ID A0A0M0J875_9EUKA Unreviewed; 905 AA.
AC A0A0M0J875;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=Ctob_000759 {ECO:0000313|EMBL:KOO22532.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO22532.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(2015).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283,
CC ECO:0000256|RuleBase:RU000394}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOO22532.1}.
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DR EMBL; JWZX01003271; KOO22532.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0J875; -.
DR OrthoDB; 314559at2759; -.
DR Proteomes; UP000037460; 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 CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
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:SF194; KINESIN-LIKE PROTEIN KIF6; 1.
DR PANTHER; PTHR24115; KINESIN-RELATED; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50191; CRAL_TRIO; 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};
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:UP000037460}.
FT DOMAIN 6..339
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 726..896
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT REGION 557..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 95..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 905 AA; 98428 MW; 3968D3A6A576BB37 CRC64;
MPSSTAITTF LRLRPSKHGS GYFAVDPSAP NKVEVSVPPE EAAGLHVNHK RNQWKFSFDG
VLETRATQEE VFERVAEPVV ASVFEGYNGT VFAYGQTGSG KTFTLTGGVN AFGERGIIPR
TLSALFARIA ADTEAEYTVR ISYLEIYNET GFDLLDSRQA AVQAVTEDAD GSVRLKGLSS
HVVGSEEAAL NLLFVGDTNR AVSETSMNAV SSRSHCVFTV ALEARPHGSS TVRRSKLHLV
DLAGSERVGK SGASGTTLNE AIHINSSLFQ LELVIMALHE RQTASSRHVP YRNSMLTSVL
RDSLGGNCKT VMVATVHPAV SHTDESISTC KFAQRVAMVK NEVSVNEEVD QAVLIARLQD
ENRKLREAGG GAGGSAEDDP TKQLSAEELQ QLHRDVRAFV SDADPQVTLA WGPGKRLAKL
KEALGTALEG QAGNQAGSQA GEERMRAQLT LETTLYKGGV ASLKELKGEI ESLQLQLQRS
QQRLQADFES WHTAVVRWLK SQEIPADVYL REARAALEAA VEQVLIDRPV NPLLAIGQHL
CAYQVQAELA LVQRSSSTSS RMPTHELEVE AAPVQRSSGT SSRMPTHELE AEAAPVQRSS
STSSRMPTHE LEGESAPVQN FKTERSDSTM PESVSIVAAV APVQTPTAKE QLLLPKMLAA
LAVRGVKPRP LGAGETKEDA LLRYLRARHH NVEKAANQYA ATIKWREEHH VDHLRTLTPD
EALGAPVAGM RHFVPHAQTG IDRKGCPIIF KVMGANCRVK LAVEAGYSLD AIGRYNVWLN
ESYMDALAAA KAREWSVVID AAGWHLGLFD SYGFKFLKQT ATTDSSHYPE LLSTMLIVNA
PPVLAVAWRV IRTWVDEDTR EKIDILSSET SRARLHKMAD PAQLPAQYGG TAKPLPGWPP
EAGVP
//
