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 Q2SBE7

Entry ID Method Resolution Chain Position Source
AF-Q2SBE7-F1 Predicted AlphaFoldDB

No variants for Q2SBE7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2SBE7

No associated diseases with Q2SBE7

6 regional properties for Q2SBE7

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 42 - 53 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 15 - 171 IPR002300-1
domain Aminoacyl-tRNA synthetase, class Ia 417 - 590 IPR002300-2
domain Aminoacyl-tRNA synthetase, class Ia 619 - 659 IPR002300-3
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 700 - 823 IPR013155
domain Leucyl-tRNA synthetase, editing domain 221 - 403 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
MEELYHPKKV EQEAQKFWEE TDAFKVDEEP GKEKFYCLSM FPYPSGKLHM GHVRNYTIGD
70 80 90 100 110 120
VISRYQRMQG KNVLQPMGWD AFGLPAENAA LKNNVAPAKW TYENIAYMKN QLKLLGFGYD
130 140 150 160 170 180
WNRELATCRP EYYKWEQWFF TRLYEKGLVY KKMSTVNWDP VDETVLANEQ VIDGKGWRSG
190 200 210 220 230 240
AVVERREIPQ WFIKITDYAE QLLNDLDKLE NWPEQVKTMQ RNWINKSEGV EFHFKLKDHD
250 260 270 280 290 300
GDLQVYTTRP DTIMGVTYVA IAPQHPLALE AAASNPQLAK FLDECKNTKV AEADMATMEK
310 320 330 340 350 360
RGMDTGFFVI HPLTNEPAPI WVANFVLMDY GSGAVMSVPG HDERDHEFAL KYGLPIKQVI
370 380 390 400 410 420
SVIDADEVDI QEKAITEKGI LVNSGEFTGM TSQEAFDAVA EKLTAMGIGE KKINYRLRDW
430 440 450 460 470 480
GVSRQRYWGA PIPMMTQEDG TEVPVPLADL PVRLPEDVEM DGVKSPIKAD PNWSKRSYNG
490 500 510 520 530 540
QPATQETDTF DTFMESSWYY ARFCCPNLES AMLDPAAANY WLPVDYYVGG IEHAILHLLY
550 560 570 580 590 600
SRFFHKLLRD EGLVDSDEPF KKLLCQGMVI AETFYREDPS SKKTYFNPRD VRVELDTQGN
610 620 630 640 650 660
SPKAFLIEDG QPVIIGPKEK MSKSKNNGVD PQELIDKYGA DTVRLFTMFA APPEQSLEWS
670 680 690 700 710 720
ESGVEGQHRF LRRLWKLVHT HVEKKGAAPL NVAELNETQR TLRRKTHETI KKMTDEFNHR
730 740 750 760 770 780
MAINTGIAMV MELLNELSRF EDDSPQGLAV VQEALETAVL VLAPIVPHIS HGLWRELGHE
790 800 810 820 830 840
DVVMNAPWPQ LDEKALEKDS IELVVQVNGK LRARIQAAAS ANKDELEKLA FDDENVQRFM
850 860
EDKTVVKVIV VPGKLVNIVV K