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 Q254X5

Entry ID Method Resolution Chain Position Source
AF-Q254X5-F1 Predicted AlphaFoldDB

No variants for Q254X5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q254X5

No associated diseases with Q254X5

4 regional properties for Q254X5

Type Name Position InterPro Accession
conserved_site Aminoacyl-tRNA synthetase, class I, conserved site 42 - 52 IPR001412
domain Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding 676 - 784 IPR013155
domain Methionyl/Leucyl tRNA synthetase 38 - 171 IPR015413
domain Leucyl-tRNA synthetase, editing domain 219 - 361 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
MRYDPSLIEK KWQEFWKEHK SFKANEADDK PKYYVLDMFP YPSGAGLHVG HLIGYTATDI
70 80 90 100 110 120
VARYKRAKGF SVLHPMGWDS FGLPAEQYAV RTGTHPRETT QKNIENFRKQ LSAMGFSYDE
130 140 150 160 170 180
GREFATSDPE YYRWTQKLFL LLYEKGLAYM ADMAVNYCPE LGTVLSNEEV ENGLSIEGGY
190 200 210 220 230 240
PVERRMLRQW ILRITAYSDQ LLEGLEGLDW PENVKQLQRN WIGKSEGALV RFKVNNQNFL
250 260 270 280 290 300
EVFTTRPDTL CGVSFLVIAP EHPEVGQLIA EDRREEVEAY ICRAQSKSER DRISESKIKS
310 320 330 340 350 360
GVFTGTYAKH PITGADIPIW VSDYVILGYG SGVVMGVPAH DERDREFAET FSLPIYEVLD
370 380 390 400 410 420
TDGYCIHSNH GDFLLDGLWG REAQDYVIAY LQKKNLGESK VAYKLRDWLF SRQRYWGEPI
430 440 450 460 470 480
PIIHFEDGTC RPLEDDELPL LPPEIQDYRP EGFGQGPLAK VKEWVDIHDK KTNRQGRRET
490 500 510 520 530 540
HTMPQWAGSC WYYLRFCDAL NSQAPWSNEK EKYWMPVDLY IGGAEHAVLH LLYSRFWHRV
550 560 570 580 590 600
FYDAGMVSTP EPFKKLINQG LVLATSYRIP GKGYVYPEDA HEDNGVWMST SGEELEVRQE
610 620 630 640 650 660
KMSKSKLNGV DPQILIEEFG ADALRMYAMF SGPLDKNKLW CNQGVSGCRR FLNRFYELVT
670 680 690 700 710 720
SSLVQDIDDP KGMYLAHRLV HRVGEDIEKM SLNTIPSSFM EFINEFVKLD IYPKSALAMV
730 740 750 760 770 780
VRALAPIAPH ISEELWTILG NAPGIDQAGW PEVDPKYLED TSVTFVIQVN GKLRARLDIS
790 800 810
KNAAREEVLS LAREAVSRYL EDKEVKKEIF VPNRLVNFVL