Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q75DT8

Entry ID Method Resolution Chain Position Source
AF-Q75DT8-F1 Predicted AlphaFoldDB

No variants for Q75DT8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q75DT8

No associated diseases with Q75DT8

1 regional properties for Q75DT8

Type Name Position InterPro Accession
domain Proteasome component (PCI) domain 319 - 493 IPR000717

Functions

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

7 GO annotations of cellular component

Name Definition
cytoplasmic stress granule A dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress.
eukaryotic 43S preinitiation complex A protein complex composed of the 40S ribosomal subunit plus eIF1A, eIF3, and eIF2-GTP-bound methionyl-initiator methionine tRNA.
eukaryotic 48S preinitiation complex A protein complex composed of the small ribosomal subunit, eIF3, eIF1A, methionyl-initiatior methionine and a capped mRNA. The complex is initially positioned at the 5'-end of the capped mRNA.
eukaryotic translation initiation factor 3 complex, eIF3e An eukaryotic translation initiation factor 3 complex that contains the PCI-domain protein eIF3e.
eukaryotic translation initiation factor 3 complex, eIF3m An eukaryotic translation initiation factor 3 complex that contains the PCI-domain protein eIF3m.
incipient cellular bud site The portion of the budding yeast plasma membrane where a daughter cell will emerge. The yeast marks this spot with bud-site selection proteins before bud emergence occurs. Actin is polarized to this spot just prior to and during bud emergence.
multi-eIF complex A multifactor complex composed of multiple translation initiation factors and the initiatior tRNAiMet, which is ready to bind to the small (40S) ribosome to form the 43S preinitiation complex. In S. cerevisiae, this complex is composed of eIF1, eIF2, eIF3, and eIF5.

2 GO annotations of molecular function

Name Definition
mRNA binding Binding to messenger RNA (mRNA), an intermediate molecule between DNA and protein. mRNA includes UTR and coding sequences, but does not contain introns.
translation initiation factor activity Functions in the initiation of ribosome-mediated translation of mRNA into a polypeptide.

2 GO annotations of biological process

Name Definition
formation of cytoplasmic translation initiation complex Joining of the large subunit, with release of IF2/eIF2 and IF3/eIF3. This leaves the functional ribosome at the AUG, with the methionyl/formyl-methionyl-tRNA positioned at the P site.
translation reinitiation A gene-specific translational control mechanism where the small ribosomal subunit remains attached to the mRNA following termination of translation, then resumes scanning on the same mRNA molecule and initiates again at a downstream start site. Reinitiation depends on de novo recruitment of the ternary complex that is required to recognize the next AUG codon.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAPPVLRPEN ALKRADELIS VGEPQAALQS LLDYITSRRI RFADPAAIEP IVFKFLELGV
70 80 90 100 110 120
ELKRGKVIKD GLYQYRKHVQ SSTEGLKSVG AVSRRFIDLI EKKMSSEQAK ANAEESTEED
130 140 150 160 170 180
LEGGVTPENL LISVYEQDQS VGGFNDEAVT SWLRFTWESY RTVLDLLRNN SQLEITYSGV
190 200 210 220 230 240
VNRAMQFCLK YNRKNEFKRL ADMLRQHLDA ANYQQQKSKQ YTVDLSDPDT LQRYLDQRIL
250 260 270 280 290 300
QVNVSVKLGL WHEAFRSIED VHHLLSMSTR DPKPSVLANY YQNMAKVFFV SSNYLLNSVA
310 320 330 340 350 360
LQKFYDLYQQ NPKATDEDFK FYASQLVLSA LSIQQDDLPV VGYDPLARLA GFLNLESKPT
370 380 390 400 410 420
RSQVIEAVSD SKIFSRADEP VKKLYELLNS DFDVNTLKES LASLLPELNS KSYFTQYVEP
430 440 450 460 470 480
LKSFTIRKAF ISASKQFGSI KLDELFEHTS LPSPFDLSPL DLEKSLLQAA MNDYVSFSID
490 500 510 520 530 540
HDAGVVSFME DPFELLGGST ATNADDEQRN DDGYEETHVE EEPEPILTRN SAVRTQLIEL
550 560 570 580 590 600
AKALKETEGF PHASYVDKVR MARNELIRQN NAIIASEKEA AEERARQLEY EKQSASGVPL
610 620 630 640 650 660
TAEQVVEERQ RRMKEEKEAA EARMEAEARR RAEEKREREL AAINEKTMLK MIEDINAKGL
670 680 690 700 710 720
IFIDPKEAKN MTLEKFKKLT VELVSKDKKD LDERMSHAFK RVDHIERAYR KLEAPLWEKD
730 740 750 760 770 780
AQKQKERDLE SYNKLKQMMV EKAKKDHEEN LRIHDRLVKI YPSYLHFREK VIAAQKSQIE
790 800 810 820 830 840
ALRAENAAKL EAAKNARLQE VRQQRYNELI ARRKEELAAK EHDDRQRMLQ DRLTKERKER
850 860 870 880 890 900
ERVNKEKDEA ARKQREIEEA VERTIKRNVS ATPAPPVRSA PPARAAPPPR ASNEQVASPA
910 920
PQPEKKLTYA EKMKLRRAGR A