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 O62431

Entry ID Method Resolution Chain Position Source
AF-O62431-F1 Predicted AlphaFoldDB

No variants for O62431

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O62431

No associated diseases with O62431

3 regional properties for O62431

Type Name Position InterPro Accession
domain Glutathione S-transferase, N-terminal 22 - 101 IPR004045
domain Glutathione S-transferase, C-terminal 135 - 210 IPR004046
domain Glutathione S-transferase, C-terminal-like 106 - 225 IPR010987

Functions

Description
EC Number 6.1.1.18 Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
aminoacyl-tRNA synthetase multienzyme complex A multienzyme complex found in all multicellular eukaryotes composed of eight proteins with aminoacyl-tRNA synthetase activities (abbreviated as: ArgRS, AspRS, GluProRS, GlnRS, IleRS, LeuRS, LysRS, MetRS where RS is the enzyme, preceded by the amino acid it uses as a substrate) as well as three non-synthetase proteins (p43, p38, and p18) with diverse functions. Several of these subunits are known dimers, so the total polypeptide count in the multisynthetase complex is at least fifteen. All of the enzymes in this assembly catalyze the same reaction, the covalent attachment of an amino acid to either the 2'- or 3'-hydroxyl of the 3'-terminal adenosine of tRNA, but using different substrates.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
glutamine-tRNA ligase activity Catalysis of the reaction: ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln).

1 GO annotations of biological process

Name Definition
glutaminyl-tRNA aminoacylation The process of coupling glutamine to glutaminyl-tRNA, catalyzed by glutaminyl-tRNA synthetase. The glutaminyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a glutamine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P13188 GLN4 Glutamine--tRNA ligase Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P47897 QARS1 Glutamine--tRNA ligase Homo sapiens (Human) PR
10 20 30 40 50 60
MATKEELLSL GLSDSKVAET LKNVKLTETI GSIVKLASES GEISKQKGTL LYQLATKLKP
70 80 90 100 110 120
QVAAHTPLVV KYIMNDGIKT EPQLSAAIEY LLSHTVKGIQ VPDFEKSCGV GVVVTIDDIE
130 140 150 160 170 180
AAVTKVIGQH REKIVAERYS FPAGKLLGEL RALLPWADGA ITKKEVDLRF LELLGPKTAE
190 200 210 220 230 240
DLAPKKKEKK PEGPKPSKDA AAAATAPGTK NQKEASPEEF ADGAETMDEL LRTRAHFHKV
250 260 270 280 290 300
GENFKQDGYV TTPKTAELLK AHVAAVGGKV VTRFPPEPNG VLHIGHAKAI NINFGYAKAM
310 320 330 340 350 360
GGVCNLRFDD TNPEKEEEKF FSAIEDIVHW LGYDPARVTH SSDNFQQLYL WAVKLIQKGL
370 380 390 400 410 420
AFVCHQKVEE MRGFEVQLSP WRERPIEENI QLFEDMKNGK FDEGEATLRL KLTLEEGKVD
430 440 450 460 470 480
PVAYRIKYVP HHRTGNQWCI YPTYDYTHCL CDSIENITHS LCTKEFQSRR SSYYWLCNAL
490 500 510 520 530 540
DIYCPVQWEY GRLNVNYTVV SKRKILKLIT TKTVNDWDDP RLFTLTALRR RGIPSEAINR
550 560 570 580 590 600
FVAKLGLTMS QMVIDPHVLD ATVRDYLNIH APRTMAVLEG LKLTIENFSE LNLPSSVDVP
610 620 630 640 650 660
DFPSDPTDPR KHSVSVDREI FIEKSDYKPD DSDKSFRRLT PKQAVGLKHI GLVLRFVKEV
670 680 690 700 710 720
KDAEGHVTEV VVKAEKLSEK DKPKAFIHWV AKPVSCEVRL YDRLFKSKNP EDAQLVPGGF
730 740 750 760 770 780
LSDINPDSLT VVYNALIDQS IAKSKVYDRF QFERIGFFCV DRDSTSSTLV FNRTVMLKDG
GASGKN