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 Q8SR10

Entry ID Method Resolution Chain Position Source
AF-Q8SR10-F1 Predicted AlphaFoldDB

No variants for Q8SR10

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8SR10

No associated diseases with Q8SR10

7 regional properties for Q8SR10

Type Name Position InterPro Accession
repeat WD40 repeat 22 - 62 IPR001680-1
repeat WD40 repeat 64 - 103 IPR001680-2
repeat WD40 repeat 187 - 223 IPR001680-3
repeat WD40 repeat 226 - 264 IPR001680-4
repeat WD40 repeat 424 - 460 IPR001680-5
domain Lethal giant larvae homologue 2 279 - 379 IPR013577
domain Lethal giant larvae (Lgl)-like, C-terminal domain 823 - 958 IPR013905

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

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.

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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MADLEKILER LGISPEKRCQ VIKKEQVVRN MEKIFLGRDL SNRLLYTLAC IAPKNADLGL
70 80 90 100 110 120
LADLVDARVI KHESMLKECL RYTEKKDVSM EEMTRFVKRN EVSSEDVRKF VAKMRSDRVA
130 140 150 160 170 180
KKDMVSKARK AMPCADFRVV VEEINKVPDD VDGGDEKRPL EGGWLEEGEI KKLPKPSEIP
190 200 210 220 230 240
QINEEIRQAH LRRTGGRVVT RFPPEPNGIL HIGHAKAINL NFEYAKKFGG YTYLRYDDTN
250 260 270 280 290 300
PKNEEAEYFD SIYEDVRWLG FEPYKVTASS DYFDKMTEFG FQLIRKGKAY VCHLSQDEIC
310 320 330 340 350 360
ERRRQYVSDG TNDRSHLSQY RDRPVSENLR LFQEMVDGKW EEGKACLRFK MDTDTKNPLM
370 380 390 400 410 420
LDLVGIRILD VVHPRKNVKY TVYPTYEFAL CVSDSLEDVT HSFCTREFYT RQESYNWLLV
430 440 450 460 470 480
QLEIYKPIQW EFSRLNISNT VLSKRKLLPL KKYGIELDDP RLFTIKGMRR RGFPPEAINQ
490 500 510 520 530 540
FCRSLGFTFA ETTVDVKKLE NFVRDNLNRT SRRIMCVKEP LKVTIMNSTP CSISIPDLPG
550 560 570 580 590 600
SSVVRDVPFT PVIYIEKSDF MEKGDKDFLR LTPEQPVGLY MLYPIRVVKV TPDGIVAERW
610 620 630 640 650 660
DGVPRKFIHW VSEDSVEVEM RMYSSLWTSF SPKDATYLEE MNKDSLKVFH GLCDKRISDA
670 680 690
RIEDRFQFQR IGYFCVDKDT TKENIVVNLT IPLKNIA