ID A0A2T4AY22_9HYPO Unreviewed; 362 AA.
AC A0A2T4AY22;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=TBCC-domain-containing protein {ECO:0000313|EMBL:PTB61982.1};
GN ORFNames=BBK36DRAFT_1163522 {ECO:0000313|EMBL:PTB61982.1};
OS Trichoderma citrinoviride.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=58853 {ECO:0000313|EMBL:PTB61982.1, ECO:0000313|Proteomes:UP000241546};
RN [1] {ECO:0000313|Proteomes:UP000241546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUCIM 6016 {ECO:0000313|Proteomes:UP000241546};
RG DOE Joint Genome Institute;
RA Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B., Kuo A.,
RA Aerts A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y.,
RA Rahimi M.J., Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D
CC function by capturing and stabilizing tubulin in a quasi-native
CC conformation. Cofactor E binds to the cofactor D-tubulin complex;
CC interaction with cofactor C then causes the release of tubulin
CC polypeptides that are committed to the native state.
CC {ECO:0000256|ARBA:ARBA00026055}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the TBCC family.
CC {ECO:0000256|ARBA:ARBA00008848}.
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DR EMBL; KZ680226; PTB61982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4AY22; -.
DR OrthoDB; 127089at2759; -.
DR Proteomes; UP000241546; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0015631; F:tubulin binding; IEA:InterPro.
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; IPR031925; TBCC_N.
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 Pfam; PF16752; TBCC_N; 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:UP000241546}.
FT DOMAIN 189..315
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 96..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 362 AA; 39740 MW; 8E6587505751A5BD CRC64;
MDPKEKFYRH FRDSVEGLQD QIAQLTNLSS IGGERQDATD NILAGISKLQ NEVADAAEFT
PAYDRRQYSD AIKGLQDKLN ETLAKFAPKT RFQFRRTGTD HVDMGAPEND PRLNPGSLSR
RPHSPTSAPG AASSMMEENR GIVGDLLSTG KNYNEELAKP DLSSIRKPSF SAAQSIDISE
HNGLHIILPS SASRATAAGC LRDLKNCVID LSIPTAQGAP FPGLILKDID RCLIVAGRVN
GPIHINNVTN SILVVVARQV RIHNCKNVDI YLHCASHPII EDCSGMRFAP LPECYLTEAD
KSIENQWDQV DDFKWLKTTP SPNWATLSEA QRLSEEVWTK IVPGQPGIGV EKVLAKVGIP
PK
//
