ID   A0A0D9VG31_9ORYZ        Unreviewed;      1054 AA.
AC   A0A0D9VG31;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
OS   Leersia perrieri.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX   NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR02G13680.3, ECO:0000313|Proteomes:UP000032180};
RN   [1] {ECO:0000313|EnsemblPlants:LPERR02G13680.3, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.A.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:LPERR02G13680.3, ECO:0000313|Proteomes:UP000032180}
RP   NUCLEOTIDE SEQUENCE.
RA   Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA   Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA   Zhang J., Wing R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:LPERR02G13680.3}
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   EnsemblPlants; LPERR02G13680.3; LPERR02G13680.3; LPERR02G13680.
DR   Gramene; LPERR02G13680.3; LPERR02G13680.3; LPERR02G13680.
DR   Proteomes; UP000032180; Chromosome 2.
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; 2.
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:UP000032180}.
FT   DOMAIN          129..381
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          995..1024
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          406..433
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          719..749
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          944..978
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        12..31
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         208..215
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1054 AA;  117226 MW;  FC353646F144EED0 CRC64;
     MRSLFSSRLS RVPASPPPPS ASAPSPSTPP STPTAAYACS APRSXXXTPS SHGRHRRFHK
     ENVDPASSPA APGGGPYDHS PYRSPSGKPL AAKNRSLPPR PPLKRKLLDV SAVPATDTAA
     NGCGGGDSGV QVVVRVRPPS RAEEDEGAGK EVCVRKTGPG SVEIQGQGFT FDSVADEAST
     QEDIFQLVGR PLVENCLAGF NSSIFAYGQT GSGKTYTMWG PLSALSDGTA SKERGLTPRV
     FELLFSRIKE IYNEQITDLL DPMQRNLQIR EDVGTASVYV ESVTKEFVST IKDVTQLLEK
     GLANRRTEAT TANAESSRSH CVFTCFIKSE SKNMEDGSNF TRTSRINLVD LAGSERQKLT
     NAAGDRLKEA GNINRSLSQL GCKSETLSTL RFAHRAKDIK NNAVVNEQRE DDVNVLREQI
     KQLKEELHRV RSNGSFPGSN GSPSAGWNAQ NSLLLKMSLN RPTAFPPIKD ESDEEMEIDD
     NDVEKPCNLE KTSSSFYGDI EESRCKSNLA ASIQKGLQVI ESHRNSVAWR RSSIGLNTRL
     MDGHLSVPVC KVDVAIQTDP EESEPRENTM ALIPSSQTEA TMDENRDNSD HMDLQLVTVD
     GTIHSNDLKQ QGQVLKAVEK VLAGAIRREM LRDKQCAKQA AEIQQLKRLV QQYKHERECN
     AAIAQIREEK IARLETLVDG ILPTEEVMHA ENLALQDENK ILHQKYENHP EVFSAKIELE
     RIQEELERYR NFKDEKEVLL EEIQNLKNQL HYMLSSSTTL CRPPVEMVQA INTASDRPTI
     SALEEAGDDG HSIAEAAESR WITLTEELRV ELEKCRSLSD HLQLELESEK KCSEELKGAL
     EMAMQGHARI LEQYCELQEK HASLRSMCHA INDGIEDVKK EAAKAGVRGA ESKFINALAR
     EISNLRYQRE KERRFWMDEN KGLQQQLSDT AEAVQAAGEL LVRLNDAEEF ASLAQKRAEL
     AEQEMNKAFE EIDDLKRNHE QEVLVLNQRF AESKLPSNVV QSPEPSETGP ARYDTGGSFG
     DEQWREEFKP FQSVEVSKSS DPSSWFYGYD KCNI
//