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Database: UniProt
Entry: C5WX96_SORBI
LinkDB: C5WX96_SORBI
Original site: C5WX96_SORBI 
ID   C5WX96_SORBI            Unreviewed;       317 AA.
AC   C5WX96;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=EB1 C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SORBI_3001G205000 {ECO:0000313|EMBL:EER91426.1};
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:EER91426.1, ECO:0000313|Proteomes:UP000000768};
RN   [1] {ECO:0000313|EMBL:EER91426.1, 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 MAPRE family.
CC       {ECO:0000256|ARBA:ARBA00010729}.
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DR   EMBL; CM000760; EER91426.1; -; Genomic_DNA.
DR   RefSeq; XP_002464428.1; XM_002464383.1.
DR   AlphaFoldDB; C5WX96; -.
DR   STRING; 4558.C5WX96; -.
DR   EnsemblPlants; EER91426; EER91426; SORBI_3001G205000.
DR   GeneID; 8065799; -.
DR   Gramene; EER91426; EER91426; SORBI_3001G205000.
DR   KEGG; sbi:8065799; -.
DR   eggNOG; KOG3000; Eukaryota.
DR   HOGENOM; CLU_041744_0_1_1; -.
DR   InParanoid; C5WX96; -.
DR   OMA; HAIQNIL; -.
DR   OrthoDB; 11676at2759; -.
DR   Proteomes; UP000000768; Chromosome 1.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR   GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR   GO; GO:0035371; C:microtubule plus-end; IBA:GO_Central.
DR   GO; GO:0051233; C:spindle midzone; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0035372; P:protein localization to microtubule; IBA:GO_Central.
DR   GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IBA:GO_Central.
DR   GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR   GO; GO:0009652; P:thigmotropism; IBA:GO_Central.
DR   Gene3D; 1.20.5.1430; -; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR004953; EB1_C.
DR   InterPro; IPR036133; EB1_C_sf.
DR   InterPro; IPR027328; MAPRE.
DR   PANTHER; PTHR10623:SF6; EB1, ISOFORM F-RELATED; 1.
DR   PANTHER; PTHR10623; MICROTUBULE-ASSOCIATED PROTEIN RP/EB FAMILY MEMBER; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF03271; EB1; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF140612; EB1 dimerisation domain-like; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS51230; EB1_C; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Microtubule {ECO:0000256|PROSITE-ProRule:PRU00576};
KW   Mitosis {ECO:0000256|ARBA:ARBA00022776};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000768}.
FT   DOMAIN          14..116
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          188..257
FT                   /note="EB1 C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51230"
FT   REGION          127..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..287
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   317 AA;  34883 MW;  21A50ED604DC09D2 CRC64;
     MAASNIGMMD GAYFVGRNEI LAWINTTLQL GLSKVEEAAS GAVACQLMDA AHPGAVPMHK
     VNFDAKTEYE MIQNYKVLQD VFNKLKITKH IEVNKLIKAR PLDNLEFMQW LKRYCDSVNG
     GFMTNYNASE RRESSKGGKD TNRRASVPSH TPAKSATTGH KAQTSHGAKR ASGQTASAPP
     PRSAKPSPAA NSGGPAPAYD EQITELKLLV DSLEKERDFY FTKLRDIEML SQNPEVEHVS
     VQTIQNILYA SEEDAQQLPP ALSPIMEASE ERPKQEMANK RKSISDLDEF GMSSSSRQRL
     SDISDVQLCG SPLTSFS
//
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