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Database: UniProt
Entry: A0A1R2CT42_9CILI
LinkDB: A0A1R2CT42_9CILI
Original site: A0A1R2CT42_9CILI 
ID   A0A1R2CT42_9CILI        Unreviewed;       852 AA.
AC   A0A1R2CT42;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=SteCoe_5137 {ECO:0000313|EMBL:OMJ92148.1};
OS   Stentor coeruleus.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC   Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX   NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ92148.1, ECO:0000313|Proteomes:UP000187209};
RN   [1] {ECO:0000313|EMBL:OMJ92148.1, ECO:0000313|Proteomes:UP000187209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM001 {ECO:0000313|EMBL:OMJ92148.1};
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:OMJ92148.1}.
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DR   EMBL; MPUH01000067; OMJ92148.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R2CT42; -.
DR   OrthoDB; 179989at2759; -.
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; PTHR47968; CENTROMERE PROTEIN E; 1.
DR   PANTHER; PTHR47968:SF17; 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; 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          6..331
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   COILED          401..484
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          527..641
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          709..810
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         89..96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   852 AA;  97591 MW;  FD13C19818FF4A5F CRC64;
     MEDQNNVRVV CRFRPLNDLE CQRAQGLCVS FSDQTVCVNS QSDSAENLKF TFDKVFTPES
     SQEAVYNFAA KPIVEGVMQG FNGTVFAYGQ TSSGKTFTMS GPDLEDPITM GIIPRMVNTV
     FDFISDTDNN TEFTVKISFC EIYMEKIKDL LNPTEGNLKI HEDKIKGVFI EGLTEMYVSN
     DIEVHEIMKE GNENREVAST YMNAVSSRSH SLFIITVNQT NSKDFSGKVG KLFLVDLAGS
     EKVAKTGAAG LRLEEAKHIN KSLTALGQVI NSLTDGKSTH IPYRDSKLTR VLQDSLGGNS
     KTSLIVTCSP SPYNEAETIS SLRFGIRAKA IKNKPKVNRE HTVAELKLLL AKCQEEVEKR
     DRIIAKLENK LKSQGDSLLD ISTCSRQSQE KIDADDIMAE IDELKYRLEE QIDISKKLKD
     NNDKLLRELA EIKSERSMMI QQLEETQQRT SYAEKSVKEQ EVVIEKLVLT KDSLEKSIEI
     AMKNKISSDK IITEKDSEIF QLKQDLLMNS PQKQRKSITF AVSPAELQKV KSQNSELKKE
     LELTKDQLKA TVKEYNKVID ENEILRDKQS SSYRKTETFK TVSPEVVSLK EEIEDFKMML
     NQLQSESEVQ KLQINEKDIE MLKIKEENEN LKKKISDIQG TIDEILTTKP PEPQIPETKI
     KSPELHKHEE NFAEMLLAKE KSQYEEQRKR WDSERKDIMH DLENRINRVI ELEITLDLAK
     EAHRNLEKNI GKNEKELIAK NQYMEKYISK LGSELQKEQL LKEKIKTECE YNEKKLKEQL
     DRVRVLEAEC EEFKKKQLRL ESRLKFAEEE AYNANNMRNR PSINHGNVRK PIKGGFNAER
     LTIMSPIAEV GN
//
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