ID A0A0A8L2Q7_9SACH Unreviewed; 276 AA.
AC A0A0A8L2Q7;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=WGS project CCBQ000000000 data, contig 00012 {ECO:0000313|EMBL:CDO92537.1};
GN ORFNames=KLDO_g856 {ECO:0000313|EMBL:CDO92537.1};
OS Kluyveromyces dobzhanskii CBS 2104.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=1427455 {ECO:0000313|EMBL:CDO92537.1, ECO:0000313|Proteomes:UP000031516};
RN [1] {ECO:0000313|EMBL:CDO92537.1, ECO:0000313|Proteomes:UP000031516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS2104 {ECO:0000313|Proteomes:UP000031516};
RA Nystedt B., Astrom S.;
RT "The genome of Kluyveromyces dobzhanskii.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the MAPRE family.
CC {ECO:0000256|ARBA:ARBA00010729}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDO92537.1}.
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DR EMBL; CCBQ010000016; CDO92537.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A8L2Q7; -.
DR OrthoDB; 11676at2759; -.
DR Proteomes; UP000031516; 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:0007010; P:cytoskeleton 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Microtubule {ECO:0000256|PROSITE-ProRule:PRU00576};
KW Mitosis {ECO:0000256|ARBA:ARBA00022776}.
FT DOMAIN 5..106
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 175..256
FT /note="EB1 C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51230"
FT REGION 112..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 162..203
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 122..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 276 AA; 31969 MW; 127582BFAA48656C CRC64;
MAGIGESRSE LLLWLNDLLK LDYTKVEQCG TGAAYCQIMD SIYGDLPMNR VNFSAGSEYE
YFTNYKILQS CLTKHKIEKS VMVERLVKCR FQDNLEFLQW IKKYWTQNKD ESEYNAETRR
KGRAGPSTSS ALPVNKRPIS GSTASKPLLR NVRNTVIQNN IRKSSSEQLL TLQTELSETK
NQMSDLEKEC SQYKDLNTAY LKERDFYFGK LRDIEILAQS TQDLCDEGIY ENDKELRSFL
TRVQQILYAT EEQVELFGEE KVQQPSTNSI IDEETF
//
