GenomeNet

Database: UniProt
Entry: J3LJ82_ORYBR
LinkDB: J3LJ82_ORYBR
Original site: J3LJ82_ORYBR 
ID   J3LJ82_ORYBR            Unreviewed;      1016 AA.
AC   J3LJ82;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Kinesin motor domain-containing protein {ECO:0000259|PROSITE:PS50067};
OS   Oryza brachyantha (malo sina).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB03G11080.1};
RN   [1] {ECO:0000313|EnsemblPlants:OB03G11080.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB03G11080.1};
RX   PubMed=23481403;
RA   Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA   Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA   Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA   An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA   Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA   Chen M.;
RT   "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT   Oryza genome evolution.";
RL   Nat. Commun. 4:1595-1595(2013).
RN   [2] {ECO:0000313|EnsemblPlants:OB03G11080.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2013) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000256|PROSITE-ProRule:PRU00283}.
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DR   AlphaFoldDB; J3LJ82; -.
DR   STRING; 4533.J3LJ82; -.
DR   EnsemblPlants; OB03G11080.1; OB03G11080.1; OB03G11080.
DR   Gramene; OB03G11080.1; OB03G11080.1; OB03G11080.
DR   eggNOG; KOG0239; Eukaryota.
DR   HOGENOM; CLU_006519_1_0_1; -.
DR   OMA; CMLCILV; -.
DR   Proteomes; UP000006038; Chromosome 3.
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; 2.60.120.430; Galactose-binding lectin; 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; IPR021720; Malectin_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR47972:SF18; KINESIN-LIKE PROTEIN KIN-14R; 1.
DR   PANTHER; PTHR47972; KINESIN-LIKE PROTEIN KLP-3; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF11721; Malectin; 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|PROSITE-ProRule:PRU00283};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW   Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW   ProRule:PRU00283};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006038}.
FT   DOMAIN          409..687
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000259|PROSITE:PS50067"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          906..1016
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          249..357
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          690..860
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        913..927
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        961..975
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        976..1010
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         479..486
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ   SEQUENCE   1016 AA;  113477 MW;  5713FF09E8130AE7 CRC64;
     MEGEEERCPA DPTPMDFSWT NDWEKRACDG AGDGDEAESA PAPPAPTPQE VAESMVLVPG
     PRVVLSGLTR GDCRADDSVL VINAGGTAIE GCEPPSKFSG DSFFEGGDAI ETSENIVDGG
     DYPSLYHSAR YGNFSYKFDG LAPGDYFLDL HFAEIVNTYG PKGIRAFDVL VQEEKANILT
     CMTHDFVSQF IFRFCLNLMY MPWLGVTGPF RSCIQCDNLN HELVVANLVA EGNALCKRCS
     GHVGNSPIQT RTSKLISKYE KQIEELTNQC NMKSDECYMA WSSVESTNQE LERLKIELHQ
     KVVRSDNIEQ VLDSQADQLR NVSQKYENAK KLWAAAISNL ENKIKSMKKE QALLSLEAHD
     CANAVPDLSK MIGAVQALVA QCEDLKLKYY EEMTKRKKLH NIVQETKGNI RVFCRCRPLS
     KDETSSGYKC AVDFDGAKDG DIAVVTGGTA KKSFKFDRVY MPTDNQVLDG YNVCIFAYGQ
     TGTGKTFTME GTERNRGVNY RTLEELFKIA EERKETVTYN LSVSVLEVYN EQIRDLLASS
     PSSKKLEIKQ AGEGSHHVPG IVEAKVENIK EVWDVLQAGS NARAVGSNNV NEHSSRSHCM
     LCIMVRAKNL MNGECTRSKL WLVDLAGSER LAKTDVQGER LKEAQNINRS LSALGDVISA
     LATKNSHIPY RNSKLTHLLQ DSLELGPAKR QVDTAELQKV KQMLERARQE VRLKDDSLRK
     LEDNCQSLEN KAKGKEQLYK NLQEKVKELE NQLDSKMHSQ ITSEKQQNQL SGKLKETEEM
     CATLQQKIAE LERKLKLQQQ SESEVAVLKQ TIVELEIRLR EQEDQRSVAE SKAMEIGQEL
     LETQRTEAVL QIKLRELENA LQERTTILDT KMIHDSTNCM QVASTPGEAK AQLLTREEAM
     SEKEHHILRS SDSVNKRVTN NSSVVGAPEV VNEKKRKGDA RNPSIGGELE NQPVAARKRS
     LQGDTRLKRK STEPLAKNTG RTTATSKTAT ATHKMAPTTR ATTRQQPANK TRGWVR
//
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