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 Q1GB78

Entry ID Method Resolution Chain Position Source
AF-Q1GB78-F1 Predicted AlphaFoldDB

No variants for Q1GB78

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q1GB78

No associated diseases with Q1GB78

5 regional properties for Q1GB78

Type Name Position InterPro Accession
domain Translational (tr)-type GTP-binding domain 10 - 277 IPR000795
domain Small GTP-binding protein domain 14 - 147 IPR005225
conserved_site Tr-type G domain, conserved site 57 - 72 IPR031157
domain Peptide chain release factor 3, C-terminal 386 - 510 IPR032090
domain Peptide chain release factor 3, GTP-binding domain 11 - 276 IPR041732

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 release factor activity, codon specific A translation release factor that is specific for one or more particular termination codons; acts at the ribosomal A-site and require polypeptidyl-tRNA at the P-site.

1 GO annotations of biological process

Name Definition
regulation of translational termination Any process that modulates the frequency, rate or extent of translational termination.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNKELLDKVN KRRTFAIISH PDAGKTTITE QMLLLGGVIR SAGTVKARKT GNYATSDWME
70 80 90 100 110 120
IEKKRGISVT SSVMQFEYQG KRINILDTPG HQDFSEDTYR TLMAVDAAVM VIDSARGIEP
130 140 150 160 170 180
QTKKLFKVVR QRGIPVFTFM NKLDRDGREP LDLVAELEEV LGIEGVAMNW PIGMGQSLLG
190 200 210 220 230 240
LYDLANQRVE LYHPEEGQDR FIALADGKAP AGSPLADDPQ FEETLGEIEL LEGAGASFDR
250 260 270 280 290 300
AKVLAGQQTP VFFGSALTNF GVETFLEQFV DLAPAPGEHE VNGDEELKPD DDEFSGFIFK
310 320 330 340 350 360
IQANMNPQHR DRIAFVRVCS GEFSKGLDVT LARTGKQVRL NNAVEFESSA RVQVSEAVAG
370 380 390 400 410 420
DIVGLYDTGN FQIGDSVYAG KRKLEFPPLP EFTPELFMRV SPKNVMKQKS FHKGMNQLVQ
430 440 450 460 470 480
EGAVQLYRNY QTDDYILGAV GQLQFEVFQY RMKNEYNSEV EMTSIGHRVA RWINPDQLDP
490 500 510 520
KMSSSRNLLV KDRFGNPLFL FENAFAERWF HDKYPDVELT EKL