ID A0A0M0JNG9_9EUKA Unreviewed; 1459 AA.
AC A0A0M0JNG9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Kinesin motor domain containing protein {ECO:0000313|EMBL:KOO28131.1};
GN ORFNames=Ctob_003836 {ECO:0000313|EMBL:KOO28131.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO28131.1, 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 -!- 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:KOO28131.1}.
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DR EMBL; JWZX01002616; KOO28131.1; -; Genomic_DNA.
DR OrthoDB; 239968at2759; -.
DR Proteomes; UP000037460; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR012668; CHP02466.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
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; PTHR47971:SF8; KINESIN-LIKE PROTEIN KIF24; 1.
DR PANTHER; PTHR47971; KINESIN-RELATED PROTEIN 6; 1.
DR Pfam; PF13759; 2OG-FeII_Oxy_5; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00248; ANK; 2.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000037460}.
FT REPEAT 829..861
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 862..894
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 952..987
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 1162..1459
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 922..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1252..1259
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1459 AA; 161161 MW; 996EE89E16EF4089 CRC64;
MGCDNSKMEA RDSERDPRWD VEGFSRWAEA CQLAWVRVGY LRELNELGKP IPYQQLAPRG
SLWIGVPPPD VQLYAISPYT WLGEKGPREE WSRPPTDNEQ MHSDPDGFLL QHMVEYLNQD
GALDDDLALM LHISAMCFAP TKREVALWDA YMEGSMYINT HYRIKCVPVC EVPETFSGEP
VLERMWGIHE FFLSAYCQRI VNPTAPLIKP NLTPEKLRGA HELLKSAPCT SEPERERVLR
LRRQAFSSML PAREDAVGFQ KVCEQSGFRW VFVRFVQELA ARGGPAPRCQ DLPYGTYVEG
RVPEGVRHYV VSHGWAAHLH FDPSGSKIHL LAATLGRMGA ARDDVVFIDY MSLTQAGGWV
PKAYLRFNPG AQRHVEKEAD GSVKKEADGS VLLSGRTEAQ ERRFRFALFE TTRLYAFRPA
HGPNVIILPD LAPPESFPEP GEITREWNTV CQPPREEQKS AWGFSKSIKY ENAGWPCAEY
AVSRMNKNIA NSEDEPVRGY LTENTCEDER VVRLNEDICD AMGLPWYETL CNGLEGRYQG
LLSQQRAYVS VTQARMKIFG WWEPEGAAST PFNGLNRLRR RGWIGEKPGL TFMWTTPVLR
LSMLEADAEP LLELAERIAR SFGDFSSRCV TRRGETANDA FFAEQHSAWE KDDDRFLAAF
DGGTGLLLHQ LRAAWVKNIE AYVSGSVGEE AAAALFGGAD TLPLFIWASV HQGCSTHTAH
VHENSAVSGV FYVRVPARSG AISFEVGTAM HAFARDQPPI GIDIARRAAS HLWGMKTTPT
NSDRDETAFD PEATGKKLFD AAVNGRGKVV REILAAAGRG PYIDYKNSFG QTPLYMASYG
GKHECVKMLL EHGAGVDLQT ASGRTALIAA ALDEKPECVK LLLEYGASVS AVDAKGKSAL
DHARAKGFTA IVSMLELSVQ RSPKNSVPRG NRSPKSLEIS DCAPPPLRSP GERGRMVEQA
FRRIDSDGDG RLSRAKVLSA CNDDDEVRAL LGLPHHVLQK IVDAAFDRLR DDTRMIELDE
FQRVFADAHE AHAQVCDEID EIDEIDEIDE IDEIDERLIL TVFADALLLR ADPGRTRMST
PRKNDVNARI EEMAVQREER RLHAIRHKQQ RAADAIAAEA YGGLDSLAFL SAIRDYRELH
GIGTPEGWPE GSTVWRSESG SSTRVCVRVR PMLAAEISRL DFEVVSSENH RAVAVHVPRV
KVDLTKAIES HCFGFDGCFN AADGNDAIYA ACVQPLVAHV FSGGYATCFA FGQTGSGKTC
TMAGHGNPAA KDGNEIGIYA LAADDVMQAA GEAGFAVRVG VSFFEVYRGL VLDLLGGCSR
CEVREDGDGT IHVVGLREVR VHDASGLLEL VHQAGRVRAT GATSANETSS RSHAILRITI
REPIPGQWPV VGMLSLVDLA GSERAADAQH ADEQTRIEGA EINKSLLCLK VYACKTDVFE
LLRTRLDAVQ ARLGGIKGG
//
