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 B0R806

Entry ID Method Resolution Chain Position Source
AF-B0R806-F1 Predicted AlphaFoldDB

No variants for B0R806

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B0R806

No associated diseases with B0R806

2 regional properties for B0R806

Type Name Position InterPro Accession
domain Phenylalanyl-tRNA synthetase 220 - 497 IPR002319
domain Aminoacyl-tRNA synthetase, class II 237 - 497 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
MQLPTQQVAV LDAASTDDPQ RIEALAADTD YPPETIAGAA LALEAEGLVA VTETTTTTVS
70 80 90 100 110 120
LTDEGHAYAT DGLPEVRLYR AALDAGADDA PVEMGSVIGA AGLDGPQVDI ALSNYARKGY
130 140 150 160 170 180
GTIDSGALAA DPDADPENDP EADALATLTD GDSVDDDAVV DQLASRDLVT VSERTVRSVT
190 200 210 220 230 240
LTEAGVTELM AGVEATDEVG ELTPELLASG EWADVEFADY NVAADAADHT PGKTHVLRQA
250 260 270 280 290 300
AERVTDVLVG MGFQEMAGPH VDADFYINDC LFMPQDHPAR NHWDRFALSN PARIDELPDA
310 320 330 340 350 360
LVERVERAHR EGAGDDGDGY HSPWDEDFAR ALALRGHTTS LTARHLAGLA DADVEAPARY
370 380 390 400 410 420
FSVEKAYRND TLDATHLLEF FQIEGWVLAD DLSVRDLMGT FREFYSQFGI HDLQFKPTYN
430 440 450 460 470 480
PYTEPSFELF GRHPETGELI EIGNSGIFRP EMLDPLDVDG DVMAWGLALE RLLMLMTGFE
490 500
DIRDVHGTLC DVGFLRNAEV VY