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 Q5QY15

Entry ID Method Resolution Chain Position Source
AF-Q5QY15-F1 Predicted AlphaFoldDB

No variants for Q5QY15

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5QY15

No associated diseases with Q5QY15

5 regional properties for Q5QY15

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 40 - 51 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 14 - 630 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 673 - 821 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 884 - 946 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 629 - 763 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
MDKTYSPAAI EQDLYQQWED KGYFKPSGKG DPYSIMIPPP NVTGSLHMGH AFQHTIMDTL
70 80 90 100 110 120
TRYQRMDGLN TLWQVGSDHA GIATQMVVER QLAAQGQTRQ ELGRDAFIDK IWEWKEQSGG
130 140 150 160 170 180
TITQQMRRLG DSVDWDRERF TMDEGLSDAV REVFVKLHED NLIYRGKRLV NWDPALQTAI
190 200 210 220 230 240
SDLEVENKEQ QGYIWYLRYP LADGEKTEDG KDHLVVATTR PETMLGDVCV AVHPDDERFA
250 260 270 280 290 300
HLVGKFLELP IVNRRIPIVA DHHVDSEFGT GCVKVTPAHD FNDYEIGKRH QTGMISIFDD
310 320 330 340 350 360
TAHVMAKAGL YTSTGETLEE LNGFNGILPE QYAGKERFEA RKQLVAEFDE LGLLEKIEKH
370 380 390 400 410 420
TNKIPYGDRG GVPIEPHLTD QWYVRVEPMA KQATAAVEDG RIEFVPKQYE NMYFSWMRDI
430 440 450 460 470 480
QDWCISRQLW WGHRIPAWYD EQGNVYVGRT EEEVREKHNL GDTPLQQDED VLDTWFSSAL
490 500 510 520 530 540
WTFSTLGWPK NTEDLKTFHP TDVLVTGFDI IFFWVARMIM MTMHFMKDEE GQPQVPFKKV
550 560 570 580 590 600
YVTGLIRDEE GQKMSKSKGN VLDPLDMIDG ISADELVAKR TANLMQPKMR EKIEKRTRKE
610 620 630 640 650 660
FPEGITAHGT DALRFTLTAL ASTGRDINWD MKRLEGYRNF CNKLWNASRY VLMSTEEHDC
670 680 690 700 710 720
GLENDDMTLS LADEWIIARF NSTVKDFRQA LDTYRFDQAA AIAYEFTWNQ FCDWYLELTK
730 740 750 760 770 780
PVLQNGTESQ QRGTRHTLVN VLEQLLRLLH PVMPYITETI WQRVKPLVGN TDDTIMLQPF
790 800 810 820 830 840
PRVEDNVSHQ AMQDMEWLKR VILAIRNIRG EMDLSPNKPL PLLLSNADAM AKGRIQNNES
850 860 870 880 890 900
FLSSLAKLES IEFIESDDDA PASMTALVDT LKLHIPMAGL IDKEAELQRL QKSIEKANKE
910 920 930 940
WQRLNGKLSN DNFVSKAPEA VIAKEREKLS EAETTLKQLQ EQQDKIKAL