TBCD_DICDI
ID TBCD_DICDI Reviewed; 1480 AA.
AC Q55G93;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Tubulin-specific chaperone D;
DE AltName: Full=Tubulin-folding cofactor D;
GN Name=tbcd; ORFNames=DDB_G0268516;
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 first 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 TBCD family. {ECO:0000305}.
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DR EMBL; AAFI02000003; EAL73711.2; -; Genomic_DNA.
DR RefSeq; XP_647291.2; XM_642199.2.
DR AlphaFoldDB; Q55G93; -.
DR STRING; 44689.DDB0266638; -.
DR PaxDb; Q55G93; -.
DR PRIDE; Q55G93; -.
DR EnsemblProtists; EAL73711; EAL73711; DDB_G0268516.
DR GeneID; 8616097; -.
DR KEGG; ddi:DDB_G0268516; -.
DR dictyBase; DDB_G0268516; tbcD.
DR eggNOG; KOG1943; Eukaryota.
DR HOGENOM; CLU_003043_0_0_1; -.
DR InParanoid; Q55G93; -.
DR OMA; CWALART; -.
DR PhylomeDB; Q55G93; -.
DR PRO; PR:Q55G93; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0048487; F:beta-tubulin binding; IBA:GO_Central.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
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; IEA:InterPro.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR033162; TBCD.
DR InterPro; IPR022577; Tubulin_specific_chaperoneD_C.
DR PANTHER; PTHR12658; PTHR12658; 1.
DR Pfam; PF12612; TFCD_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 3: Inferred from homology;
KW Chaperone; Reference proteome; Repeat.
FT CHAIN 1..1480
FT /note="Tubulin-specific chaperone D"
FT /id="PRO_0000345005"
FT REPEAT 482..520
FT /note="HEAT 1"
FT REPEAT 886..922
FT /note="HEAT 2"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1437..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1480 AA; 169174 MW; FA517B174B5165A7 CRC64;
MENSEDISLN SSEKSIESSV VNLEDQQQSQ QQTQQQTCQK TFVQEAPELT ILIDKLIQLK
HSNKDELISN TTRIIYIIDQ YLEQPTLLDI HLNDIIQPLI NFIKSNYINN SNNNNTTTTT
TTIMTETEIV IKKLSIKNSF RIIYVLSKVR GFKTIVKLFQ HEAIDLLPVL DQLEISYHQW
VNINKQRDRL NEISVSYSSG INLKNYIKPE EESEQEVVDE NNNNINNNHN IDDEYNENII
SWEEVYVLAL WVSLLVIIPF KFSSLDSASS GTASAAGDGG DGDGDGQLKS ISSRILKLGK
LALSDVSKIR DSFSELLSKL LNRPDMKFEQ KQFIKWCTNS IQLISNNNNN NNQNNSSNNN
ILLIIGIYST LATMFKKGNR LDFLPIDMNL YEKIMEANKY LSLSGSERIT KKIFLKLLQR
IAIIMLPPVS ASWRYQKIIK PLLLKGELIK QINNNNNNNN NENNNEEGEE EEEEIPEEID
EILEEIMKSL KDKDTIIRWT SAKAIGRIVN LLPKDMGDQV IGLVIDQMFE KNEFIDADPS
AWHGGCLALA ELARRGLLLP ERLDVVVPLV IRALFFDIIK GTYSIGSHVR DSACYLCWAL
ARTYHNSILS PYLLPICRNL VVVSLYDREI NCRKSASAAF QEMVGRHQGL VPNGIEIVTS
ADFFTVGNKN NSFTSLTTFI GKFQIDYYPI VIKHLATIKI YNWDLEIRQL ASKSIHLLTN
INPNDIVSNY LPLIIPNTQS DLVHVKHGAS LAISEILISL FENNNINLLS DNLKMMILMT
IKNTKNEKLF KGKGGVLIRI GMCKIIYSIC LVEFSLDKNL SEIKKPTEST STNGNEDRAA
ALKLKIAMLK AKTASQINKP IITPPSSKST TNNNNNNNNN NLNDNEIAFN IILGYLNENL
NHPNEEVQKE ASKAFELLFS KYISSNEKIS LLLELIDSHC KTLKFDINRS ARRGSSLLLG
SLPFNSANLS YDLLSKVVNE LILSIFQDDP KFKDIETRVN SISSLYKIGI YILNLIFKNQ
ENEQKEEEDF KKSKNYNLFI KIWNCLGLAT NDYSIDKRGD IGSWVRELSC KVLFDFIKFI
ITNQNSSTTT TTASTTDLSI ENLINEKMIT EFICKLFQLS GEKLDKIRDV ACKIIHELLW
IENPSSINNI PHKEELKKII VKDQDVHFNW FRTEESLPLI CKVLKFNCYL YPLLFGLFSS
LGGTSKYLIN DSIQSIKQYF SSFDNDEKER FEKIISFSKA ILEITNNTTQ RMIQPTFRSI
YNLLSTHIFD FLIINNLNEQ SIFETILFNC YQIIESNQDD IYLLLNSIEL FSYFFIQFEN
NNNEYIKDYS LKALLLLLSN LKYPKVRKLA SDQLKKSTRL FINNNGDDET PSLIKSLIFN
TKWDDSVDLI IEPLKSLLLL LNQKHLLELL SENPTKKPIP LAPPITSIEE LKDKIQNPHK
QSDDNNNNNN GELINNNTEN NNNNNFDDNL PEDSQDLMEI
