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 A1K9L8

Entry ID Method Resolution Chain Position Source
AF-A1K9L8-F1 Predicted AlphaFoldDB

No variants for A1K9L8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A1K9L8

No associated diseases with A1K9L8

5 regional properties for A1K9L8

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 45 - 56 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 16 - 674 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 726 - 876 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 931 - 995 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 673 - 815 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 AIEARRYPEW ESRGYFDAGL DTSNPNAFCI LLPPPNVTGT LHMGHGFNQT
70 80 90 100 110 120
IMDALTRYHR MRGDNTLWQP GTDHAGIATQ IVVERQLDAQ GVSRHDLGRE KFLEKVWEWK
130 140 150 160 170 180
EYSGGTITRQ MRRLGTSPDW KRERFTMDEG LSKTVTETFV RLYNEGLIYR GKRLVNWDPK
190 200 210 220 230 240
LGTAVSDLEV VSEEEDGKLY HILYPFSDGP VGDLRGLTVA TTRPETLLGD VAVMVHPEDE
250 260 270 280 290 300
RYAHLIGKTV ALPLTGRHIP IIADDYVDRE FGTGCVKVTP AHDFNDYAVG QRHQLDMIVV
310 320 330 340 350 360
LKLDGSVPAV AERYTTDGQP REGVAMPAGV AGLDRVPARD KVVAELEALG LMLEIKAHKL
370 380 390 400 410 420
QVPRGDRTNV VIEPMLTDQW FVAMSKPGAD GKSITAKALE VVASGEIKFY PENWVNTYNQ
430 440 450 460 470 480
WLNNIQDWCI SRQLWWGHRI PAWYDDEGRI YVAANEEAAL HAWKADLEAE IARLQGEVQS
490 500 510 520 530 540
RQSQGQTAEQ YPDLAERLSV LHARYEEGTL RQEEDVLDTW YSSALWPFST LDWTPEWPQK
550 560 570 580 590 600
SNPALDLYLP STVLVTGFDI IFFWVARMVM MTKHITGKIP FKHVYVHGLI RDAEGQKMSK
610 620 630 640 650 660
SKGNVLDPID LIDGIGIDEL VQKRTFGLMN PKQAQSIEKK TRKEFPEGIP AFGTDALRFT
670 680 690 700 710 720
FASLASPGRD IKFDLARCEG YRNFCNKLWN ATRFVLMNCE GQDCGMDPHE PGTCVPGGYL
730 740 750 760 770 780
DFSFADRWIV SRLQRTEAEV AAQFEAYRFD LVARAVYEFV WDEYCDWYLE LAKVQIQTGT
790 800 810 820 830 840
PEQQRATRRT LLRVLETVLR LAHPLIPFIT EELWETVAPL AGRKDADSIM LARYPQADMG
850 860 870 880 890 900
RIDEASEAQV AELKALIYAC RNLRGEMNIS PAQRLPLVAA GNAELLGRYA PYLAGLAKLS
910 920 930 940 950 960
EVEIVAEIGA DELAPVAVAG ETRLMLKVEI DIAAERERLT KEIARLEGEV AKAEGKLGNA
970 980 990
SFVDRAPAAV VQQERDRLAG FKATLEQLRP QLAKLAGR