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 Q2JHX0

Entry ID Method Resolution Chain Position Source
AF-Q2JHX0-F1 Predicted AlphaFoldDB

No variants for Q2JHX0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2JHX0

No associated diseases with Q2JHX0

5 regional properties for Q2JHX0

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 43 - 54 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 14 - 173 IPR002300-1
domain Aminoacyl-tRNA synthetase, class Ia 633 - 672 IPR002300-2
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 726 - 840 IPR013155
domain Leucyl-tRNA synthetase, editing domain 223 - 408 IPR025709

Functions

Description
EC Number 6.1.1.4 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.
leucine-tRNA ligase activity Catalysis of the reaction: L-leucine + ATP + tRNA(Leu) = AMP + diphosphate + 2 H(+) + Leu-tRNA(Leu).

1 GO annotations of biological process

Name Definition
leucyl-tRNA aminoacylation The process of coupling leucine to leucyl-tRNA, catalyzed by leucyl-tRNA synthetase. The leucyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a leucine-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
MDARYNPQAI ESKWQAHWRE IGLDRTPELK DGSRKFYALS MFPYPSGNLH MGHVRNYTIT
70 80 90 100 110 120
DVIARHKRMQ GYAVLHPMGW DAFGLPAENA AIDRGIPPAK WTYQNIAQMR EQLQRLGLSY
130 140 150 160 170 180
DWEREITTCA PDYYKWTQWL FLQFFKAGLA YQKEAPVNWD PVDQTVLANE QVDAEGRSWR
190 200 210 220 230 240
SGALVEKRML KQWFFKITAY ADQLLADLEK LSGWPERVRT MQENWIGQSV GAKVIFKTEA
250 260 270 280 290 300
GDELAVFTTR PDTLWGATFM VMSPEHPLVD KLTTAEQLQA VRAYQAQAAA RSEIERSAED
310 320 330 340 350 360
REKTGVWTGS YAINPVNQER IPIWIADYVL MGYGTGAIMA VPAHDQRDFE FARKFGLPIK
370 380 390 400 410 420
RVVQPPEGSL SSTDRASGTE SSELQAAWTG EGVMINSGPL DGIPVGKGPG QSVERAIAWL
430 440 450 460 470 480
EAQGLGEKQI NYRLRDWLIS RQRYWGCPIP VIHCPHCGIV PVPEKDLPVL LPEDVELTGR
490 500 510 520 530 540
GGSPLAQLED WVKVKCPTCG AEARRETDTM DTFICSSWYF LRFSDARNDR EIFRKDRVNA
550 560 570 580 590 600
WLPVDQYVGG IEHAILHLLY SRFFTKVLRD RGLLDFDEPF LRLLTQGMVQ GRTYYNPNKS
610 620 630 640 650 660
GKDRWIPAAL VKDPDNPTDP ETGEPLEVIY ATMSKSKGNG VDPEEVLAHY GADTARMFIL
670 680 690 700 710 720
FKAPPEKDLE WDDADVEGQF RFLNRVWRQV YEFVVRGGGT ESWRGRVSEL LPAKVEVGSL
730 740 750 760 770 780
TKAEKDLRRA IHTAIKEVSE DLENDYQFNT AIAELMKLSN ALGEAGIPDS PVYAEGIRTL
790 800 810 820 830 840
VLLMAPFAPH IAEELWQALG GADSVHRQSW PSYDPAALVA DTVTIVIQVN GKLRGSFEAP
850 860 870 880
AEVTPEEQEQ LALRSEAAQK YLEGATPKKV VVVPKKLVNF VL