TBCE_DICDI
ID TBCE_DICDI Reviewed; 525 AA.
AC Q55CN0;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Tubulin-specific chaperone E;
DE AltName: Full=Tubulin-folding cofactor E;
GN Name=tbce; ORFNames=DDB_G0269990;
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 second step of the
CC tubulin folding pathway.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TBCE family. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72345.1; -; Genomic_DNA.
DR RefSeq; XP_646451.1; XM_641359.1.
DR AlphaFoldDB; Q55CN0; -.
DR STRING; 44689.DDB0266639; -.
DR PaxDb; Q55CN0; -.
DR EnsemblProtists; EAL72345; EAL72345; DDB_G0269990.
DR GeneID; 8617411; -.
DR KEGG; ddi:DDB_G0269990; -.
DR dictyBase; DDB_G0269990; tbcE.
DR eggNOG; KOG3207; Eukaryota.
DR HOGENOM; CLU_017716_5_1_1; -.
DR InParanoid; Q55CN0; -.
DR OMA; VELDVGW; -.
DR PhylomeDB; Q55CN0; -.
DR PRO; PR:Q55CN0; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0043014; F:alpha-tubulin binding; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007023; P:post-chaperonin tubulin folding pathway; IBA:GO_Central.
DR GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
DR Gene3D; 2.30.30.190; -; 1.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR044994; TBCE.
DR PANTHER; PTHR15140; PTHR15140; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF12799; LRR_4; 1.
DR SMART; SM01052; CAP_GLY; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SUPFAM; SSF74924; SSF74924; 1.
DR PROSITE; PS00845; CAP_GLY_1; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
DR PROSITE; PS51450; LRR; 8.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm; Cytoskeleton; Leucine-rich repeat;
KW Reference proteome; Repeat.
FT CHAIN 1..525
FT /note="Tubulin-specific chaperone E"
FT /id="PRO_0000345022"
FT DOMAIN 33..77
FT /note="CAP-Gly"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT REPEAT 300..321
FT /note="LRR 1"
FT REPEAT 326..347
FT /note="LRR 2"
FT REPEAT 362..383
FT /note="LRR 3"
FT DOMAIN 441..481
FT /note="LRRCT"
FT REGION 414..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 525 AA; 60899 MW; A3B5319CB8FCB80D CRC64;
MSNENEKSIV EYFYIGERVK GDDGSVGTIR YQGKVDGFEG NWYGIEWDDP KRGKHQGTVK
GKQYFKCINK GSGSFMKYEK LIKGETFMKS ISDKFHQKID NYDDLYVDST KEDIKIQIQM
IGMNQTRENQ KKFIAQTLLS ASYLPISEID ESPLIYNNFK NLIELNLSNC LLNSWTQIVK
LLKQLPNLNR LHLCNNRLSF NIDEFKKEVN SNNEYGNSID DCNVKDLILV NSNLSNWSIV
SSICKYLFKN IESICLSSNS IENINLFKSI LNNDNENENE NENEIVEQQQ QQQPQYLFPT
LKSLDLANNN IKSFNDILSS LGNLPQLTEL NLNNNQITDI EFNGDVDDGN KSNNGKTNQF
KNLKRIYLSN NKINDWKYLD KLDELQSLDE LSFRNNPIVD SLLISNSNNS NTNENEIEND
IENNNNNIKK DNNNNNKNNK NNKNNKTIFL NRLNIIPRLS NLKKLNLSDI TLLERKDAEL
YFLYENYNSI DKFKNNKKLN YLISIHGEPV YTKMSLQLEK EENGK
