ID   KN7J_ARATH              Reviewed;         930 AA.
AC   Q9FIG8;
DT   08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT   08-JUN-2016, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Kinesin-like protein KIN-7J {ECO:0000305};
GN   Name=KIN7J {ECO:0000305};
GN   OrderedLocusNames=At5g42490 {ECO:0000312|Araport:AT5G42490};
GN   ORFNames=MDH9.19 {ECO:0000312|EMBL:BAB10490.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA   Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT   features of the regions of 1,081,958 bp covered by seventeen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:379-391(1998).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   GENE FAMILY.
RX   PubMed=11472632; DOI=10.1186/1471-2164-2-2;
RA   Reddy A.S., Day I.S.;
RT   "Kinesins in the Arabidopsis genome: a comparative analysis among
RT   eukaryotes.";
RL   BMC Genomics 2:2-2(2001).
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=16448571; DOI=10.1186/1471-2164-7-18;
RA   Richardson D.N., Simmons M.P., Reddy A.S.;
RT   "Comprehensive comparative analysis of kinesins in photosynthetic
RT   eukaryotes.";
RL   BMC Genomics 7:18-18(2006).
RN   [5]
RP   REVIEW.
RX   PubMed=22038119; DOI=10.1007/s00709-011-0343-9;
RA   Zhu C., Dixit R.;
RT   "Functions of the Arabidopsis kinesin superfamily of microtubule-based
RT   motor proteins.";
RL   Protoplasma 249:887-899(2012).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. KIN-7 subfamily.
CC       {ECO:0000303|PubMed:16448571}.
CC   -!- CAUTION: The kinesin motor domain is truncated at the C-terminus in
CC       comparison with other members of the gene family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AED94816.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAB10490.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB016888; BAB10490.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED94816.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; NP_199064.1; NM_123614.2.
DR   AlphaFoldDB; Q9FIG8; -.
DR   SMR; Q9FIG8; -.
DR   iPTMnet; Q9FIG8; -.
DR   PaxDb; Q9FIG8; -.
DR   PeptideAtlas; Q9FIG8; -.
DR   PRIDE; Q9FIG8; -.
DR   GeneID; 834256; -.
DR   KEGG; ath:AT5G42490; -.
DR   Araport; AT5G42490; -.
DR   TAIR; locus:2162351; AT5G42490.
DR   HOGENOM; CLU_013407_0_0_1; -.
DR   InParanoid; Q9FIG8; -.
DR   OrthoDB; 224479at2759; -.
DR   PRO; PR:Q9FIG8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FIG8; baseline and differential.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; -; 1.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR021881; NACK_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF11995; DUF3490; 1.
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   3: Inferred from homology;
KW   ATP-binding; Isopeptide bond; Microtubule; Motor protein;
KW   Nucleotide-binding; Reference proteome; Ubl conjugation.
FT   CHAIN           1..930
FT                   /note="Kinesin-like protein KIN-7J"
FT                   /id="PRO_0000436468"
FT   DOMAIN          9..273
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          449..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          655..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..485
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..526
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..559
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        655..682
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         95..102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   CROSSLNK        805
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:F4JQ51"
SQ   SEQUENCE   930 AA;  106099 MW;  1FCD466DF7F34DF4 CRC64;
     MASGGKGEKI LVSVRVRPQN EKEKARNDIC DWECVNNTTI VCNNNLPERS LFPSTYTFDK
     VFGFDSPTKQ VYEDGAKEVA LCVLGGINSS IFAYGQTSSG KTYTMCGITK FAMDDIFCYI
     QKHTDRKFTL KFSAIEIYNE AVRDLLSGDN NQRRLLDDPE RGTVVEKLIE ETIQDRTHLE
     ELLTVCETQR KIGETSLNEV SSRSHQILRL TIESTGREYS PDSSSTLAAS VCFIDLAGSE
     RASQTLSAGT RLKEGCHINR SLLTLGTVIR KLRFDPCDIA QSQVENLLKS TAEERSSRMD
     EQSMFSSMDF DADFRRRSYD STDLGEPSII NNLTERNFEF LENSEEDDFL LDDKTPQFSR
     HNLYDDWEEL VQITDERLED ACKEVRCIEP EAEQSSGQPA ACESHDSLDD IKAENEDMEI
     STPAEKENVD LSLKTIDVNA KPETYELTLK NSDLEIGPSV EAQESQESVN EEEQMKNEER
     KMSPSTKQAE QCLNKEENAQ SEQQSTEDCE LNSLPINNQS EATVEVELTP NDAKLDEDAT
     SRDKWESKQQ QEADKDCNES SVCKNIGTDD NDNDTYMALK EKVKEMQKKI EYLMSMHTAE
     QQQSPSFRRD FKSPPEYFTA KRSRSCRENL LSVRSPHWFE SLEVSNNTSP TWRVMQTKAS
     PGRPNTSSIS FDSGSSTSID TRSLKDYDPE MGNSFREFVA GLEEMAKKHH SIDSTPELDY
     GIPYAPTKTE RMEIRPESPA DSVAANGQYS ISSSDFERQQ RKIIELWAAC NVPLVHRTYF
     FLLFKGDPSD YVYMEVELRR LSFLKQTISN DMETSRMQTV KALTREKEWI SKQLPKKFPW
     NQRIGLYQKW GVEVNSKQRS LQVAHKLWTN TQDMDHIKES ASLVAKLLGF VEPSRMPKEM
     FGLSLLPRTE NVKSSGWRFT KSFSAIRLTR