ID   A0A0D9ZJC7_9ORYZ        Unreviewed;      1131 AA.
AC   A0A0D9ZJC7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
OS   Oryza glumipatula.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM04G08450.1};
RN   [1] {ECO:0000313|EnsemblPlants:OGLUM04G08450.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A., Panaud O., Oliveira A.C.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OGLUM04G08450.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-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   AlphaFoldDB; A0A0D9ZJC7; -.
DR   STRING; 40148.A0A0D9ZJC7; -.
DR   EnsemblPlants; OGLUM04G08450.1; OGLUM04G08450.1; OGLUM04G08450.
DR   Gramene; OGLUM04G08450.1; OGLUM04G08450.1; OGLUM04G08450.
DR   eggNOG; KOG4280; Eukaryota.
DR   HOGENOM; CLU_009194_0_0_1; -.
DR   Proteomes; UP000026961; Unassembled WGS sequence.
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; 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   Microtubule {ECO:0000256|ARBA:ARBA00022701};
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:UP000026961}.
FT   DOMAIN          137..458
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          33..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          465..492
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          799..836
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          910..947
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          982..1065
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        72..86
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         217..224
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1131 AA;  124783 MW;  9D80D68CCA953A56 CRC64;
     MSTALRRAWS SLNGNDNVLP YFLCITLNEH GRHPATPPPP SLSAGGGGGD TPPSRRRVPK
     ENVDPGSSPA GHSPFRSPTS SAKPLGNRNR GLLPPRPPSS NPLKRKLDVS PAAAADSSGG
     AAAAAAGGGG GPAPDSGVQV VVRIRPPCRV EEEDDARAPD LCVRKTATNS VAIQGQDFTF
     DAVADEVSTQ EDIFKLVGLP LVENCLSGFN SSIFAYGQTG SGKTYTMWGP LSALSEDSTC
     SERGLTPRVF EQLFSRIKEI YNEQITDLLD PSPKSLQIRE DVRTACVYVE SLTKELVFTT
     KDVTQLLVKG LSNRRTGATS ANADSSRSHC VFTCVIKSES KNLEDGSNST RTSRINLVDL
     AGSERQKLTH AFGDRLKEAG NINRSLSQLG NLINILAEIS VSGKQRHVPY RDSKLTFLLQ
     ESLGGNAKLA MICAVSPSQS CKSETLSTLR FAQRAKSIKN NAVVNEQKEE DVNMLREQIR
     QLKDELHRMK SGGSDGSNGS FSTGWNARRS LHLLKMSLSR PTTFQTIHED SGDVEMEIDE
     NDVEKPYNQD NMVISPPGDK ECKELQASLK INGGTSLDVF DGENLMPTKR SCSDDRYKLN
     LAASIQRGLQ VIENHQNNGA WRRASVGFNA RIVDVQPCKV DVAIQTEPEE SEARDNPLAL
     ISSHVLGTSA TVSNDPNACR DLQLVQYDAG ITRDEPKQQQ ILKAVEKVLA GAIRREMARD
     EQCVKQAAEI QQLNRLVQQY KHERECNAVI AQTREGKIAR LESLMDGTLP TEEFINEEYL
     SLMNEHKILQ QKYENHPELL RAEIELKRLQ EELELCRNYI DEKEVLQEEI QDLKSHLHFM
     LSSSASIRRL WPPVQLSQGV GPSPVTNDAD GDTNAVDTSD WAEAESKWVT LTEELRVELE
     ANKSLVGRLR SELESEKKCS EEVKEALQTA MQGHARILEQ YAELEERHIG LLAMHRKIRE
     GVEDVKARAA KAGVKGAELR FINSLAAEMA VLRAENKGLQ DQLGDTAEAV QAAGELLVRL
     KEAEEAEALA QRRALLAEQE TEKAYQEIDN LKKNYDQEIV ALNQRLSESS HHHETTLAIE
     ACDMETAKYD KVGSPGDQQW REEFNQKGGS FEVSKSTDLN SWFSGYDKCN I
//