ID   KINH_BOTFU              Reviewed;         880 AA.
AC   Q86ZC1;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Kinesin heavy chain;
GN   Name=klp1;
OS   Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=40559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12742059; DOI=10.1016/s1087-1845(03)00022-7;
RA   Schoch C.L., Aist J.R., Yoder O.C., Gillian Turgeon B.;
RT   "A complete inventory of fungal kinesins in representative filamentous
RT   ascomycetes.";
RL   Fungal Genet. Biol. 39:1-15(2003).
CC   -!- FUNCTION: Kinesin is a microtubule-associated force-producing protein
CC       that may play a role in organelle transport. Its motor activity is
CC       directed toward the microtubule's plus end.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC   -!- DOMAIN: Composed of three structural domains: a large globular N-
CC       terminal domain which is responsible for the motor activity of kinesin
CC       (it hydrolyzes ATP and binds microtubule), a central alpha-helical
CC       coiled coil domain that mediates the heavy chain dimerization; and a
CC       small globular C-terminal domain which interacts with other proteins
CC       (such as the kinesin light chains), vesicles and membranous organelles.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. Kinesin subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00283}.
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DR   EMBL; AY230415; AAO59277.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q86ZC1; -.
DR   SMR; Q86ZC1; -.
DR   PRIDE; Q86ZC1; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; 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   Gene3D; 3.40.850.10; -; 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; PTHR24115; PTHR24115; 2.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW   Motor protein; Nucleotide-binding.
FT   CHAIN           1..880
FT                   /note="Kinesin heavy chain"
FT                   /id="PRO_0000125360"
FT   DOMAIN          4..327
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          388..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          428..849
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        396..410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         85..92
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   BINDING         235..242
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   880 AA;  98369 MW;  6BF118EDDA3EF3A6 CRC64;
     MSNSIKVVCR FRPQNRIENE QGAQPVVKFE ADDTCALDSN GAAGSFTFDR VFGMSSRQKD
     IFDFSIKPTV DDILNGYNGT VFAYGQTGAG KSYTMMGTNL DNDDGRGVIP RIVEQIFASI
     LSSPGTIEYT VRVSYMEIYM ERIRDLLQPQ NDNLPIHEEK NRGVYVKGLL EVYVSSVQEV
     YEVLKRGGDA RVVASTNMNA ESSRSHSIFV ITITQKNVET GSAKSGQLFL VDLAGSEKVG
     KTGASGQTLE EAKKINKSLS ALGMVINNLT DGKSSHIPYR DSKLTRILQE SLGGNSRTTL
     IINCSPSSYN AEETLSTLRF GMRAKAIKNK AKVNAELSPA ELKALLRKAQ SQVTTFETYV
     STLEGEVQLW RKGESVPKEQ WAPPLAGVSG AKAAAAQTPR PSTPSRLATE SRAETPVAER
     SATPGIPIDK DEREEFLRRE NELQDQITEK ETQIAAAEKT LRDTKEELTY LKERDTKVNK
     DNEKLTSEAN EFKMQLERLA FESKEAQITM DSLKEANAEL TAELDELKQQ LLNVKMSAKE
     STAALDEKEK RKAEKMAQMM AGFDLGGDVF SENEATIKKV IDHIDSLHEQ SSAGEAIPPD
     EFEELKAKLV ETQGIVRQAE LSMFGSSSND ANVKRREELE QRLQVLEQEY EDLLERNLGE
     GDVAEIKERL EKAYSNNQDI KVELVEDLKK EVAQKSAEIE KFKAVNEDLQ QRVKSGSASN
     GTAPGSASGK TVQQQIAEFD VMKKSLMRDL QNRCERVVEL EISLDETREQ YNNVLRSSNN
     RAQQKKMAFL ERNLEQLTHV QRQLVEQNGS LKKEVAIAER KLIARNERIQ SLESLLQDSQ
     EKLTTASHRY GFPLYFRIDF NHTSIALLTF PLDSKPNCQQ