ID A0A1G4MF29_LACFM Unreviewed; 309 AA.
AC A0A1G4MF29;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=LAFE_0F05402g1_1 {ECO:0000313|EMBL:SCW02391.1};
GN ORFNames=LAFE_0F05402G {ECO:0000313|EMBL:SCW02391.1};
OS Lachancea fermentati (Zygosaccharomyces fermentati).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4955 {ECO:0000313|EMBL:SCW02391.1, ECO:0000313|Proteomes:UP000190831};
RN [1] {ECO:0000313|Proteomes:UP000190831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the MAPRE family.
CC {ECO:0000256|ARBA:ARBA00010729}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT598490; SCW02391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4MF29; -.
DR STRING; 4955.A0A1G4MF29; -.
DR OMA; WIKRFWD; -.
DR OrthoDB; 11676at2759; -.
DR Proteomes; UP000190831; Chromosome f.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000190831}.
FT DOMAIN 5..106
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 184..266
FT /note="EB1 C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51230"
FT REGION 116..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 178..212
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 124..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 309 AA; 35474 MW; CB5761C5BBAD6F9D CRC64;
MSGVGESRTE LLTWLNDLLK LNYTKIEQCG TGAAYCQIMD SIYGDVPMHR VKFNSTAEYE
FMTNFKILQS CFTKHKVEKI IYVEKLVRCR FQDNLEFLQW LKRYWTQHKD ESIYDPDSRR
KFRPTANSAP TSGSIINVAK RRTSSGPRSS LTGATRSGSL PSRNQGALGT RRVTTEQLLS
MQAELSQAQA NIQSLQKELT QYKEAMPIME RERDFYFGKL RDIEILSQST KDLCKEGVYE
NESEALVKFL NKVQQILYAT EEGFEVIEED SQPVSQSQDA LGYEKLPTEN LVDAKHQPPQ
NLITDEETF
//
