ID A0CEW7_PARTE Unreviewed; 120 AA.
AC A0CEW7;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Tubulin-specific chaperone A {ECO:0000256|RuleBase:RU364030};
GN ORFNames=GSPATT00037773001 {ECO:0000313|EMBL:CAK69334.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK69334.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK69334.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK69334.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
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; CT868067; CAK69334.1; -; Genomic_DNA.
DR RefSeq; XP_001436731.1; XM_001436694.1.
DR AlphaFoldDB; A0CEW7; -.
DR STRING; 5888.A0CEW7; -.
DR EnsemblProtists; CAK69334; CAK69334; GSPATT00037773001.
DR GeneID; 5022516; -.
DR KEGG; ptm:GSPATT00037773001; -.
DR eggNOG; KOG3470; Eukaryota.
DR HOGENOM; CLU_130569_1_2_1; -.
DR InParanoid; A0CEW7; -.
DR OMA; SSHEEYK; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0048487; F:beta-tubulin binding; IEA:InterPro.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
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:UP000000600}.
FT COILED 30..62
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 120 AA; 13914 MW; 0D7B148D709C4503 CRC64;
MAENNKDLKQ LKIKTAALKR IQKEFFGYQK EELKQNERIQ KLKNQNAEEA DIKKQEEVLQ
ETVQMYPNII GRLVESVNEL QVWLDGKLND PLIDTSEEKT KALEAITEAQ DFLKANNPAQ
//
