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 Q5NXL5

Entry ID Method Resolution Chain Position Source
AF-Q5NXL5-F1 Predicted AlphaFoldDB

No variants for Q5NXL5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5NXL5

No associated diseases with Q5NXL5

5 regional properties for Q5NXL5

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 45 - 56 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 16 - 624 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 676 - 824 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 881 - 946 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 623 - 765 IPR033705

Functions

Description
EC Number 6.1.1.9 Ligases forming aminoacyl-tRNA and related compounds
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
aminoacyl-tRNA editing activity The hydrolysis of an incorrectly aminoacylated tRNA.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
valine-tRNA ligase activity Catalysis of the reaction: L-valine + ATP + tRNA(Val) = L-valyl-tRNA(Val) + AMP + diphosphate + 2 H(+).

1 GO annotations of biological process

Name Definition
valyl-tRNA aminoacylation The process of coupling valine to valyl-tRNA, catalyzed by valyl-tRNA synthetase. The valyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a valine-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
MELAKSFEPA AIEARWYPEW ESRGHFDAGL DKSNPNAFCI LLPPPNVTGT LHMGHGFNQT
70 80 90 100 110 120
IMDALTRYHR MRGFNTLWQP GTDHAGIATQ IVVERQLDAK GVSRHDLGRE KFVEKVWEWK
130 140 150 160 170 180
EYSGGTITRQ MRRLGTSPDW KRERFTMDEG LSKTVTETFV RLYNEGLIYR GKRLVNWDPK
190 200 210 220 230 240
LGTAVSDLEV VSEEEDGFLW HITYPFSDGP VGDLKGLTVA TTRPETMLGD VAVMVHPEDE
250 260 270 280 290 300
RYAHLIGKTV RLPLCERDIP IIGDDYVDRE FGTGCVKVTP AHDFNDYAVG LRHNLPMISI
310 320 330 340 350 360
LRLDAHVSDD APEKYRGMDR FVAREVIVQD LEAQGLLAGI KPHKLMVPRG DRTSAVIEPM
370 380 390 400 410 420
LTDQWFVAMT KPGADGRSIT AKALECVASG EIRFYPENWI NTYNQWLNNI QDWCISRQLW
430 440 450 460 470 480
WGHQIPAWYA DVEGDSRVWV AHDEAEAKSL AAKDGFTGRL RRDDDVLDTW YSSALWPFST
490 500 510 520 530 540
LDWTAEWPEK SNDALDLYLP SSVLVTGFDI IFFWVARMVM MTKHITGKIP FRDVYVHGLI
550 560 570 580 590 600
RDAEGQKMSK SKGNVLDPID LIDGISADEL AKKRTFGLMN PKQAQSIEKK TRKEFPEGIP
610 620 630 640 650 660
AFGTDALRFT FASLATPGRD IKFDLSRCEG YRNFCNKLWN ATRFVLMNCE GQDCGISAAA
670 680 690 700 710 720
GSAACNTANL DFSFADRWIV SKLQRTEAEV AQHFRDYRFD LVSKAVYEFV WDEYCDWYVE
730 740 750 760 770 780
LAKVQIQSGT EAQQRATRRT LLRVLETVLR LAHPLIPFIT EELWQTVAPL AGRKDTDSIM
790 800 810 820 830 840
LARYPEADLS RLDEASEAKI AELKAIVGTC RNLRSEMNIS PAQRMPLVAA GEATILTSYA
850 860 870 880 890 900
PYLAGLARLS EVAVVDEIGT DELAPVAVAG RFKLMLRVEI DIAAERERIA KEIARLEGEM
910 920 930 940
TKAESKLANE SFVARAPATV VQQERERLAS FVATLEKLRP QLEKLGAR