Q55G93

PR
Gene name
tbcd (DDB_G0268516)
Protein name
Tubulin-specific chaperone D
Names
Tubulin-folding cofactor D
Species
Dictyostelium discoideum (Slime mold)
KEGG Pathway
ddi:DDB_G0268516
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-68 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q55G93

Entry ID Method Resolution Chain Position Source
AF-Q55G93-F1 Predicted AlphaFoldDB

No variants for Q55G93

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q55G93

No associated diseases with Q55G93

2 regional properties for Q55G93

Type Name Position InterPro Accession
repeat HEAT, type 2 482 - 519 IPR021133
domain Tubulin-specific chaperone D, C-terminal 1111 - 1291 IPR022577

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

2 GO annotations of molecular function

Name Definition
beta-tubulin binding Binding to the microtubule constituent protein beta-tubulin.
GTPase activator activity Binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP.

4 GO annotations of biological process

Name Definition
microtubule cytoskeleton organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising microtubules and their associated proteins.
post-chaperonin tubulin folding pathway Completion of folding of alpha- and beta-tubulin; takes place subsequent to chaperonin-mediated partial folding; mediated by a complex of folding cofactors.
protein folding The process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure.
tubulin complex assembly The aggregation and bonding together of alpha- and beta-tubulin to form a tubulin heterodimer.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MENSEDISLN SSEKSIESSV VNLEDQQQSQ QQTQQQTCQK TFVQEAPELT ILIDKLIQLK
70 80 90 100 110 120
HSNKDELISN TTRIIYIIDQ YLEQPTLLDI HLNDIIQPLI NFIKSNYINN SNNNNTTTTT
130 140 150 160 170 180
TTIMTETEIV IKKLSIKNSF RIIYVLSKVR GFKTIVKLFQ HEAIDLLPVL DQLEISYHQW
190 200 210 220 230 240
VNINKQRDRL NEISVSYSSG INLKNYIKPE EESEQEVVDE NNNNINNNHN IDDEYNENII
250 260 270 280 290 300
SWEEVYVLAL WVSLLVIIPF KFSSLDSASS GTASAAGDGG DGDGDGQLKS ISSRILKLGK
310 320 330 340 350 360
LALSDVSKIR DSFSELLSKL LNRPDMKFEQ KQFIKWCTNS IQLISNNNNN NNQNNSSNNN
370 380 390 400 410 420
ILLIIGIYST LATMFKKGNR LDFLPIDMNL YEKIMEANKY LSLSGSERIT KKIFLKLLQR
430 440 450 460 470 480
IAIIMLPPVS ASWRYQKIIK PLLLKGELIK QINNNNNNNN NENNNEEGEE EEEEIPEEID
490 500 510 520 530 540
EILEEIMKSL KDKDTIIRWT SAKAIGRIVN LLPKDMGDQV IGLVIDQMFE KNEFIDADPS
550 560 570 580 590 600
AWHGGCLALA ELARRGLLLP ERLDVVVPLV IRALFFDIIK GTYSIGSHVR DSACYLCWAL
610 620 630 640 650 660
ARTYHNSILS PYLLPICRNL VVVSLYDREI NCRKSASAAF QEMVGRHQGL VPNGIEIVTS
670 680 690 700 710 720
ADFFTVGNKN NSFTSLTTFI GKFQIDYYPI VIKHLATIKI YNWDLEIRQL ASKSIHLLTN
730 740 750 760 770 780
INPNDIVSNY LPLIIPNTQS DLVHVKHGAS LAISEILISL FENNNINLLS DNLKMMILMT
790 800 810 820 830 840
IKNTKNEKLF KGKGGVLIRI GMCKIIYSIC LVEFSLDKNL SEIKKPTEST STNGNEDRAA
850 860 870 880 890 900
ALKLKIAMLK AKTASQINKP IITPPSSKST TNNNNNNNNN NLNDNEIAFN IILGYLNENL
910 920 930 940 950 960
NHPNEEVQKE ASKAFELLFS KYISSNEKIS LLLELIDSHC KTLKFDINRS ARRGSSLLLG
970 980 990 1000 1010 1020
SLPFNSANLS YDLLSKVVNE LILSIFQDDP KFKDIETRVN SISSLYKIGI YILNLIFKNQ
1030 1040 1050 1060 1070 1080
ENEQKEEEDF KKSKNYNLFI KIWNCLGLAT NDYSIDKRGD IGSWVRELSC KVLFDFIKFI
1090 1100 1110 1120 1130 1140
ITNQNSSTTT TTASTTDLSI ENLINEKMIT EFICKLFQLS GEKLDKIRDV ACKIIHELLW
1150 1160 1170 1180 1190 1200
IENPSSINNI PHKEELKKII VKDQDVHFNW FRTEESLPLI CKVLKFNCYL YPLLFGLFSS
1210 1220 1230 1240 1250 1260
LGGTSKYLIN DSIQSIKQYF SSFDNDEKER FEKIISFSKA ILEITNNTTQ RMIQPTFRSI
1270 1280 1290 1300 1310 1320
YNLLSTHIFD FLIINNLNEQ SIFETILFNC YQIIESNQDD IYLLLNSIEL FSYFFIQFEN
1330 1340 1350 1360 1370 1380
NNNEYIKDYS LKALLLLLSN LKYPKVRKLA SDQLKKSTRL FINNNGDDET PSLIKSLIFN
1390 1400 1410 1420 1430 1440
TKWDDSVDLI IEPLKSLLLL LNQKHLLELL SENPTKKPIP LAPPITSIEE LKDKIQNPHK
1450 1460 1470
QSDDNNNNNN GELINNNTEN NNNNNFDDNL PEDSQDLMEI