ID A0A1Y2UHI8_9PEZI Unreviewed; 381 AA.
AC A0A1Y2UHI8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=C-CAP/cofactor C-like domain-containing protein {ECO:0000259|PROSITE:PS51329};
GN ORFNames=M434DRAFT_400868 {ECO:0000313|EMBL:OTA82841.1};
OS Hypoxylon sp. CO27-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001938 {ECO:0000313|EMBL:OTA82841.1, ECO:0000313|Proteomes:UP000194361};
RN [1] {ECO:0000313|EMBL:OTA82841.1, ECO:0000313|Proteomes:UP000194361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO27-5 {ECO:0000313|EMBL:OTA82841.1,
RC ECO:0000313|Proteomes:UP000194361};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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; KZ112616; OTA82841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2UHI8; -.
DR STRING; 1001938.A0A1Y2UHI8; -.
DR Proteomes; UP000194361; 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:UP000194361}.
FT DOMAIN 206..332
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 381 AA; 41862 MW; B2FD10EE0497BAAE CRC64;
METQVFIPFR PSPPHNHAGG VTQRNMSDPK ERFFRYFQAE ITAIQSQIDD LATISPVGGE
RQDCIDTVLA GISRLSNEVM DAGDYIPAYD QRTYSQAMKA LTDKLNEATA KFAPKSRFQF
KSKSSKPAST SEPQVDSRVR PSFSNIGSKH SPVPDAAKRD AEESAASSAK RYNEELEQQS
GVRRPSFSNA KNIAIYDHSG LHIMLPSTAS RATSSGSLTN LERCVVDMTA PTSAGTPFAG
LALKNIKQSL IIAGHVAGPV HITGLHNSIV VVAARQVRIH ECKDVDVYLH CASHPIIEDC
SGMRFAPLPE LYATKLEIKG ENQWDQVDDF KWLKSEPSPN WTVLPEDKRI PEDIWKNSVC
GGPSLSTDDI LRKVGILGDR S
//
