ID A7SRC2_NEMVE Unreviewed; 569 AA.
AC A7SRC2;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=NEMVEDRAFT_v1g192682 {ECO:0000313|EMBL:EDO33740.1};
OS Nematostella vectensis (Starlet sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Edwardsiidae; Nematostella.
OX NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO33740.1, ECO:0000313|Proteomes:UP000001593};
RN [1] {ECO:0000313|EMBL:EDO33740.1, ECO:0000313|Proteomes:UP000001593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX PubMed=17615350; DOI=10.1126/science.1139158;
RA Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA Technau U., Martindale M.Q., Rokhsar D.S.;
RT "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT genomic organization.";
RL Science 317:86-94(2007).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS469760; EDO33740.1; -; Genomic_DNA.
DR RefSeq; XP_001625840.1; XM_001625790.1.
DR AlphaFoldDB; A7SRC2; -.
DR STRING; 45351.A7SRC2; -.
DR EnsemblMetazoa; EDO33740; EDO33740; NEMVEDRAFT_v1g192682.
DR eggNOG; KOG0245; Eukaryota.
DR HOGENOM; CLU_001485_2_3_1; -.
DR InParanoid; A7SRC2; -.
DR OMA; PRICENM; -.
DR PhylomeDB; A7SRC2; -.
DR Proteomes; UP000001593; Unassembled WGS sequence.
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:0008574; F:plus-end-directed microtubule motor activity; 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; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR000253; FHA_dom.
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:SF6; KINESIN-LIKE PROTEIN KIF1C ISOFORM X1; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF00498; FHA; 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 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}; Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Microtubule {ECO:0000256|RuleBase:RU000394};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000001593}.
FT DOMAIN 3..359
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT BINDING 102..109
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:EDO33740.1"
SQ SEQUENCE 569 AA; 63635 MW; 9D62C2330B3E6097 CRC64;
MASVKVAVRV RPLNNRENNM GAKTIIEMEG KKTRIYNVKG TNVTGEGERK NYVKDFSFDY
SYWSVDERSR HFVNQERVFK DLGTDVVKAA FEGYNACIFA YGQTGSGKTY TMMGHNGDTG
LIPRICENMF HRMTENSNAD DGVSFRTEVS YLEIYQERVR DLLRPPTKGR AAHSLRVREH
PKEGPYVQDL TKHLVSDYAA IEHLMEQGNS HRVTASTGMN DVSSRSHAIF TMNFTQAKFD
MELPCETASK INLVDLAGSE RADATGATGE RLKEGANINK SLVTLGTVIS ALADASTGHG
SHGSHHKFIP YRDSVLTWLL KDSLGGNSKT IMIATISPAD VNYAETMSTL RYANRAKNIM
NKPTINEDPN VKLIRDLRSQ IEKLKAMISP VSQLKALKDL LGEAELAAAK KLSENEARVT
QLTDKWKDRW KETQKLLQER EMKLQEEGVG IKMDSILPHL VLVDDDLLST GITVYHLKEG
KTTVGLTNPN STQDIVISGP DTQANHCEFE HTKSGTVILS PLESLCYVNN NEINKPTRLK
QGDVIILGQT NVFRFNHPKE AAELREKRK
//
