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 Q83C15

Entry ID Method Resolution Chain Position Source
AF-Q83C15-F1 Predicted AlphaFoldDB

No variants for Q83C15

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q83C15

No associated diseases with Q83C15

6 regional properties for Q83C15

Type Name Position InterPro Accession
domain tRNA-binding domain 39 - 147 IPR002547
domain Ferrodoxin-fold anticodon-binding domain 697 - 791 IPR005121
domain B3/B4 tRNA-binding domain 211 - 384 IPR005146
domain tRNA synthetase, B5-domain 400 - 475 IPR005147
domain Phenylalanly tRNA synthetase, tRNA-binding-domain 45 - 146 IPR033714
domain Phenylalanyl tRNA synthetase beta chain, core domain 473 - 685 IPR041616

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
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKLSEQWLRE WVNPPVDTEK LTAQLTMAGL EVDSVKPAAR TLEKVVVGEV IAREKHPDAD
70 80 90 100 110 120
RLSVCRVDVG EDEPLEIVCG APNVRTGLKV AVVLVGGVVG DLKVKKTKLR GVVSNGMICS
130 140 150 160 170 180
EREMGLSEQH EGIMELPADA PIGKNIQEYL TLDDYILDIE LTPNRGDCAS VRGIAREVGA
190 200 210 220 230 240
INRLPIKGPN LVTVSATIND VFPVEVKAEK ACPRYIGRVI RGVDSHSQTP LWICERLRRS
250 260 270 280 290 300
GLRTIHPVVD VMNYVMLELG QPLHAFDLSR LVEGIEVRFA KADEKITLID ETEIALTERM
310 320 330 340 350 360
LVIADKSRPQ ALAGIMGGAN SAVNEKTEAI FLESAYFSPG EIALTARHYD MQTDSSYRFE
370 380 390 400 410 420
RGVDFKLQTL AMERATELLI QITGGSPGPL IEVCSETHLP KIPRIILRPE RIKRLLGIEI
430 440 450 460 470 480
NEDEVSKLLE LLGMRVVKEK NNWVVTVPSH RFDIKEEADL IEELAHLYGY DRIPQLRMEG
490 500 510 520 530 540
EYTIAPFSET QLSSARLRCL MTDRGYHEAV TYSFVNDELQ TLLNPEVTSI ALSNPLTAEM
550 560 570 580 590 600
NVMRTSLWPG LIQVLKYNQA RQTHRIRLFE IGMCFNAAGN EWQQVTKLGG LVAGDAHSLQ
610 620 630 640 650 660
WAEKGRRVDF YDVKGDLSAL FTLTRTEAHF RFAEGHHPAL HPGQSAALYY KDQCIGYLGA
670 680 690 700 710 720
LHPELVDQLE LTAAPFLFEM ELNAIKTSIL PKYHPLSKFP SIRRDIAIVV DRDVPVGNIE
730 740 750 760 770 780
EEIKSTAGQL LIITQVFDIY ESGKHIEFGK KSVALGLTFQ DPSRTLIDGE VKQIIERVLA
790
ALERKFNAKL RA