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 Q492V1

Entry ID Method Resolution Chain Position Source
AF-Q492V1-F1 Predicted AlphaFoldDB

No variants for Q492V1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q492V1

No associated diseases with Q492V1

3 regional properties for Q492V1

Type Name Position InterPro Accession
domain Phenylalanyl-tRNA synthetase 94 - 330 IPR002319
domain Phenylalanine-tRNA ligase, class II, N-terminal 22 - 87 IPR004188
domain Aminoacyl-tRNA synthetase, class II 121 - 321 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

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.

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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSLDPVKKLV ILAKSNIMQS NNMDALEAIR IKFLGKKGYL NQHIKNLNDT SLDIKPKLGA
70 80 90 100 110 120
AINQAKEDIY TLLIERKNIL QSKNIKNTLI TDTLDVTLPG RLSDIGTHHP ITSTIKRMKI
130 140 150 160 170 180
FFNTLGFSVI HGPEIEDDYF NFDALNIPKY HPSRDEHDTF WFDEKRLLRT HTSGVQIRAM
190 200 210 220 230 240
INKTPPIRII SFGRVYRKDY DQHHTPMFHQ MEGLIVDSNV NFSYLKKILY DFLYNFFETD
250 260 270 280 290 300
IILRFRPSYF PFTEPSAEID VMKKQETGNW LELLGCGMVH PKILHHVDID TEKFSGFAFG
310 320 330
IGIERLTMLQ YNIDDIRVFF KNDLQFLDQF K