ID   TBCC_DICDI              Reviewed;         420 AA.
AC   Q54PY1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Tubulin-specific chaperone C;
DE   AltName: Full=Tubulin-folding cofactor C;
DE            Short=CFC;
GN   Name=tbcc; ORFNames=DDB_G0284313;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: Tubulin-folding protein; involved in the final step of the
CC       tubulin folding pathway. {ECO:0000250}.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TBCC family. {ECO:0000305}.
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DR   EMBL; AAFI02000064; EAL65345.1; -; Genomic_DNA.
DR   RefSeq; XP_638664.1; XM_633572.1.
DR   AlphaFoldDB; Q54PY1; -.
DR   SMR; Q54PY1; -.
DR   STRING; 44689.DDB0266636; -.
DR   PaxDb; Q54PY1; -.
DR   EnsemblProtists; EAL65345; EAL65345; DDB_G0284313.
DR   GeneID; 8624493; -.
DR   KEGG; ddi:DDB_G0284313; -.
DR   dictyBase; DDB_G0284313; tbcC.
DR   eggNOG; KOG2512; Eukaryota.
DR   HOGENOM; CLU_654579_0_0_1; -.
DR   InParanoid; Q54PY1; -.
DR   OMA; CKIRANS; -.
DR   PhylomeDB; Q54PY1; -.
DR   PRO; PR:Q54PY1; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0015631; F:tubulin binding; IEA:InterPro.
DR   GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
DR   Gene3D; 2.160.20.70; -; 1.
DR   InterPro; IPR017901; C-CAP_CF_C-like.
DR   InterPro; IPR016098; CAP/MinC_C.
DR   InterPro; IPR027684; TBCC.
DR   InterPro; IPR031925; TBCC_N.
DR   InterPro; IPR012945; Tubulin-bd_cofactor_C_dom.
DR   PANTHER; PTHR15139; PTHR15139; 1.
DR   Pfam; PF07986; TBCC; 1.
DR   Pfam; PF16752; TBCC_N; 1.
DR   PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Reference proteome.
FT   CHAIN           1..420
FT                   /note="Tubulin-specific chaperone C"
FT                   /id="PRO_0000337256"
FT   DOMAIN          216..366
FT                   /note="C-CAP/cofactor C-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00659"
FT   REGION          31..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..193
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          9..142
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        31..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   420 AA;  48767 MW;  3E5A747CED21CEA0 CRC64;
     MSNNNNNNNN NNDEENSKLD IVKKQFQEKE KQRLQSKLEK REISNKEQID QSSSNIASET
     LLLINNLSDD IENRLNEISN NTNENKAEDL KESYNQMEES LSEINSITTM SSHILTSYDV
     KSILENIDNL RKQIDKSKEK YMPKQKLSLT RKKTKTTTVS TKTTSSKEDT NETFNNNNNN
     NNDNDNTDNN NNKISTEPIF NLINIKGFKN KELFYPPKKE EEIGNQDINN NNNNNNNNNN
     NNNNNNNNNN NNNNNNNNSN SINDLFISDL TDCTVILDMK VLTALKINNL VNCKIRANSP
     IDGSIFIDNC INSIFSLVSR QIRIHYCTDC QFNIFVKSNP IIEGSKQIKF SSYLQNLKQQ
     QQQQQQQEQE KVLSSFDNKR FKEYSFDLES NNIDSDKWKL VNDFDWIQQK QSPNWSLVEY