ID A0A078FP22_BRANA Unreviewed; 977 AA.
AC A0A078FP22;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN Name=BnaC02g01900D {ECO:0000313|EMBL:CDY14073.1};
GN ORFNames=GSBRNA2T00078608001 {ECO:0000313|EMBL:CDY14073.1};
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:CDY14073.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY14073.1, 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. {ECO:0000256|PROSITE-ProRule:PRU00283,
CC ECO:0000256|RuleBase:RU000394}.
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DR EMBL; LK032040; CDY14073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078FP22; -.
DR STRING; 3708.A0A078FP22; -.
DR PaxDb; 3708-A0A078FP22; -.
DR EnsemblPlants; CDY14073; CDY14073; GSBRNA2T00078608001.
DR Gramene; CDY14073; CDY14073; GSBRNA2T00078608001.
DR OMA; EATRCHE; -.
DR Proteomes; UP000028999; 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 CDD; cd01374; KISc_CENP_E; 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; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF9; KINESIN MOTOR DOMAIN-CONTAINING 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:UP000028999}.
FT DOMAIN 72..391
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 393..469
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 665..692
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 734..856
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 915..942
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 9..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..620
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 152..159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 977 AA; 109157 MW; 082D12D0A860F748 CRC64;
MAPRQVPKSR KAGSSSKLKA ANSSPASSTA SSPILYPETS VDSHSSPTSS SVRSKAQYTR
RVPQNASQSK ENVTVTVRFR PLSPREIRRG EEIAWYADGE TIVRNEHTQS IAYAYDRVFG
PTTTTRQVYD VSAQHVVNGA MEGTNGTIFA YGVTSSGKTH TMHGDQRSPG IISLAVKDAF
DIIQETPRRE FLLRVSYLEI YNEVVNDLLN PVGQNLRIRE DEQGAFIEGI KEEVVLSPAH
ALSLIAAGEE HRHIGSTSFN LLSSRSHTMF TLTIESSPLG GNNEGEAVHL SQLNLIDLAG
SESSKAATSG LRRKEGSYIN KSLLTLGTVI SKLTDRKASH VPFRDSKLTR LLQSSLSGHG
RVSLICTVTP ASSCTEETHN TLKFAHRAKH IEIQAAQNKI IDEKSLIKKY QNEIRQLKEE
LEELKQGIKP VSQLKDISED NIVLLKQKLE EEEDAKAALL SRIQRLTKLI LVSAKTPQTS
RVSHRVVPRR RHSFGQEELA YLPYKRRDLM DEENLELYVS GEANPEIIDN DAFREEKKTR
KHGLLNWLKL KKKDNGLGES SISDKSSAVK SNSILSTPQG EGSNFHTESK LSEGSPLADQ
RLEPGEDIES LEDSSHEIET PEARRRTIDQ MDILREQQKI LSEEMALQSK SFKQLSEEAI
KAPQNEEIKA EIINLNDNIK AKNDQIAELG KQILDFVMAS HDALDKSDIV QAVSEMRAQL
NEKSFELEVK AADNRIIQEQ LNQKTCECEA LQEEVANLKQ QLSDALELGE DMRSITSHMQ
QNEEKVIQAQ AFEIEELKLK AAELSELKEE LELRNQKLAE ESSYAKELAS AAAVELRALS
EEVASLMNRN ERLAADLAAA HKSSVTPRGK TGNPRNGRKE SPLVKRKEQQ DGSLMELKRE
LSVIKEREVS FEAALVEKVQ REAELQRTIE ESKEREAYLE NELANMWVLV AKLRRSQGDS
SDISVSETRQ QTGHFGT
//
