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Database: UniProt
Entry: A0A6A3IW96_9STRA
LinkDB: A0A6A3IW96_9STRA
Original site: A0A6A3IW96_9STRA 
ID   A0A6A3IW96_9STRA        Unreviewed;      1003 AA.
AC   A0A6A3IW96;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN   ORFNames=PR001_g22631 {ECO:0000313|EMBL:KAE8986331.1}, PR003_g23807
GN   {ECO:0000313|EMBL:KAE9296246.1};
OS   Phytophthora rubi.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=129364 {ECO:0000313|EMBL:KAE8986331.1, ECO:0000313|Proteomes:UP000429607};
RN   [1] {ECO:0000313|EMBL:KAE8986331.1, ECO:0000313|Proteomes:UP000429607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCRP249 {ECO:0000313|EMBL:KAE8986331.1,
RC   ECO:0000313|Proteomes:UP000429607}, and SCRP333
RC   {ECO:0000313|EMBL:KAE9296246.1, ECO:0000313|Proteomes:UP000434957};
RA   Adams T.M., Armitage A.D., Sobczyk M.K., Bates H.J., Dunwell J.M.,
RA   Nellist C.F., Harrison R.J.;
RT   "Genomic investigation of the strawberry pathogen Phytophthora fragariae
RT   indicates pathogenicity is determined by transcriptional variation in three
RT   key races.";
RL   Submitted (SEP-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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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:KAE8986331.1}.
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DR   EMBL; QXFV01002544; KAE8986331.1; -; Genomic_DNA.
DR   EMBL; QXFT01002568; KAE9296246.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6A3IW96; -.
DR   Proteomes; UP000429607; Unassembled WGS sequence.
DR   Proteomes; UP000434957; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR029329; DUF4472.
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; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR   PANTHER; PTHR47969:SF15; ZGC:66125; 1.
DR   Pfam; PF14739; DUF4472; 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; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000434957}.
FT   DOMAIN          11..366
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          793..826
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          915..938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          403..451
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          603..653
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          685..792
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          940..985
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        811..826
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1003 AA;  110879 MW;  92D9A9398C3BAA34 CRC64;
     MDASVVPKGV AVQIHAYIGP TPAKPDNSAL RVKDGKQIEV ANGSTGETLG LQLDYVYQQA
     TEADVVERSL RSLVAASVEG VNVSVLAVGS TKSQKNRVLF FPMADQSLAA AVFQTLLDTL
     QSKVSTLGSS GASPAAANGG VTSARKSQVI SVATFSLRVS FAELYEETIT DLLAASKGDS
     SDNKLALVIE DDPALGKTIK NLTQSPPLTS LTDFRRVLDA GLSARRSNNG LYGNSSEFSS
     AVLRISVKQT FAFRDAATQE LHSFFDLVDL PATDRLARTG AAVRLSEGPL LNKSLFALQE
     VFESLTHKSG DEVSVRYQGS QLTTVLQDAL GGNCLTFVLM CLSPGDMAGS TATLQLGRML
     PRISTFPVVN NDMLRGLRRR QLMVQKQLAG AAKDNPTGEK LGLADYERRL HDLEGKLAQN
     ALERRVLRED KDALTAQLGE LRTKYRELFD NELSLRTELL TCEQDKLALS KAFVAFQLEC
     DTQVQQLDSD KFELETRLLK AEQLVVEIQQ DDTTKAAQIQ DLCAKMNELV ADKTRLGGEL
     ALLQKAAKTA ESARDAEAKK NQQLSLELIV AVNQKHKCQG EVEALATQLR SRQAQVDGHL
     AECTQLRSDN DALRQQVAGL EDKLEAMRKD VVRRELELER AELAAKKEQL ETQQAGRDAD
     SKRQLSVQQL SQELETQRAA FAADKRLLEL QLERGQHDLA RETREKQHLM NALTSKNEEN
     EELVLALERA RHDLQAQLET FRLKLALLQQ SCSSGERASE SGAGIQELKE LVASYQVRER
     ELRDELNSTR NANFRLARRL RGPGQDTTEP PQNPDDRDRE DGGEQVERLR GRLAAAEQQV
     ASEMERRAEQ SLVLAELEAQ NATLVQELKE TQRSEQTPAA RDSESGVRAI TEMHAALARQ
     LEEVRRLTVQ QQQVTRIVDT AAPPSQSQPR TDNASDPNEL QSLRAAKTQL ESRLSSSKAQ
     WMALLEQVER RCAELLTKNV MLSEDNENLR HHLTKARMKA PRH
//
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