ID   A0A1D6DUK2_MAIZE        Unreviewed;      1117 AA.
AC   A0A1D6DUK2;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Kinesin-like calmodulin binding protein {ECO:0000313|EMBL:ONM12491.1};
GN   ORFNames=ZEAMMB73_Zm00001d001928 {ECO:0000313|EMBL:ONM12491.1};
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:ONM12491.1};
RN   [1] {ECO:0000313|EMBL:ONM12491.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM12491.1};
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}.
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DR   EMBL; CM007648; ONM12491.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6DUK2; -.
DR   ExpressionAtlas; A0A1D6DUK2; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13200; FERM_C_KCBP; 1.
DR   CDD; cd01366; KISc_C_terminal; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 6.10.250.760; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 1.25.40.530; MyTH4 domain; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
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; IPR000857; MyTH4_dom.
DR   InterPro; IPR038185; MyTH4_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR011254; Prismane-like_sf.
DR   PANTHER; PTHR47972:SF16; KINESIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF00784; MyTH4; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00139; MyTH4; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56821; Prismane protein-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   PROSITE; PS51016; MYTH4; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
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          499..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1088..1117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         822..829
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1117 AA;  127658 MW;  A84E491F4851FB1E CRC64;
     MGIDSPAIIS LEERIEFVEK LYKHTLKRSE LRDELFAQIS KQTRNNPDRG WSIRAWELMY
     LCASSMPPSK DIGAYLSEYI HFVAHGATTD ADVRVLALNT LNALKRSVKA GPRITIPAWE
     EIEALLTSRK LTTIVFFLDE TFEEITYDMA TTVADAVEEL AGIIKLSVYS SFSLFECRKV
     VNGSKSSEIG NEEYIGLDDN KYIGDLLSEF KSAKDRNKGE ILHCKLVFKK RLFRESDEAV
     TDPMFVQLSY VQLQHDYILG NYPVGRDDAS QLSALQILVE IGFIDNPESC VEWISLLERF
     LPRQVAITRA KRDWELDIIS RFQLMEHLSK DDARQQFLRI LRTLPYGNSV FFSVRKIDDP
     IGLLPGKIIL GINKRGVHFF RPVPKEYLHS AELRDIMQFG SSNTAVFFKM RVAGVLHIFQ
     FETKQGEEIC VALQTHINDV MLRRYSKARS GNSVTSQNDV NQAYKPPNIE MFEKRVQELT
     KTAEDSQKKA DQLREDLQLK TKQETEMQEE LEGLRDTLQS ERQSSKDIKN ELDKLKSLCD
     EKESALQAAL MEKSRLETRL TSGQGRERDT LTTVGSINND IEMLAKLEEE LKSYQKELDA
     SKEVSKKLML EKNILDQKVQ RLERMKNEEK SAMEKVYADE CCKLKSQIAE LEQKLEVATR
     SLNVAESNLA VRNAEVDSLQ NSLKELDELR EFKADVDRKN QQTVEILKRQ GAQLVELENL
     YKQEQVLRKR YYNTIEDMKG KIRVFCRLRP LSDKELSFEE KNIVCSPDEF TISHPWKDEK
     SKQHIYDRVF DANTSQEEVF EDTKYLVQSA VDGYNVCIFA YGQTGSGKTF TIYGSENNPG
     LTPRATSELF RVIKRDGNKY SFSLKAYMVE LYQDNLVDLL LPRNAKQLKL EIKKDSKGVV
     TVENVTVVSI SSIEELRAII SRGSERRHTA GTNMNDESSR SHLILSIIIE STNLQTQSYA
     RGKLSFVDLA GSERVKKSGS AGKQLKEAQS INKSLSALAD VIGALSSDGQ HIPYRNHKLT
     MLMSDSLGGN AKTLMFVNVS PAESNLEETY NSLMYASRVR CIVNDTSKHV APKEIMRLKK
     LIAYWKEQAG KRSDEDELEE IQEERISKER SDNRMTS
//