ID   DSK1_CYLFU              Reviewed;         624 AA.
AC   Q39493;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Diatom spindle kinesin-1;
GN   Name=DSK1;
OS   Cylindrotheca fusiformis (Marine diatom).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Bacillariophyceae; Bacillariophycidae; Bacillariales; Bacillariaceae;
OC   Cylindrotheca.
OX   NCBI_TaxID=2853;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8636234; DOI=10.1083/jcb.133.3.595;
RA   Wein H., Foss M., Brady B., Cande W.Z.;
RT   "DSK1, a novel kinesin-related protein from the diatom Cylindrotheca
RT   fusiformis that is involved in anaphase spindle elongation.";
RL   J. Cell Biol. 133:595-604(1996).
CC   -!- FUNCTION: Involved in anaphase spindle elongation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. MCAK/KIF2 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00283}.
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DR   EMBL; U51680; AAB05681.1; -; mRNA.
DR   AlphaFoldDB; Q39493; -.
DR   SMR; Q39493; -.
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; 1.
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..624
FT                   /note="Diatom spindle kinesin-1"
FT                   /id="PRO_0000125423"
FT   DOMAIN          95..411
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          1..85
FT                   /note="Globular"
FT                   /evidence="ECO:0000255"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          426..624
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        478..509
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..528
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         186..193
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   624 AA;  70308 MW;  DC996BFEC22BE155 CRC64;
     MNAANRRKST STVGITGRKD ATRMKIEQME KERKERRKTM MQRKEARKQE HMKNIEAGNP
     GDVDFIGLVE EWRREQENKI GDKSPPSLFA STNSNICIAV RKRPISDKER QKLDHDSVSC
     FQNKVWIHSA KLKVDGITKY LTHNSFQLDH TFGEDSTTEQ IYLATTLPLV DHVVSTQGRA
     TVFCYGQTGS GKTYTMNGIQ QILAYDLYGQ LAEHTDDLEI TVAFFELYSG NVLDLLHGCQ
     RCKLLEDGNG EVNITGLREV PAPTPEAFLQ VIEEGHSLRT TQKTEANDAS SRSHAICQVF
     LRDYGGNLRG KLGLVDLAGS ERGSDTKQHN SQRRTESADI NTSLLALKEC IRALGQKSAH
     VPYRGSKLTL ILKDCFSPDS KTTMVATVSP GASAADHSLN TLRYADRIKE QRVSSNGQRG
     KAAKASNREI MPSKERLMRI AAATEQADDQ HSAFVQKMLA EHDQVQADAN DYAFTEQVDE
     EEADDEEGDY EEESEDLDYE DSEGQDYEEA VESQYDHSQE AQEGEEELRR TVQAVFELEE
     ALLNQHMSNI QANAEMLTQE GKLLQSVQAG GLSEDEMHNY AIQLAEFLDK KESLIYKLQS
     KLDEFQEQLA REQELARQVQ LTQY