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 Q8R5Z1

Entry ID Method Resolution Chain Position Source
AF-Q8R5Z1-F1 Predicted AlphaFoldDB

No variants for Q8R5Z1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8R5Z1

No associated diseases with Q8R5Z1

3 regional properties for Q8R5Z1

Type Name Position InterPro Accession
conserved_site Translation initiation factor 3, conserved site 72 - 85 IPR019813
domain Translation initiation factor 3, N-terminal 22 - 90 IPR019814
domain Translation initiation factor 3, C-terminal 97 - 183 IPR019815

Functions

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

1 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

3 GO annotations of molecular function

Name Definition
GTP binding Binding to GTP, guanosine triphosphate.
GTPase activity Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate.
translation initiation factor activity Functions in the initiation of ribosome-mediated translation of mRNA into a polypeptide.

1 GO annotations of biological process

Name Definition
translational initiation The process preceding formation of the peptide bond between the first two amino acids of a protein. This includes the formation of a complex of the ribosome, mRNA or circRNA, and an initiation complex that contains the first aminoacyl-tRNA.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKVRVHELAK KYEIKNKEFL EILKKDIGIT VTSHLSNLDE DQVNKIDDYF AKMNMLKVET
70 80 90 100 110 120
VEPVKVHKEK KEEKPIRKIM DEDENDEGEG YSQKNNKKAK FQQTKNKKNN NITFEEDGNS
130 140 150 160 170 180
HKNKGKKKKG RRTDFILKTV EATPDVVEED GIKIIKFRGE LTLGDFAEKL GVNSAEIIKK
190 200 210 220 230 240
LFLKGQMLTI NSPITLSMAE DLAADYDVLI EEEQEVELDF GEKFDLEIED KAADLKERPP
250 260 270 280 290 300
VITIMGHVDH GKTSLLDAIR TTNVVGGEAG GITQKIGAYQ VERDGKRITF IDTPGHEAFT
310 320 330 340 350 360
DMRARGAQVT DIAILVVAAD DGVMPQTVEA ISHAKVAKVP IIVAVNKIDK PEANPMKVKQ
370 380 390 400 410 420
ELMEHGLVSA EWGGDVEFVE VSAKQKINLD GLLDTILITA EILELKGNNK KRAKGVVLES
430 440 450 460 470 480
RLDPKIGPIA DILVQEGTLK IGDVIVAGEV QGKVKALLND KGERVNNATV SQPVEVIGFN
490 500 510 520 530 540
NVPDAGDTMY VIQNEQHAKR IVEEVRKERK IQETTKKTIS LESLSDQFKH EDLKELNLIL
550 560 570 580 590 600
RADSKGSVDA LRDSLLKLSN DEVAVSIIQA ASGAITESDV KLAEAAGAII IGYNVRPTTK
610 620 630 640 650 660
ALKEAEVSKV EIRTSGIIYH ITEDIEKALA GMLEPEYREE YLGRIEIKKV FKVSKVGNIA
670 680 690 700 710 720
GCIVIDGKVK NDSNIRILRD NVVIYEGKLA SLKRFKDDAK EVVAGQECGL GVENFNDIKD
730
GDVVEAFEMV EVKRTLK