ID A0A087GSE5_ARAAL Unreviewed; 1059 AA.
AC A0A087GSE5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN OrderedLocusNames=AALP_Aa6g289700 {ECO:0000313|EMBL:KFK32797.1};
OS Arabis alpina (Alpine rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK32797.1, ECO:0000313|Proteomes:UP000029120};
RN [1] {ECO:0000313|Proteomes:UP000029120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT "Genome expansion of Arabis alpina linked with retrotransposition and
RT reduced symmetric DNA methylation.";
RL Nat. Plants 1:14023-14023(2015).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR EMBL; CM002874; KFK32797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087GSE5; -.
DR EnsemblPlants; KFK32797; KFK32797; AALP_AA6G289700.
DR Gramene; KFK32797; KFK32797; AALP_AA6G289700.
DR Proteomes; UP000029120; Chromosome 6.
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; 2.60.120.430; Galactose-binding lectin; 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; IPR021720; Malectin_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47972:SF18; KINESIN-LIKE PROTEIN KIN-14R; 1.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF11721; Malectin; 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 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:UP000029120}.
FT DOMAIN 415..737
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 343..408
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 758..924
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 11..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..1013
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1059
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 498..505
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1059 AA; 120249 MW; EF914C05CF73CB6A CRC64;
MEDIQINPTV PVDPEVTSPS SPEIPNSQFT TEKLEIGDTS MDMCEDSLAD SMVCDPNSRL
VPRGFTKANH TSDETIMFIN AGGDGSKVLD SELNILKDNY FEGGDVLRTD ESIVEAGDYP
FVYQSARVGN FCYMLNDLVP GEYFIDFHFA EIINTNGPKG IRVFNVYVQD EKVLAEFDIF
SVVGANRPLL LVDLRVMVMN DGLIRVRFEG INGSPVVCGI SLRKAPQVSV LRTSQDYIKC
ENCATEIEIS PTQKRLMRAK AHEKYEKKIE ELSERYQHKT NECHEAWMSL TSANEQLEKV
MMELDNKTYE ARSLDQTVVT QADCLKSINS KYDNDKRRWA TAIVTLQEKI EIMKREQFQL
SQEAHECVES IPELYKMVDG VQALVSQCED LKQKYSEEQA KRKELYNYIQ ETKGNIRVFC
RCRPLNKEET STRCATTVDF DGAKDGELGV ITGNNSKKSF KFDRVYTPKD GQVDVFADAS
PMVVSVLDGY NVCIFAYGQT GTGKTFTMEG TPQNRGVNYR TVEQLFEVAR ERRETISYDI
SVSVLEVYNE QIRDLLATSP ASKKLEIKQS SEGYHHVPGL VEAKVENINE VWNVLQAGSN
ARSVGSNNVN EHSSRSHCML SIMVKAKNLM NGDCTKSKLW LVDLAGSERL AKTDVQGERL
KEAQNINRSL SALGDVIYAL ATKSSHIPYR NSKLTHLLQD SLGGDSKTLM FVQISPSEHD
VSETLSSLNF ATRVRGVELG PARKQVDTGE IQKMKAMVEK ARQESRSKDE SIKKLEENIQ
NLEGKNKGRD HSYRSLQEKT KELESQLDTL HNQSEKQNAQ LLERLKSRDE TCANLQQKVK
ELECKLRERQ QSDSAAYHQK VKDLENKLKE SEGNSLVWQQ KIKELETKLK DEQSQEAVLL
RQKIKELEVR LKEQELHIQQ MATTREFPDV SSATPNEVKS CFKEDNFGNE NAESSNILRT
SNRLKTASTR RNDSLNPNEM TRKKRVSRSN ETENNGDDHM KEKRIRKSDP PKVLPRVVRP
TRPGSSNQVP VAQKKVVINR EQQVPVGKER DPRKKIWSR
//
