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 Q9ZK61

Entry ID Method Resolution Chain Position Source
AF-Q9ZK61-F1 Predicted AlphaFoldDB

No variants for Q9ZK61

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9ZK61

No associated diseases with Q9ZK61

5 regional properties for Q9ZK61

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 49 - 60 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 17 - 571 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 614 - 740 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 807 - 869 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 570 - 695 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
MKQEPTTYQP EEIEKKIYEI CSHRGYFEIN GNEKIQEKGK RFCLMMPPPN VTGILHIGHA
70 80 90 100 110 120
LTLSLQDILV RYKRMDGYKT LYQPGLDHAG IATQNVVEKQ LLSQGVKKED LGREKFIQKV
130 140 150 160 170 180
WEWKEKSGGA ILEQMKRLGV STAFSRTRFT MDKGLQRAVK LAFLKWYEKG LIVQDNYMVN
190 200 210 220 230 240
WCTKDGALSD IEVEYEERKG ALYYIRYYLE NQKDYLVVAT TRPETLFGDS AIMVNPNDER
250 260 270 280 290 300
YKHLVGQQVI LPLINRTIPI IADAHVEMGF GTGCVKVTPG HDFNDYEVGK RHHLETIKIF
310 320 330 340 350 360
DEKGILNAHC GEFENLERLE ARDKVVAALK ENALLEKIEE HVHQVGHCYR CHNVVEPYVS
370 380 390 400 410 420
KQWFVKPEIA QSSIEKIQQG LARFYPSNWI NNYNAWMREL RPWCISRQLF WGHQIPVFTC
430 440 450 460 470 480
ENNHQFVSLD TPLSCPTCKS EKLEQDKDVL DTWFSSGLWA FSTLGWGQEK SDLFNESDLK
490 500 510 520 530 540
DFYPNTTLIT GFDILFFWVA RMLFCSESLL GELPFKDIYL HALVRDEKGE KMSKSKGNVI
550 560 570 580 590 600
DPLEMIEKYG ADSLRFTLAN LCATGRDIKL STTHLENNKN FANKLFNAAS YLKLKQESFK
610 620 630 640 650 660
DKERLNEYQT ALGRYAKSRL NLVTKEVRNA LDNYRFNDAT TLLYRFLWGE FCDWFIEFSK
670 680 690 700 710 720
VENEAIDELG SVLKEALKLL HPFMPFISES LYHKLSNTEL ENAHSIMVMP YPKEIAQDEK
730 740 750 760 770 780
LEHEFEVIKD CIVSLRRLKI MLETPPIVLK EASVGLREKI ENTERLQNYA QKLAKLEKVS
790 800 810 820 830 840
VITYKPLKSV SDVGEFCQTY ADLENLDLSP LIARLKKQLE KLEKEKLKLN LHNENFVKNA
850 860 870
PKSVLEKARE SLKTLLEKEG KIQQELDLLE QP