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Database: UniProt
Entry: A0A2P6SDT2_ROSCH
LinkDB: A0A2P6SDT2_ROSCH
Original site: A0A2P6SDT2_ROSCH 
ID   A0A2P6SDT2_ROSCH        Unreviewed;        65 AA.
AC   A0A2P6SDT2;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   22-FEB-2023, entry version 17.
DE   RecName: Full=Tubulin-specific chaperone A {ECO:0000256|RuleBase:RU364030};
GN   ORFNames=RchiOBHm_Chr1g0341741 {ECO:0000313|EMBL:PRQ56842.1};
OS   Rosa chinensis (China rose).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC   Rosa.
OX   NCBI_TaxID=74649 {ECO:0000313|EMBL:PRQ56842.1, ECO:0000313|Proteomes:UP000238479};
RN   [1] {ECO:0000313|EMBL:PRQ56842.1, ECO:0000313|Proteomes:UP000238479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Old Blush {ECO:0000313|Proteomes:UP000238479};
RA   Bendahmane M.;
RT   "The Rosa genome provides new insights in the design of modern roses.";
RL   Nat. Genet. 0:0-0(2018).
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:PRQ56842.1}.
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DR   EMBL; PDCK01000039; PRQ56842.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P6SDT2; -.
DR   STRING; 74649.A0A2P6SDT2; -.
DR   EnsemblPlants; PRQ56842; PRQ56842; RchiOBHm_Chr1g0341741.
DR   Gramene; PRQ56842; PRQ56842; RchiOBHm_Chr1g0341741.
DR   OMA; KGDDPYD; -.
DR   Proteomes; UP000238479; Chromosome 1.
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:UP000238479}.
FT   REGION          31..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..46
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   65 AA;  7433 MW;  D6AEAED374CB15B6 CRC64;
     MATVRNLKIK TGTCKRLVKE FHSYEKEVER EAAKTADMKG KGADPYDLKQ QENVLAESRM
     MIPDC
//
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