ID A0A0D3AB35_BRAOL Unreviewed; 1334 AA.
AC A0A0D3AB35;
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:0000259|PROSITE:PS50067};
GN Name=106313485 {ECO:0000313|EnsemblPlants:Bo1g101480.1};
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:Bo1g101480.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo1g101480.1, 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:Bo1g101480.1}
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-12 subfamily.
CC {ECO:0000256|ARBA:ARBA00034488}.
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DR RefSeq; XP_013606760.1; XM_013751306.1.
DR STRING; 109376.A0A0D3AB35; -.
DR EnsemblPlants; Bo1g101480.1; Bo1g101480.1; Bo1g101480.
DR GeneID; 106313485; -.
DR Gramene; Bo1g101480.1; Bo1g101480.1; Bo1g101480.
DR eggNOG; KOG4280; Eukaryota.
DR HOGENOM; CLU_009194_0_0_1; -.
DR OMA; GDQQWRE; -.
DR OrthoDB; 467304at2759; -.
DR Proteomes; UP000032141; Chromosome C1.
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; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR044986; KIF15/KIN-12.
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; PTHR37739:SF16; KINESIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR37739; KINESIN-LIKE PROTEIN KIN-12D; 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 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 95..430
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1285..1304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 437..464
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1075..1140
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1210..1251
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1334 AA; 148190 MW; 34ACCFA92B95B998 CRC64;
MKHFMMPRNA VVRDIGEPQS PNPSLTKSKS QRKTRSAKEN APPPDPNSLP PDYRSSPAKL
KSPLPPRPPS ANPLKRKLIA EAASDNGVAG VSDSGVKVIV RVKPPSKGEE EEMIVKKISS
DALTINDHTF TFDSIADPDS TQDEIFQLVG APLVENCLAG FNSSVFAYGQ TGSGKTYTMW
GPANGLLEEH LIGDQRGLTP RVFELLFARI SEEQVKHAER QLSYQCRCSF LEIYNEQITD
LLDPSQKNLM IREDVKSGVY VEYLTEENVK NLKDLSGLLI KGLANRRTGA TSVNAESSRS
HCVFTCVVES HCKSAADGLS NFKTSRINLV DLAGSERQKS TGAAGERLKE AGNINRSLSQ
LGNLINILAE ISQTGKQRHI PYRDSRLTFL LQESLGGNAK LAMVCAVSPS QSCRSETFST
LRFAQRAKAI QNKAVVNEVM QDDVNFLREV IRQLREELQR VKNNGNNPAN PNAAYATSWN
ARRSMSLLRS FGLSHPKSLA NGDDDGDTEM EIDEEAVERL CAQIGLQSSP PAEENNPDTS
RVEKINPSLH TVALEDENYE NSHLQSSDGQ STGKQFPENT DVNMEDASCQ TENHEAVTIN
NEPTVEETGI TAAVQTMDHG SSVLPHLITN SLGSPISDTD HDNSLGKAEN IPSCQDLVPG
ALASSIASVA DASDDTEHFS IIPASPCLSI DPASASHVLI TPTESVSPRI RNSRKSLRTS
SMSTASQKYI ERANQVTTEI VEPSSAVSTE MLNLPSALST QKSGAFPVPT NQLAASLHRG
MKILDSYRQS TAQRRSTFGF SYKALECKPS TVLSKADVGV QTYPEADIIA EENPKEVVCI
KCKCIAECDV QETSDISNRQ SVTVDNSEKS SFQVPKAVEK VLAGSIRREM ALEEYCTKQA
SEISQLNRLV QQYKHERECN AIIGQTREDK IVRLEGLMDG VLSKDDFLDE EFASLMHEHK
LLKDMYENHP EVLQTRIELK RAQEELESFK NFYGEMGERE VLLEEIQDLK AHVHCYTDTS
LTSSRKRGSL LKLTYTCDPN PAPPLNAIPE SVEESPEKTL EQERLRWTEA ERNWISLAEE
LKNELDTNRK LMEKQKRELD TEKRCTEELT EAMQMAMKGH ARMIEQYADL EEKHIQLLAR
HRRIREGIDD VKKAAARAGV KGAESRFINA LAAEISALKV QREKEAQYFR DENKSLQSQL
RDTAEAVEAA GELLARLKEA EEGLKIAQKR ATDAEYQASE AYKQIEKLKS KQETGISTLN
QQQHIAESHN HIESLQASLH GDDMAKYDEP VEEPSASSGD EQWREEFEPF YKKDAELAKL
AEPSWFSGYD RCNI
//