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 Q04FL2

Entry ID Method Resolution Chain Position Source
AF-Q04FL2-F1 Predicted AlphaFoldDB

No variants for Q04FL2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q04FL2

No associated diseases with Q04FL2

5 regional properties for Q04FL2

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 43 - 53 IPR001412
domain Aminoacyl-tRNA synthetase, class Ia 417 - 608 IPR002300
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 661 - 767 IPR013155
domain Methionyl/Leucyl tRNA synthetase 35 - 158 IPR015413
domain Leucyl-tRNA synthetase, editing domain 223 - 404 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
MSYDHKAIEK RWQTYWDEHK TFKTAPETSG KPKYYVMNMF PYPSGQGLHV GHPESYTATD
70 80 90 100 110 120
IMARFNRMRG FNVLQPMGWD AFGLPAEQYA IKTGHNPADF TNENIKHFKK QVKSLGFSYD
130 140 150 160 170 180
WDREINTTDP EYYKWTQWIF EQLYKKGLAY EDEIMVNWAP DFPGGGIVVA NEEVIDGKTE
190 200 210 220 230 240
RGSYPVYRVP MKQWVLRITK YAERLLSDLD DLDWPEAIKE QQRNWIGKST GAAVFFKVDG
250 260 270 280 290 300
KSDYQVEVYT TRPDTLFGAS YMVLAPEHDL VDKITTSECR ADVDAYKAKI ASKSDLERTD
310 320 330 340 350 360
LNREKTGAFT GAYGINPVNG EKIPIWIADY VLSSYGTGAI MAVPAHDTRD YEFAKKFDLP
370 380 390 400 410 420
IRQVIKGGDI SKEAFTGDGT HINSAFLDVL DKKQAIEKII DWLEEHDAGH KQVNYKLRDW
430 440 450 460 470 480
IFSRQRYWGE PIPVIHWEDG KQTLVPESEL PLRLPHLNQD QMKPSGTGES PLANAKSWLE
490 500 510 520 530 540
VTRQDGVKGR RETNTMPQWA GSSWYFLRYI DPHNDKVLAD PEKLKYWMNV DLYVGGAEHA
550 560 570 580 590 600
VLHLLYARFW HKFLYDLGIV PTKEPFQKLV NQGMILGTNH EKMSKSKGNV VNPDEIVDSY
610 620 630 640 650 660
GADALRVYEM FMGPLTQSKP WSTESLAGIR RYLDRVWRIF TSDGDGINPI IVSENDHKLD
670 680 690 700 710 720
KIFNQTVKKV TEDYAAMRFN TAISQMMVFI NETFKAEKLP KKYMNAFLQL LNPVAPHITE
730 740 750 760 770 780
ELWQRMGHQE TIAYATWPTY DESQIIEKQI EMAVQINGKV RAKINTPVDI SRDELAKMAT
790 800
DNPDVKKQVA DKNIVKIIAI PGKIINIVVK