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 Q8DSL1

Entry ID Method Resolution Chain Position Source
AF-Q8DSL1-F1 Predicted AlphaFoldDB

No variants for Q8DSL1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8DSL1

No associated diseases with Q8DSL1

6 regional properties for Q8DSL1

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 46 - 57 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 18 - 429 IPR002300-1
domain Aminoacyl-tRNA synthetase, class Ia 435 - 560 IPR002300-2
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 610 - 754 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 814 - 878 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 559 - 698 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
MSTQLSPKYN PAEVEADRYQ KWLDADVFKP SGDQKAKPYS IVIPPPNVTG KLHLGHAWDT
70 80 90 100 110 120
TLPDIIIRQK RMQGFDTLWL PGMDHAGIAT QAKVEARLAE DGISRYDLGR EKFLDKVWEW
130 140 150 160 170 180
KDEYAATIKE QWGKMGISVD YSRERFTLDE GLSKAVRKVF VELYKKGWIY RGEFIINWDP
190 200 210 220 230 240
KARTALSDIE VIHKDVEGAF YHMNYMLEDG SRALEVATTR PETMFGDTAV AVNPNDDRYK
250 260 270 280 290 300
DLIGQNVILP IVNKLIPIVA DEHADPEFGT GVVKITPAHD PNDFLVGQRH NLPQVNVMND
310 320 330 340 350 360
DGTMNELAGE FAGMDRFEAR KATVKKLEEI GALVEIEKMT HSVGHSERTG VPIEPRLSTQ
370 380 390 400 410 420
WFVKMDQLAK NAIANQDTDD KVDFYPPRFN DTFLQWMENV HDWVISRQLW WGHQIPAWYN
430 440 450 460 470 480
ADGDMYVGEE APEGDGWKQD EDVLDTWFSS ALWPFSTMGW PDTDSEDFKR YFPTSTLVTG
490 500 510 520 530 540
YDIIFFWVSR MIFQSLEFTG CRPFQNVLIH GLIRDEQGRK MSKSLGNGID PMDVVDKYGA
550 560 570 580 590 600
DALRWFLSNG SAPGQDVRFS YEKMDAAWNF INKIWNISRY ILMNNEGLSL DQASKNVVLV
610 620 630 640 650 660
TNGKAGNVTD RWILHNLNET IAKVTENFDK FEFGVAGHIL YNFIWDEFAD WYVELTKEVL
670 680 690 700 710 720
YSEDEAEKVI TRSVLLYTLD KILRLLHPIM PFVTEEIFGQ YADGSIVTAA YPTVNPAFEN
730 740 750 760 770 780
QTAHSGVESL KDLIRAVRNA RAEVNVAPSK PITILVKTSD SNLEDFFKAN VNYIKRFTNP
790 800 810 820 830 840
ETLEISSAIA TPELAMSAVI TGAEIFLPLA DLLNVEEELA RLNKELAKWQ KELDIVAKKL
850 860 870 880
SNDRFVQNAK PEIVQKERDK QIDYQTKYDA TVERIKEMEK LIK