ID U5CYU8_AMBTC Unreviewed; 415 AA.
AC U5CYU8;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=AMTR_s00056p00107210 {ECO:0000313|EMBL:ERN15130.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN15130.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283,
CC ECO:0000256|RuleBase:RU000394}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR EMBL; KI392510; ERN15130.1; -; Genomic_DNA.
DR AlphaFoldDB; U5CYU8; -.
DR STRING; 13333.U5CYU8; -.
DR EnsemblPlants; ERN15130; ERN15130; AMTR_s00056p00107210.
DR Gramene; ERN15130; ERN15130; AMTR_s00056p00107210.
DR eggNOG; KOG0239; Eukaryota.
DR HOGENOM; CLU_053962_1_0_1; -.
DR OMA; HTNSRAT; -.
DR Proteomes; UP000017836; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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; PTHR47972:SF14; KINESIN-LIKE PROTEIN KIN-14O; 1.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 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|RuleBase:RU000394};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Microtubule {ECO:0000256|RuleBase:RU000394};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175,
KW ECO:0000256|RuleBase:RU000394};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU000394};
KW Reference proteome {ECO:0000313|Proteomes:UP000017836}.
FT DOMAIN 1..156
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 209..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..197
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 288..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 415 AA; 44793 MW; E1BF6B579211EB66 CRC64;
MHTVESTADV IELMQIGLMN RAIGATALNE RSSRSHSVLT VHVRGLDLKT GAALRGSLHL
VDLAGSERVD RSEATGDRLK EAQHINKSLS ALGDVISALA QKSSHVPYRN SKLTQILQSS
LGGQAKTLMF VQLNPDVESY SETISTLKFA ERVSGVELGA AKSSKESKDI RDLMEQVVSL
KEVLARKDAE IERLQTLRDL KFQPLDPYLT GDKRSMSTGK LTLSPGRPSI GAGLHKNRKA
GSGRPVGPLD SVKAASDIDN CSEYSDRNSE AGSQQSLEDF KHLKDFDGQA KYDTGGEREQ
SVRTGDVDLL GFGEADSEER LSDISDGGLS MGTETDGSIS SVVEFTLFPD ASKPVDNSEK
RLKVPSRVPR PPMKPGQTAS ARVPSKLSTK NASSSRRAST DQAHSSSSKS SKRWQ
//
