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 Q74JZ8

Entry ID Method Resolution Chain Position Source
AF-Q74JZ8-F1 Predicted AlphaFoldDB

No variants for Q74JZ8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q74JZ8

No associated diseases with Q74JZ8

5 regional properties for Q74JZ8

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 45 - 56 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 17 - 559 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 605 - 753 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 811 - 876 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 560 - 693 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
MADLAPKYNP NEVEKGRYQE WLDEDLFKPS GDKKAHPYSI VIPPPNVTGK LHLGHAWDTA
70 80 90 100 110 120
IQDTLIRFKR MQGYDTLYLP GMDHAGIATQ AKVEAKLRTQ GKDRHEMGRE AFVKQVWDWK
130 140 150 160 170 180
DEYASIIKSQ WAKMGLSLDY SRERFTLDKG LSKAVRKVFV QLYNEGLIYR GEYIINWDPK
190 200 210 220 230 240
LETALSDIEV IHKDDKGAFY HIKYPFADGS GFVEIATTRP ETMFGDTAVA VAPGDERYKD
250 260 270 280 290 300
IVGKELVLPL VGRHIPIIED QHVDPEFGTG LVKITPAHDP NDFQVGNRHN LERINVMNDN
310 320 330 340 350 360
GTMNEEAGKY AGMDRFEARE ALVKDLKEEG FLIKVEPIVH SVGHSERSGV QVEPRLSKQW
370 380 390 400 410 420
FVKMKPLAEK VLENQKTDDK VNFVPERFEH TLEQWMSDVH DWVISRQLWW GHRIPAWYNK
430 440 450 460 470 480
KTGETYVGLE APKDSENWEQ DPDVLDTWFS SALWPFSTLG WPDENSEDFK RYFPTNTLVT
490 500 510 520 530 540
GYDIIFFWVS RMIFQSLHFT GKRPFDDVVL HGLIRDPQGR KMSKSLGNGV DPMDVVDEYG
550 560 570 580 590 600
ADALRWFLLN GTAPGQDTRY DPKKMGAAWN FINKIWNASR FVIMNLPEDA KPAHMPDTSK
610 620 630 640 650 660
FDLADSWIFD RLNHTVSEVT RLFDEYQFGE AGRELYNFIW NDFCDWYIEI SKVALNGDDE
670 680 690 700 710 720
ELKTRKQENL IWILDQILRL LHPIMPFVTE KLWLSMPHDG KSIMVAKYPE THKEFENKEA
730 740 750 760 770 780
DSQMAFLIEV IKAVRNIRME VNAPMSSPID IMIQIDDDNN KAVLDNNAEY VENFLHPKAL
790 800 810 820 830 840
SVAADIEAPK LAKTAVIPGA QIFVPLTELV NVDEELAKME KEEKRLEAEV ERAEKKLSNQ
850 860 870
GFVAHAPEAV INKEKEKKAD YESQLAGVRE RMKELKESK