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 Q24SP5

Entry ID Method Resolution Chain Position Source
AF-Q24SP5-F1 Predicted AlphaFoldDB

No variants for Q24SP5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q24SP5

No associated diseases with Q24SP5

5 regional properties for Q24SP5

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 42 - 53 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 423 - 622 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 666 - 786 IPR013155
domain Methionyl/Leucyl tRNA synthetase 40 - 183 IPR015413
domain Leucyl-tRNA synthetase, editing domain 221 - 409 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
MQEKYLFSEI EPKWQKKWVD RKDYQAEEHS DKPKFYALAM FPYPSGNLHM GHVRNYSIVD
70 80 90 100 110 120
VIARFKRMRG YNVLHPIGWD SFGLPAENAA IKNQTPPAEW TWKNIANMKR QLQEMGISYD
130 140 150 160 170 180
WEREVTTCHP DYYKFTQWIF LEFYKHGLVY KKKAGVNWCP SCATVLANEQ VVDGACERCD
190 200 210 220 230 240
TAVTKKDLEQ WFFKITDYAQ VLLDDLEKLP GWPDKVKTMQ KNWIGRSEGA EVEFDLENHG
250 260 270 280 290 300
DKIRVYTTRV DTIFGVSYVV LAPEHPLVQK LIAGTEYEND VQAFIERMKG LNEIARTSTE
310 320 330 340 350 360
TEKEGLFTGA YCINPYSGEK VPIWIANYVL FEYGTGAVMG VPAHDERDFE FAGKYKLPIK
370 380 390 400 410 420
TVILPEGTPV EEKDTPLQAA FVEEGMMVNS GEYDGLKNVE AWEKMCDKAE HDGFGERKVN
430 440 450 460 470 480
FRLRDWLISR QRYWGAPIPM IYCDHCGIVP VPQDQLPVML PDDVVFKAGE NPLTTSESFK
490 500 510 520 530 540
QTICPTCGGK ARRETDTMDT FMCSSWYFLR YTDPHNAQLP FAKEAADHWM NVDQYVGGVE
550 560 570 580 590 600
HAILHLLYSR FFTKALRDFG YLKVDEPFAN LLTQGMVCLG GAKMSKSKGN VVSPEEIISK
610 620 630 640 650 660
YGADTARLFI LFAAPPERDL EWNDQGVEGC YRFLNRVWRL AAQYEEVLKT TGAGANEFGE
670 680 690 700 710 720
LDKAAKDMRR QTHQTIQRVT SDVGARFNFN TAVSAIMELV NALYLYKEQP QVNLAVAREA
730 740 750 760 770 780
LESILILLAP FAPHITEEIW SELGHEDSIH SREWPQVDEE ALVQEEVTVV LQINGKVKER
790 800 810 820
IQVPAQISAA ELEAQVRQLP RLGEWTQGKQ ILKIVTVPGK LVNVVVK