ID   A0A1D6GMY4_MAIZE        Unreviewed;       857 AA.
AC   A0A1D6GMY4;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=ZEAMMB73_Zm00001d013859 {ECO:0000313|EMBL:AQK64613.1};
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:AQK64613.1};
RN   [1] {ECO:0000313|EMBL:AQK64613.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQK64613.1};
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       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; CM000781; AQK64613.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6GMY4; -.
DR   ExpressionAtlas; A0A1D6GMY4; baseline and differential.
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   CDD; cd16649; mRING-HC-C3HC5_CGRF1-like; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1.
DR   PANTHER; PTHR47968:SF35; KINESIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF13920; zf-C3HC4_3; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU000394};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000394};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175,
KW   ECO:0000256|RuleBase:RU000394};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000394};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   REGION          342..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          237..312
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          550..577
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          660..708
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   857 AA;  95655 MW;  0005596AEE2B86D4 CRC64;
     MHGDQNCPGI IPLAIKDVFS MIQDSPGREF LLRVSYLEIY NEVINDLLDP TGQNLRVRED
     AQGTYVEGIK EEVVLSPGHA LSFIAAGEEH RHVGSNNFNL FSSRSHTIFT LMIESSARGD
     EYDGAMYSQL NLIDLAGSES SKTETTGLRR REGSYINKSL LTLGTVIGKL SEGRATHIPY
     RDSKLTRLLQ SSLSGHGHVS LICTITPASS NMEETHNTLK FASRAKRVEI YASRNRIIDE
     KSLIKKYQKE ISSLKQELDQ LRRGMIGGAS REEILSLRQQ LEAGQVKMQS RLEEEEEAKA
     ALMSRIQRLT KLILVSTKNN IPALTDGHQS HNSLSEQDKL ITSQDSSTLV QTEGTTKDPL
     SSALPDSLDE INQLRSGTGE QSSVTGSATD SMQVGFTASD HMDLLIEQIK MLAGEVAFGT
     SSLKRLIEQS IDDPEATKDQ IENLEREIQQ KRRHMRALEK QIMESGEASV ANASMMDMQQ
     TITKLTAQCS EKAFDLELKS ADNRVLQEQL HQKNLEIYDL QEKVLRVEQQ LSAKVDISPE
     KETDCAQQET IDLKSKLQSK EAEIEKLKYE HLKISEEHCD LINQNHKLSE EAAYAKELAS
     SAAVELKNLA EEVTKLSVLN AKQAKELLVA QEMAHSRVHG RKGRTASRGR DEVGTWSLDL
     EDMKMELQAR RQREAALEAA LAEKELLEEE YKKKFDEAKK KELSLENDLA GMWVLVAKLK
     RGALGISDLN VDDRTVNLAD ITNSTKENKG GKNFALVEKQ ASEDSVKSLS SEEHTSPEFE
     PLLVRLKAKI QEMKEKDIDP LTDKDGNSHV CKVCFESAAA AVLLPCRHFC LCKPCSLACS
     ECPLCRTRIA DRIITFT
//