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Database: UniProt
Entry: A0A445DXD3_ARAHY
LinkDB: A0A445DXD3_ARAHY
Original site: A0A445DXD3_ARAHY 
ID   A0A445DXD3_ARAHY        Unreviewed;       958 AA.
AC   A0A445DXD3;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Kinesin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Ahy_A03g014280 {ECO:0000313|EMBL:RYR67836.1};
OS   Arachis hypogaea (Peanut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX   NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR67836.1, ECO:0000313|Proteomes:UP000289738};
RN   [1] {ECO:0000313|EMBL:RYR67836.1, ECO:0000313|Proteomes:UP000289738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC   TISSUE=Leaves {ECO:0000313|EMBL:RYR67836.1};
RA   Chen X.;
RT   "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT   genome evolution and oil improvement.";
RL   Submitted (JAN-2019) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RYR67836.1}.
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DR   EMBL; SDMP01000003; RYR67836.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A445DXD3; -.
DR   STRING; 3818.A0A445DXD3; -.
DR   Proteomes; UP000289738; Chromosome a03.
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; 1.20.5.170; -; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
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:SF17; KINESIN MOTOR CATALYTIC DOMAIN PROTEIN; 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|PROSITE-ProRule:PRU00283};
KW   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|PROSITE-ProRule:PRU00283};
KW   Reference proteome {ECO:0000313|Proteomes:UP000289738}.
FT   DOMAIN          26..128
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          482..788
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          142..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          834..958
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          342..401
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          795..829
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        157..178
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..857
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        901..924
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         565..572
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   958 AA;  107428 MW;  1A4A9D285D66297A CRC64;
     MGSPKPISTG ICKNGFIVSI HGEVEAKHRL LLVQWISTLL PSLNLPINIT DDVLRACLRD
     GIVLCQILNK LRPGSVPVVS EFDHEENLKS FLKAMDGLGL PQFSISDLEK GSMKVVVDCL
     LSLRAKSLQN VFWDNNSSTT NSKVGSPHGI TAPSVPFPPS FETTTKHHRS LSSPFLTESP
     TSLLHQGHKF HEGFEVFQGK EESYADLSPT KISEMVKSVS LDNAPTQSLL GVVNGILEET
     VEKRNGEMPY RVACLLRKVS QELERRMSAQ AEHSRTQSNL FKVREEKYQS RIRVLEALAT
     GNNIEEDEAE KFAVEENKPD DRDFERSMKK QEDKILEISA LTEDLETRKK ALELKCSRLE
     VEAMEAKAEI EQKTKAYEQQ LEEWRNKCKE LESSYVSKYN KWNMKKNQML NVVNFQSSNL
     EKMKLSWESI KQDVMQEQKV YAEECNQLGV NLKSLAHAAE NYQVVVAENR KLFNEIQELK
     GNIRVYCRIK PFTAGAKEKQ SIIEHIGEDN LVVANPTKQG KDALRSFKFN KVFGPEATQA
     DVYADIQALT RSVLDGYNVC IFAYGQTGSG KTYTMTGPTG ATSENLGVNY RALNDLFRLS
     TSRTSSIEYE IGVQMVEIYN EQPEGLAVPD ASMFHVNAPS DVIKLMDIGL KNRAISATAM
     NERSSRSHSV VTIHVRGKDL NSGSTLVGNL HLVDLAGSER VDRSEVTGDR LREAQHINKS
     LSAFGDVIFS LSQKSSHVPY RNSKLTQLLQ ASLGGHAKTL MFIQINSDVN SYSETMSTLK
     FAERVSGIEL GAARSNKESK DVKELMEQVA SLKNSVSKKD EEIERLQLLH FKQLQRPSTS
     RSPRDESLRR TKSSIGGDKT PRESWSYTDA DFDERSNNNS DYGYGSESSK SSDKMDKPKT
     LQRSVQSMKK ASVRVPSPTK TQRDPPKMSP APGGYKEKRQ YWPPKTTRFK TVAVTATR
//
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