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Database: UniProt
Entry: A0A482XR37_LAOST
LinkDB: A0A482XR37_LAOST
Original site: A0A482XR37_LAOST 
ID   A0A482XR37_LAOST        Unreviewed;       868 AA.
AC   A0A482XR37;
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-like protein {ECO:0000256|RuleBase:RU000394};
GN   ORFNames=LSTR_LSTR006233 {ECO:0000313|EMBL:RZF48266.1};
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:RZF48266.1, ECO:0000313|Proteomes:UP000291343};
RN   [1] {ECO:0000313|EMBL:RZF48266.1, ECO:0000313|Proteomes:UP000291343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lst14 {ECO:0000313|EMBL:RZF48266.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:RZF48266.1};
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       ECO:0000256|RuleBase:RU000394}.
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:RZF48266.1}.
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DR   EMBL; QKKF02002619; RZF48266.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A482XR37; -.
DR   STRING; 195883.A0A482XR37; -.
DR   InParanoid; A0A482XR37; -.
DR   Proteomes; UP000291343; Unassembled WGS sequence.
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   Gene3D; 2.60.40.4330; Kinesin-like protein Kif23, Arf6-interacting domain; 1.
DR   InterPro; IPR032384; Kif23_Arf-bd.
DR   InterPro; IPR038105; Kif23_Arf-bd_sf.
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:SF600; KINESIN-LIKE PROTEIN KIF23; 1.
DR   PANTHER; PTHR24115; KINESIN-RELATED; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF16540; MKLP1_Arf_bdg; 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}; Reference proteome {ECO:0000313|Proteomes:UP000291343}.
FT   DOMAIN          28..437
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          662..685
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          813..849
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          564..645
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        179..195
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        668..685
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        814..830
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         112..119
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   868 AA;  98571 MW;  3C92BF05F056D0F1 CRC64;
     MKRVKQQQTV KSTIKKARSN ESDKEKHPLQ VYCRVRPLQN ENESSCVNIE PPNSLLLTVT
     DANRAALQRQ TRFVFKHVFD ETTTQEQVFK ETSLPLVQNL ISGRNGLLFT YGVSNSGKSF
     TMDGTPENHG IMPRSISVLF NSIKPHQAPK YLFKPDRLIG FDVQSEPDAL LERQRELMSS
     MKNPKSAKKR DACGDMMRGG PASTEKLSVN EENVYSVFIT YIEIYNNCVY DLLEDCQSDD
     CTRVRALQPK IIREDGTKNM YVHGVDEVEV STPEEAVEIF YRGQKRRRLA HTALNTESSR
     SHSVFTIRLV QAPLDLAGGE MALNDKKLLS ISQLSLVDLA GSERTSRSKT AGVRLREAGN
     INNSLMTLRS CFELLRENQQ NGTSKMIPYR ESRLTHLFKN YFDGEGDVRM IICVNPRAED
     CDELNHVLKF AEMSQEVKVN RIRPAKEVQC PSTVKRKPPV NKPDELVPPA SSSSNLNASF
     LMSCRFQQPF PVPDFTNPAN NGFITETLQV LLARKEKAKE LQSHIKSYAS TFRAGLEGVF
     GELSSAQDES KRLAESNREK DQTIGELQRK IHQMDSEKLN LKMRCTSTEH YLRTRENELA
     DKEQQLSKEQ EAREREKMRL KDQISQKTEK LTKELQRQKS QMEMEMWQRD RRLRKVKKIL
     DNGPMSAPAS RFTPSTATGN SESDVEPLRL RNRVLASQFR TPSKYTESND DNVVSYSASK
     VGRGRENTAT IPRTYRRSRS AGPGDVWLDH RPPNVPPDTV FQPVMKKSHP VTKLTDIKRV
     NKSSKYCLTV LDKDSDGDIE TCLYKGDVLP TPSGGAQGTF NDVEILRQKS PTDSPQRKRS
     SARNATPFDD VENRCALSVE CHAKKSRR
//
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