ID A0A1D6M3L8_MAIZE Unreviewed; 776 AA.
AC A0A1D6M3L8;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 22-FEB-2023, entry version 32.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=ZEAMMB73_Zm00001d038131 {ECO:0000313|EMBL:AQK85745.1};
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:AQK85745.1};
RN [1] {ECO:0000313|EMBL:AQK85745.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:AQK85745.1};
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}.
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DR EMBL; CM000782; AQK85745.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6M3L8; -.
DR ExpressionAtlas; A0A1D6M3L8; 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:0016787; F:hydrolase activity; 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; cd01366; KISc_C_terminal; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 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 PANTHER; PTHR47972:SF2; KINESIN MOTOR DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 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 ECO:0000256|RuleBase:RU000394}; Hydrolase {ECO:0000313|EMBL:AQK85745.1};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000394};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394}.
FT REGION 524..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 206..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 776 AA; 86273 MW; 23AC4FE05BBF261F CRC64;
MVGKLFAVED AAVGGDVEQE EPKKEAMAGV GEALRSFMEE FGDQGEDSII LSPRLQEICT
PDRPTALRFL GKKYNNLMER YKKQVVKCSE ECDPRYNGLK KKYTDECAER RRLYNELIEL
RGNIRVFCRC RPLSSNELAR GCSSVVEIDS SQETELQFVP NEKERKPFKF DHVFGPEDDQ
EAVFSETVPV VGSVMDGFNV CIFAYGQTGT GKTFTMEGVP ENRGVNYRAL EELFRISEKR
SASVAYTFSV SILEVYNEKI RDLLDESNDQ SKRLDIKQNA DGTQEVHGLV EAPIYNIDGV
WEKLKFGAQN RSVGSTNANE LSSRSHSLVR VTVRSEHLVT YQRSRSHMWL VDLAGSERIA
KTGVEGDRLK ESQFINKSLS ALGDVISALA SKNSHIPYRN SKLTHLLQSS LGGDCKTLMF
VQISPSSMDS GETLSSLNFA SRVRAVEHGP AARKQADPAG SLKLKQMTEK LQHEEKENAQ
LNQSLQLMQL KYASRENVFR TLNEKVKDAE QACRNYQQRI RELENELGNE KRASRDSARS
SRPPLVPTRQ RQPQGRTNSF APPSGPSRWR LKAPAKHNKE NIPVAMNKPN AGDDPNKPVG
RARRVSLAPV IRQIPIQPKR RSSMAVLPSV REHLSVLNDK KAGSRLSQAN MARGSLGAFG
LNLVPGTPLA GHGGPVDATP DGAKFRRFDF GSSSKFTSPA PNVGMWNKMV TPQQKLGMAP
AGAKLCFSIQ KRVTPPHVRA KPGLGIFDPA LRENMVVGRA GNALRVLNPK RRQSVI
//