ID A0A0L8H411_OCTBM Unreviewed; 459 AA.
AC A0A0L8H411;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
GN ORFNames=OCBIM_22022784mg {ECO:0000313|EMBL:KOF84036.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF84036.1};
RN [1] {ECO:0000313|EMBL:KOF84036.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF84036.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF84036.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) 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}.
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DR EMBL; KQ419298; KOF84036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L8H411; -.
DR STRING; 37653.A0A0L8H411; -.
DR EnsemblMetazoa; Ocbimv22022784m; Ocbimv22022784m.p; Ocbimv22022784m.g.
DR OMA; ECKEDIT; -.
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; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR031852; Vik1/Cik1_MT-bd.
DR PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR PANTHER; PTHR47972:SF45; PROTEIN CLARET SEGREGATIONAL; 1.
DR Pfam; PF16796; Microtub_bd; 1.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283}.
FT DOMAIN 307..459
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 126..205
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 408..415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 459 AA; 51858 MW; 384B3DE5CE71E2FC CRC64;
MNNQRRVLAD TANCSSKLPK LTPKLTKRKN SPNETEPVKK MRFEKPVSKI RTNLTSSSRL
ASSRSIPGYN PRRETMPARG NAIMNSTVAK TDKGVAAVRP TLAVSPIEAS KQKLKKRPAW
DLKGRIQDME EQLKNKNSLE QQLYEMTSRI DQLVSQKEHL TGTVTEKEQF ATNVSKEVED
LKRTLRTKEN EIDEMSHKFR REMDEITRRE STLSAQLNGK ELEVIALQSS LAEQSAAHAT
IRADLEVAKL NFESAQKDLV SKGLQINELK QTVQDLEAII ENNKQKMLEH ETVRRKLHNT
ILELKGNIRV FCRVRPLLTD EINSGQGVIS HINFPDIDGR TVELESVCPN THNESLSTSV
AEKSRKKLNF TFDKVFQPET TQAEVFNEIS QLVQSALDGY NVCIFAYGQT GSGKTYTMEG
GNVEDEETMG MIPRATIQVF ETVELLVEKG WKVSCHLKT
//