ID A0A0S4J9R7_BODSA Unreviewed; 1049 AA.
AC A0A0S4J9R7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Kinesin, putative {ECO:0000313|EMBL:CUG86974.1};
GN ORFNames=BSAL_00980 {ECO:0000313|EMBL:CUG86974.1};
OS Bodo saltans (Flagellated protozoan).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Eubodonida; Bodonidae; Bodo.
OX NCBI_TaxID=75058 {ECO:0000313|EMBL:CUG86974.1, ECO:0000313|Proteomes:UP000051952};
RN [1] {ECO:0000313|Proteomes:UP000051952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR EMBL; CYKH01001418; CUG86974.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4J9R7; -.
DR VEuPathDB; TriTrypDB:BSAL_00980; -.
DR Proteomes; UP000051952; 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; 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:SF418; KINESIN-LIKE PROTEIN KIF12; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Reference proteome {ECO:0000313|Proteomes:UP000051952}.
FT DOMAIN 3..677
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 44..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 692..719
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 142..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..208
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140..147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1049 AA; 113029 MW; 38685AF3EB2E8A15 CRC64;
MPNVRVVVRC RPSTLDNSRH GNEVLHSPSS SSWSFDAQTI RLSTGGQDAS HGTVSSSRRQ
TFGASSSPHS TAPTLEKAFQ FNRVYALGET QESFFNAEVR PLLNSALGNN TTSSTTVVQS
DSPVENANEA PRHVVLFAYG QTGSGKTHTV DGQRAATTAS KEERAAAGAP TDPKPLTRQA
SGQPKDNVTE DRDDDGDFIE EQEGDEDHQY DENPSSSDTT AAQQQHQQRA AEGVAPRALR
YIFDSWKDQR RSKDYNANGD LSMASSLLNS NDGGVNHDDA VESGATCDGF ELVKVSVSFL
EIYNEKLYDL LSATCRTGAG SPQDQLMKKK KKASKVPTTV EALAAMHATS LRLRRCPDAS
AHGPAKFEVE NLTKLSCVTV DEALEYYYYA VSKKIFRAHN LNSQSSRAHS IFTIYLTFRD
LSGGASGVVP GGASAFDGTL TGGGGRGILD QASFVTSEIA IVDLAGSERL HSILPQGHHH
DTLGSNATNH NSQRPPASPR HSAGTAANSF GASHQQQQQR PSSGPVGGGN VYLEGIRKQQ
QQTALITESI HINKSLLTLG KVIMALSSGS SSSRAGGGST ADPQPPTTPL AASARGNSRG
VGTPRGGGHP TTTAANRSTT TAVIKHTPFR DSKLTMVMNH ALGGNALTVM VACIHTDPSQ
VHESLSTLFY ATRTNKIANV VVSLEDPKTQ RIKSLLAEVQ RLKGELQASQ TTIEDLSMML
AKGNVRGGVP WVDRGDSGQQ KSVAYQKATT PAAEVGHDPK EETDGAVKMN SDHTIIHEEQ
KLLTDTLSSK LHEACLKLKT ALEANTRLRS AFDVERQRSA AIERDQERML EENLRLREKL
DLYDSLLLAQ IAINRQYDEK GDTPSSRNNV SAVADARKRC GKPNLRASAA GIESLTAVFF
QQQKKLLTGG SQQQQQQQQQ PTLLSPRVSQ KLSSHHNHKN QYSSLSPKRQ TRRSYDTHET
LHLTSSSWSD TQATTWRQPH SQLVPSPPPA SLSYGESQHQ QQQQQRPASA STRTPNTAAT
PIVGGGSFRS GLPLHLLVGG SSQSSSTKL
//
