KN7D_ORYSJ
ID KN7D_ORYSJ Reviewed; 1007 AA.
AC Q6YZ52; B9F3I3;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 06-JUL-2016, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Kinesin-like protein KIN-7D, chloroplastic {ECO:0000305};
DE Flags: Precursor;
GN Name=KIN7D {ECO:0000305}; Synonyms=K16 {ECO:0000303|PubMed:16672264};
GN OrderedLocusNames=Os02g0775400 {ECO:0000312|EMBL:BAS81163.1},
GN LOC_Os02g53520 {ECO:0000305};
GN ORFNames=OJ1448_G06.23 {ECO:0000312|EMBL:BAD17149.1},
GN OsJ_08573 {ECO:0000312|EMBL:EEE57896.1},
GN OSJNBb0013K01.4 {ECO:0000312|EMBL:BAD17367.1},
GN OSNPB_020775400 {ECO:0000312|EMBL:BAS81163.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [5]
RP FUNCTION, ATP-BINDING, AND SUBUNIT.
RX PubMed=16672264; DOI=10.1093/jb/mvj074;
RA Umeki N., Mitsui T., Umezu N., Kondo K., Maruta S.;
RT "Preparation and characterization of a novel rice plant-specific kinesin.";
RL J. Biochem. 139:645-654(2006).
RN [6]
RP FUNCTION, ATP-BINDING, AND SUBUNIT.
RX PubMed=16751590; DOI=10.1093/jb/mvj098;
RA Umeki N., Mitsui T., Koike Y., Maruta S.;
RT "Intermolecular cross-linking of a novel rice Kinesin k16 motor domain with
RT a photoreactive ATP derivative.";
RL J. Biochem. 139:831-836(2006).
RN [7]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19106179; DOI=10.1093/aob/mcn248;
RA Guo L., Ho C.M., Kong Z., Lee Y.R., Qian Q., Liu B.;
RT "Evaluating the microtubule cytoskeleton and its interacting proteins in
RT monocots by mining the rice genome.";
RL Ann. Bot. 103:387-402(2009).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 77-419 IN COMPLEX WITH ADP, AND
RP COFACTOR.
RX PubMed=20849820; DOI=10.1016/j.bbrc.2010.09.043;
RA Tanaka K., Umeki N., Mitsui T., Fujimoto Z., Maruta S.;
RT "Crystallographic analysis reveals a unique conformation of the ADP-bound
RT novel rice kinesin K16.";
RL Biochem. Biophys. Res. Commun. 401:251-256(2010).
CC -!- FUNCTION: Probable minus end-directed motor protein with a microtubule-
CC enhanced ATPase activity. Binds ATP/ADP in vitro. Retains total
CC enzymatic activity even after the removal of the ADP bound in the
CC active site. {ECO:0000269|PubMed:16672264,
CC ECO:0000269|PubMed:16751590}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20849820};
CC -!- SUBUNIT: Binds microtubules (PubMed:16672264). Homodimer
CC (PubMed:16751590). {ECO:0000269|PubMed:16672264,
CC ECO:0000269|PubMed:16751590}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. KIN-7 subfamily.
CC {ECO:0000303|PubMed:19106179}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK068672; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAD17149.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAD17367.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAS81163.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EEE57896.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP004853; BAD17149.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP005538; BAD17367.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014958; BAS81163.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM000139; EEE57896.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK068672; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015627269.1; XM_015771783.1.
DR AlphaFoldDB; Q6YZ52; -.
DR SMR; Q6YZ52; -.
DR STRING; 4530.OS02T0775400-01; -.
DR PaxDb; Q6YZ52; -.
DR PRIDE; Q6YZ52; -.
DR GeneID; 4330897; -.
DR KEGG; osa:4330897; -.
DR eggNOG; KOG0242; Eukaryota.
DR HOGENOM; CLU_498199_0_0_1; -.
DR InParanoid; Q6YZ52; -.
DR OrthoDB; 101117at2759; -.
DR Proteomes; UP000000763; Chromosome 2.
DR Proteomes; UP000007752; Chromosome 2.
DR Proteomes; UP000059680; Chromosome 2.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IDA:UniProtKB.
DR Gene3D; 3.40.850.10; -; 1.
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 Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chloroplast; Coiled coil; Microtubule; Motor protein;
KW Nucleotide-binding; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..53
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 54..1007
FT /note="Kinesin-like protein KIN-7D, chloroplastic"
FT /id="PRO_0000436625"
FT DOMAIN 83..402
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 403..495
FT /evidence="ECO:0000255"
FT COILED 687..716
FT /evidence="ECO:0000255"
FT COILED 754..791
FT /evidence="ECO:0000255"
FT COILED 836..907
FT /evidence="ECO:0000255"
FT COILED 942..982
FT /evidence="ECO:0000255"
FT COMPBIAS 23..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT CONFLICT 189
FT /note="D -> G (in Ref. 4; AK068672)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1007 AA; 111676 MW; E740C4FBB01638C1 CRC64;
MATRPASRQR RASSAAAAVA VVRSSPQPQQ QQQQQLPIPQ SGSPTSTTTT TTSSSRLTPE
LSLDGPASPL FAGLDEDPAP KENVTVTVRF RPLSPREIRQ GEEVAWYADG DTVVRSEQNP
SVAYAYDRVF APTTTTRQVY DVAAQHVVSG AMEGVNGTIF AYGVTSSGKT HTMHGDQRSP
GIIPLAVKDA FSIIQETPNR EFLLRVSYLE IYNEVVNDLL NPAGQNLRIR EDPQGTFVEG
IKEEVVLSPA HALSLIAAGE EHRHVGSTNF NLLSSRSHTI FTLTVESSPC GESNEGEAVT
FSQLNLIDLA GSESSRAETT GVRRKEGSYI NKSLLTLGTV ISKLTDGKAT HIPFRDSKLT
RLLQSSLSGQ GRVSLICTVT PASSNSEETH NTLKFAHRAK RIEVQASQNK IIDEKSLIKK
YQNEIRRLKE ELEQLKMGII TGTPVKDAGE DNIILWKQKL EDGNVKLQSR LEQEEEAKAA
LLARIQRLTK LILVSTKATQ TSRFSPHPGP RRRHSFGEEE LAYLPYKRRD IVLDNESNEL
LSPVEGLGMT LEDSKEEKKN RKGILNWFKL RKREGGASIL TSSEGDKSSL TKSTAPSTPI
GESVNFPSEP RISNSLVGES ASVDLFSIGH GEFATDSLHG EETPLASRKT IDHVDLLREQ
LKILSGEVAL HTSVLKRLTE EAGRSPNNEK IQMEMKKVND EIKGKKHQIA SLERQIPHSI
SNNQGMADKL ELTPSYAELL EQLNEKSFDL EVKAADNRVI QDQLNEKTTE CMELQEEVAH
LKEQLYQTLQ AKDSLSNSIM MQKNAGINHE TDNHADQELS VPREVPGETS PKEPQSVEID
ELKQKVCELI EVKAQLETRN QKLLEESTYA KGLASAAGVE LKALSEEVTK LMNQNEKLAS
ELASVRSPTP RRANSGLRGT RRDSISRRHE PAPRRDNNAG YEREKALEAV LMEKEQKEAE
LQRRIEESKQ KEAFLESELA NMWVLVAKLK KSQGHDLEDF DTKYIGS
