ID A0A0D3AD39_BRAOL Unreviewed; 904 AA.
AC A0A0D3AD39;
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-like protein {ECO:0000256|RuleBase:RU000394};
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:Bo1g123370.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo1g123370.1, 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:Bo1g123370.1}
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 AlphaFoldDB; A0A0D3AD39; -.
DR SMR; A0A0D3AD39; -.
DR STRING; 109376.A0A0D3AD39; -.
DR EnsemblPlants; Bo1g123370.1; Bo1g123370.1; Bo1g123370.
DR Gramene; Bo1g123370.1; Bo1g123370.1; Bo1g123370.
DR eggNOG; KOG0246; Eukaryota.
DR eggNOG; KOG0700; Eukaryota.
DR HOGENOM; CLU_001485_19_0_1; -.
DR OMA; PFIPKEM; -.
DR Proteomes; UP000032141; Chromosome C1.
DR GO; GO:0005795; C:Golgi stack; IEA:EnsemblPlants.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0009531; C:secondary cell wall; IEA:EnsemblPlants.
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:0090058; P:metaxylem development; IEA:EnsemblPlants.
DR GO; GO:0007019; P:microtubule depolymerization; IEA:EnsemblPlants.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0009834; P:plant-type secondary cell wall biogenesis; IEA:EnsemblPlants.
DR GO; GO:1903338; P:regulation of cell wall organization or biogenesis; IEA:EnsemblPlants.
DR GO; GO:0010090; P:trichome morphogenesis; IEA:EnsemblPlants.
DR CDD; cd01367; KISc_KIF2_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; PTHR47971:SF8; KINESIN-LIKE PROTEIN KIF24; 1.
DR PANTHER; PTHR47971; KINESIN-RELATED PROTEIN 6; 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 237..570
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 211..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 748..779
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 625..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..708
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 326..333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 904 AA; 102055 MW; 70060B7843FC2B82 CRC64;
MQIHGWKFQI RRKRNEFADF MFESPHFVSI RSPKLAPQRR SQRHMGGHMQ QTNAAAATAL
YDAGPANDAG DAVMARWLQS AGLQHLGSPV ASTGNNDQRH LPNLLMQGYG AQTAEEKQRL
FNLMRNLNFN GESTSESYTP TYQASSAMPS SEGFFSPEFR GDFGAGLMDL HAMDDTELLS
EHVITEPFEP SPFMPSVNKE FEEDFNLPAN RQQRQQTDAE PLGSLPKSEK ENTSVAKIKV
VVRKRPLNKK EIARKEEDVV TVSDNSLTVH EPKLKVDLTA YVENHEFCFD AVLDEDVSND
EVYRATIEPI IPIIFQRTKA TCFAYGQTGS GKTYTMKPLP IRAVEDLMRL LRQPVYSNQR
FKLWLSYFEI YGGKLFDLLS ERKKLCMRED GRQQVCIVGL QEYEVSDVQI VKDFIEKGNA
ERSTGSTGAN EESSRSHAIL QLVVKKHVEV KETRRKNNDA KELPGKVVGK ISFIDLAGSE
RGADTTDNDR QTRIEGAEIN KSLLALKECI RALDNDQLHI PFRGSKLTEV LRDSFVGNSR
TVMISCISPS VGSCEHTLNT LRYADRVKSL SKSGNSKKDQ TANSMPPVNK EALLASNDVE
DIFEPPQEVN VQETGRRIEK ESYTTSTTDF RQPTSFREES GIPSISMDKG RSETNNSSFG
GSASQRNHLS SYPQETSDRE EKVKKVSPPR GKAWREEKPD RPPQNLSKRD VRSSDIPTLT
SFRQNTSETA SRQYETDTSL DENIDALLEE EEALIAAHRK EIEDTMEIVR EEMKLLAEVD
QPGSMIENYV TQLSFVLSRK AAGLVSLQAR LARFQHRLKE QEILSHSNPR SNHSSAPSQT
LPHANFLHRT RQTNSPLCIM QRSFTLEELM NVPAGWRRRY HDDVTVMVIT FGTDQRTSKA
SPFV
//