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Database: UniProt
Entry: A0A1R2CN35_9CILI
LinkDB: A0A1R2CN35_9CILI
Original site: A0A1R2CN35_9CILI 
ID   A0A1R2CN35_9CILI        Unreviewed;       736 AA.
AC   A0A1R2CN35;
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_7291 {ECO:0000313|EMBL:OMJ90375.1};
OS   Stentor coeruleus.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC   Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX   NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ90375.1, ECO:0000313|Proteomes:UP000187209};
RN   [1] {ECO:0000313|EMBL:OMJ90375.1, ECO:0000313|Proteomes:UP000187209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM001 {ECO:0000313|EMBL:OMJ90375.1};
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:OMJ90375.1}.
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DR   EMBL; MPUH01000104; OMJ90375.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R2CN35; -.
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   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:SF73; KINESIN HEAVY CHAIN ISOFORM X1; 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          9..335
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   COILED          340..374
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          481..508
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          533..685
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         93..100
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   736 AA;  84021 MW;  D6E9DD0C56A6327B CRC64;
     MSKSSQSGNI KVFCRFRPLN PHEKLTSDLI KLEHDSNISV TVFPQTEHSI PLTFTYDYIF
     TSESTQEDVF TIAAKPIIED VIQGFNGTIF AYGQTASGKT HTMTGHDIFD PYTMGIVPRM
     ISKVFDSIES ADENVEFAVK VSYCELYLEK INDLVEVDKK ALKIRQDRSK GVYIANLSEH
     YVASDFDVFE LLRVGTENRQ VSCNKMNTKS SRSHTLFSLT ITQNNALDLS ARVGRLYLVD
     LAGSERVSKT NAEGQRLKEL KTINKSLNTL GQVINQLTDG KASHVPYRDS KLTRILQDSL
     GGNSKTAIII TCSPALSNES ETISTLRFGF RAKSIKNKPK VNRELTMAEL KLKLAKIEEE
     LRKKAIKIST LEQALSQNEV TLPIDTTILT EHTDESDDLK NTDTDDFFAE LEDARNKLTT
     LVDENFKYKT SSIELKSNLD QMNDNNINQT ALISVLEMKI VNMETAIYNK VELTSKLSIE
     KDVLTTKLEE VQNKKLELER IYNEKLVESN DLKFQVKMHV GDDEISSEPV DLIEQLKNKL
     MSEQQKYKKN QTEMQGLQIR LNQALQELTR DKRNEEKELL NREIQARNEK IKFLEDELET
     ITENHRSVKK ILSEDEETLK QRTDELERTL DELTNMYKQL LAKQSSVNIE KQLNIRKITR
     LNEKIKLLED ELKTKREQLM TAEVEANRFL DDMASQSIFN RIKVPIKGGG GKGVRASMAN
     RLSIRPNRAY ASMVSH
//
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