ID A0A1R2BDX2_9CILI Unreviewed; 821 AA.
AC A0A1R2BDX2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=SteCoe_26021 {ECO:0000313|EMBL:OMJ74957.1};
OS Stentor coeruleus.
OC Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ74957.1, ECO:0000313|Proteomes:UP000187209};
RN [1] {ECO:0000313|EMBL:OMJ74957.1, ECO:0000313|Proteomes:UP000187209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WM001 {ECO:0000313|EMBL:OMJ74957.1};
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 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:OMJ74957.1}.
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DR EMBL; MPUH01000719; OMJ74957.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R2BDX2; -.
DR OrthoDB; 180030at2759; -.
DR Proteomes; UP000187209; 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; cd01369; KISc_KHC_KIF5; 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; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR PANTHER; PTHR47969:SF15; ZGC:66125; 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:UP000187209}.
FT DOMAIN 3..330
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT COILED 335..362
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 420..475
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 589..644
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 88..95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 821 AA; 93259 MW; 9E55E44A45CB79F1 CRC64;
MSGIRVICRL RPQNKVEAEA GGKECIDYTN TSMKIKVQDR ADEFSVHEFT FDHVCGPEVA
QSDLFEFAAR PVVGGVLNGY NGTIFAYGQT GSGKTFTMEG PDIMNTQYKG IIPRMMDALF
EGLVNASESS EFTLKVSYLE IYLEKIHDLL DPAKNNLQVK EDKIRGIYIQ DATEIYVGSP
IEMLKAMSNG SANRAIAATR MNQRSSRSHS IFCVYVEQKD TKAGSKTSGK LYFVDLAGSE
SVGKTNVSGK QLEEAKMINK SLSALGNVIN ALTDKNASFI PYRDSKLTRI LQESLGGNSE
TTLVIACSMN SYNDKETLST LRFGQRAKKI QNKPIVNQEK SAKELMKQLE LAQKEINKQS
EIINSIRTHI SQNYSSNQKL MSEISDIVQG SYAVQGFHAV QPTHAHIQVA KTESENSLVL
LKQHIELVKL NEELQEIKVE KQELEDELQF RNKDVREYEI QVANLQAMLQ EERESRSFSE
KASNDTQQIL DLCTIAKNCE KLRLNLVLAY NEIPKTEQWA EVVLKSIQET LISLQVLDND
TKMQTSDMST ILDDKVNNSS ESFFMEYKDV VGDNSLDSSK VVDNKALKIV ELANEIDKIK
SVVEKKNKKI SHLKEILNQK TENIETLQKQ LDMKVRNIEE ERASVIIEMK YKDEEIIELK
QLLTMERERL VQNLRLDSPK QKIIDMEDRL EHLSLDRQRL FEDIVTLRKT IDQKDEIINK
LTFRNERLER QINFQGFKNV QNPLGQSTEI NILTKKVRKP IKGGGGDIWN FQKSNQTIIT
TEKQDIQDPQ KKNHVKIQRL RNSQGGGFQS LVKDIFGGIL G
//
