ID A0A1D6E8U5_MAIZE Unreviewed; 1037 AA.
AC A0A1D6E8U5;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Kinesin KP1 {ECO:0000313|EMBL:ONM16825.1};
GN ORFNames=ZEAMMB73_Zm00001d003368 {ECO:0000313|EMBL:ONM16825.1};
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:ONM16825.1};
RN [1] {ECO:0000313|EMBL:ONM16825.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM16825.1};
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
CC {ECO:0000256|ARBA:ARBA00004245}.
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; ONM16825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6E8U5; -.
DR ExpressionAtlas; A0A1D6E8U5; baseline and differential.
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:0007018; P:microtubule-based movement; IEA:InterPro.
DR Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
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 PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR PANTHER; PTHR47972:SF28; PROTEIN CLARET SEGREGATIONAL; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
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; 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 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 316..383
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 718..759
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 30..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 467..474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1037 AA; 115859 MW; 0FE5F6AA7329649E CRC64;
MAAADGARRS RVPAGEAFRG GLLRGTAQRP RPLQGSQPRQ SWRRPQGACQ RNCGEKENVT
TFFPCDSNEF FFSSSASPPK VVENPVITVQ TFDGPAQSAI QYFENMRNFL VAVSAMNLLT
FETSDIEKGG SSMKVVDCIL CLKGYHEWKI SGGIGIWRYG GIVKIASSSK RPASHLNRGG
GSDQQMLEFV HLLSEVSLEE SRVEEAQHSL FQRFVLQVVR AFLLEWGEAE DLPLDDMVIE
TVLEQACKEF TILLASHRNQ VRSLLRKMMK DDNGTLSKMD LIETITKCLK ENGECMSSSL
RLPRGSHGHL DDVGLLENQQ EGLEKLKMSF NEMKLQVEST RAEWEEDLRR LESYFEAQNH
NAYQKLLEEN RKLYNQVQDL KGSIRVYCRV KPFPKAQSDQ RSTVDHIGEN GEILIANPQK
QGKDGRKIFT FNKIFGPSTS QSEVFADTQP LIRSVMDGYN VCIFAYGQTG SGKTYTMSGP
DVTAEETWGV NYRSLNDLFE ISQTRADSIT YDVKVQMIEI YNEQVRDLLM TDGANKRLEI
RNNSHVNGLN IPDANIVPVK CAQDVLDLMK VGQRNRAVGS TALNERSSRS HSVLTVHVQG
KEVISGSTLR GCLHLVDLAG SERVDKSEAT GERLTEAKHI NKSLSALGDV ISALAQKSSH
VPYRNSKLTQ VLQDALGGQA KTLMFVHVNP ETDSFSETMS TLKFAERVAT IELGAARANK
EAGQVKDLKE EIAKLKLALD EKENEVAQFK DLANRVTSEM RNARTRSPLT ASMSLKPEVS
QESSVDTCTS EIRSSSSGKQ RRFRSPLSVR ELDDKSPVIS RELYLSARKY KTPSPPVRSS
LSVERGSFAK IVENTGSIDC TPISKVEVPP KVWSSNSKTT PSSVLTAQSL RKFRDSEENR
TKIPPAVRQS MAKNRSESTP KTHNEEKPAN RHHSGTKARS EARNTRDSSE IENEFAGDEP
TFHFNRTAKK LPTKVMSRQS QNIDVSVRAS VRGEMEPLTE GRQRRNWSKP PHAERTNMPL
PDIRRSVSLP RGKNPLV
//
