ID A0A3B0J1N7_DROGU Unreviewed; 616 AA.
AC A0A3B0J1N7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Blast:Kinesin-like protein subito {ECO:0000313|EMBL:SPP74887.1};
GN ORFNames=DGUA_6G002592 {ECO:0000313|EMBL:SPP74887.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP74887.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) 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; OUUW01000001; SPP74887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0J1N7; -.
DR STRING; 7266.A0A3B0J1N7; -.
DR OMA; IDGDHTF; -.
DR OrthoDB; 3109027at2759; -.
DR Proteomes; UP000268350; Unassembled WGS sequence.
DR GO; GO:0015630; C:microtubule cytoskeleton; IEA:UniProt.
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 CDD; cd00106; KISc; 1.
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 PANTHER; PTHR24115:SF1014; KINESIN-LIKE PROTEIN SUBITO; 1.
DR PANTHER; PTHR24115; KINESIN-RELATED; 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; 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 Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}.
FT DOMAIN 77..469
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 REGION 592..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..616
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 159..166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 616 AA; 70252 MW; 4E9B93ACE3E1EC7B CRC64;
MSDLNEGPMR EKRSFIMARD PSVDRRFRPR PHKQLRLFDD IHESTESTDG SDTESEYASN
AGDDATSVDD SSEVDTGPQV FLRLRPVSVA STGYSLSEDG KCLITSAKSE NSSNNVNRME
KHFGFTSIFD GSVGQRDIYD MCVGPRILEE ECVTIMTYGT SGSGKTYTLL GDQLRAGVIP
RGLEHIFTIY LGNLYSTPKL KLINGCIVFL QDDATLREMQ ISMKLLNLCP DINAQHERLR
QEIRSDHTFE TKTEPDLSVM IWVSFVEIYN ELVYDLLSIP PRQDNLGAVQ RKPLKIACNK
GQVFIKGLTT VFVKSSEEAL RLLRLGQQRS TYASTSVNSN SSRSHCVFTV DVLKYSRSGM
TTQCSYKFCD LAGSERVNNT GTIGLRLKEA KNINTSLMTL GRCLDAASTS RKKSSTDVIP
FRDSKLTMLL QAALLGKERL AMIVTVTPLE KYYEENLNVL NFASIAKNIV FKEPMIKQHS
TRYSGFFDNP KADGQYDYIK ALEEDNISLR EEIDRLKFDH VLKMQLLEER LRKELTDTFQ
EMIRVNKKQW EEQSEKQKLM AEREFEFKLD SQKRIYEEQI EDLKDEIDYL KNPASETSIE
SMDEIEDDPI EIHDDE
//
