ID A0A0D2AYJ2_9EURO Unreviewed; 251 AA.
AC A0A0D2AYJ2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=EB1 C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV06_03328 {ECO:0000313|EMBL:KIW44891.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW44891.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW44891.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW44891.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the MAPRE family.
CC {ECO:0000256|ARBA:ARBA00010729}.
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DR EMBL; KN847334; KIW44891.1; -; Genomic_DNA.
DR RefSeq; XP_016265107.1; XM_016404102.1.
DR AlphaFoldDB; A0A0D2AYJ2; -.
DR GeneID; 27355402; -.
DR VEuPathDB; FungiDB:PV06_03328; -.
DR HOGENOM; CLU_041744_2_1_1; -.
DR OrthoDB; 11676at2759; -.
DR Proteomes; UP000053342; Unassembled WGS sequence.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000053342}.
FT DOMAIN 2..103
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 160..237
FT /note="EB1 C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51230"
FT REGION 136..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 251 AA; 27736 MW; D1EB67FF2A4C28E9 CRC64;
MGESRQELLA WLNGLLQLNI TKVEQCGTGA AFCQLFDSIF MDLPMGRVKF NVNTEYAYIQ
NFKVLQNCFT RHGIDRTVPV EQLIKCKMQD NLEFLQWSKR FWDQYFPGHD YDAVARRKAS
GTAGAAPAAV APAASSRVST GASTTRKTGA TPINRAGPRA LSAAGGSSAA LKQENDQLKE
AIGGLEKERD FYFSKLRDIE LLLQTAVEQD PSLEADENGL IKQIQTILYS TEEGFEIPDL
EANGAEEPET F
//
