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 Q72UY6

Entry ID Method Resolution Chain Position Source
AF-Q72UY6-F1 Predicted AlphaFoldDB

No variants for Q72UY6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q72UY6

No associated diseases with Q72UY6

5 regional properties for Q72UY6

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 42 - 52 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 12 - 144 IPR002300-1
domain Aminoacyl-tRNA synthetase, class Ia 471 - 661 IPR002300-2
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 714 - 822 IPR013155
domain Leucyl-tRNA synthetase, editing domain 269 - 458 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
MQYPFQEVES FWQKFWEEHK SFQTNIRSSK PKFYCLDMFP YPSGAGLHVG HPEGYTATDI
70 80 90 100 110 120
LSRFKRMKGF EVLHPMGWDA FGLPAERYAM QTGIHPAITT KDNIDNFRRQ IQMIGLSYDW
130 140 150 160 170 180
SRELSTTDPD YYKFTQWIFI QLYQSWFNPE LKKAESINEL IRRFSNQGSN GLDYRQFNSE
190 200 210 220 230 240
EWKNFSPVEK EKILSDFRLV YQAEIPVNWC EALGTVLANE EVEEWVGKGY EVVRKPMRQY
250 260 270 280 290 300
MMRITAYADR LLEDLELVEW PPSTLEMQKN WIGKSEGLEI TFPFLKPLQS GLEGIRIFTT
310 320 330 340 350 360
RPDTIFGVTY MVVAPEHPIV SEITTPEQKQ KVEEYQKTSS LKSDLDRMEL NKEKTGVFTG
370 380 390 400 410 420
TFVFNPADPS QKIPVWISDY VLYGYGTGAI MAVPAHDQRD FEFARTFGLK IIPVIEGEIS
430 440 450 460 470 480
EAAFDSKTST CINSSSSEIS INGLDYTSAS SKIISWAESK KIGRKKIQFK LRDWLFARQR
490 500 510 520 530 540
YWGEPIPLVH YPSGVTKPIP ESELPLVLPN LEEFKPSGTG ESPLALAKDW LQYKDPSTGE
550 560 570 580 590 600
IGTRETNTMP QWAGSCWYYL RYIDPKNGRF LCDPELEKKW MPVNLYVGGS EHAVLHLLYS
610 620 630 640 650 660
RFWHKFLFDI GAVSTKEPFD KLIHQGLILG EDKRKMSKSL GNVVNPDDVI KEYGADSLRL
670 680 690 700 710 720
FEMFMGPLEM VKPWSTRGVE GVFRFLNRIW RLFHSGSQES FRLDDVEPTP EELKILHKTI
730 740 750 760 770 780
QKVNEDIPNF SFNTAIAQLM IFVNEFTPSD RRPKKVLESF ILLLAPFAPH IAEELWKRSG
790 800 810 820 830 840
KMESLSYEKF PEADPQYLVE SEILIVVQVN GKLRDEFKAP KDVSQSDAIS MAKNLDKIKG
850 860
ILEGKTIRKE IYVPGKLVNL VIG