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

3 structures for P33893

Entry ID Method Resolution Chain Position Source
4N0H X-ray 195 A B 16-329 PDB
4N0I X-ray 200 A B 16-329 PDB
AF-P33893-F1 Predicted AlphaFoldDB

15 variants for P33893

Variant ID(s) Position Change Description Diseaes Association Provenance
s02-74685 3 R>Q No SGRP
s02-74515 60 P>S No SGRP
s02-74300 131 K>N No SGRP
s02-74260 145 A>T No SGRP
s02-73960 245 P>S No SGRP
s02-73755 313 P>Q No SGRP
s02-73697 332 R>S No SGRP
s02-73694 333 I>M No SGRP
s02-73638 352 N>S No SGRP
s02-73467 409 K>R No SGRP
s02-73449 415 P>R No SGRP
s02-73356 446 N>S No SGRP
s02-73351 448 E>K No SGRP
s02-73269 475 V>A No SGRP
s02-73270 475 V>I No SGRP

No associated diseases with P33893

3 regional properties for P33893

Type Name Position InterPro Accession
domain Aspartyl/Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, catalytic 30 - 316 IPR006075
conserved_site Glutamyl-tRNA(Gln) amidotransferase, subunit B, conserved site 177 - 191 IPR017958
domain Asn/Gln amidotransferase 373 - 537 IPR018027

Functions

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

2 GO annotations of cellular component

Name Definition
glutamyl-tRNA(Gln) amidotransferase complex A protein complex that possesses glutamyl-tRNA(Gln) amidotransferase activity, and therefore creates Gln-tRNA by amidating Glu-tRNA; usually composed of 3 subunits: A, B, and C. Note that the C subunit may not be required in all organisms.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity Catalysis of the reaction: L-glutamine + glutamyl-tRNA(Gln) + ATP = L-glutamate + glutaminyl-tRNA(Gln) + phosphate + ADP.

2 GO annotations of biological process

Name Definition
glutaminyl-tRNAGln biosynthesis via transamidation A tRNA aminoacylation process in which glutaminyl-tRNAGln is formed by a tRNA-dependent two-step pathway. In the first step a non-discriminating glutamyl-tRNAGlx synthetase generates the misacylated L-glutamyl-tRNAGln species, and in the second step it is amidated to the correctly charged L-glutaminyl-tRNAGln by a glutamyl-tRNAGln amidotransferase.
mitochondrial translation The chemical reactions and pathways resulting in the formation of a protein in a mitochondrion. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein; the mitochondrion has its own ribosomes and transfer RNAs, and uses a genetic code that differs from the nuclear code.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q2R2Z0 GATB Glutamyl-tRNA(Gln) amidotransferase subunit B, chloroplastic/mitochondrial Oryza sativa subsp japonica (Rice) PR
C5Y3V8 GATB Glutamyl-tRNA(Gln) amidotransferase subunit B, chloroplastic/mitochondrial Sorghum bicolor (Sorghum) (Sorghum vulgare) PR
Q9FV81 GATB Glutamyl-tRNA(Gln) amidotransferase subunit B, chloroplastic/mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MLRLARFYSL ARTKAIHSHG APFRPEYALK CGLEIHTQLN TKNKLFSQST NSATSLVDAP
70 80 90 100 110 120
NHHTSYYDIA LPGTQPVLNL EAILFAMKLS LALGSQVNSI SQFDRKHYFY GDQPQGYQLT
130 140 150 160 170 180
QHYRPFARGG KINLSKELDD IDESAKEIGI LQLQIEQDTG KSHYTETDKD VITLVDLNRS
190 200 210 220 230 240
NVPLIELVTK PDFSDIKQVR AFIKKYQNLV RHLHISSGDL ETGAMRVDVN LSINEYARVE
250 260 270 280 290 300
LKNLPNTSSI INAIKYEYQR QVELISVGDT SSLMEPETRG WTGSSTVKLR SKETTIDYRY
310 320 330 340 350 360
MPDPELPYIN LAPDVISGVR GLMPQLPDDI MRILMKKPYQ LSLKDAKILT YNSNQNDMYN
370 380 390 400 410 420
HEALRSYYLD TFREFSKLAG ERSNAKLPTN WIIHEFLGDL NKLQIPLAKA KEILPPPVFA
430 440 450 460 470 480
QFLKLLHEEV ISATSGKMLL FHILENFEQS NCQDLSIPDF SKLIEKFELH AINQVDPQEL
490 500 510 520 530 540
MDLCNDVIAQ HTDDTFIRNL VTGKKKSSLK FLIGQGMRRS QGRIKANEFE KKFKEILNIQ
W