ID A0A2B7XC40_9EURO Unreviewed; 120 AA.
AC A0A2B7XC40;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Tubulin-specific chaperone A {ECO:0000256|RuleBase:RU364030};
GN ORFNames=AJ79_06470 {ECO:0000313|EMBL:PGH06686.1};
OS Helicocarpus griseus UAMH5409.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Helicocarpus.
OX NCBI_TaxID=1447875 {ECO:0000313|EMBL:PGH06686.1, ECO:0000313|Proteomes:UP000223968};
RN [1] {ECO:0000313|EMBL:PGH06686.1, ECO:0000313|Proteomes:UP000223968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH5409 {ECO:0000313|EMBL:PGH06686.1,
RC ECO:0000313|Proteomes:UP000223968};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-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|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:PGH06686.1}.
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DR EMBL; PDNB01000115; PGH06686.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7XC40; -.
DR STRING; 1447875.A0A2B7XC40; -.
DR OrthoDB; 2534019at2759; -.
DR Proteomes; UP000223968; 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:UP000223968}.
FT REGION 28..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 120 AA; 13533 MW; FA85FA4ADD780028 CRC64;
MAPQTPLAIA TSALQRLVKE EASYHRELEQ QQERIKRLEA EQPTDDDDGN KEYILRQERQ
ALEETRKVLP NMKQKISEAI AKLDHLLVEE GQKGMGSNVS EINAGKDAIS HAKTAVREIS
//
