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 Q493Z9

Entry ID Method Resolution Chain Position Source
AF-Q493Z9-F1 Predicted AlphaFoldDB

No variants for Q493Z9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q493Z9

No associated diseases with Q493Z9

4 regional properties for Q493Z9

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 47 - 58 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 19 - 635 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 680 - 831 IPR013155
domain Valyl tRNA synthetase, anticodon-binding domain 634 - 769 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
MSNYIVEKIY NPKNIEEPIY KFWEYGDYFS PHGNTSQESY CIMMPPPNIT GQLHLGHAFQ
70 80 90 100 110 120
QTIMDVLIRY QRMQGKNTLW QTGTDHAGIA TQMLVEHKIY NNTGKTRHDY TRDELIKNIW
130 140 150 160 170 180
AWKSQSEQFI TYQMKRLGNS VDWKRQRFTM DTEMSYAVTE AFIRLYRKNL IYRGKRLVNW
190 200 210 220 230 240
DCKLQTAISD LEVINKKTKG SIWYIYYKLD NATISSNSHH LIVATTRPET MLGDTAVAVH
250 260 270 280 290 300
PEDTRYKNYI GQYVIAPITN RRIPIISDKN VDMFKGTGCL KITPAHDFND YIIGKRHGLP
310 320 330 340 350 360
MINIFSLNGK ILKKLEVFNS SGQLTDQLYC KIPQIFHNLD SDNARKKIIS ECNALKLLHN
370 380 390 400 410 420
IEPHDLTIPY SDRTGTIIEP MLTDQWYIRV KHLTQHAIDA VNLNIINFVP KQYKNMYFSW
430 440 450 460 470 480
MNNLQDWCIS RQIWWGHKIP AWYDDNNTIY VGYCEKDIRI KNKLNNNVIL HREKDVLDTW
490 500 510 520 530 540
FSSSLWTFAA LGWPKNTNLL NVFHPTNIII SGFDIIFFWI ARMIMLTMHF IKNDNGSAQI
550 560 570 580 590 600
PFKTVYITGL IRDELGQKMS KSKGNIIDPI DIIDGISIEN LLKKRTKNML QPQLSKHIIN
610 620 630 640 650 660
NTIKQFPNGI KPHGTDALRF TLVALASSGR DIHWDMQRLT GYRNFCNKLW HASRFVLMHT
670 680 690 700 710 720
KNQDCGISIN INEKSFSLAD RWIITKFHQT VQIFHKKLEI YRFDEIANIL HEFIWHQFCD
730 740 750 760 770 780
WYLELTKPIL YHGNALELRG TRYTLITLLE SLLRLTHPII PFITEKIWQE VKTVTGNNGT
790 800 810 820 830 840
TIMLQPFPKY DESVIDMKSV IDIEWIKNAV LAIRTARVNM NISYNIPLQI VFRDTSSEVK
850 860 870 880 890 900
KRITENSKIL CHIAQLKSIH FISKGTIYPK SMTMPLDSSE LLIRIPDTFN KENEINRLKK
910 920 930 940 950
ESELINRKIE TIQKLLDDNN FINQAPKSVI KDKQALLNYY ELIQNKLIDQ CAIMKKL