ID   A0A1D6NS28_MAIZE        Unreviewed;      1046 AA.
AC   A0A1D6NS28;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   22-FEB-2023, entry version 34.
DE   SubName: Full=Kinesin-like protein KCA2 {ECO:0000313|EMBL:AQL01078.1};
GN   ORFNames=ZEAMMB73_Zm00001d044903 {ECO:0000313|EMBL:AQL01078.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:AQL01078.1};
RN   [1] {ECO:0000313|EMBL:AQL01078.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQL01078.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM000785; AQL01078.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6NS28; -.
DR   ExpressionAtlas; A0A1D6NS28; baseline and differential.
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   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
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:SF22; KINESIN-LIKE PROTEIN KIN-14A-RELATED; 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; 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   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283}.
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          593..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          657..717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          830..859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          466..507
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        593..623
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..675
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..717
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         223..230
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1046 AA;  115438 MW;  9F9518D57BF6C0AB CRC64;
     MADSRRTWSW DVSGFEPPQP ATTQAASAPT AMPRAPPTAM MPRPSAGAPR ASAGAVPVAD
     QLDQLVDSVQ LAREDCLELR QEASDLLEYS NAKLGRVTRY LGFLADRTRK LDQAALETEA
     RITPLIHEKK RLFNDLLTLK GNVKVFCRCR PLFEDEGPSV LEFPDDFSIR VNTGDESLTN
     PKKDYEFDRV YGPHIGQGEL FLDVQPFVQS ALDGYNISIF AYGQSRSGKT HTLEGSSHDR
     GLYLRSFEEL FDLSNSDTTS TAHFNFYFTA CELYNDQVRD LLSESSSTVP KVRMGVQESF
     VELVQEKVEN PLEFSAALKI ALQNRSVNSP KAMVSHLIIT IHIHYRNYVT GEHLYSKLSL
     VDLPASECLL EEDANRDNVT DFLHVSKSLS VLGDAFASLS AKKEPVLYGN SRITQILADS
     LGSSSKILLI VHVSPSASNL SRTLSTLSFS ARARNAELSL GNRDTIKKWK DVANDSRKQL
     HDKEKEVLDL RQEVIGLKHS LKEANDQCIL LFNEVQKAWR VSSSLQADLK SENLMLAEKH
     KTEKEQNNQL RDQISHLLKV EQEQNLKMQE RDLTIQSLQT KLKSIESQLN EALNASDARS
     TIGSESASVI SSPKITESTA DSSSVTKRLE EELAKRDALI EKLHEENEKL FDRLTEKSGL
     GSAPQASSPS ANKPANGQGR EIGRSDSSKS RSPDVFASPV SQDKTGNSGA IVKSSNELAK
     TTPAGEYLTS ALMDFDPDQF EGFAAIADGA NKLLMLVLAA VIKAGAAREH EILAEIRDAV
     FSFIRKMEPK KVMDTMLVSR VKILYIRSLL AKSPELQSIK VSPVERFLEK SNTGRSRSSS
     RGSSPGRSPV HHHGHGSRTA LVDEHVHGFK VNIKQEKKSK FSSIVLKLRG IEEETWRQHV
     TGGKLREITE EAKAFSIGNK ALAALFVHTP AGELQRQIRA WLAENFEFLS VTGADAAGGA
     AGQLELLSTA IMDGWMAGLG TAQPPTTDAL GQLLSEYTKR VYTSQLQHLK VSFPRLIIRL
     TKCIRALCLI LHNFAGHSWH IGNGGG
//