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 Q6F1B1

Entry ID Method Resolution Chain Position Source
AF-Q6F1B1-F1 Predicted AlphaFoldDB

No variants for Q6F1B1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6F1B1

No associated diseases with Q6F1B1

5 regional properties for Q6F1B1

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 46 - 57 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 18 - 564 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 612 - 746 IPR013155
domain Valyl-tRNA synthetase, tRNA-binding arm 822 - 873 IPR019499
domain Valyl tRNA synthetase, anticodon-binding domain 564 - 701 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
MKKELEAKYS YEIVEENRYE WWIQNEYFKA NPDSKKPKFS IVLPPPNVTG KLHIGHAWDG
70 80 90 100 110 120
SLQDAIIRFK KLNGFDVLYL PGMDHAGIST QVKVEAKLRE QGISRFELGR EKFLEQAWKW
130 140 150 160 170 180
KHEYAAIIRQ QWSKLGLAFD YSMEKFTLDD DINKIVTEIF VDFYNKGLIY KGKRIVNWDP
190 200 210 220 230 240
MQKTAISNVE VIYKEVEGFM YHFKYMIQGT NEFLNVATTR PETMFADQCL VVNPKDERYT
250 260 270 280 290 300
SFIGKKAINP VNNQAIPIIA DDYVELDFGT GVMKCTPAHD LNDFEIAVRH NLEKPICMNE
310 320 330 340 350 360
DGTINEMGGE EYQGLDRFEA RNKIIENLTK EKTFIKAEPM IHQVGFSERS NAIVEPYLSD
370 380 390 400 410 420
QWFVKMDSFA DMILKLQESN DKIKFFPERF DQVLKKWMEN IHDWTISRQL WWGHRIPAWY
430 440 450 460 470 480
NKEDKTKIYV GMEAPKDAEN WIQDEDVLDT WFSSGLWPFA TLMRGEGFES KYFKEYLPNG
490 500 510 520 530 540
VLVTGHDIIF SWVSRMIFQT IEYTGQIPFK DVLIHGLVRD EHGAKMSKSL GNGIDPMDVI
550 560 570 580 590 600
VNNGSDSLRF SLLTNSTPGQ DIRYSDSKVK AAWNFINKLW NASRYVLMNL EEDFKPWEEQ
610 620 630 640 650 660
AILNSNSLNE TDKWVLTEFS KVSKQVNYLI DKYEFAIAGK MLYDFVWNTY CSWYIEFAKV
670 680 690 700 710 720
NLNNPKTKEA TQQTIVYLLK NILIMLHPYL PFVTEHIYKT LDMKNSILEE SWFDKEFVFE
730 740 750 760 770 780
TDYINVVIEL INSIREFRAT NNIKNNVLLN WNATNGNLEI ITKYNLEINN FLNEFVNANL
790 800 810 820 830 840
SINESLVSET TSLSVLDFFI EIPNDDFIDK EKMLEELATK KKELENEISR SERMLSNENF
850 860 870
ISKAAPSKIE EEKEKYELYK QQLELIQDKL NKM