ID K0RKT9_THAOC Unreviewed; 973 AA.
AC K0RKT9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=THAOC_26037 {ECO:0000313|EMBL:EJK54343.1};
OS Thalassiosira oceanica (Marine diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC Thalassiosiraceae; Thalassiosira.
OX NCBI_TaxID=159749 {ECO:0000313|EMBL:EJK54343.1, ECO:0000313|Proteomes:UP000266841};
RN [1] {ECO:0000313|EMBL:EJK54343.1, ECO:0000313|Proteomes:UP000266841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK54343.1,
RC ECO:0000313|Proteomes:UP000266841};
RX PubMed=22835381; DOI=10.1186/gb-2012-13-7-r66;
RA Lommer M., Specht M., Roy A.S., Kraemer L., Andreson R., Gutowska M.A.,
RA Wolf J., Bergner S.V., Schilhabel M.B., Klostermeier U.C., Beiko R.G.,
RA Rosenstiel P., Hippler M., Laroche J.;
RT "Genome and low-iron response of an oceanic diatom adapted to chronic iron
RT limitation.";
RL Genome Biol. 13:R66-R66(2012).
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:EJK54343.1}.
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DR EMBL; AGNL01035957; EJK54343.1; -; Genomic_DNA.
DR AlphaFoldDB; K0RKT9; -.
DR EnsemblProtists; EJK54343; EJK54343; THAOC_26037.
DR eggNOG; KOG0247; Eukaryota.
DR OMA; TIIWIVD; -.
DR Proteomes; UP000266841; Unassembled WGS sequence.
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 Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR24115:SF1014; KINESIN-LIKE PROTEIN SUBITO; 1.
DR PANTHER; PTHR24115; KINESIN-RELATED; 1.
DR Pfam; PF00225; Kinesin; 2.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 3: Inferred from homology;
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:UP000266841}.
FT DOMAIN 194..638
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..967
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 303..310
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 973 AA; 106964 MW; 9C63D74C0C221297 CRC64;
MSNESEGGAP SMESCDECRD DAETRRAPAA VFGRLEQESR GAVASHAGGN DEDEEQGDMN
ITRLDDEESN LDINSVISGM EEDEEGNIIG EQDQFEVFGK NLSSCFDNVG RIASSTSQRP
PLPPTRDVVI PTNKPSAAAV PQVVPGAGDK RLSVFLRVRP PVCSNGTKGN EGAANTIEII
ETKSAANQRG YAPTLPTTVR TYPPLNSNAA KVVRCGGKVP TAASSCNSKK APSSKSLIDD
GRADNDSTEV RGVKEYSYSG VFGPKSTQSE VYNNIAAPLV DGLFPRDMDS ESLGESALLF
TLGVTNAGKT HTVMGTGFET KGGKKSTDYP GENWGIIPRA LHHILTRIDG NNSAAATNAG
GPKLQMYMSY LEIYNESIYV RKSLGFSRLS TVCSRHIALP SVQDLLPQKT QNAASRRPCD
GPPTLKLRES RRGRIFVRDL ARHAVSSVQQ GLELAQMAKT NRHTASNNIN SQSSRSHSIC
QLEISLVPTA QKSSDADLSE YETDDESVCS RSSAGRRKSL QRKSTIIWIV DLAGSERSKK
TRSHSSRQQK EAAIINASLM NLMRCLREML NHQPKKKGSS SKAGVIPFRE SKLTHMFMNH
LTGPSASRTC MIVNVNPASD DYDETQHVLG YATTARSVTI SAVDYNRKRR ILAKESRVKL
SPKKALVGVV KKLSPKKRKG GAQQIESMPH ANKRMRSHNH TSTSGSSTKF GGLLNKPRPK
TSHQVTQVDA DAQEELERLR EENFKLKITV EDLGQQLVDC EAEVRGEVVN MMDEQLQETK
QWYESRIDSL KEQITSMQSS PGKSQRNEVD LLERIEECEN EMQRMGEDHK DELSKMALAQ
RRLVQQHESE LRAERQRGER LQQDLGASRH QYTELKASHD NILANLESMK ARQETEDAAA
KENPDEPSNT SSFAFKNLPR ERVSAVASTS SIIDVTSPKK KRGWFKSPGK GKKIGLAEPD
DGERSPLGKI NTK
//
