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Database: UniProt
Entry: A0A1X2I0Q0_9FUNG
LinkDB: A0A1X2I0Q0_9FUNG
Original site: A0A1X2I0Q0_9FUNG 
ID   A0A1X2I0Q0_9FUNG        Unreviewed;       297 AA.
AC   A0A1X2I0Q0;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Calponin homology domain-containing protein {ECO:0000313|EMBL:ORZ06857.1};
GN   ORFNames=BCR42DRAFT_383557 {ECO:0000313|EMBL:ORZ06857.1};
OS   Absidia repens.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=90262 {ECO:0000313|EMBL:ORZ06857.1, ECO:0000313|Proteomes:UP000193560};
RN   [1] {ECO:0000313|EMBL:ORZ06857.1, ECO:0000313|Proteomes:UP000193560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 1336 {ECO:0000313|EMBL:ORZ06857.1,
RC   ECO:0000313|Proteomes:UP000193560};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) 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:ORZ06857.1}.
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DR   EMBL; MCGE01000037; ORZ06857.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2I0Q0; -.
DR   STRING; 90262.A0A1X2I0Q0; -.
DR   OrthoDB; 11676at2759; -.
DR   Proteomes; UP000193560; 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   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:UP000193560}.
FT   DOMAIN          2..103
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   DOMAIN          220..297
FT                   /note="EB1 C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51230"
FT   COILED          228..255
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   297 AA;  33522 MW;  213A5011EDE4EE11 CRC64;
     MTESRTELVI WVNNLLQLQY TKVEQLGTGI AYSQIIDSIY GDVHLAKIKF FAKHEYEYIE
     NYKVLQRAFE KHKINKIIPV ERLVKCRFQD NLEFLQWIKM FWDSNYQGQA YDALGRRQRG
     INKAATILSS ASAPSRQMIH GRLSNRGNFS DMASYASSST ASSSTAATPI DTIGGNVYSG
     YGRNCQSPSS ASTLSVDSNS IKAKRSRIYA LGSPQSSPLP KPSQSRILVD LNQQLAELEV
     AAKQLNSEKE FYFTKLLNIE NVLDQHGMYD AERTTEPLVK SPVLKKIQTI LFDEETI
//
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