ID   A0A0E0MPM0_ORYPU        Unreviewed;       992 AA.
AC   A0A0E0MPM0;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   22-FEB-2023, entry version 36.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
OS   Oryza punctata (Red rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC12G17070.1};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC12G17070.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OPUNC12G17070.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283,
CC       ECO:0000256|RuleBase:RU000394}.
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DR   AlphaFoldDB; A0A0E0MPM0; -.
DR   EnsemblPlants; OPUNC12G17070.1; OPUNC12G17070.1; OPUNC12G17070.
DR   Gramene; OPUNC12G17070.1; OPUNC12G17070.1; OPUNC12G17070.
DR   HOGENOM; CLU_007631_1_0_1; -.
DR   Proteomes; UP000026962; Chromosome 12.
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; cd01366; KISc_C_terminal; 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; PTHR47972:SF35; KINESIN-LIKE PROTEIN KIN-14Q; 1.
DR   PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 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|ARBA:ARBA00022701, 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:UP000026962}.
FT   DOMAIN          320..646
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          734..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          963..992
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          171..205
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          241..306
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          674..715
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         403..410
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   992 AA;  108547 MW;  50D3D5E94CF5BDDE CRC64;
     MEMEEEGSGR GGDRAAAHGS GGRRIGSVAS FAAGGASPEE ASASVRKTVK MAETCDFIPY
     GDDDVDGGNS EAPACRRGAA ARHRIAPLEL FSVPSPPQDP PSPANCSAAL EASNNAVVAP
     EVHPPEGISS IISTGGGEQE TTMGLQSVHE TPHIEENEGK CSYCGQLKQE YSLLLREKEE
     CRRVLEDLMR ENELKSRECH EAQASLHELR MELMRKSMHV GSLAFAVEGQ VKEKSRWCQL
     LNDLSEKFKA LKAEHQILLQ ESLECKRFVA DATQMTTTIQ QHVNKYASLE CEFKDLKEKF
     TEEAKERKDL YNKLIELKGN IRVFCRCRPL NGEEIEEGAS LAVDFESAKD GELIVRGHVS
     SKKVFKFDSV FNPEEDQEKV FEKTAPFATS VLDGYNVCIF AYGQTGTGKT FTMEGIEGAR
     GVNYRTLDEL FRIIKERQGL FQYEITVSVL EVYNEQIHDL LLTGTQPGAT TKRLEVRQVA
     EGVHHVPGLV EARVTNMNEA WDVLQTGSKA RVVGSTNANE HSSRSHCMHC VMVKGENLMN
     GEQTKSKLWL IDLAGSERVA KTDAQGERLK EAQNINKSLS ALGDVISALA TKSQHIPFRN
     SKLTHLLQDS LSGDSKTLMF VQISPNENDV GETLCSLNFA SRVRGIELGQ ARKQVDVGEL
     SRYKLMAGRA KQDSKNKDAQ IKSMEETIQS LEAKNKAKDL LTMNLQEKIK ELEAQLLVER
     KIARQHVDNK IAQDHLHQQQ QQSMKPENSP YLTRSPMAER NLNSTAEKPA LLHKDFGIAK
     QMFSDSNTDT YSINHLMSMS SEKENNPVGG AQPTKARRVS LCGGAHHHQQ QQPAAPPRRG
     SLIPLPRRNS LMLPLPLPKP ATPAAAASPL DMITEQCSSP PVIAPNDNRA GIGGGGGGGR
     NKRIINSILR RSLQKKVIIR PPLMAAHQSG RRAGAGVVGA TTHGGGGGGG GGGMMRARRV
     PVSGGRGGGG VQHNREKERG WNNATSLRQL NS
//