ID A0A0D3DIE0_BRAOL Unreviewed; 1049 AA.
AC A0A0D3DIE0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=106306279 {ECO:0000313|EnsemblPlants:Bo7g119380.1};
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:Bo7g119380.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo7g119380.1, 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:Bo7g119380.1}
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}.
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DR RefSeq; XP_013598292.1; XM_013742838.1.
DR AlphaFoldDB; A0A0D3DIE0; -.
DR STRING; 109376.A0A0D3DIE0; -.
DR EnsemblPlants; Bo7g119380.1; Bo7g119380.1; Bo7g119380.
DR GeneID; 106306279; -.
DR Gramene; Bo7g119380.1; Bo7g119380.1; Bo7g119380.
DR KEGG; boe:106306279; -.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_004957_0_0_1; -.
DR OMA; NDKCSEN; -.
DR OrthoDB; 5476186at2759; -.
DR Proteomes; UP000032141; Chromosome C7.
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 CDD; cd16649; mRING-HC-C3HC5_CGRF1-like; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF35; KINESIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
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};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 97..414
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 1002..1037
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 430..498
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 692..755
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 784..811
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 855..903
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 177..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1049 AA; 115880 MW; 23DE9431237CE81C CRC64;
MASSSSRTRS SSPFSNNRPA SPSSSTSSSH LSNRLLPRSS STSGGGIGSR SMTPSRTFSD
YGPIGSESFG TGSSVPYPSE ELLGEPVEET ISSERDSISV TVRFRPLSDR EYQRGDEVAW
YPDGDTMVRH DYNPLTAYAF DKVFGPQANT MDVYDVAARP VVKAAMEGVN GTVFAYGVTS
SGKTHTMHGD QESPGIIPLA IKDVFSIIQD TPGREFLLRV SYLEIYNEVI NDLLDPTGQN
LRVREDSQGT YVEGIKEEVV LSPGHVLSFI AAGEEHRHVG SNNFNLMSSR SHTLFTLMIE
SSATGDEYDG VIFSQLNLID LAGSESSKTE TTGLRRKEGS YINKSLLTLG TVIGKLSEGK
ATHIPYRDSK LTRLLQSSLS GHGHVSLICT ITPASSSNEE THNTLKFASR AKSIEIYASR
NQIIDEKSLI KKYQREISIL KLELDQLRRG MLVGVSHEEL ISLKQQLEEG QVKMQSRLEE
EEEAKAALMS RIQKLTKLIL VSTKNSRTGY LGDVPTHQRS LSAGNDDKFA SLLDNDNLGS
PSSTLALVSD GSLGFNHRRS SSKLNGENSP GAEITQGVIT PDEIDLLVEQ VKMLAGEIAF
SMSTLKRLVD QSVNDPENSQ TQIQDLEREI QEKQGQMRAL EQLIIESGEA SIANASLVEM
QQKVMSLMTQ CNEKSFELEI KSADNCILQE QLQKKCTENK ELHEKVNLLE QRFKAVSSEK
SASSGEYADE LKRKIQSQEI KNEKLKLEHV QIVEENSGLR VQNQKLAEEA SYAKELASAA
AVELKNLASE VTKLSLQNTK LEKELAAARD LAQTRNPMNG VNSRKYNDGS RSGIKGRISS
GRSSGDEFHS RSLDLEDLKM ELKARKQREA VLESALSEKE FIEEEYRKKA EEAKRREEAL
ENDLANMWVL VAKLKKDNGA SSEVNGTATD PAREIEKNQS NTVLKERQVS SAPRQPEVVV
VAKTEETPKE EPLVARLKAR MQEMKEKEMK SQANGDANSH ICKVCFESPT AAILLPCRHF
CLCKSCSLAC SECPICRTKI SDRLFAFPS
//
