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 Q5X728

Entry ID Method Resolution Chain Position Source
AF-Q5X728-F1 Predicted AlphaFoldDB

No variants for Q5X728

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5X728

No associated diseases with Q5X728

5 regional properties for Q5X728

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 40 - 51 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 14 - 599 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 642 - 793 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 856 - 914 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 598 - 734 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
MDKTYSPEAI EKALYKKWES HHYFQPRGEG KRFCIMLPPP NVTGSLHMGH GFQHTIMDAL
70 80 90 100 110 120
TRYHRMLGDK TLWQPGTDHA GISTQLVVER QLEAQGVSRK DLTREQFLDK VWQWKEESGN
130 140 150 160 170 180
TITQQMRRLG ASVDWSRERF TMDEGLSAAV QKVFVQLYEE GLIYRGTRLV NWDPKLGTAV
190 200 210 220 230 240
SDLEVLSEEE DGFLWHIRYP VVDSEEFLIV ATTRPETLLG DCAVAIHPDD SRFRHLIGKQ
250 260 270 280 290 300
VHLPLCDRTI PVIADDYVDK EFGSGCVKIT PAHDFNDHEV GKRHQLPQIN ILTKKGTINK
310 320 330 340 350 360
NAPLKYQGMD RFVAREQIIK DLEKEGLLAK TEPHKLKVPR GEKSNVIIEP LLTDQWYVKT
370 380 390 400 410 420
KPLAEPAIAA VKKGDIRFIP ETWDKTYFQW MDNIEDWCIS RQLWWGHRIP AWYDNHGNIY
430 440 450 460 470 480
VGYSENDVRF KHKIDQSTPL KQDEDVLDTW FSSALWPFST LGWPERTPEL EQFYPTSVLV
490 500 510 520 530 540
TGFDIIFFWV ARMIMMGLKF TGKIPFKEVF ITGLIRDSEG HKMSKSKGNV LDPLDIVDGI
550 560 570 580 590 600
DLDSLIAKRT SNLMLNSVRD RITKATRKEF PEGISAYGTD ALRFTYCSLA STGRNVRFDL
610 620 630 640 650 660
GRVEGYRNFC NKLWNAARYV LLNTDEEQID FGDGAFQYSP ADQWILSRLQ NTVSKVHHYF
670 680 690 700 710 720
ETYRFDLLAN TLYEFVWHEY CDWYLELSKP ILQDDQALSA MKRGTRRTLI HVLDQILKLL
730 740 750 760 770 780
HPLMPFITEE IWQKTTKFTS ENGISIMLST YPKVNEEFIN PAIEEELDWL KSAIQSLRTI
790 800 810 820 830 840
RSEMSISPAK LIPLYIRNIT PELKERIAKY EKILKTLSKI DKINYLAPDE KVPVSATAVL
850 860 870 880 890 900
GEIELLIPMA DLIDKEAELS RLNKELAKLN KDIELAQGKL NNPKFTDKAP EEIIAKEKDK
910 920
LAQAQVAKDK LLQHKNRIES L