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 Q8XZ24

Entry ID Method Resolution Chain Position Source
AF-Q8XZ24-F1 Predicted AlphaFoldDB

No variants for Q8XZ24

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8XZ24

No associated diseases with Q8XZ24

3 regional properties for Q8XZ24

Type Name Position InterPro Accession
domain Phenylalanyl-tRNA synthetase 91 - 326 IPR002319
domain Phenylalanine-tRNA ligase, class II, N-terminal 19 - 87 IPR004188
domain Aminoacyl-tRNA synthetase, class II 119 - 317 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
MQFPESWLRS FVNPPIATAE LSHRLTMAGL EVEEVDPVAP PFSQIVVGHV VEVNKHPDAD
70 80 90 100 110 120
RLNVCKVDAG TGELLQIVCG APNVSVGIKV PCALVGAELP PGDDGKPFKI KIGKLRGVES
130 140 150 160 170 180
YGMLCSAREL KLSEEHGGLL ILPEDTPVGA DIRKVLDLDD QIFIIKLTPN KADCLSIHGV
190 200 210 220 230 240
AREVSALTGA PITLPTMAPV AVTLSDKLPV KVEAPDLCGR FAGRIIRGVN ARAKTPAWMV
250 260 270 280 290 300
SRIERAGMRS VSALVDISNY VMLELGRPSH VFDLDKIHGG LTVRWGKPGE QLKLLNGDTV
310 320 330 340 350 360
TVDDKVGVIS DEQAIESLAG IMGGDKTAVT LDTQNIYVEA AFWWPAAIQG RARRYNFSTD
370 380 390 400 410 420
AGHRFERGVD YATIVEHIER ISALILDICG GQAGPIDDQI VNCPKREPVR MRVARAARVL
430 440 450 460 470 480
GIPLSHEVVS DVFKRLGLTF SVDGDVFVVE PPSYRFDIEI EEDLIEEVAR IYGFEQIPAK
490 500 510 520 530 540
PPVAENAMRP TNEARRTMHD VRHAVAARDY HEVVNFAFVE TEWEADFAGN TQPIPLLNPI
550 560 570 580 590 600
ASQYSVMRST LIGGLLDKVR YNLNRKASRV RLFEVGRVFR RDAEVADGGL SVAGYAQPMR
610 620 630 640 650 660
VGGIAYGPAA EEQWGVPARA VDFFDVKGDV ESLLWPLQAR FERAEHSALH PGRAARVVLD
670 680 690 700 710 720
GRAVGWIGEL HPRWLQKYEL PTAPVVWELD LDAITAVGLP AYREVPRVPA VTRDIALVVR
730 740 750 760 770 780
QDVGVQDLVD AFEKAAAGMP WQRYLQGVVL FDEFRPKAAT AAIGAQEKSL AFRITLQDTD
790 800
STLQDDLVEA ATQQLIRAAG DAFGARLRA