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 Q5ZJQ2

Entry ID Method Resolution Chain Position Source
AF-Q5ZJQ2-F1 Predicted AlphaFoldDB

No variants for Q5ZJQ2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5ZJQ2

No associated diseases with Q5ZJQ2

5 regional properties for Q5ZJQ2

Type Name Position InterPro Accession
domain Phenylalanyl-tRNA synthetase 213 - 442 IPR002319
domain Aminoacyl-tRNA synthetase, class II 232 - 443 IPR006195
domain PheRS DNA binding domain 2 137 - 168 IPR040586
domain PheRS, DNA binding domain 1 1 - 64 IPR040724
domain PheRS, DNA binding domain 3 78 - 135 IPR040725

Functions

Description
EC Number 6.1.1.20 Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
phenylalanine-tRNA ligase complex An enzyme complex that catalyzes the ligation of phenylalanine to tRNA(Phe), forming L-phenylalanyl-tRNA(Phe).

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
magnesium ion binding Binding to a magnesium (Mg) ion.
phenylalanine-tRNA ligase activity Catalysis of the reaction: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).
tRNA binding Binding to a transfer RNA.

2 GO annotations of biological process

Name Definition
phenylalanyl-tRNA aminoacylation The process of coupling phenylalanine to phenylalanyl-tRNA, catalyzed by phenylalanyl-tRNA synthetase. The phenylalanyl-tRNA synthetase is a class-II synthetase. However, unlike other class II enzymes, The activated amino acid is transferred to the 2'-OH group of a phenylalanine-accepting tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification.
protein heterotetramerization The formation of a protein heterotetramer, a macromolecular structure consisting of four noncovalently associated subunits, of which not all are identical.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P08312 pheS Phenylalanine--tRNA ligase alpha subunit Escherichia coli (strain K12) PR
Q9Y285 FARSA Phenylalanine--tRNA ligase alpha subunit Homo sapiens (Human) PR
Q505J8 Farsa Phenylalanine--tRNA ligase alpha subunit Rattus norvegicus (Rat) PR
Q1JPX3 farsa Phenylalanine--tRNA ligase alpha subunit Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MSPSVAELLL QRLERTPPGP EGGLCSLEAA AALGLDHQTL VGAVKSLQAL GEVIEAETRA
70 80 90 100 110 120
TTRWELSAEG EEVLRDGSPE VRLFRSVPSE GLPQSDAMKL PGAQVGFSKA MANKWLRLDK
130 140 150 160 170 180
GAPGGPRIFR AVDAVQDVVQ SSLRQVQEGN GGSLSERERT DLKRRKLLLE VTLKSYWIRK
190 200 210 220 230 240
GSAFSTAVVR QETDLTPEMI ATGSWRKLPF KAYNFSALGL PPTCGHLHPL LKVRSQLRQI
250 260 270 280 290 300
FLEMGFTEMP TDNFVESSFW NFDALFQPQQ HPARDQHDTF FLQDPAEAPE LPANYMARVK
310 320 330 340 350 360
KVHSQGGYGS QGYKYEWKVE EARKNLLRTH TTSASARALY HLARQGKFTP VKYFSIDRVF
370 380 390 400 410 420
RNESLDATHL AEFHQVEGVV ADRGLTLGHL MGTLQQFFTK LGISKLRFKP AYNPYTEPSM
430 440
EVFSYHEGLK KWVEVGNSGV FRS