ID   TBCB_CAEEL              Reviewed;         229 AA.
AC   Q20728;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   29-APR-2008, entry version 52.
DE   Tubulin-specific chaperone B (Tubulin folding cofactor B) (CoB).
GN   ORFNames=F53F4.3;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 135-229.
RX   PubMed=12221106; DOI=10.1074/jbc.M208512200;
RA   Li S., Finley J., Liu Z.J., Qiu S.H., Chen H., Luan C.H., Carson M.,
RA   Tsao J., Johnson D., Lin G., Zhao J., Thomas W., Nagy L.A., Sha B.,
RA   DeLucas L.J., Wang B.C., Luo M.;
RT   "Crystal structure of the cytoskeleton-associated protein glycine-rich
RT   (CAP-Gly) domain.";
RL   J. Biol. Chem. 277:48596-48601(2002).
RN   [3]
RP   STRUCTURE BY NMR OF 1-120.
RX   PubMed=15364906; DOI=10.1074/jbc.M409422200;
RA   Lytle B.L., Peterson F.C., Qiu S.H., Luo M., Zhao Q., Markley J.L.,
RA   Volkman B.F.;
RT   "Solution structure of a ubiquitin-like domain from tubulin-binding
RT   cofactor B.";
RL   J. Biol. Chem. 279:46787-46793(2004).
CC   -!- FUNCTION: Binds to alpha-tubulin folding intermediates after their
CC       interaction with cytosolic chaperonin in the pathway leading from
CC       newly synthesized tubulin to properly folded heterodimer (By
CC       similarity).
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
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity).
CC   -!- SIMILARITY: Belongs to the TBCB family.
CC   -!- SIMILARITY: Contains 1 CAP-Gly domain.
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DR   EMBL; Z77663; CAB01212.1; -; Genomic_DNA.
DR   PIR; T22581; T22581.
DR   RefSeq; NP_506367.1; -.
DR   UniGene; Cel.3444; -.
DR   PDB; 1LPL; X-ray; 1.77 A; A=135-229.
DR   PDB; 1T0Y; NMR; -; A=1-120.
DR   PDB; 1TOV; X-ray; 1.77 A; A=132-229.
DR   PDBsum; 1LPL; -.
DR   PDBsum; 1T0Y; -.
DR   PDBsum; 1TOV; -.
DR   Ensembl; F53F4.3; Caenorhabditis elegans.
DR   GeneID; 186176; -.
DR   KEGG; cel:F53F4.3; -.
DR   NMPDR; fig|6239.3.peg.20325; -.
DR   WormBase; WBGene00009987; F53F4.3.
DR   WormPep; F53F4.3; CE10958.
DR   ArrayExpress; Q20728; -.
DR   InterPro; IPR000938; Cytoskel-assoc-prot_CAP-Gly.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Microtubule.
FT   CHAIN         1    229       Tubulin-specific chaperone B.
FT                                /FTId=PRO_0000083546.
FT   DOMAIN      170    212       CAP-Gly.
FT   STRAND        4     13
FT   STRAND       18     23
FT   HELIX        28     39
FT   TURN         43     45
FT   STRAND       46     51
FT   STRAND       53     60
FT   STRAND       65     67
FT   TURN         68     72
FT   STRAND       77     83
FT   HELIX       137    143
FT   STRAND      151    154
FT   STRAND      162    170
FT   STRAND      173    177
FT   STRAND      179    187
FT   STRAND      189    195
FT   STRAND      207    211
FT   HELIX       213    215
FT   STRAND      216    219
SQ   SEQUENCE   229 AA;  25441 MW;  C465365DAE378A0F CRC64;
     MTEVYDLEIT TNATDFPMEK KYPAGMSLND LKKKLELVVG TTVDSMRIQL FDGDDQLKGE
     LTDGAKSLKD LGVRDGYRIH AVDVTGGNED FKDESMVEKY EMSDDTYGKR TDSVRAWKKK
     MQEEQGSAAP MENESDKLNE EAAKNIMVGN RCEVTVGAQM ARRGEVAYVG ATKFKEGVWV
     GVKYDEPVGK NDGSVAGVRY FDCDPKYGGF VRPVDVKVGD FPELSIDEI
//