ID   A0A1D6PYV0_MAIZE        Unreviewed;      1013 AA.
AC   A0A1D6PYV0;
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-related protein8 {ECO:0000313|EMBL:AQK51626.1};
GN   ORFNames=ZEAMMB73_Zm00001d049938 {ECO:0000313|EMBL:AQK51626.1};
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:AQK51626.1};
RN   [1] {ECO:0000313|EMBL:AQK51626.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQK51626.1};
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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000256|ARBA:ARBA00004186}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. KIN-5/BimC subfamily.
CC       {ECO:0000256|ARBA:ARBA00034704}.
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DR   EMBL; CM000780; AQK51626.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1D6PYV0; -.
DR   ExpressionAtlas; A0A1D6PYV0; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
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   GO; GO:0007051; P:spindle organization; IEA:UniProt.
DR   CDD; cd01364; KISc_BimC_Eg5; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR047149; KIF11-like.
DR   InterPro; IPR047241; KIF11-like_kin_motor_dom.
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; PTHR47970; KINESIN-LIKE PROTEIN KIF11; 1.
DR   PANTHER; PTHR47970:SF12; KINESIN-LIKE PROTEIN KIF11; 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|PROSITE-ProRule:PRU00283};
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
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};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        117..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          948..969
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          982..1013
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          404..454
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        985..1000
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         98..105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1013 AA;  113700 MW;  C0A693C162D0D843 CRC64;
     MSSRHDKEKS VNVQVLLRCR PFSDDELRNN APQVITCNDY QREVAVTQNI AGKQFDRVYA
     FDKVFGPTAK QKELYDQAII PIVNEVLEGF NCTIFAYGQT GTGKTYTMEG ECRRAKASLL
     FFMTIMVPGC LIRWSPIMQE CLQSGPKGQL PADAGVIPRA VKQIFDTLER QNTEYSVKIT
     FLELYNEEIT DLLAPEEISK AAFEDKQKKA LPLNLMEDGK GGVLVRGLEE EIVTNASEIF
     SLLERGSAKR RTAETLLNKQ SSRSHSLFSI TIHIKEATPE GEELIKCGKL NLVDLAGSEN
     ISRSGAKEGR AREAGEINKS LLTLGRVITA LVEHLGHVPY RDSKLTRLLR DSLGGRTKTC
     IIATVSPSVH CLEETLSTLD YAHRAKSIKN RPEVNQKMMK STLIKDLYGE IDRLKAEVYA
     AREKVGVYIP KDRYQQEENE RKAMADQIEQ MNASLEVNHK LISDLQQNYD SELQHSADLS
     KKLEVTEKCL DHTSNLLSTT KEDLKQAQYN LNEKDYIISE QKKAENALTH QTYVLRSDLE
     QYTRDNTSLY SKIARGDKLS ATNRSVVNTF QTDLASKLDI LSNTLNASID QQNMHLKSVE
     DLCQSYVDSH DKATSELKKK ILASKSLYMS HMEAFLNVVL VHKASANGTL EDISSLSAAS
     CCSLDQLLVC VEGEAQNIFN DIHNLLTIHR SEMTHFTQEL RESFQISLDR TKEMSTYIIG
     LFDKYVEETS KLHSHSNNTH EAQMKSIEDF QMVYEVGVRL SSLGDAARGN KAFLDEHTSA
     MEFVTKDAKR KWETFAEQAE NDCKAGSSFS AAKHSRMETM LQECACTVDS AVQQWKKSHA
     AVNDLSRKQV AEVEALVRQP RTAIENNEQH ELEVASSRAV AEEDASNNSK DIAQGVENLL
     EEARNSSSRV VSTVEAHFGE LQMLQESHSS QAAGINMHAD KALQTSYKDY EPSGETPVRS
     EPNVPSKGSI ESLRAMPVET MMNEFRENHP YEHESSKESK LSQIPRLPLA TIN
//