ID A0A482WL66_LAOST Unreviewed; 1127 AA.
AC A0A482WL66;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Kinesin motor domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=LSTR_LSTR003608 {ECO:0000313|EMBL:RZF34198.1};
OS Laodelphax striatellus (Small brown planthopper) (Delphax striatella).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Auchenorrhyncha; Fulgoroidea;
OC Delphacidae; Criomorphinae; Laodelphax.
OX NCBI_TaxID=195883 {ECO:0000313|EMBL:RZF34198.1, ECO:0000313|Proteomes:UP000291343};
RN [1] {ECO:0000313|EMBL:RZF34198.1, ECO:0000313|Proteomes:UP000291343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lst14 {ECO:0000313|EMBL:RZF34198.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:RZF34198.1};
RX PubMed=29136191; DOI=.1093/gigascience/gix109;
RA Zhu J., Jiang F., Wang X., Yang P., Bao Y., Zhao W., Wang W., Lu H.,
RA Wang Q., Cui N., Li J., Chen X., Luo L., Yu J., Kang L., Cui F.;
RT "Genome sequence of the small brown planthopper, Laodelphax striatellus.";
RL Gigascience 6:1-12(2017).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RZF34198.1}.
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DR EMBL; QKKF02032524; RZF34198.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A482WL66; -.
DR STRING; 195883.A0A482WL66; -.
DR InParanoid; A0A482WL66; -.
DR Proteomes; UP000291343; Unassembled WGS sequence.
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:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR CDD; cd22708; FHA_KIF16; 1.
DR CDD; cd01365; KISc_KIF1A_KIF1B; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR InterPro; IPR000253; FHA_dom.
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 InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR47117:SF6; KINESIN-LIKE PROTEIN KIF1C ISOFORM X1; 1.
DR PANTHER; PTHR47117; STAR-RELATED LIPID TRANSFER PROTEIN 9; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF00787; PX; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|PROSITE-ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00283}; Reference proteome {ECO:0000313|Proteomes:UP000291343}.
FT DOMAIN 3..346
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT DOMAIN 994..1121
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT REGION 579..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 632..734
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 842..869
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 99..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 1127 AA; 127619 MW; 40864A886084BB3C CRC64;
MASVKVAVRV RPFNQREIDM DAKCILRMEG KKTRITNTSQ KGTERQGDQH KFFTFDHSYW
SFDHNDPHYI SQEQVFNDLG TDVVDAAFEG YNACVFAYGQ TGSGKTYTMM GSKNNQGLIP
RICEALFKRM ALGANYRIEV SYLEIYNEKV KDLLRKDSGH NLKVRQHPTK GPCVMDLSRH
LVSEYCHIQD LMEQGNNQRT TASTNMNDVS SRSHAIFTLM FVQAQGGLYN DVPTETVSKV
HLVDLAGSER ADASGATGQR LKEGAHINKS LVTLGSVISA LAELSAGGSR KAGGFIPYRD
SVLTWLLKDS LGGNSKTIMI AAVSPADCNY SETLSTLRYA NRAKNIINKP TINEDENVKL
IRELREEITK LKSMMTENEC TTEVQPKVLA VLQEKEAQEK VLREEWNEKW RETQKILQEQ
KALGLRKAGA GAGIVLDSDM PHLIGIDDDL LSTGVTLYHL NDGETLVGSS DADGDRQDII
LNGIDVEKHH CSITLKNGVA TLVPHHDALC WVNGLQVNKP TRLSQGCNIL LGRTNLFRYN
DPVEVEKLKK EGNSHSSLNL SRLSLMSCST PDLCRDVDNN NTSSFRNDSR SDRKRPGSVI
SEFGSSTLEC RRSREDILDE NSIIREDELN QSKNLHEREE ELKKSIEQFT ADQESKMQFL
ASEHKRIVEL QANLERKKEE LTLLEVKQTQ FRRDSLNGTS EIDVNVLNSF KDSISNMEQE
LKQQNEALGV IVRNADENEK NFKRQNLNLS ILPGGLASQP LATSSPNITL NSNRIAEDLE
SPLSDSPRNL NLQTRSMLRK MSVDVDLETD SLYQMKYLTQ QISNQRRLIM KCLESEINSD
ELNKHISVLQ ELKREYVRLE QRMQQETDDN SSKENFKMDA SGAQSSTMSH DMCDSDDLST
SADDTISESL MGSRIFKSRD CLNCAVLSRS SRDIRYRILQ DRLQMSLAPP SFSASNQDVN
QLTSSNNYSL TRSMPSLNRI SVWERRLNDS DWDQRLIVSV PNFLIRGAGR NTHYVYEVVV
CVEGETYSIL RRYRRFRELH LTMKHKYGDQ VAKLSFPPRK LFLWQMDGEL LAKERRPLLE
IYLKRLLAIC SSISTCPLHN SCSKTALHQF STFFKKGVFE TGKYGTS
//
