ID A0A2J6LLH7_LACSA Unreviewed; 1123 AA.
AC A0A2J6LLH7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=LSAT_5X102121 {ECO:0000313|EMBL:PLY88180.1};
OS Lactuca sativa (Garden lettuce).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC Lactucinae; Lactuca.
OX NCBI_TaxID=4236 {ECO:0000313|EMBL:PLY88180.1};
RN [1] {ECO:0000313|EMBL:PLY88180.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28401891; DOI=10.1038/ncomms14953;
RA Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., Xia L.,
RA Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., Xu H.,
RA Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.;
RT "Genome assembly with in vitro proximity ligation data and whole-genome
RT triplication in lettuce.";
RL Nat. Commun. 8:14953-14953(2017).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-14 subfamily.
CC {ECO:0000256|ARBA:ARBA00010899}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PLY88180.1}.
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DR EMBL; NBSK01003224; PLY88180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6LLH7; -.
DR STRING; 4236.A0A2J6LLH7; -.
DR EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_5X102121_mrna; cds-PLY88180.1; gene-LSAT_5X102121.
DR Gramene; rna-gnl|WGS:NBSK|LSAT_5X102121_mrna; cds-PLY88180.1; gene-LSAT_5X102121.
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; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47972:SF42; CALPONIN-LIKE DOMAIN-CONTAINING PROTEIN-RELATED; 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; 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}.
FT DOMAIN 18..148
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 730..1057
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 212..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 668..730
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 261..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..450
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 809..816
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1123 AA; 127960 MW; 9FC2210FA9FF6A49 CRC64;
MAETVATFTF SVGSMVEEVL QQQGLKLVEA NVPSKPNSKI GVVAAKDLPA EPSENAFRMG
LRSGIIFCKF INKIEPGAIS KIVEAPFDSV IIPDGEPLST SPYFENITNF LSAIEERQLP
SFEASDLEQG GRLLRVVNCV LALKAYGDWK KAGANGKFRW GYRKPSSERK EMVHKSLDMD
KCDDLWKEEV KDKVVEIVLS KLTQELERKV ETHKEQIAAN PPKEVDPNKA LRRAKSRDAK
SLDRRKSKKE EFIKMLNKEK DENAIPETRR KEEKKSFSSI INEMKKKATE DAVKSPMEIE
RRTPASTFAK KWGEVANEKA NTDTKKLGSD INNEMDKKST TDAMKNDPME KKATPDVKKS
TVDVSVKMEE KPTTVAIPKT DSVPSKNIIS YELEEEEEEE SEEEEESEEE EDSPESGSEK
GEEVEEEEEE EEKEEVEEEE EADEEEEAME AEHDAMQKEM ESELLEMQNT DTSDMSDAMK
KEMELKIIEK KKEMERKEME MKKEMERLEM EKKKEREAKE LQKKKEKEAR ELQKKKEREE
QELQRKKERE QKELERKKER EQKEAERLKG KEQKEEEKRK EREQREMEKK KEMEKMEMEK
KAKREMRENE RKKEMERKME IEKKKEMERK KEMERRAIED AKDKKYYDWV NSECDRYALP
NRDFDMMIQA LKNLFSTAKA DLETLRTNYQ KEFNALGNQM RNLAQAASGY KKVVEENRRL
YNEVQDLKGN IRVYCRSRPS GGKAGCVDCI DEGTMEVITG VKNGKEIRKP FTFNRVFGPG
ATQALVYKDT QPLIRSVLDG YNVCIFAYGQ TGSGKTWTMT GPDVFTEETM GVNYRALNDL
FGIREERKGM ISYTVSVQML EIYNEMIRDL LLTDGVSKKY PFPYHDIRLG AADGINVPDA
NLVPVTTTED VIRLMNLGHN NRAVGSTQMN ARSSRSHSCL TVHVAGKDLT TGTTVRGCMH
LVDLAGSERA DKTEATGDRL KEATFINKSL SALGDVIASL AQRSAHVPYR NSKLTLLLQD
ALGGQAKTLM FIHVRGDPDT VGETISTLKF AERVSSVELG AAKSNKDIIE LKELKEHVAF
LKSQLEKAGG ELPDMEAAAA PAKKAAASSP AAKTAAKPAP KKK
//
