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

5 structures for P08312

Entry ID Method Resolution Chain Position Source
3PCO X-ray 302 A A/C 1-327 PDB
6OZ5 X-ray 250 A A/C 2-327 PDB
6P24 X-ray 212 A A/C 2-327 PDB
6P26 X-ray 316 A A/C 2-327 PDB
AF-P08312-F1 Predicted AlphaFoldDB

2 variants for P08312

Variant ID(s) Position Change Description Diseaes Association Provenance
98 G>D thermosensitive mutant pheS5; might cause subunit disaggregation due to electrostatic repulsion [UniProt] No
191 G>D decreased affinity for Phe [UniProt] No

No associated diseases with P08312

3 regional properties for P08312

Type Name Position InterPro Accession
domain Phenylalanyl-tRNA synthetase 92 - 326 IPR002319
domain Phenylalanine-tRNA ligase, class II, N-terminal 20 - 87 IPR004188
domain Aminoacyl-tRNA synthetase, class II 116 - 305 IPR006195

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

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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.

1 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.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q5ZJQ2 FARSA Phenylalanine--tRNA ligase alpha subunit Gallus gallus (Chicken) PR
Q9Y285 FARSA Phenylalanine--tRNA ligase alpha subunit Homo sapiens (Human) PR
Q9BRP7 FDXACB1 Ferredoxin-fold anticodon-binding domain-containing protein 1 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
MSHLAELVAS AKAAISQASD VAALDNVRVE YLGKKGHLTL QMTTLRELPP EERPAAGAVI
70 80 90 100 110 120
NEAKEQVQQA LNARKAELES AALNARLAAE TIDVSLPGRR IENGGLHPVT RTIDRIESFF
130 140 150 160 170 180
GELGFTVATG PEIEDDYHNF DALNIPGHHP ARADHDTFWF DTTRLLRTQT SGVQIRTMKA
190 200 210 220 230 240
QQPPIRIIAP GRVYRNDYDQ THTPMFHQME GLIVDTNISF TNLKGTLHDF LRNFFEEDLQ
250 260 270 280 290 300
IRFRPSYFPF TEPSAEVDVM GKNGKWLEVL GCGMVHPNVL RNVGIDPEVY SGFAFGMGME
310 320
RLTMLRYGVT DLRSFFENDL RFLKQFK