ID C3YMN7_BRAFL Unreviewed; 1394 AA.
AC C3YMN7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
DE Flags: Fragment;
GN ORFNames=BRAFLDRAFT_234346 {ECO:0000313|EMBL:EEN58378.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN58378.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN58378.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN58378.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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; GG666531; EEN58378.1; -; Genomic_DNA.
DR RefSeq; XP_002602366.1; XM_002602320.1.
DR STRING; 7739.C3YMN7; -.
DR eggNOG; KOG0241; Eukaryota.
DR InParanoid; C3YMN7; -.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 6.10.250.2520; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR022164; Kinesin-like.
DR InterPro; IPR022140; Kinesin-like_KIF1-typ.
DR InterPro; IPR032405; Kinesin_assoc.
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 InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR47117:SF3; KINESIN FAMILY MEMBER 14-LIKE; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF12473; DUF3694; 1.
DR Pfam; PF12423; KIF1B; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF16183; Kinesin_assoc; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 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};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}.
FT DOMAIN 1..307
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT COILED 636..663
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 56..63
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EEN58378.1"
FT NON_TER 1394
FT /evidence="ECO:0000313|EMBL:EEN58378.1"
SQ SEQUENCE 1394 AA; 157163 MW; A652C0CB27563FF5 CRC64;
PFFPPLQTFA FDHCFWSMDE TNTEKFSSQE TVFKCVGADI LENAFQGYNA CIFAYGQTGS
GKSYTMMGTA DNGGLIPRLC ISLFESIMSK SNEILSFKVE VSYMEIYNEK VRDLLDPGTT
KHNLKVREHK ILGPYVDGLQ ILAVTKYEDI EKLMNEGNKS RTVAATSMNE ESSRSHAVFN
IIVTQTLKDL ASGVTGEKVS KVSLVDLAGS ERAAKTGAAG ERLKEGSNIN KSLSTLGLVI
STLADQSAGK GHKNKFVPYR DSVLTWLLKD NLGGNSKTAM IATISPALDN YEETLSTLRY
ADRAKRIVNH AVINEDPNAR IIEKLREEVD KLKVQLTEAE SLKAPDLKER LVESEKLMKD
MTTTWEEKLA KTEKLHQERQ QALEKMGISV QTSGIKVEQD KNFLVNLNAD PSLNELLVYY
LKVENISKFK VQYVLCIFKL GCLKSLKEDY KTSQLWFDFL RCCVNGDCVT QKTLLRNGNR
IFLGNHHFFR INCPRSGPTV TMNSLHNHTM PVVRYIFAPL PLGSVASTPD VEVSRADYDF
AQNEVMMVEL MNDPIQNAMK SLESQHEKDK EGALEKQREM YEKKLEVLRQ QLSSPVQNKQ
TVESFGGLSH GVSNPNLHPR YTQWVEERDE LFRQGLAKLR EEIVKANALV REANSLAQEL
EKMTEFHVTL QIPASNLSPN RKRGIIISEP AIQVKRKGRS TQVWSMEKLE NRIIDMRDYY
QEVMEQGREI QVREGDMEDR EDPFYESQEN HNLIGVANVF LECLYHDIRF EYAVPIISQQ
GEASGRLHVE VVKVAGTIPD RLQADARSDG SSSESHSSFE IIDQEGEGAP LGGPLTFRVS
ALRYLTQGFS LFPQLKILEA TDLPPSLSHF VFCQYTFWGH PSSVVVPPVI NPELPSYRSV
KGTTMRFEHS REFTVNVTEE FMDFLENGAW SIEVWGHRSA GFDSTKPGWE VDHVSQKAKS
LSDRWGELIR KIELWVEIQE LNEQGEYTPV ELQVKPEVLT GGVFQLRQGH SRRIQVKVKP
VHNSGTLPII CESITSIAVG CVAARSKLQK GLDSYQEDDL TLLRERWSEA LMRRRDYLDK
QIQQMINKEY KTDNDKEREG SLIDQWVCLT EERNAVLVPA PNSGIPGAPA DWSPPHGMEI
HIPVLFLDLN ADDMSTPGLR EGPQAAGVNS ILPKEHGTKL FNLPIIKYME KDVKESLTLS
QLLNQGSHLY LRQMFKSQSF SINTVCAVAS WDSSIHDSIN LNRITPSNER VYLITKVTVR
LSHPASMELV LRKRVCVNIY KKQGFMASLK KNLDIGQKDM VTACGITYEV VSNIPKASEE
IEDRETLAMM AVSGVDNETT EGESYIEKYT KGVSAVESIL ALDRLRQEVA VKETLAAIGR
PLRKVASVPN IQQV
//
