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 Q5E7U0

Entry ID Method Resolution Chain Position Source
AF-Q5E7U0-F1 Predicted AlphaFoldDB

No variants for Q5E7U0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5E7U0

No associated diseases with Q5E7U0

5 regional properties for Q5E7U0

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 42 - 53 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 14 - 631 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 679 - 832 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 892 - 950 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 630 - 768 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
MEKTYNPQSI EQTLYQTWEE KGYFKPHGDT SKEAYSIMIP PPNVTGSLHM GHAFQDTIMD
70 80 90 100 110 120
TLIRAERMKG KNTLWQVGTD HAGIATQMVV ERKIAAEEGK TKHDYGRDAF IDKIWEWKNE
130 140 150 160 170 180
SGGTITKQLR RLGASVDWDR ERFTMDDGLS AATQEVFVRL YEEDLIYRGK RLVNWDPKLH
190 200 210 220 230 240
TAISDLEVEN KDKKGFMWHF RYPLANGVKT ADGKDYIVVA TTRPETMLGD TGVAVNPEDP
250 260 270 280 290 300
RYKDLIGKEI LLPIVNRLIP IVGDEHADME KGTGCVKITP AHDFNDYEVG KRNQLPMINI
310 320 330 340 350 360
LTFNADIRES AEVFTTNGEV SDVYSTEIPA KYQGMERFEA RKTIVAEFEE LGLLEEIKDH
370 380 390 400 410 420
DLTVPYGDRG GVVIEPMLTD QWYVRTAPLA EPAVKAVEDG QIQFVPKQYE NMYFAWMRDV
430 440 450 460 470 480
QDWCISRQLW WGHRIPAWYD NDGKVYVGRT EEEVREKNNL APVVVLRQDD DVLDTWFSSA
490 500 510 520 530 540
LWTFGTQGWP ENTDALKTFH PSEVLVSGFD IIFFWVARMI MMTMHFVKDE EGNAQVPFKT
550 560 570 580 590 600
VYMTGLIRDE NGDKMSKSKG NVLDPIDMID GIDLESLVEK RCGNMMQPQL AKKIEKNTRK
610 620 630 640 650 660
TFENGIEPYG TDALRFTLAA MASTGRDINW DMKRLEGYRN FCNKLWNASR YVLMNTEEHD
670 680 690 700 710 720
CGMSLSAEER ANMEFSLADK WIESQFELAA KEFNAHLDNY RLDMAANTLY EFIWNQFCDW
730 740 750 760 770 780
YLELTKPVLW KGTEAQQQAT RYMLITVLEK TLRLAHPVLP YITESIWQSV KPLVDGVEGD
790 800 810 820 830 840
TIMTQALPQF NEENFNADVV ADLEWVKAFI TSIRNLRAEY DIAPSKGLEV MIKVADEKDA
850 860 870 880 890 900
ARIEANKVVL SSLAKLDEIK VLANGEETPA CATSLVGKSE LMIPMAGLID KDAELARLAG
910 920 930 940 950
EVKKTQGEIK RIEGKLGNEG FVAKAPEAVI AKEREKLEGY QETLVKLEAQ QETIAAL