ID W5MDV0_LEPOC Unreviewed; 834 AA.
AC W5MDV0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000006559.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000006559.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283,
CC ECO:0000256|RuleBase:RU000394}.
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DR EMBL; AHAT01004425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MDV0; -.
DR STRING; 7918.ENSLOCP00000006559; -.
DR Ensembl; ENSLOCT00000006567.1; ENSLOCP00000006559.1; ENSLOCG00000005434.1.
DR eggNOG; KOG0247; Eukaryota.
DR GeneTree; ENSGT00940000164689; -.
DR InParanoid; W5MDV0; -.
DR OMA; HAYQCAM; -.
DR Proteomes; UP000018468; Linkage group LG9.
DR Bgee; ENSLOCG00000005434; Expressed in ovary and 8 other cell types or tissues.
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:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd01368; KISc_KIF23_like; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
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 PANTHER; PTHR24115:SF408; KINESIN-LIKE PROTEIN; 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; 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 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:UP000018468}.
FT DOMAIN 64..489
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 160..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 834 AA; 94243 MW; 0008CE945CA75E54 CRC64;
MSAKIDFTDE SSVLAHPDRD AMESTPHDHH FDNLHRGVLS ELSTISATTV SAQVESGGNL
EEQQLKVYLR VRPFSKEELS NNEDQGCVVL ENSETAVLQA PKDSLSMKNS ERGIGQAAHK
FSFSQIFGPE TTQTRFFENT VRSLVYSYLE GQNSLVFSYG VTNAGKTHTI QGSSNDPGIL
PQALDVIFDH IKGRKYEHMD LKPYLSNDVQ YLDHDQVKQE KCTKAAVLAL LKEEGFPKTS
HSILKSQPEP SFSFSSVSYD QTAGPFDMTD SAAETDSSLF SVWVSFSEIY NESVYDLLEP
IPTSKNKKRI ALRVCEDSSG NSYVRGLKWI NVQSTEEACK ILRVGNKNRS AASTKMNHSS
SRSHSIFTIK LMKIHGTEVR RMSELSLCDL AGSERCNKTK TFGERLKEAG NINNSLLILG
KCIAALRQNQ NAKRRNGYVP FRESKLTRLF QSIFCGKGRA CMIVNINQCA STYDETLHVM
KFSAVAKQVV QIIPSKTLES IAPRLVGKDG KPLIRDGVID NEALEMYLSE EELLDDDDES
DMSVLPQEEL LNIIETLKEK LLAERRKNVV QEIEIRKEMG DAMLQQLLES EEIRNRQIEE
LKDSYEEKLE NTFEMYKDAI KEHAYQCALE RVEEEYVPVD EFLAEQERVQ DLTKKLAEME
QKLRSFQSNP SDPQTMTSSN QYSLEFESGS SESKRNDALP EANALSEKLQ EEKNKVIKSL
EKKVVELNKT LQEAAESFMK KQTEIKVLQQ KITDQDQEIE KLQNTTLELE TLVSRLREEL
EQLNRISKEA PEQPKPKKGL LANIKASVSS PVKLSRTLKK SAKSTQSSSR KRAL
//
