ID   A0A1I7Y2D8_9BILA        Unreviewed;       964 AA.
AC   A0A1I7Y2D8;
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   Steinernema glaseri.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Steinernematidae;
OC   Steinernema.
OX   NCBI_TaxID=37863 {ECO:0000313|Proteomes:UP000095287, ECO:0000313|WBParaSite:L893_g1175.t1};
RN   [1] {ECO:0000313|WBParaSite:L893_g1175.t1}
RP   IDENTIFICATION.
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; A0A1I7Y2D8; -.
DR   WBParaSite; L893_g1175.t1; L893_g1175.t1; L893_g1175.
DR   Proteomes; UP000095287; Unplaced.
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:SF15; ZGC:66125; 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          5..326
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          360..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          728..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          913..964
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          487..682
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          816..850
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        913..931
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         82..89
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   964 AA;  110622 MW;  8DC2EA5C3A1FC0E0 CRC64;
     MASIPVKVCV RVRPLNGKEN REGSKECVEF YGENQVALSG RFFTFDRVFN PRSSQDDVYD
     SCASHLIDNL FKGFNCTILA YGQTGSGKTF TMGTEETTDS ISSTTRGIIP RMVESIFTRV
     AATEDPTLFT VSVSMLEIYD EKVYDLLGEQ RSDPLAIRES NKGVYVQDLS WNPVRSLTDT
     MAYLERGCGL RKKGGTAMNE QSSRSHAVFA VVVQRAEDEQ APSFEAKLHL VDLAGSERLK
     KTMAEGERKK EGIRINEGLL ALGNVISALS DGLKHIPYRN SCITRILQDS LGGNSYTVMI
     ACVSPAESNN EETLSTLRYA DRTKKIKNNP VVNTDPTSAA LKLLQEENRA LKREIARLKA
     SRAERSSDSD DEEMTEQGSN TDLEMEEKIL ELQEMCHRHL REKADLVSKH VHANDMLEKL
     HAKFEAARSL LETDEVNINE LRELLAVDIE EANESVHSIP PDNEDAEDQE HSIEAVAQTV
     HSINGDVERL KQMIDDRQKA VAEAAEKNEK YSHQYNESRE EIRKLNSEVT KLLEEKEMLN
     RKLKEITNHG KVSDEYRRRL KELEREQSAL KVKLKEYARY ESMKKESDKA LARARSELES
     AKKMRVEMMK KLRVESAKFM RMKTLLDRAN AQIQRAERKR EFEVAASKRT HEMQLNVMRR
     KLADSQAQAK RLQRQFARQT GKSRRNNKNI LDLPGYVKQE LDVAVNIWET QQLLKEYAEQ
     RKKLEAERKR LHQQRKGEPF TKRRRTEVSP PKEISADRFE EDLNALQHSI DVRQKEIAQL
     EERCAEMKPN SHEDRWAVCD TPELCSVALN NLFDLAQKAR VEVVQKSKKI TDLTRELKDA
     KEEAQELLRT GRTRRLSSDL NTTNIIDHKR PRVSRVLDHG FLDTLEVIPD VEGDDSFEDK
     NDERFPTPVE CRVRRRRDPD TSDKAPTKLN FDDDEEDEEV PIRPFGSNLH NTEGTRNRIK
     FPDV
//