ID A0A1J9RDG5_9PEZI Unreviewed; 600 AA.
AC A0A1J9RDG5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Tubulin-specific chaperone e {ECO:0000313|EMBL:OJD38576.1};
GN ORFNames=BKCO1_400082 {ECO:0000313|EMBL:OJD38576.1};
OS Diplodia corticola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Diplodia.
OX NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD38576.1, ECO:0000313|Proteomes:UP000183809};
RN [1] {ECO:0000313|EMBL:OJD38576.1, ECO:0000313|Proteomes:UP000183809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD38576.1,
RC ECO:0000313|Proteomes:UP000183809};
RA Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA Esteves A.C.;
RT "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT hemibiotrophic lifestyle of Diplodia corticola.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OJD38576.1}.
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DR EMBL; MNUE01000004; OJD38576.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J9RDG5; -.
DR STRING; 236234.A0A1J9RDG5; -.
DR OrthoDB; 11880at2759; -.
DR Proteomes; UP000183809; Unassembled WGS sequence.
DR GO; GO:0043014; F:alpha-tubulin binding; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR044994; TBCE.
DR PANTHER; PTHR15140:SF6; TUBULIN-SPECIFIC CHAPERONE COFACTOR E-LIKE PROTEIN; 1.
DR PANTHER; PTHR15140; TUBULIN-SPECIFIC CHAPERONE E; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
PE 4: Predicted;
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Reference proteome {ECO:0000313|Proteomes:UP000183809};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 24..70
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
SQ SEQUENCE 600 AA; 66014 MW; 6CD690AC6CFB7875 CRC64;
MASAFHPGKR LSFNRDLCTV RYVGQVQGTK GEWLGVEWDD PTRGKHDGSH AGVRYFECRR
KHPTAGSFVR PNRPSDPPVS YVEALKQKYA SEPVEDPSVS NIDIVVFGKA PENVPVNSAG
KVIMISGKEA EEVGFDKIRK KLANLKELRI VLLDGMCMER PFSKLFEQAG EMAVDQLTDV
KDASPSIQEL DLSRNLFEEW REVASICVQL ESLRRLKVDG NRLRDLELDG CLSSAFTHVS
TLSLEDTLLS WEDVTNMCSA LPSLATLSLT SNAFDKLGQT SLPSTITELI LEKNYFRSLD
DLRCLTKLPN LRSLKLKNNL ISGILGPHSA GGEPLVFSDS VSEVDLVHNS IEDWAFIDNL
PSVFPGLTSL RISSNPLYHG LQAVDGKPLT ADDGYMLTIA RLGKLKIMNF STISAKERLN
AETYYLSQIG AELSSAPEGQ ESKVIATHGR YSELCAEYGE PTIVRLDASA VKPNSLAARL
IKFTFYPGNS VKAKLGASRG AAEEFSAELP RSFTVYSMLG VVGKRLAMAP LELRLFWETG
DWVPVGEEVA AGGEEWDSSD DEDGKAGEGK VVREVEWVAG TKMVGTWVEG MEARVRIEVQ
//