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 Q4FQL0

Entry ID Method Resolution Chain Position Source
AF-Q4FQL0-F1 Predicted AlphaFoldDB

No variants for Q4FQL0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q4FQL0

No associated diseases with Q4FQL0

5 regional properties for Q4FQL0

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 65 - 76 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 38 - 656 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 704 - 856 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 920 - 982 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 655 - 797 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
MSNPNNIESS KTNLTTSIQA ALSQLENAYN PSEVEAGMYQ GWEDSGYFQP TFDKDESFSI
70 80 90 100 110 120
ALPPPNVTGS LHMGHGFNNA IMDALTRYHR MDGDNTLWQP GTDHAGIATQ MVVERRLEAE
130 140 150 160 170 180
GIKRRDMSRE DFIDKVWEWK EESGGNITRQ IRRLGSSVDW SRERFTMDDG LSNAVKEVFV
190 200 210 220 230 240
RLFDDGLIYR GKRLVNWDPK FQTALSDLEV ENVDEKGSLW HFRYHFTDTD ITTQDGKNYL
250 260 270 280 290 300
VVATTRPETS LGDTAVAVNP KDERYAHLIG KTITLPITGR IVPIVADDYV DIEFGTGCVK
310 320 330 340 350 360
ITPAHDFNDY ELGRRHELPL INILDAHAHI LPAMEVYPDL QTREPTLETT PADYAGLERF
370 380 390 400 410 420
AARKLLVEQA GEQGWLEKIE DYALKAPRAE RGGAIVEPWL TDQWYVAVKE LAQPAIAAVE
430 440 450 460 470 480
DGQIEFVPAQ YKNMYMAWMN GIQDWCISRQ LWWGHRIPAW YDEEGSIYVA RDEAEVRSKY
490 500 510 520 530 540
NLAADVKLRQ DDDVLDTWFS SGLWTFSTLD WADVNADPRV METFHPTSVL VTGFDIIFFW
550 560 570 580 590 600
VARMIMMTMH FVKNEDGTPQ IPFKTVYVHG LVRDGNGQKM SKSKGNVLDP IDIIDGIELE
610 620 630 640 650 660
ALVEKRTSNM MNPKDAAKIE KQTRKEFPEG IPAFGTDALR FTFTSLASTG RDINFDLKRV
670 680 690 700 710 720
EGYRNFCNKI WNASRFVLMN CVDKEGNAQA IDQTANADVW ELPEKWIMSR LNSTITNIHQ
730 740 750 760 770 780
HFDQYRLDMV SHDIYEFIWN EYCDWYVELA KASLNDDSVS DERKAQIRYV LLHVLETALR
790 800 810 820 830 840
FSHPIMPYLT EQIWQTIAPL LNRKETDSIV IAAYPQTDNS QISEQTEADM AWLQELIASV
850 860 870 880 890 900
RNIRGEMKLG NAVRLPVLLQ NISAAEDTRL SRIANQFKAL AKVESLTILK EGDEVPLSSS
910 920 930 940 950 960
SMVGQLRVLV PMKGLIDPTA ELARLGKSYD KLKGQSEGIA RKLGNEGFVS KAPVEVVDAE
970 980
KAKLAELEGQ LTAMTAQMEE LKNL