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 Q3BP98

Entry ID Method Resolution Chain Position Source
AF-Q3BP98-F1 Predicted AlphaFoldDB

No variants for Q3BP98

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q3BP98

No associated diseases with Q3BP98

5 regional properties for Q3BP98

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 43 - 54 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 17 - 663 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 704 - 856 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 916 - 980 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 662 - 794 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
MTTLASSYDP SSFESRLYAQ WEAAGYFVPS GKGEPYTVLL PPPNVTGTLH MGHAFQQTLM
70 80 90 100 110 120
DALVRYHRMR GYDTLWQVGT DHAGIATEMV VSRNLALEGK GQTRDSLGRE GFIAKVWEWK
130 140 150 160 170 180
AESGDTIERQ MRRLGTSSDW SRSTFTMDPQ PSAAVNEAFV RWYEQGLIYR GQRLVNWDPV
190 200 210 220 230 240
LKTAISDLEV ENVEEDGFLW SIRYPLADGV SYEHVEHDAD GNETLRETRD YLVVATTRPE
250 260 270 280 290 300
TMLGDTAVMV HPEDARYLTL HDARIVLPLT GRHVPVITDD YVDRAFGTGV VKVTPAHDFN
310 320 330 340 350 360
DYQVGERHNL PLVNLFTVDA KIIDPREQYP DDEYPVVDQG IDWRELNQVQ RRRTGQHFAY
370 380 390 400 410 420
SIPSAYVGLD RYEARKLVLA HLEDEGRLVE TKPHKLQVPR GDRTGQVIEP YLTDQWFVKM
430 440 450 460 470 480
DALAKRGLEL VESGQIKFVP PNWINTYRHW MENIQDWCIS RQLWWGHRIP AWFDEAGTCY
490 500 510 520 530 540
VGHDEAEVRA KHGLGADVAL HQDSDVLETW FSSQLWPFST LGWPDAQAMA ERGFARYLPS
550 560 570 580 590 600
SVLVTGFDII FFWVARMIMA TDSFTGQVPF RDVYITGLIR DAQGQKMSKS KGNVLDPLDI
610 620 630 640 650 660
IDGISIEDLV AKRTHGLMQP RMAEKIEKAT RKEFPDGIIV HGADALRFTI AALATHGRDI
670 680 690 700 710 720
KFDLGRAEGY KNFCNKLWNA TRFVLMNTEG ARFTGVPQPR TEAEKWILAR LDKATAETHA
730 740 750 760 770 780
HYANYRFDLL AQSLYEFAWN AFCDWFVELA KPALNNQDAD AAASTRHTLL YVLESLLRLL
790 800 810 820 830 840
HPLTPFVTEE LWQQVAPRLG ITTATISLQS FPQPGDVDTS SYATAEADVE WLKSMVSALR
850 860 870 880 890 900
RVRSELNVPP SKQVRLLLQA DTADDRPRVA RLASQLSFLL KLERIDWLDA GQDTPPSAAA
910 920 930 940 950 960
IVGELTLLVP LEGLVDMDAE RTRLDKEIKR VEGEIAKCNG KLGSATFVQN APAAVVEQER
970
ARLNDWTTQL TGLREQRAKI