ID A0A319CWZ3_9EURO Unreviewed; 411 AA.
AC A0A319CWZ3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Tubulin-specific chaperone c {ECO:0000313|EMBL:PYH89179.1};
GN ORFNames=BO71DRAFT_423187 {ECO:0000313|EMBL:PYH89179.1};
OS Aspergillus ellipticus CBS 707.79.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448320 {ECO:0000313|EMBL:PYH89179.1, ECO:0000313|Proteomes:UP000247810};
RN [1] {ECO:0000313|EMBL:PYH89179.1, ECO:0000313|Proteomes:UP000247810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 707.79 {ECO:0000313|EMBL:PYH89179.1,
RC ECO:0000313|Proteomes:UP000247810};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TBCC family.
CC {ECO:0000256|ARBA:ARBA00008848}.
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; KZ826044; PYH89179.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A319CWZ3; -.
DR STRING; 1448320.A0A319CWZ3; -.
DR Proteomes; UP000247810; Unassembled WGS sequence.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:InterPro.
DR Gene3D; 2.160.20.70; -; 1.
DR Gene3D; 1.20.58.1250; Tubulin Binding Cofactor C, N-terminal domain; 1.
DR InterPro; IPR017901; C-CAP_CF_C-like.
DR InterPro; IPR016098; CAP/MinC_C.
DR InterPro; IPR006599; CARP_motif.
DR InterPro; IPR027684; TBCC.
DR InterPro; IPR038397; TBCC_N_sf.
DR InterPro; IPR012945; Tubulin-bd_cofactor_C_dom.
DR PANTHER; PTHR15139; TUBULIN FOLDING COFACTOR C; 1.
DR PANTHER; PTHR15139:SF0; TUBULIN-SPECIFIC CHAPERONE C; 1.
DR Pfam; PF07986; TBCC; 1.
DR SMART; SM00673; CARP; 1.
DR PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Reference proteome {ECO:0000313|Proteomes:UP000247810}.
FT DOMAIN 211..365
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 147..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 411 AA; 45160 MW; 944ABFEA68262909 CRC64;
MSMPEFDPAR RPSQAENQTI LTSEIPLKER FFRYFQHEIT GILTPDFPVA LQEQMDRLAD
TSLVGGERTD ATDHCLAGIA RLSNEVKDAA SYIPTYDQRI YAEAIKALQD KLSETRAAVE
PRPKFSFKTK KNASAISLSD AAELAAQGRR SIPGFPSPGT SSVSSSATQT PMYPSTPLNE
PETRLQLQRP ELAPTSIPAI SVADEDDKLK PEHAGTFAAT SVSSVSVNNH HNLHIMLPSS
GSTATVPASI TALRHCVVDM SIPTANGKPY ASLTIKNIKQ SLLVCGQING PAHITGVENS
IIVVDCRQFR MHNCSNVDVY LSSSSNPIIE DCTAIRFGRK PRVYTLDHDR RDDEDRWSQV
EDFKWIKPEP SPNWSLLDAE DAVPEEVWAE IVPGGPGWSL DDILRAIKIT V
//
