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 Q4L703

Entry ID Method Resolution Chain Position Source
AF-Q4L703-F1 Predicted AlphaFoldDB

No variants for Q4L703

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q4L703

No associated diseases with Q4L703

5 regional properties for Q4L703

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 44 - 55 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 16 - 559 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 604 - 751 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 810 - 875 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 559 - 695 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
MNMEPKYNPR EVEAGRYEEW VKNDYFKPSE DKSKETYTIV IPPPNVTGKL HLGHAWDTTL
70 80 90 100 110 120
QDIITRMKRM QGYDTLYLPG MDHAGIATQA KVDAKLKEQG ISRHDIGREK FLEHAWSWKE
130 140 150 160 170 180
EYASFIRQQW AKLGLGLDYS RERFTLDDGL SKAVRKVFVD LYNKGIIYRG ERIINWDPEA
190 200 210 220 230 240
RTALSDIEVI HEDVQGHFYH FKYPYADGDG YIEIATTRPE TMLGDTAIVV NPNDDRYKDV
250 260 270 280 290 300
IGKKVILPIV GRELPILADE YVDIDFGSGA MKVTPAHDPN DFEIGQRHSL ENIIVMDENG
310 320 330 340 350 360
KMNDKADKYA GLDRFECRKQ LVEDLKAQDL VIKIEEHVHS VGHSERSGAV VEPYLSTQWF
370 380 390 400 410 420
VKMKPLAQRS LDNQKTDDRI DFYPPRFENT FNRWMEEIRD WTISRQLWWG HQIPAWYHKE
430 440 450 460 470 480
TGEIYVGEEA PKDIDNWVQD EDVLDTWFSS ALWPFSTLGW PNIDADDFKR YYPTNALVTG
490 500 510 520 530 540
YDIIFFWVAR MIFQGLEFTD RRPFNDVLLH GLVRAEDGRK MSKSLGNGVD PMDVIEEYGA
550 560 570 580 590 600
DSLRYFLATG SSPGHDLRYS TEKVESVWNF INKIWNGARF SLMNIGDEFK FEDIDLTGNL
610 620 630 640 650 660
SLADKWILTR LNETIETVTN LSEKYEFGEV GRALYNFIWD EFCDWYIEMS KIPMNGEDEA
670 680 690 700 710 720
QKQTTRSVLS YTLDQIMRML HPFMPFVTEK IWQSLPHEGE TIVKASWPTV REELVFEESK
730 740 750 760 770 780
QTMQQLVEII KSVRQSRVEV NTPLSKAIPI YIQAKDENIK ATLIENEDYI HKFCNPSDLT
790 800 810 820 830 840
IDTHIDIPEK AMTAVVIAGK VVLPLEGLID MDKEIARLEK ELDKLQKELD RVDKKLSNEN
850 860 870
FVNKAPEKVI NEEKEKQQRY QEKYDGVKNR IEQLKA