ID A0A1D6FTQ2_MAIZE Unreviewed; 1033 AA.
AC A0A1D6FTQ2;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Kinesin-related protein3 {ECO:0000313|EMBL:AQK94927.1};
GN ORFNames=ZEAMMB73_Zm00001d010790 {ECO:0000313|EMBL:AQK94927.1};
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:AQK94927.1};
RN [1] {ECO:0000313|EMBL:AQK94927.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQK94927.1};
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. KIN-14 subfamily.
CC {ECO:0000256|ARBA:ARBA00010899}.
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DR EMBL; CM000784; AQK94927.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6FTQ2; -.
DR SMR; A0A1D6FTQ2; -.
DR IntAct; A0A1D6FTQ2; 3.
DR STRING; 4577.A0A1D6FTQ2; -.
DR InParanoid; A0A1D6FTQ2; -.
DR ExpressionAtlas; A0A1D6FTQ2; baseline and differential.
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; 2.
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 InterPro; IPR031852; Vik1/Cik1_MT-bd.
DR PANTHER; PTHR47972:SF44; KINESIN-LIKE PROTEIN KIN-14K; 1.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16796; Microtub_bd; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; 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|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}.
FT REGION 167..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 310..383
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 988..1026
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 580..587
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1033 AA; 116360 MW; BC0DFFF54F8B89B2 CRC64;
MGSVDGRGVE GIHEANRRAQ LIGWMNALLP EFSLPPDSSS EELRELLSDG VVLCRLVNTL
IPGVLEASLF FSCIICGSWE GYAPSDQRLG NVKKFLSVVS DMGLPGFSLK DLDEGLMSSV
VECLLVLRGS VDPRLGDDIP PDVTRTPLRK QWGVQEMDKP QVPAAALGKR SPAEDMRNGV
ADSKTHQKTS VFSGQKVREV FQLKRGSYSD LTAAKISEMM HSNSLDNAPT QSLISVVNGI
LDESIERKKG EIPHRVVYLL RKVVQEIEHR LCIQAEHIRS QNVTIKTREQ KYCSKIKALE
MLVNGTNEEN QMAINRLQIV KNEKSQIEEK KELCEKDVQR LMKEKEYSKS IIMNLTKDME
AMNRLHEQQL EQIGRKAKEM EEQLTTRVKE VEYLLLQSNK KVEELEIASR LKSQLWDQKE
NIFQSYMDNQ QLVIKDIRIL SQSYENDMYA LQMQWRNEIS NLGSGLKCLV DAAENYHKVL
TENQKLFNEV QELKGNIRVY CRVRPFLSGQ DKKSTTIDYM GENGELLISN PFKQGKDGHR
MFKFNKVFTP FASQAEVFSD IQPLIRSVLD GFNVCIFAYG QTGSGKTYTM SGPTTSKQDW
GVNYRALNDL FDISLSRRNA FSYEVGVQMV EIYNEQVRDL LSNDIAQRRY PFYLMEIGQA
NRAVGSTALN ERSSRSHSIL TVHVRGMDLK NGSTSRGCLH LIDLAGSERV EKSEVTGDRL
KEAQYINKSL SALGDVIFAL SQKSAHVPYR NSKLTQVLQS SLGGQAKTLM FVQINPDVES
YSETISTLKF AERVSGVELG AARSNKEGKD IKELLEQVLV LLDLSLTRVY LFPILFNFRS
MVCILLKVLK QQHFTNFVQV ASLKDTILRK DMEIEQIQVI KDKVKSPNLL LDRNVPGLTK
TTANQPSQLL SGERMLKSSD RVLSDRQSYG EVNVDPNHHV MDTAPVSIDE AGYENNASDD
GLSGETENDN SAAEMTAERL HRFPSRISRF TLTKNGQPSM SRSNPKDAKT PSNTKAPSSR
LTGGSSARSK RRQ
//