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 Q505J8

Entry ID Method Resolution Chain Position Source
AF-Q505J8-F1 Predicted AlphaFoldDB

No variants for Q505J8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q505J8

No associated diseases with Q505J8

No regional properties for Q505J8

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q505J8

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
Q5ZJQ2 FARSA Phenylalanine--tRNA ligase alpha subunit Gallus gallus (Chicken) PR
P08312 pheS Phenylalanine--tRNA ligase alpha subunit Escherichia coli (strain K12) PR
Q9Y285 FARSA Phenylalanine--tRNA ligase alpha subunit Homo sapiens (Human) PR
Q1JPX3 farsa Phenylalanine--tRNA ligase alpha subunit Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MADNPVLEQL LRRLEVADGG LDSAELATQL GVEHQAVVGA VKSLQALGEV IEAELRSTKC
70 80 90 100 110 120
WELTTEGEEI AREGSHEARV FRSIPLEGLV QSELMQLPSG KVGFSKAMSN KWIRVDKSAA
130 140 150 160 170 180
DGPRVFRVVD SIEDEVQRRL QQVQAGQAEK LAEKERNELR KRKLLTEVIL KTYWVSKGKG
190 200 210 220 230 240
FSTSVSKQEA ELSPEMISSG SWRDRPFKPY NFSARGVLPD SGHLHPLLKV RSQFRQIFLE
250 260 270 280 290 300
MGFTEMPTDN FIESSFWNFD ALFQPQQHPA RDQHDTFFLR DPAEALQLPM DYVQRVKRTH
310 320 330 340 350 360
SQGGYGSQGY KYTWKLEEAR KNLLRTHTTA ASARALYRLA QKKPFTPAKY FSIDRVFRNE
370 380 390 400 410 420
TLDATHLAEF HQIEGVIADH GLTLGHLMGV LREFFTKLGI TQLRFKPAYN PYTEPSMEVF
430 440 450 460 470 480
SYHQGLKKWV EVGNSGVFRP EMLLPMGLPE NVSVIAWGLS LERPTMIKYG INNIRELVGH
490 500
KVNLQMVYDS PVCRLDIEPR SSKTQEAA