ID A0A2J6PJI7_9HELO Unreviewed; 393 AA.
AC A0A2J6PJI7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=TBCC-domain-containing protein {ECO:0000313|EMBL:PMD14056.1};
GN ORFNames=NA56DRAFT_611183 {ECO:0000313|EMBL:PMD14056.1};
OS Hyaloscypha hepaticicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD14056.1, ECO:0000313|Proteomes:UP000235672};
RN [1] {ECO:0000313|EMBL:PMD14056.1, ECO:0000313|Proteomes:UP000235672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD14056.1,
RC ECO:0000313|Proteomes:UP000235672};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (MAY-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; KZ613525; PMD14056.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6PJI7; -.
DR STRING; 1745343.A0A2J6PJI7; -.
DR OrthoDB; 127089at2759; -.
DR Proteomes; UP000235672; 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:UP000235672}.
FT DOMAIN 195..346
FT /note="C-CAP/cofactor C-like"
FT /evidence="ECO:0000259|PROSITE:PS51329"
SQ SEQUENCE 393 AA; 42977 MW; DA8B015714D64012 CRC64;
MLDKMEDPMA PIQQPSVLTH ADVKDRFYRH FQQECTEIQD QIALLGDYSL VGGEKQDAIN
HVLSSISRLS TEVSDSSGLI PAYDQRIYAQ AIKALEEKLE ETRSKFAPKS RFKFKTTQKN
SSAVSINDAA ELAAKQRLEH PSISGIGSSA ESSIATTPAH LMSPPNEIDT KDTLGDLPSF
PKNYNEEMTK GTSGPIRKPS FSQATNVNIS GHNGLHIILP SSASRATSSG SLTKLTRCIV
DMSVPTANNA PFAGLALKNI KGSLIIVGHV AGAAHITGVE NSIIVVASRQ VRMHDCNNVD
IYLHCASRPI IEDCSNIRFS PIPDCYMNSS VDLIQNQWDQ VDDFKWLKSE HSPNWSVLPE
EKRLQEDMWT TVVPGGPGVG TEDILRKIGI AAR
//
