ID A0A210R381_MIZYE Unreviewed; 603 AA.
AC A0A210R381;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=KP79_PYT16653 {ECO:0000313|EMBL:OWF55341.1};
OS Mizuhopecten yessoensis (Japanese scallop) (Patinopecten yessoensis).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Pectinida; Pectinoidea; Pectinidae;
OC Mizuhopecten.
OX NCBI_TaxID=6573 {ECO:0000313|EMBL:OWF55341.1, ECO:0000313|Proteomes:UP000242188};
RN [1] {ECO:0000313|Proteomes:UP000242188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PY_sf001 {ECO:0000313|Proteomes:UP000242188};
RX PubMed=28812685; DOI=10.1038/s41559-017-0120;
RA Wang S., Zhang J., Jiao W., Li J., Xun X., Sun Y., Guo X., Huan P.,
RA Dong B., Zhang L., Hu X., Sun X., Wang J., Zhao C., Wang Y., Wang D.,
RA Huang X., Wang R., Lv J., Li Y., Zhang Z., Liu B., Lu W., Hui Y., Liang J.,
RA Zhou Z., Hou R., Li X., Liu Y., Li H., Ning X., Lin Y., Zhao L., Xing Q.,
RA Dou J., Li Y., Mao J., Guo H., Dou H., Li T., Mu C., Jiang W., Fu Q.,
RA Fu X., Miao Y., Liu J., Yu Q., Li R., Liao H., Li X., Kong Y., Jiang Z.,
RA Chourrout D., Li R., Bao Z.;
RT "Scallop genome provides insights into evolution of bilaterian karyotype
RT and development.";
RL Nat. Ecol. Evol. 1:120-120(2017).
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:OWF55341.1}.
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DR EMBL; NEDP02000696; OWF55341.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A210R381; -.
DR STRING; 6573.A0A210R381; -.
DR EnsemblMetazoa; XM_021514735.1; XP_021370410.1; LOC110461308.
DR OrthoDB; 129693at2759; -.
DR Proteomes; UP000242188; 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:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR Gene3D; 1.10.150.280; AF1531-like domain; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
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 InterPro; IPR010994; RuvA_2-like.
DR PANTHER; PTHR24115:SF1000; KINESIN-LIKE PROTEIN KIF22; 1.
DR PANTHER; PTHR24115; KINESIN-RELATED; 1.
DR Pfam; PF12836; HHH_3; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00278; HhH1; 2.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 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}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
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}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000242188};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 7..329
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 347..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 86..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 603 AA; 68012 MW; 5D602FD14BDD3BBF CRC64;
MDKKKSKVTV VVRVRPILKA EDKNCVSCVA NSIEIFNHRN VNENIKYDFT TVYDMTATQQ
KLFQECLKPK LLHALQGQNV SIFAYGPTGA GKTHTMLGTS SNPGVIPRVI NGVFQKISEE
KKACKGEQWK YNVSFSYLEI YNEKVMDLLD VKNSDLPIRE DGDKNIFVPG LAKREIESFD
EFKVHFGPAS NNRTVAVTKL NDRSSRSHCI LRLDLRKSQL CAPFRELHGK IYLIDLAGSE
DNRRTGNQGI RLKESGAINK SLFVLGEVVD AINNHLPRVP YRNSKLTRLL QDSIGGSCHS
VMITNIAPEQ RYYYDTYCTL NFASKSKKIV NSTCVRETIP SRQELARKTP VRPDDDEASL
PKKARMSVKV ANTPPTMQDP APFLSPLLRR QNRLEETVNR RLEDLEKNIL NQMREMAHTN
GQPASNPDFM SQLQKQLEAS RQQLQTIAHH TPPSSPVPPR VLADKTNASP VKTKKSKLKR
QKSENDISCS PLFAAQPRVF KKGFRSSASS SRLLDTKSPK TDDSCGSIDL QMSINEEFLT
RLNTSTVKDL QSLQTVGVKR AKLIFEWREA YGLFSNYEDL KKIPGFTDKY IGNLLKSNLV
AVS
//
