ID A0A1I8ES47_WUCBA Unreviewed; 475 AA.
AC A0A1I8ES47;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
OS Wuchereria bancrofti.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Wuchereria.
OX NCBI_TaxID=6293 {ECO:0000313|WBParaSite:maker-PairedContig_4218-snap-gene-0.5-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-PairedContig_4218-snap-gene-0.5-mRNA-1}
RP IDENTIFICATION.
RC STRAIN=pt0022
RC {ECO:0000313|WBParaSite:maker-PairedContig_4218-snap-gene-0.5-mRNA-1};
RG WormBaseParasite;
RL Submitted (NOV-2016) 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 AlphaFoldDB; A0A1I8ES47; -.
DR STRING; 6293.A0A1I8ES47; -.
DR WBParaSite; maker-PairedContig_4218-snap-gene-0.5-mRNA-1; maker-PairedContig_4218-snap-gene-0.5-mRNA-1; maker-PairedContig_4218-snap-gene-0.5.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
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; 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; PTHR47969; CHROMOSOME-ASSOCIATED KINESIN KIF4A-RELATED; 1.
DR PANTHER; PTHR47969:SF32; KINESIN-LIKE PROTEIN; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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}.
FT DOMAIN 4..327
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT COILED 342..473
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 87..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 475 AA; 53762 MW; 16F20901FD51EF0A CRC64;
MAESVRVICR CRPLNNREIN LNSQICVQMD QSCGQVILQG ETGCPKQFTF DSVYYMDATS
EQIYNEIVYP LVESVIQGYN GTIFAYGQTG SGKTYSMQGD DNISSQKGII SRAFEHIFEA
TATTDDAKFL VHASYLEIYN EEVHDLLSTN HTKKLEIKEH SERGIYVAGL SMHVCNDYKT
CQRLMKEGSE NRHVGATLMN KDSSRSHSIF TVYVEVALNN GSIRIGKLNL VDLAGSERQT
KTGTVGDRFK EATKINLSLS ALGNVISAFV DGKSKHIPYR DSKLTRLLKD SLGGNMKTIM
LACISPSSDN YDETLSTLRY ANRAKNIKNK PKINEDPKDA LLREYQEEIQ RLKAMIQGDS
NTNSNLNQLD EEREQLKAEF NAAINELRLQ YQNEQKSKAK LQEEYATLKE QYEKAAEALE
NDRNLDVGEA KKRLQILEKQ FVGGEQANNE ALKEQRQIKM KEAEKKMERL AGKFF
//
