ID   A0A1V8V742_9PEZI        Unreviewed;       379 AA.
AC   A0A1V8V742;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=C-CAP/cofactor C-like domain-containing protein {ECO:0000259|PROSITE:PS51329};
GN   ORFNames=B0A51_01063 {ECO:0000313|EMBL:OQO31715.1};
OS   Rachicladosporium sp. CCFEE 5018.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Cladosporiales; Cladosporiaceae; Rachicladosporium.
OX   NCBI_TaxID=1974281 {ECO:0000313|EMBL:OQO31715.1, ECO:0000313|Proteomes:UP000192386};
RN   [1] {ECO:0000313|Proteomes:UP000192386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCFEE 5018 {ECO:0000313|Proteomes:UP000192386};
RA   Coleine C., Masonjones S., Stajich J.E.;
RT   "Genomes of endolithic fungi from Antarctica.";
RL   Submitted (MAR-2017) 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   -!- SIMILARITY: Belongs to the TBCC family.
CC       {ECO:0000256|ARBA:ARBA00008848}.
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:OQO31715.1}.
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DR   EMBL; NAEU01000017; OQO31715.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8V742; -.
DR   STRING; 1974281.A0A1V8V742; -.
DR   Proteomes; UP000192386; Unassembled WGS sequence.
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; 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   PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000192386}.
FT   DOMAIN          174..332
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51329"
FT   REGION          127..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..152
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   379 AA;  41152 MW;  DE24E279E4FC90EE CRC64;
     MAAMAGDETE ATLPPSERFF RYFQHEVTAL QDQMLRLDNT GISGGERADA ADHCLAGIAR
     LSNEVKDASS YIPAYDQRTY SEAIKALSKK LEDSRQRAIP KQKFSFRSST FTTRKNESAI
     SLNDAAKRAK EKLPGPASET SADSSFATTP IYPASPTPEL VQDGDSGTPT ASAPSSSDAA
     RARTMSFSQS TKVTINNHDG QHIILPSSAS HATSSGTLSN LRRCVIDMST PTSEDHAFAG
     LTLRNISDSL IICGHVDGAA HVTNVTNSIL VVASRQLRLH ESQNCDIYLH AAGRPIIEDC
     KDVRFAPLPE IFLNDADRMI ENQWDAVDDF KWLSAELSPN WQILEKEKRV PAAMWQEVVP
     GGPTFGAAEI LNTLKVGSA
//