ID A0A0D2ET94_9EURO Unreviewed; 117 AA.
AC A0A0D2ET94;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 22-FEB-2023, entry version 24.
DE RecName: Full=Tubulin-specific chaperone A {ECO:0000256|RuleBase:RU364030};
GN ORFNames=PV05_09778 {ECO:0000313|EMBL:KIW51019.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW51019.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW51019.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW51019.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) 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|RuleBase:RU364030}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|RuleBase:RU364030}.
CC -!- SIMILARITY: Belongs to the TBCA family. {ECO:0000256|ARBA:ARBA00006806,
CC ECO:0000256|RuleBase:RU364030}.
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DR EMBL; KN847322; KIW51019.1; -; Genomic_DNA.
DR RefSeq; XP_013311603.1; XM_013456149.1.
DR AlphaFoldDB; A0A0D2ET94; -.
DR STRING; 348802.A0A0D2ET94; -.
DR GeneID; 25331686; -.
DR HOGENOM; CLU_130569_0_0_1; -.
DR OrthoDB; 2534019at2759; -.
DR Proteomes; UP000054342; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0048487; F:beta-tubulin binding; IEA:InterPro.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:UniProtKB-UniRule.
DR GO; GO:0007021; P:tubulin complex assembly; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.58.90; -; 1.
DR InterPro; IPR004226; TBCA.
DR InterPro; IPR036126; TBCA_sf.
DR PANTHER; PTHR21500; TUBULIN-SPECIFIC CHAPERONE A; 1.
DR PANTHER; PTHR21500:SF0; TUBULIN-SPECIFIC CHAPERONE A; 1.
DR Pfam; PF02970; TBCA; 1.
DR SUPFAM; SSF46988; Tubulin chaperone cofactor A; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU364030};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|RuleBase:RU364030};
KW Cytoskeleton {ECO:0000256|RuleBase:RU364030};
KW Microtubule {ECO:0000256|RuleBase:RU364030};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342}.
FT REGION 96..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 52..79
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 117 AA; 13448 MW; 8F2754D7D520A2EC CRC64;
MAPSQLQVAI SSLKRLLKEE ASYYKEQEHQ ETRIAKLEKD ETDEDGNREF TLKQERQALE
ETKKVIPTLR ERITSAREKL ENMLDMAGND EERNAAVEVL KTAKEQQKDD PISGVST
//