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Database: UniProt
Entry: A0A0M0JI91_9EUKA
LinkDB: A0A0M0JI91_9EUKA
Original site: A0A0M0JI91_9EUKA 
ID   A0A0M0JI91_9EUKA        Unreviewed;       871 AA.
AC   A0A0M0JI91;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=Ctob_001689 {ECO:0000313|EMBL:KOO26037.1};
OS   Chrysochromulina tobinii.
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC   Chrysochromulinaceae; Chrysochromulina.
OX   NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO26037.1, 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:KOO26037.1}.
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DR   EMBL; JWZX01002898; KOO26037.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M0JI91; -.
DR   OrthoDB; 125885at2759; -.
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; cd00106; KISc; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 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:SF999; KINESIN-LIKE PROTEIN KIN-UB; 1.
DR   PANTHER; PTHR24115; KINESIN-RELATED; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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          22..345
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          407..452
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        8..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         110..117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   871 AA;  94801 MW;  FC1268A6594038AD CRC64;
     MAPKKTSSAA KDKGEGEEGA SRVHVVVRIR PPVRKDEKFG EGSEALQYDA EKNMLFLLAK
     DDTGKAIPKQ YVFDKVLWKD SVQQDAWEAA GLSVVKSVLQ GYTGCVMCYG QTGAGKTFTL
     ANEKPGQEGV MIQAFHYIFN TLKEERELKY EVQIAYQQVY LDGISDLLQP NTPVELREDP
     KEGVYVSGAK WQDCTTTQEA IATLQKGNSN RATSATKMNA DSSRSHAILM LKVKCTGGTR
     TLNGMLYLVD LAGSERIKKS GVEGAGLDEA KAINQSLTTL GRCIEVLASG KKEKPPFRES
     KLTRLLSNAI GGGAKTTLIV CTAPTMTDQF ETTNTLDFGQ QAMNVVVRAK VNASTDYGSL
     TASLLQQRDK KQKAIRELEA TVLRELGPKL DEVYDLEAKC KDSAMQVELM EEKVDMEKDR
     CAKAKALGET EAEADQAKMV QLLNERAKTT EELERVLLSL STDPEMKRIQ TEHEQEKADV
     TKRSMLLQEQ LRTSESAERA EGRKVEAKLD GVIHTARNLG QIAVYFLQTG AMEEAANFFM
     RAKAIFDDCL GTEHPQTVQW HEDLFFLIHA PTIQAMVKDA QRTIAPPEGF DASALDAMED
     EGGMPAQNWW MGNLFDMNTR TGDRGDEDED LSSQWWMQNL YTMGSHSSGP RVDDSAEEAS
     YMHVIFGTPR GGTNTSRGVN TARGGPAFTP RGTLVALSQA GGKAGAALSL GMPLKQAGIP
     ENSAAEDAVN MGFAKDWVTQ IFATPRGHGG DDDEKSMALR VAEAAQWLHE NFGLGGVSGS
     DTATSSGSSM AGTRTPRTAE MENAYAAMSQ LFTPRGKQDT SLRGLTVKTD DAVMAAAMKA
     ALSTPRQSSQ VVDDAPMAGA VNKMFKGRQA L
//
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