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 Q89AG3

Entry ID Method Resolution Chain Position Source
AF-Q89AG3-F1 Predicted AlphaFoldDB

No variants for Q89AG3

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q89AG3

No associated diseases with Q89AG3

5 regional properties for Q89AG3

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 43 - 54 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 15 - 632 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 677 - 824 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 891 - 952 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 632 - 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
MIKKYFDPLR MEKSLYEFWE KNGYFKPQNN KGKPNFCIVM PPPNITGNLH IGHAFQQTIM
70 80 90 100 110 120
DILIRYNRMI GKNTFWQVGT DHAGIATQIV VEKKILKEEN KTVQQLGKKE FLERIWKWKN
130 140 150 160 170 180
TSKNVITSQM RRLGISVDWT HEKFTLDPQI SFAVRKVFMT LYDECLIYKR KKLVNWDPVL
190 200 210 220 230 240
KTVISDLEVK NRNVIGNMWY IKYYLVKNHS IKISQEYYLV IATTRPETLF GDTAIAVHPN
250 260 270 280 290 300
DSRYKKYIGC YALVPIINRI IPIISDEFVD VNKGTGCVKI TPAHDFNDYE IAMRHNLSII
310 320 330 340 350 360
NVFTRNGKIT DVIEEYDISG EKSCIYKQNV PLRFHHLDRF IARKIIVKEL IALKLLIKIQ
370 380 390 400 410 420
KHNLAIPYGE RSGSVIEPLL TDQWYLRVEP LAKIAVEAVK SGKIIFIPKK YEKIYYSWMN
430 440 450 460 470 480
NIKDWCISRQ LLWGHRMPIW YDKKNNIYVG LDEKHIREKY HISDDIFLIQ ETDVLDTWFS
490 500 510 520 530 540
SSLWMFSSLG WPNNKDLFKN FYSTDVVVSG FDIIFFWIAR MIMLSMHLIK DHNGNGRVPF
550 560 570 580 590 600
KKVYITGLIC DEHGKKMSKS KGNVVDPLDM IDGISLDALI QKRIKSTVFS THSKKIITQI
610 620 630 640 650 660
QSLYPNGINS SGVDALRFTC AALSTPTRYI KWNINRLYGY RNFCNKLWNA SRFILMNLTH
670 680 690 700 710 720
EVEPVKLILI KPMSLSDRWI VAEFHNLVKR YRTALDNYRF DIAANVLYEF VWNKFCDFYI
730 740 750 760 770 780
ELVKSFINSC SMLELKSTRC TLVYILDSVL RLAHPIIPFI TEEIWQKLQV FVKKNDKNTI
790 800 810 820 830 840
MLQSFPKYDV KLVNKTILED MDWIKNIFII IRSFRMDLKI SHTTLISISF KNVSSKIHKL
850 860 870 880 890 900
IEEHKDYIKK IAYLDNVSII LSNVDSMLFF KSYIVLGAEL LIPYSKIFPK EKELKNLNKE
910 920 930 940 950
ISKIQLAINK LQQRLSNEEF IGKAPIHVVK KYKNQLQIYI EHKTQLCHKK LTMLRD