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Database: UniProt
Entry: A0A498IRB0_MALDO
LinkDB: A0A498IRB0_MALDO
Original site: A0A498IRB0_MALDO 
ID   A0A498IRB0_MALDO        Unreviewed;       800 AA.
AC   A0A498IRB0;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=DVH24_017071 {ECO:0000313|EMBL:RXH86018.1};
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH86018.1, ECO:0000313|Proteomes:UP000290289};
RN   [1] {ECO:0000313|EMBL:RXH86018.1, ECO:0000313|Proteomes:UP000290289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC   TISSUE=Young leaf {ECO:0000313|EMBL:RXH86018.1};
RA   Hu J.;
RT   "A high-quality apple genome assembly.";
RL   Submitted (OCT-2018) 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}.
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:RXH86018.1}.
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DR   EMBL; RDQH01000336; RXH86018.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498IRB0; -.
DR   STRING; 3750.A0A498IRB0; -.
DR   Proteomes; UP000290289; Chromosome 10.
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   CDD; cd01366; KISc_C_terminal; 1.
DR   Gene3D; 1.10.287.1490; -; 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:SF45; KINESIN-LIKE 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Microtubule {ECO:0000256|RuleBase:RU000394};
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}; Reference proteome {ECO:0000313|Proteomes:UP000290289}.
FT   DOMAIN          438..779
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          127..424
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        20..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         523..530
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   800 AA;  90313 MW;  4C340A6AADDC6E2A CRC64;
     MASRNQNRAP RSPFSKKSSL DEVPLDKRRR IETRKPEVPS SMGRQRPPLA VVKQDAAGTS
     DIGSVEGSEC ANVEFTKEEV EALLVEKLKV KKFDHKGKAE QLADYSKRLK LCIKWLQEVE
     EGHILEEEKL RNALASAEKK CADTEVEMRN KVDELNAVNS KLRENIATLE EKLAKEESEK
     LDAIASHRSE KEARDAAEKL QASLSQKLEI VREEKLVADK KVSSYQDLYN RAQEYNKSLQ
     QYNSKLQKDL ETATESLKRV EDEKRTVLET LSNLRVHNKA LQDELTKVTA SLDETLKQKE
     LLDNEIKCLR GELQQVRDDR DRHAREIQDM RDQVVKYKEN TEMSCEELDR LMRKSKALEE
     RDSSQKQEID TLKHELNAAN DKLKMVSQSA SETLTEFEEH KRIVQELQNR LAESELQILE
     GEKLRKKLHN TILELKGNIR VFCRVRPLLP DDANATDAPV VSYPTGTEAL GRGLDLVQSG
     QKFNFTFDKV FHHETSQQDV FVEISQLVQS ALDGYKVCIF AYGQTGSGKT YTMMGRPDAP
     EQKGLIPRSL EQIFQTSQAL QAQGWKYKMQ ASMLEIYNEN IRDLLCTGRS SSADLSKTEN
     GVCGKQYTIK HDANGNTYVS DLTIVDVCNI NQISSLLQQA AHSRSVGKTH MNEQSSRSHF
     VFTLRISGIN ENTEQQVQGV LNLIDLAGSE RLSRSGATGE RLKETQAINK SLSSLSDVIF
     ALAKKEDHVP FRNSKLTYLL QPCLGGDSKT LMVVNISPDS SSVGESLCSL RFAARVNACE
     IGIPRRQTSM KPADNRLSYG
//
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