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Database: UniProt
Entry: A0A078I8G7_BRANA
LinkDB: A0A078I8G7_BRANA
Original site: A0A078I8G7_BRANA 
ID   A0A078I8G7_BRANA        Unreviewed;       916 AA.
AC   A0A078I8G7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   Name=BnaC04g33010D {ECO:0000313|EMBL:CDY46382.1};
GN   ORFNames=GSBRNA2T00083921001 {ECO:0000313|EMBL:CDY46382.1};
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY46382.1, ECO:0000313|Proteomes:UP000028999};
RN   [1] {ECO:0000313|EMBL:CDY46382.1, ECO:0000313|Proteomes:UP000028999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX   PubMed=25146293; DOI=10.1126/science.1253435;
RA   Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA   Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA   Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA   Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA   Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA   Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA   Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA   Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA   Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA   Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA   Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA   Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA   Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT   "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT   Brassica napus oilseed genome.";
RL   Science 345:950-953(2014).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. KIN-14 subfamily.
CC       {ECO:0000256|ARBA:ARBA00010899}.
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DR   EMBL; LK032665; CDY46382.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078I8G7; -.
DR   STRING; 3708.A0A078I8G7; -.
DR   PaxDb; 3708-A0A078I8G7; -.
DR   EnsemblPlants; CDY46382; CDY46382; GSBRNA2T00083921001.
DR   Gramene; CDY46382; CDY46382; GSBRNA2T00083921001.
DR   OMA; SMKMGST; -.
DR   Proteomes; UP000028999; Unassembled WGS sequence.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0007017; P:microtubule-based process; IBA:GO_Central.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
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:SF32; KINESIN-LIKE PROTEIN KIN-14K; 1.
DR   PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50021; CH; 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:UP000028999}.
FT   DOMAIN          33..136
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          445..757
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          796..916
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          280..396
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        796..826
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        833..864
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        865..879
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        880..910
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         529..536
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   916 AA;  103396 MW;  8600685876BBE857 CRC64;
     MNNRIKGGSS MIGVYGRPYG SSSILSFDGS ESRQSHQSLV EWLNETLPYL KLPWEASEEE
     LRACLMDGTV FCNLLNQLSP GSMKMGSTFE LASINIERFL TAMDEMALPR FEVSDLEQGD
     MIPVLQSLKA LKASFSDAGY DKNTLSSMRR WSLPEDQSKG LDGNFNDGLQ SKEVSEINTS
     HAKILDLLKS NTLQNTSTRS LFDMLDKLLD ESVYKMNVDV SHDFASILRG IVQVVEQRIS
     NQAENLKNQN ILFRVREEKY RSRINVLENL ASGTTDENEL RSEEQDVLQL KRKKERSDAE
     LSKLKQELEV LKETHEKQFL ELELYAQEAK TVLEKQLEES ELRVVDSTNK VKELEKLCEI
     KTKIWEKKEQ TYKSFIHNQS EALQELKATS MSLKHEVLKT GENYFQDLNY YGLKLRGVVH
     AAKNYQVVVE ENRRLYNEVQ ELKGNIRVYC RIRPFLKGQN KKETSIEYTG ENGELVVANP
     LKQGKDTHRF FKFNKVFGPS STQEEVFLDT QPLIRSLLDG YNVCIFAYGQ TGSGKTYTMS
     GPSINSEEHW GVNYRALNDL FHLTQSSQNT VMYEVGVQMV EIYNEQVRDL LSDDGPIPDA
     SMHCVRSTDD VLELMNIGLM NRAVGATALN EKSSRSHSVL SVHVRGVDVK TDSELRGSLH
     LVDLAGSERI DRSEVTGDRL KEAQHINKSL SALGDVIFAL AHKNPHVPYR NSKLTQVLQN
     SLGGQAKTLM FVQINPDEDS YAETVSTLKF AERVSGVELG AARSYKEGRD VRQLMEQVSN
     LKDMIAKKDE ELQKFQNING ASPNSSRQRQ GSRLLGRTTS DSADERLQQN ESPKLSETDG
     SNLFSVTSSP LEMSEQSEQN EKANVEPSKV LKHTLKADQT RPSRLSISTS SSMALTGSKR
     QINGFSTSVK PLTRKR
//
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