ID A0A1R2CHW7_9CILI Unreviewed; 580 AA.
AC A0A1R2CHW7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=SteCoe_9499 {ECO:0000313|EMBL:OMJ88546.1};
OS Stentor coeruleus.
OC Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ88546.1, ECO:0000313|Proteomes:UP000187209};
RN [1] {ECO:0000313|EMBL:OMJ88546.1, ECO:0000313|Proteomes:UP000187209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM001 {ECO:0000313|EMBL:OMJ88546.1};
RA Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA Sood P.;
RT "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT introns.";
RL Submitted (NOV-2016) 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}.
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:OMJ88546.1}.
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DR EMBL; MPUH01000148; OMJ88546.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R2CHW7; -.
DR OrthoDB; 316647at2759; -.
DR Proteomes; UP000187209; 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 CDD; cd00106; KISc; 1.
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; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR PANTHER; PTHR47969:SF33; KINESIN-LIKE PROTEIN; 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; 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:UP000187209}.
FT DOMAIN 39..375
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 438..465
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 506..533
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 121..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 580 AA; 65600 MW; 237797AB398D965E CRC64;
MKSEAPPSQH SSASSHKIPS HPPSISGASS MLEQDGGESV KVCVRIRPMS QKELLAGNTN
CIEVQNPQLL HLKQKSNIRQ YAFHQILEEN IDQAHVFSET GVGSLLESSL DGYSCTIFAY
GQTGSGKTYT MAGSEERLGR ADYVSDESDG IIPRSISYVW QRMNSRNEKF FVKSGFFEIY
NEQVRDLLNP SSGVKHCRWN LKQGFFVEEL MVVDCLSIDD MIAVLNEGMR NRKSGSHELN
ADSSRSHSIL MTYFISEITS EEGHSIKRYG KSYFIDLAGS ERLKETQSSG GMLVETKNIN
RSLFVLGKVI SSLGDKKNRG LKPHVPYRDS KLTMVLMDSL GGSSRALMIA CVSPAISYVE
ETASTLNYAT RAMNIRNKPI LQVDSQEHLI LNLRREAHLL KMENDYLKEQ LSRATGGLPP
LMVDYANSKS ATPKETNINQ YQNEVNTLRD ENLKLREGRE NAEKSYHKLM IENQNFYLKL
ENLESTFVGA GLKDEGRPKI SQNYTINTLI NENANLKKRL NSLQQENSEI TAKYGDNTYV
NPDDFKSLQS IHTQLQYKVE ELQRRERELL DLIFKTKKKE
//
