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Database: UniProt
Entry: A0A2R6NGQ0_9APHY
LinkDB: A0A2R6NGQ0_9APHY
Original site: A0A2R6NGQ0_9APHY 
ID   A0A2R6NGQ0_9APHY        Unreviewed;       321 AA.
AC   A0A2R6NGQ0;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=C-CAP/cofactor C-like domain-containing protein {ECO:0000259|PROSITE:PS51329};
GN   ORFNames=PHLCEN_2v12573 {ECO:0000313|EMBL:PSR71564.1};
OS   Hermanssonia centrifuga.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Meruliaceae; Hermanssonia.
OX   NCBI_TaxID=98765 {ECO:0000313|EMBL:PSR71564.1, ECO:0000313|Proteomes:UP000186601};
RN   [1] {ECO:0000313|EMBL:PSR71564.1, ECO:0000313|Proteomes:UP000186601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FBCC195 {ECO:0000313|EMBL:PSR71564.1,
RC   ECO:0000313|Proteomes:UP000186601};
RA   Granchi Z., Peng M., de Vries R.P., Hilden K., Makela M.R., Grigoriev I.,
RA   Riley R.;
RT   "Genome sequence of the basidiomycete white-rot fungus Phlebia
RT   centrifuga.";
RL   Submitted (FEB-2018) 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:PSR71564.1}.
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DR   EMBL; MLYV02001271; PSR71564.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R6NGQ0; -.
DR   STRING; 98765.A0A2R6NGQ0; -.
DR   Proteomes; UP000186601; 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:UP000186601}.
FT   DOMAIN          104..275
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000259|PROSITE:PS51329"
SQ   SEQUENCE   321 AA;  35527 MW;  0576C757B6FEA2EB CRC64;
     MVCDTLCDRC DLSTRLESLK IASVISNEAL NALTLDAARL RKALTDATSF LPTYDQRQYE
     QFLKSMEQSL EELRSASAPK PKFTFKRRAR EPLATTAQHA AAVPAPHEEP VRVFVQALEA
     QSSYHLSLSG YSHKYLSWSS LPPSLSSTSD LSISDLSNCI VNLLATPSTA SVGRSTSGEI
     RTFTALHIRN LVDTVLILPP INGSALIHDL KHCTIVLGCH QFRMHTSSVV NIYLSIASNP
     IIEHCSAIQF SQYPDAFQLD VPATSSTWAV QDFSHIRPTP SPNWSKLPDD KKREDWSVDE
     QYGDADVDAV LPRFLPQSKL S
//
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