ID   A0A238FNK8_9BASI        Unreviewed;       932 AA.
AC   A0A238FNK8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   22-FEB-2023, entry version 21.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=BQ2448_7794 {ECO:0000313|EMBL:SCV74765.1};
OS   Microbotryum intermedium.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX   NCBI_TaxID=269621 {ECO:0000313|EMBL:SCV74765.1, ECO:0000313|Proteomes:UP000198372};
RN   [1] {ECO:0000313|Proteomes:UP000198372}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jeantristanb JTB J.-T., Ricardo R.;
RL   Submitted (SEP-2016) 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,
CC       ECO:0000256|RuleBase:RU000394}.
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DR   EMBL; FMSP01000023; SCV74765.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238FNK8; -.
DR   STRING; 269621.A0A238FNK8; -.
DR   OrthoDB; 5476186at2759; -.
DR   Proteomes; UP000198372; Unassembled WGS sequence.
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; 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; PTHR47968; CENTROMERE PROTEIN E; 1.
DR   PANTHER; PTHR47968:SF36; CENTROMERE-ASSOCIATED PROTEIN E; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Microtubule {ECO:0000256|RuleBase:RU000394};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW   ECO:0000256|RuleBase:RU000394};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198372}.
FT   DOMAIN          257..602
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          471..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          636..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          746..773
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        39..72
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         339..346
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   932 AA;  102077 MW;  4767B5DB7473052B CRC64;
     MQNHFVPFTQ HAAARPQTPA LDAAPRSPFV PVKKHRSITP PATPSSYHRP SKSMTMGLGS
     TSAGTNSPLS PSSQINAVPS FVVQASSPTQ MASPPRKVLT HQRSMSALAS SALVSGATHH
     SVAAGSSSHS QFANRAPSPE PMRIRARVTA AATPRCKAVL PGTEHVEAPT PRVQTSNGFN
     RAMTPSAPTP ISSHSSMYAT PRPLTARTLM KDSDWIGRSH VVASPIEDLT RGMSGMALGS
     ARVEPLPRER LPKIQDSVLV CVRVRPPAAK LALSSEVMDE TAWHVDASRA QLSLTTGGPE
     YNFDSIVTGS ENEGVYAEAG KDLVLSAMEG FDAVIFAYGQ TASGKTFTLS GNAANPGIIP
     QAVSDIFAYI RDVSLIHPNQ EFLLRASYLE IYNETLKDLL APETGPLKVR QDEKKRFFVH
     PLREEVVTGE AQVAALLRRG EKNRHTGQTD FNERSSRSHS VFQMTIESRD QDPYAPSAYP
     LRSKTPNGPR LAPGSNGCVR MSRLSLIDLA GSEQATSQLE RRSEGAFINK SLLTLEKVIA
     SLTDSSKIKP HVPYRDSKLT QILQPSLSGD ARVAVIATMN PYPMAIEESK STLRFAQRVK
     KVTLRAVVNE VMDDKALIHK YRSHASHIAH LEAQLQAAMS QPSVPSTPSY NDAQSEDEGG
     KSLSTAQYHK SSARVKGLEV QIEELRSLFV NSGNVEQRRQ STDQNVLTRR FLQLLPPRPV
     SPMKVRKSID GGDLSDSEEL SLGERLLEAQ DEIATLKDLN SSLKTRISEL ERSHLDHVRT
     SANDSAKDAR IAELVKENQE LLVVVKNGDD GEVDLKRLEF KMKREMEKRT VYAKALEEAL
     RKEQKRVNQF ERFILQHLAT QADVISGRRR SSIGTVNHAA GRPSVAGMLP IMNESSPLVV
     APQEFLDLDE LEFSEEGREQ IKKSVSMLFV PT
//