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Database: UniProt
Entry: D6WKA3_TRICA
LinkDB: D6WKA3_TRICA
Original site: D6WKA3_TRICA 
ID   D6WKA3_TRICA            Unreviewed;      1712 AA.
AC   D6WKA3;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 2.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN   Name=AUGUSTUS-3.0.2_14111 {ECO:0000313|EMBL:EFA03966.2};
GN   ORFNames=TcasGA2_TC014111 {ECO:0000313|EMBL:EFA03966.2};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA03966.2, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EFA03966.2, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA03966.2,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA   Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA   Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA   Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA   Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA   Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA   Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA   Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA   Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA   Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA   Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA   Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA   Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA   Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA   Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA   Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA   Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA   Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA   Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA   Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA   Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA   Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA   Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA   Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA   Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA   Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA   Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA   Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA   Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA   Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA   Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA   Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA   Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA   Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:EFA03966.2, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA03966.2,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT   for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
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; KQ971342; EFA03966.2; -; Genomic_DNA.
DR   STRING; 7070.D6WKA3; -.
DR   EnsemblMetazoa; TC014111_001; TC014111_001; TC014111.
DR   eggNOG; KOG0242; Eukaryota.
DR   HOGENOM; CLU_241739_0_0_1; -.
DR   InParanoid; D6WKA3; -.
DR   OMA; YEQHETL; -.
DR   Proteomes; UP000007266; Linkage group 5.
DR   GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
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:SF36; CENTROMERE-ASSOCIATED PROTEIN E; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000007266}.
FT   DOMAIN          4..324
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   COILED          347..381
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          493..545
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          608..649
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          689..1233
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1263..1371
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1482..1512
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1586..1620
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1681..1708
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         87..94
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1712 AA;  201399 MW;  D88C8B054EB03161 CRC64;
     MSTNIQVAIR IRPLIASEEA KKLQVQWGTQ KNNIFQIDDN GQKFGDVFSF DHIFGVDKTN
     TDIYDNIVKD FVESSLNGLN STIFAYGQTS SGKTYTMLGD KKHRGIMSLA IENIFEHIEN
     STDRKFLIRV SYIEIYNEKI YDLLDPSNKE VKIREFFPAT IGLQNIKEEI VTSRKQMYEC
     LRTGTLNRHI AGTKANDRSS RSHTIFKITI ESTQVSDFTS GPVQVSSLNL VDLAGSERVA
     QTKATGVRLK EGSHINKSLS ALGLVIRQLS DGQEFINFRD SKLTRLLQDS LGGNSKTLII
     ATITLASIED TCSTLAFAQR AKAVKNKPHV NEILTDADLS KRYASLNSQL QKKLEEQLRI
     NQKLQETQEV NVREMSRLQQ QMELIEHFQR GKISEIPSIP KRRHTIGFAT PMPLSSIVFK
     PDCDTSNQDP HSLLFLDEFS SKDHTALGNT LETIVEEDFI TPMKRNLEKQ RRSSYSSVCS
     EFPVEDNDAL KKITELEEEI YNEKQKQQEC EIQLKELNDK FKLREEDLCN KILELEKKLE
     NENSDNFYST IIGFKDQLLY LQQILSNEKI ETEFSNSYSE KDLTNKSYSL ELSEVKECDE
     LHLELMDKEQ EERKCLSILE ENEKLKMELI HYETKNKFLT DELDRLTTEI KQKHTLKNSN
     EMELTLDEYE LKQDYIKLKN EFTASCTENE FLQKSNEEMK RKIEKYDSLK QEYIQLKNDL
     TTSRTENDSL LKLIEEMKGR IEEYHSLNIQ LQNKLKMNRK TEEYDSLSQQ YIQLKNELTS
     SSTEKEFLLK SNEEMRRRIE EYELLEQQYI QFKNEFTTLC TENDALQNSV EEMKRGIEEY
     QSLKSEYIQL QDEFNAFCSE KESLKKSNEE MKKRTEEYEL LKQQYIQLKN EFNASCTEKD
     SLQKLNEEIK RIVEENESLK QEYIQLNNKF NASCTEKDSL QKSNEEMKRK IEENESLKEE
     YVQLKNEFSA TCREKESLQK LNEEIKRRIE ESESLKQEYI QLKNKFDASC TEKDSLQKSN
     EEMKRKIEEN ESLKEEYVQL KNEFSTTCRE KESLHKLNEE IKRKIEESES LKQEYIQLKN
     KFNASCTEKD SLLKSNEEMK RKIEENESLK QEYAQLKNEL SASCREKESL QKLIEESKRE
     VEESESLKQE HIQLKIKFND LCAEKDSWQK SNEEMKRKIE ENESLKEEYI QLKNEFSATC
     REKESLHKLN EKIKRKIEES ESLKQEYIEF KNKFTALCTE KDSLLKLEYA QLKNEFKVSC
     TEKDSLKKSN EEMRMIIEEQ KKKIENMKIC NDKLNLEIRN KETNSKEQLC TMSSQNNYLK
     NELEKLKNEV ADQKRIISAN KEKLHCNDLE LQKQKRRLLE GEEHVKELEY KIRQSSEKES
     NFRTIIEAQN VTIDKLNLKY RNILGSIMEY FISEQKSLLL IRHSQDEREN FKSIIRDLKT
     NNATLKSQVE QLRNENNCDL CAIQETIKKS HLIFKDYFSL EKTFLKAQII DLENTNEEYL
     KEMMALKDQQ RNDSTEDCSN CDKLQNEITR LTEVATSQDK LVVTLEKENS TLRKERFESV
     KQVVHLQQQI FDEQDKKSEL QYTEWMKFLQ DNNKLQQQEI RELKRKIKKY ENMHSRSVNK
     QSVGTECNLL GAPATEIDKS KNVRVEDVQN GCLHFSGKIS TIHAEVQCNI FSEPSALQEK
     YDLLKQIYRK KNNEIQSLNA EINQLKLKVS SL
//
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