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 P13188

Entry ID Method Resolution Chain Position Source
3TL4 X-ray 230 A X 1-187 PDB
4H3S X-ray 215 A A 1-809 PDB
AF-P13188-F1 Predicted AlphaFoldDB

10 variants for P13188

Variant ID(s) Position Change Description Diseaes Association Provenance
s15-649485 61 F>Y No SGRP
s15-649677 125 Y>C No SGRP
s15-649919 206 S>T No SGRP
s15-649932 210 A>V No SGRP
s15-650048 249 G>S No SGRP
s15-650960 553 V>M No SGRP
s15-651061 586 D>E No SGRP
s15-651365 688 V>L No SGRP
s15-651474 724 K>R No SGRP
s15-651584 761 E>K No SGRP

No associated diseases with P13188

5 regional properties for P13188

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 258 - 269 IPR001412
domain Glutaminyl-tRNA synthetase, class Ib, non-specific RNA-binding domain 2 166 - 244 IPR007638
domain Glutaminyl-tRNA synthetase, class Ib, non-specific RNA-binding domain, N-terminal 5 - 163 IPR007639
domain Glutamyl/glutaminyl-tRNA synthetase, class Ib, catalytic domain 251 - 564 IPR020058
domain Glutamyl/glutaminyl-tRNA synthetase, class Ib, anti-codon binding domain 568 - 746 IPR020059

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
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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.

3 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).
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.

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
P47897 QARS1 Glutamine--tRNA ligase Homo sapiens (Human) PR
O62431 qars-1 Probable glutamine--tRNA ligase Caenorhabditis elegans PR
10 20 30 40 50 60
MSSVEELTQL FSQVGFEDKK VKEIVKNKKV SDSLYKLIKE TPSDYQWNKS TRALVHNLAS
70 80 90 100 110 120
FVKGTDLPKS ELIVNGIING DLKTSLQVDA AFKYVKANGE ASTKMGMNEN SGVGIEITED
130 140 150 160 170 180
QVRNYVMQYI QENKERILTE RYKLVPGIFA DVKNLKELKW ADPRSFKPII DQEVLKLLGP
190 200 210 220 230 240
KDERDLIKKK TKNNEKKKTN SAKKSSDNSA SSGPKRTMFN EGFLGDLHKV GENPQAYPEL
250 260 270 280 290 300
MKEHLEVTGG KVRTRFPPEP NGYLHIGHSK AIMVNFGYAK YHNGTCYLRF DDTNPEKEAP
310 320 330 340 350 360
EYFESIKRMV SWLGFKPWKI TYSSDYFDEL YRLAEVLIKN GKAYVCHCTA EEIKRGRGIK
370 380 390 400 410 420
EDGTPGGERY ACKHRDQSIE QNLQEFRDMR DGKYKPGEAI LRMKQDLNSP SPQMWDLIAY
430 440 450 460 470 480
RVLNAPHPRT GTKWRIYPTY DFTHCLVDSM ENITHSLCTT EFYLSRESYE WLCDQVHVFR
490 500 510 520 530 540
PAQREYGRLN ITGTVLSKRK IAQLVDEKFV RGWDDPRLFT LEAIRRRGVP PGAILSFINT
550 560 570 580 590 600
LGVTTSTTNI QVVRFESAVR KYLEDTTPRL MFVLDPVEVV VDNLSDDYEE LATIPYRPGT
610 620 630 640 650 660
PEFGERTVPF TNKFYIERSD FSENVDDKEF FRLTPNQPVG LIKVSHTVSF KSLEKDEAGK
670 680 690 700 710 720
IIRIHVNYDN KVEEGSKPKK PKTYIQWVPI SSKYNSPLRV TETRVYNQLF KSENPSSHPE
730 740 750 760 770 780
GFLKDINPES EVVYKESVME HNFGDVVKNS PWVVDSVKNS EFYVEEDKDS KEVCRFQAMR
790 800
VGYFTLDKES TTSKVILNRI VSLKDATSK