ID C5Z3G2_SORBI Unreviewed; 903 AA.
AC C5Z3G2;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Kinesin-like protein {ECO:0000256|RuleBase:RU000394};
GN ORFNames=SORBI_3010G027500 {ECO:0000313|EMBL:EER89151.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EER89151.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:EER89151.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. Ungrouped subfamily.
CC {ECO:0000256|ARBA:ARBA00010103}.
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DR EMBL; CM000769; EER89151.1; -; Genomic_DNA.
DR RefSeq; XP_002437784.1; XM_002437739.1.
DR AlphaFoldDB; C5Z3G2; -.
DR STRING; 4558.C5Z3G2; -.
DR EnsemblPlants; EER89151; EER89151; SORBI_3010G027500.
DR GeneID; 8068414; -.
DR Gramene; EER89151; EER89151; SORBI_3010G027500.
DR KEGG; sbi:8068414; -.
DR eggNOG; KOG0240; Eukaryota.
DR HOGENOM; CLU_014436_0_0_1; -.
DR InParanoid; C5Z3G2; -.
DR OMA; HRFATNT; -.
DR OrthoDB; 463662at2759; -.
DR Proteomes; UP000000768; Chromosome 10.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IBA:GO_Central.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR CDD; cd00106; KISc; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR047149; KIF11-like.
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; PTHR47970:SF31; ARMADILLO REPEAT-CONTAINING KINESIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR47970; KINESIN-LIKE PROTEIN KIF11; 1.
DR Pfam; PF00514; Arm; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00185; ARM; 4.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50176; ARM_REPEAT; 2.
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 ECO:0000256|RuleBase:RU000394}; Coiled coil {ECO:0000256|SAM:Coils};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701, ECO:0000256|RuleBase:RU000394};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00283};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00283,
KW ECO:0000256|RuleBase:RU000394};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768}.
FT DOMAIN 66..412
FT /note="Kinesin motor"
FT /evidence="ECO:0000259|PROSITE:PS50067"
FT REPEAT 645..687
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REPEAT 686..729
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 439..477
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 525..594
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 499..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 151..158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00283"
SQ SEQUENCE 903 AA; 99338 MW; 46B6DB88CE96530F CRC64;
MASSGVRNGV GPRMSAKPDR GQGFSATPKT AAGKQRLSSA AAGGAYRRTS SGPLPSRAAS
DGVSSRVRVA VRLRPRNAEE LAADADFGDC VELQPELKRL KLRKNNWESE TYEFDEVLTE
FSSQKRVYEV VAKPVVESVM EGYNGTVMAY GQTGTGKTFT LGRLGEEDTA ARGIMVRAME
DILADITPGT DSVSVSYLQL YMEMIQDLLD PVNDNIAIVE DPRTGDVSLP GATVVEVRDQ
KSFVDLLRVG EAHRVAANTK LNTESSRSHA ILMVNVRRSV KGRTEMDVSI SGENGHSSSM
MGSLRPPIVR KSKLVVVDLA GSERIDKSGS EGHTLEEAKS INLSLSALGK CINALAESSP
HVPVRDSKLT RLLKDSFGGT ARTSLVVTIG PSPRHRGETT STIMFGQRAM KVENMVKLKE
EFDYKSLCRR LDIELDKLVA ENERQRKFFD DEVERIRAEA QCRIAESERE CKITLENEKM
KYHQEYLDSI RIMEEKWKVH QQSPKKQNKE AESTSNDTGE VHNLLQNEKM LRQSAEDEAS
DLKNQVSHWK KLEATATAEV VKLRKMLDAE ASQKEKLEEE IDVLRSQLLQ MSMEADETRR
SLDKGDGPGK IFPGLDSLVS QTRGSQPREQ SNGPKQPIAK LFEQVGLKKI LSLLESEEPD
VRVHAVKVVA NLAAEEANQE KIVEAGGLTS LLTLLRSSED ETIRRVAAGA IANLAMNETN
QDLIMDQGGV TLLSMTASDA EDPQTLRMVA GAIANLCGND KLQTRLRGEG GIKALLGMVR
CGHPDVLAQV ARGIANFAKC ESRAATQGNK VGKSLLIDDG SLPWIVKNAN NEAAPIRRHI
ELALCHLAQH EVNAKDIINE GALWELVRIS RDCSREDIRK LAYRTVTSSP TLQAEIRRLG
IKM
//
