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Database: UniProt
Entry: A0A4P1RWF3_LUPAN
LinkDB: A0A4P1RWF3_LUPAN
Original site: A0A4P1RWF3_LUPAN 
ID   A0A4P1RWF3_LUPAN        Unreviewed;       707 AA.
AC   A0A4P1RWF3;
DT   03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   03-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=TanjilG_18511 {ECO:0000313|EMBL:OIW19701.1};
OS   Lupinus angustifolius (Narrow-leaved blue lupine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX   NCBI_TaxID=3871 {ECO:0000313|EMBL:OIW19701.1, ECO:0000313|Proteomes:UP000188354};
RN   [1] {ECO:0000313|EMBL:OIW19701.1, ECO:0000313|Proteomes:UP000188354}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC   TISSUE=Whole plant {ECO:0000313|EMBL:OIW19701.1};
RX   PubMed=27557478; DOI=10.1111/pbi.12615;
RA   Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA   Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA   Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA   McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT   "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT   an emerging health food: insights into plant-microbe interactions and
RT   legume evolution.";
RL   Plant Biotechnol. J. 15:318-330(2017).
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   EMBL; CM007361; OIW19701.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4P1RWF3; -.
DR   STRING; 3871.A0A4P1RWF3; -.
DR   Proteomes; UP000188354; Chromosome LG01.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005819; C:spindle; IEA:UniProt.
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   GO; GO:0006996; P:organelle organization; IEA:UniProt.
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; PTHR47968; CENTROMERE PROTEIN E; 1.
DR   PANTHER; PTHR47968:SF13; KINESIN-LIKE PROTEIN; 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|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:UP000188354}.
FT   DOMAIN          143..473
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          33..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          526..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          631..707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          496..525
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          572..606
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        631..651
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..707
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         235..242
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   707 AA;  78751 MW;  FEB2FD1E0E94912F CRC64;
     MPVSTRSQFR NPHHGLKEKL KALTLLYEQQ KQTSTSLRNS YSKPQQNEQK NVMRENRVPH
     LTNSTVTRTF VLIEPPSNVA KENFAVGSDK IVGFSCVRKP STVLSSNIVA RKLSLGNGGM
     VESEKMETVL EKQGKVVGVG ESRILVFVRV RPMNKKEKEV GSRCCVKIAN RRDVYLSEFA
     NENDYLRLNR VRGRHFTFDA SFPDSATQHE VYSTTTSELV EAVMQGRNGS VFCYGATGAG
     KTYTMLGTLE NPGVMVLAIK DLFSKIRQRS CDGSHVVHLS YLEVYNETVR DLLSPGRPLV
     LREDKQGIVA AGLTQYRAYS TDEVMALLQQ GNQNRTTEPT RANETSSRSH AILQVVVEYR
     DRDSSMNIVN RVGKLSLIDL AGSERAHATD QRTLRSLEGA NINRSLLALS SCINALVEGK
     KHIPYRNSKL TQLLKDSLGG TCNTVMIANI SPSNLSFGET QNTVHWADRA KEIRLKVSDA
     NEDLLPIPET DRDQAKLVLE LQKENHELRV QLAKQQQKLL TLEAQSLAAH SSPTPPSATS
     LFTPPTSAQP TEKRRTRSSF LAGTCITPES NKKGAELVVR TLQRTVKALE AQIERMKKDH
     SLQLKQKDDL IHELSQKSGK QAVDEVGKRV LTRASLRPKE PNNDELKSPS HRFRSPVVPT
     AKKRSYWDIT TTNSPSIATS NGRKTRSHVI SEPTTAPPPR SSMLLQV
//
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