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Database: UniProt
Entry: A0A1D6FTQ2_MAIZE
LinkDB: A0A1D6FTQ2_MAIZE
Original site: A0A1D6FTQ2_MAIZE 
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
//
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