319137 {ECO:0000313|EnsemblPlants:Bo9g029220.1};
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:Bo9g029220.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo9g029220.1, 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:Bo9g029220.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-14 subfamily.
CC {ECO:0000256|ARBA:ARBA00010899}.
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DR RefSeq; XP_013612833.1; XM_013757379.1.
DR AlphaFoldDB; A0A0D3E3X6; -.
DR STRING; 109376.A0A0D3E3X6; -.
DR EnsemblPlants; Bo9g029220.1; Bo9g029220.1; Bo9g029220.
DR GeneID; 106319137; -.
DR Gramene; Bo9g029220.1; Bo9g029220.1; Bo9g029220.
DR eggNOG; KOG0239; Eukaryota.
DR HOGENOM; CLU_001485_1_1_1; -.
DR OMA; YRIMDES; -.
DR OrthoDB; 408385at2759; -.
DR Proteomes; UP000032141; Chromosome C9.
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 Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
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; PTHR47972:SF37; KINESIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00033; CH; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50021; CH; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000032141}.
FT DOMAIN 39..142
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 472..800
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 157..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 293..384
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 886..904
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 556..563
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1070 AA; 119366 MW; 7DD947E79C57E945 CRC64;
MNINLEQDAN MSGVYAPSDA TSFLSFDGSE TRSSLDDTKK GHQNLVEWLN QTLPYLNLPS
EASEDEVRAC LRDGTVLCNL LNQLSPGSMR MGGSFEPAYV KIERFLTAMD EMALPRFEVS
DIEQGDMVPV FQSLKALKAS FSDGGNDKNS LCARRRWSLP EDHSDPRGDD RNFTDGFQSK
EGFEIDISDA KISELLKSNS LRNTPTRTLF DMLDKLLDES VKKMNGHVSH AMASLLSALV
QVIEKRISNQ ADNLKNQNIL FRVREDKYRS RIKVLETLAA GATQENEIVT NCMERTKLEK
NRIEERERSE EKDVVRLKKE KELSDAEIRK LKQELKVVKE THANQCLELE AQAQNSKVEL
ESKLKDAELQ VAESTRKVKE LEKLYLSKSQ KWEKKECTYQ SFIDNQFGAL QALNATSASI
KQEVLRTQKK YFEDLNYYGL KLKGVADAAK NYHVVLEENR RLYNEVQELK GNIRVYCRIR
PFLPGQNSRQ TSIEYIGENG ELVVANPFKQ GKDTHRLFKF NKVFGQAATQ EEVFLDTRPL
IRSILDGYNV CIFAYGQTGS GKTYTMSGPS ITSKEDWGVN YRALNDLFNL TQIRQNTVVY
EVGVQMVEIY NEQVRDILSD GGSSRRLGVW NTALPNGLAV PDASMHSVRS TEDVLELMNI
GLMNRTVGAT ALNERSSRSH CVLSVHVRGV DVETDSVLRG SLHLVDLAGS ERVDRSEVTG
DRLKEAQHIN KSLSALGDVI FALAHKNPHV PYRNSKLTQV LQSSLGGQAK TLMFVQVNPD
GDSYAETVST LKFAERVSGV ELGAAKSNKE GRDVRHLMEQ VSSLKDVIAK KDEELQNVQK
LKGNNATVPK RGLSNLRLLG PSSPRRHSIG PSPNGRRGKP SGLFGRSTSD VDNCSEYSSK
HSDSGSQRSS DELKHRKDLH QLSKFAGGSK EIDLEDDIEL IGLGDADSED RLSDISDSCL
SMGTETDGSI SSAVELTLFP ETEKPLEITE RPEAHLAPEK PEKSAKMVKT VTKDKTSIPS
KIPKQTLKPP GQTRPSRLSI ATSSSSKALT SAKRPTISTS TSMKPLNRRR
//
