ID   KINH_GIBMO              Reviewed;         931 AA.
AC   Q86Z98;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Kinesin heavy chain;
GN   Name=KLP1;
OS   Gibberella moniliformis (Maize ear and stalk rot fungus) (Fusarium
OS   verticillioides).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=117187;
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; AY230438; AAO59300.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q86Z98; -.
DR   SMR; Q86Z98; -.
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..931
FT                   /note="Kinesin heavy chain"
FT                   /id="PRO_0000125361"
FT   DOMAIN          6..329
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          388..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          886..931
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          342..864
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        395..423
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..451
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        899..931
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         87..94
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   BINDING         237..244
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   931 AA;  103243 MW;  A1BE9C69CF84848B CRC64;
     MSSANSIKVV ARFRPQNKVE LESGGKPIVS FDGEDTCTVA SKEAQGSFTF DRVFDMGCKQ
     QDIFDFSIRS TVDDILNGYN GTVFAYGQTG AGKSYTMMGT NIDDDEGRGI IPRIVEQIFA
     SIMSSPGTIE YTVRVSYMEI YMERIRDLLA PQNDNLPVHE EKNRGVYVKG LLEIYVSSVQ
     EVYEVMRRGG NARAVAATNM NQESSRSHSI FVITITQKNV ETGSAKSGQL FLVDLAGSEK
     VGKTGASGQT LEEAKKINKS LSALGMVINA LTDGKSSHIP YRDSKLTRIL QESLGGNSRT
     TLIINCSPSS YNDAETLGTL RFGMRAKSIK NKAKVNAELS PAELKSLLKK AQGQVTNFES
     YISSLEGEIQ MWRAGEAVPK ERWATPLTTD AVARTKADAR TSTRPSTPSL ISDSRSETPA
     ISDRAGTPSL PLDKDEREEF LRRENELQDQ ISEKESQAAS AEKQLRETKE ELAYLKDHDS
     KVGKENEKLT TEVNEFKMQL ERLTFESKEA QITMDALKEA NSELTTELDE VKQQLLDVKM
     SAKESGAALD EKEKRKAEKM AKMMAGFDLG GEVFSENERH IAETIEKVDS LHELSATGDN
     IAPDEFKALK ARLVETQGIV RQAELSMYST SSSESDSRRR QELEARLEAV QAEYEEILTR
     NLGPEDIEEV KARLENAFAN RQTAQSQFVE ELKEDIAQKA AENTRMKTLI EDLQQRVKAG
     ATAPMANGKT IQQQIAEFDV MKKSLMRDLQ NRCERVVELE ISLDETREQY NNVLRSSNNR
     AQQKKMAFLE RNLEQLTQVQ RQLVEQNSAL KKEVAIAERK LIARNERIQS LESLLQDSQE
     KMAAANHKYV QLAAVKERLE LAKAGSTRGL NSPGGFSFAN AGSRIAKPLR GGGGGNDAPS
     IPTIQNLQGQ NEGNTSSGSS SKRASWFFTK S