ID   KINH_SYNRA              Reviewed;         935 AA.
AC   O43093;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Kinesin heavy chain;
DE   AltName: Full=Synkin;
OS   Syncephalastrum racemosum (Filamentous fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Syncephalastraceae; Syncephalastrum.
OX   NCBI_TaxID=13706;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9613604; DOI=10.1016/s0014-5793(98)00399-8;
RA   Grummt M., Pistor S., Lottspeich F., Schliwa M.;
RT   "Cloning and functional expression of a 'fast' fungal kinesin.";
RL   FEBS Lett. 427:79-84(1998).
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. The speed of this motor is
CC       4-5 times faster than its animal counterparts.
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; AJ225894; CAA12647.1; -; mRNA.
DR   PIR; T51930; T51930.
DR   AlphaFoldDB; O43093; -.
DR   SMR; O43093; -.
DR   PRIDE; O43093; -.
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; 3.
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   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW   Motor protein; Nucleotide-binding.
FT   CHAIN           1..935
FT                   /note="Kinesin heavy chain"
FT                   /id="PRO_0000125363"
FT   DOMAIN          5..329
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          400..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          898..935
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          342..887
FT                   /evidence="ECO:0000255"
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   935 AA;  105041 MW;  CFBDFD33B3827E28 CRC64;
     MSGNNIKVVC RFRPQNSLEI REGGTPIIDI DPEGTQLELK GKEFKGNFNF DKVFGMNTAQ
     KDVFDYSIKT IVDDVTAGYN GTVFAYGQTG SGKTFTMMGA DIDDEKTKGI IPRIVEQIFD
     SIMASPSNLE FTVKVSYMEI YMEKVRDLLN PSSENLPIHE DKTKGVYVKG LLEVYVGSTD
     EVYEVMRRGS NNRVVAYTNM NAESSRSHSI VMFTITQKNV DTGAAKSGKL YLVDLAGSEK
     VGKTGASGQT LEEAKKINKS LTALGMVINA LTDGKSSHVP YRDSKLTRIL QESLGGNSRT
     TLIINCSPSS YNEAETLSTL RFGARAKSIK NKAKVNADLS PAELKALLKK VKSEAVTYQT
     YIAALEGEVN VWRTGGTVPE GKWVTMDKVS KGDFAGLPPA PGFKSPVSDE GSRPATPVPT
     LEKDEREEFI KRENELMDQI SEKETELTNR EKLLESLREE MGYYKEQEQS VTKENQQMTS
     ELSELRLQLQ KVSYESKENA ITVDSLKEAN QDLMAELEEL KKNLSEMRQA HKDATDSDKE
     KRKAEKMAQM MSGFDPSGIL NDKERQIRNA LSKLDGEQQQ TLTVEDLVSL RRELAESKML
     VEQHTKTISD LSADKDAMEA KKIELEGRLG ALEKEYEELL DKTIAEEEAN MQNADVDNLS
     ALKTKLEAQY AEKKEVQQKE IDDLKRELDR KQSGHEKLSA AMTDLRAAND QLQAALSEQP
     FQAPQDNSDM TEKEKDIERT RKSMAQQLAD FEVMKKALMR DLQNRCEKVV ELEMSLDETR
     EQYNNVLRAS NNKAQQKKMA FLERNLEQLT NVQKQLVEQN ASLKKEVALA ERKLIARNER
     IQSLETLLHN AQDKLLNQNK KFEQQLATVR ERLEQARSQK SQNSLAALNF SRIAKPLRGN
     GAAIDNGSDD GSLPTSPTDK RDKRSSWMPG FMNSR