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Database: UniProt
Entry: A0A4Q4XTX3_9PEZI
LinkDB: A0A4Q4XTX3_9PEZI
Original site: A0A4Q4XTX3_9PEZI 
ID   A0A4Q4XTX3_9PEZI        Unreviewed;       127 AA.
AC   A0A4Q4XTX3;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   22-FEB-2023, entry version 10.
DE   RecName: Full=Tubulin-specific chaperone A {ECO:0000256|RuleBase:RU364030};
GN   ORFNames=DL769_006658 {ECO:0000313|EMBL:RYP64465.1};
OS   Monosporascus sp. CRB-8-3.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Xylariales incertae sedis; Monosporascus.
OX   NCBI_TaxID=2211644 {ECO:0000313|EMBL:RYP64465.1, ECO:0000313|Proteomes:UP000292472};
RN   [1] {ECO:0000313|EMBL:RYP64465.1, ECO:0000313|Proteomes:UP000292472}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRB-8-3 {ECO:0000313|EMBL:RYP64465.1,
RC   ECO:0000313|Proteomes:UP000292472};
RA   Robinson A.J., Natvig D.O.;
RT   "Complete Genomes of Monosporascus.";
RL   Submitted (JUN-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|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}.
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:RYP64465.1}.
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DR   EMBL; QJNZ01000489; RYP64465.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Q4XTX3; -.
DR   STRING; 2211644.A0A4Q4XTX3; -.
DR   Proteomes; UP000292472; 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   Cytoplasm {ECO:0000256|RuleBase:RU364030};
KW   Cytoskeleton {ECO:0000256|RuleBase:RU364030};
KW   Microtubule {ECO:0000256|RuleBase:RU364030};
KW   Reference proteome {ECO:0000313|Proteomes:UP000292472}.
FT   REGION          37..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          97..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   127 AA;  13577 MW;  F177F3C0E227A852 CRC64;
     MPAPSPLTIA TQAVNRLVKE EQYYQKELAQ QTERVKKLEA EAANGSGGGG GGDSDDDNAE
     FMLKQERKAL EETKTVFLPL SEKIGEAVRR LEEQIATAES EGGSADEMAK AKEALELGRT
     AGQPAAV
//
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