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 Q4FM20

Entry ID Method Resolution Chain Position Source
AF-Q4FM20-F1 Predicted AlphaFoldDB

No variants for Q4FM20

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q4FM20

No associated diseases with Q4FM20

5 regional properties for Q4FM20

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 41 - 52 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 14 - 565 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 607 - 751 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 811 - 870 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 564 - 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
MSNDKYIHTD VEDKIYSYWE KNNLFKPTKN KKQFSVVIPP PNVTGSLHMG HALNNSIQDL
70 80 90 100 110 120
LVRYHRMNNY ETLWQPGTDH AGIATQALVE KKLTADGIDK NEIGREKFIE KVWEWKEEHG
130 140 150 160 170 180
DIILNQLKKL GCSCDWSRNA FTMDENLSKS VLKVFVELHK KGLIYKDKKL VNWDTVLKTA
190 200 210 220 230 240
ISDLEVDQRE VNSKIYYIQY PIEASSDFIT IATTRPETML GDTAIAVNPK DDRFKHLVGK
250 260 270 280 290 300
FVTVPIVGKK IKIIEDEYAD PEMGTGALKI TPAHDFNDYE VGQRNNLEII NIFTEGGKVN
310 320 330 340 350 360
ENAPKEYIGL DRFEARKRII KELKEKEFFV KEENIKNKVP YGDRSNSIIE PFLTEQWFVD
370 380 390 400 410 420
AKKLSIKAKD IVNSKKTNFF PANWSKTYFQ WMNNIEPWCI SRQLWWGHQI PAWYGPDKKI
430 440 450 460 470 480
FVAINEEEAK LDAKKFYNKD VDLIRDPDVL DTWFSSGLWP FATLGWPDNK EYVDKFYPTS
490 500 510 520 530 540
VLVTGFDIIF FWVARMIMFG MEFLDKEPFK DVYVHALVKD EKGQKMSKSK GNVINPLDLI
550 560 570 580 590 600
EKYSADALRF TLLSMASPGT DVKLSEDRVK GYRNFLNKLW NANNFLITNN CDFSKIDEKP
610 620 630 640 650 660
ILSININKWI YAELIETKNK IEKNLKDYRF DEAAKNAYQF TWHSYCDWYL ELSKTILFSE
670 680 690 700 710 720
DEKAKDEVRQ VSAYVFKQIL ILLHPFIPFV TEEIWLNNKF DNTGKDFLML ANWPSGEFER
730 740 750 760 770 780
DTSINQVEKI ISIVSELRSF KNELSVSPGS FIDISIETVS KKEQSFFTEN EIILKKLGRI
790 800 810 820 830 840
KNLYNKDLDK PTATLMVSGD LFKVYFDEDV DLELIKKNLT TRQNKYQEEM NKISQRLANK
850 860 870
GFVDRAPKDI VDQEKTNYNN LKNDVERISI TIKGL