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Database: UniProt
Entry: A0A024FUQ3_9STRA
LinkDB: A0A024FUQ3_9STRA
Original site: A0A024FUQ3_9STRA 
ID   A0A024FUQ3_9STRA        Unreviewed;       110 AA.
AC   A0A024FUQ3;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   28-JUN-2023, entry version 27.
DE   RecName: Full=Tubulin-specific chaperone A {ECO:0000256|RuleBase:RU364030};
GN   ORFNames=BN9_111390 {ECO:0000313|EMBL:CCI10642.1};
OS   Albugo candida.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX   NCBI_TaxID=65357 {ECO:0000313|EMBL:CCI10642.1, ECO:0000313|Proteomes:UP000053237};
RN   [1] {ECO:0000313|EMBL:CCI10642.1, ECO:0000313|Proteomes:UP000053237}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ac Nc2 {ECO:0000313|EMBL:CCI10642.1,
RC   ECO:0000313|Proteomes:UP000053237};
RA   Gardiner A., Kemen E., Schultz-Larsen T., MacLean D., Van Oosterhout C.,
RA   Jones J.D.G.;
RT   "Recombination and specialization in a pathogen metapopulation.";
RL   Submitted (MAY-2012) 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:CCI10642.1}.
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DR   EMBL; CAIX01000335; CCI10642.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024FUQ3; -.
DR   STRING; 65357.A0A024FUQ3; -.
DR   InParanoid; A0A024FUQ3; -.
DR   OrthoDB; 2785250at2759; -.
DR   Proteomes; UP000053237; 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:UP000053237}.
SQ   SEQUENCE   110 AA;  12715 MW;  D77950830622FFA3 CRC64;
     MADKELKLKV NILRRIKKDL EYYAKEYDVQ SSRISKMRAE QKDEADIRKQ EEVLLETQTM
     LPDCQARLKE ALAALQKVYQ SCKSDADEDN ESMREILQEA TDLLEAASAC
//
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