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 Q2SDJ7

Entry ID Method Resolution Chain Position Source
AF-Q2SDJ7-F1 Predicted AlphaFoldDB

No variants for Q2SDJ7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2SDJ7

No associated diseases with Q2SDJ7

6 regional properties for Q2SDJ7

Type Name Position InterPro Accession
domain tRNA-binding domain 39 - 147 IPR002547
domain Ferrodoxin-fold anticodon-binding domain 696 - 789 IPR005121
domain B3/B4 tRNA-binding domain 211 - 384 IPR005146
domain tRNA synthetase, B5-domain 400 - 476 IPR005147
domain Phenylalanly tRNA synthetase, tRNA-binding-domain 45 - 146 IPR033714
domain Phenylalanyl tRNA synthetase beta chain, core domain 474 - 684 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
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
MKFSEYWLRE WVDPQLSSEA LVQQITMAGL EVDAAERVAK PFSGIVVGEV LSVEPHPDAD
70 80 90 100 110 120
KLRVCKVSDG QEEFQVVCGA PNVAAGMKVP FAKIGAVLSG DFKIKKAKLR GVESQGMLCS
130 140 150 160 170 180
EEELTLAEKS DGLMPLAADA PVGVDVRSYL KLDDNIIDVD LTPNRSDCLS ILGMAREVAA
190 200 210 220 230 240
LNKIPFEAPE VKKTAAVIDD VFPVRVEAPE ACPRYVGRVI KGVDLSAPTP QWMVEKLRRS
250 260 270 280 290 300
GIRSIDAVVD VTNFVMIELG QPMHAFDLNE LADGIVVRMP TPGEKLVLLD GQEITINPDT
310 320 330 340 350 360
LVIADNEKPL ALAGVMGGEH SGVSEKTKDI FLESAFFAPL HLAGKARSYG LHTDSSHRFE
370 380 390 400 410 420
RGVDYAHQAR AIERATELLL EIVGGQPGPV TEICSKEHLP AKALVNLRHA RVDELLGVHL
430 440 450 460 470 480
DRTRVEEMLA RLGLGVHKVA KDGWTFSAPT HRFDISIEVD LIEEVARLYG YNKLPVTEPM
490 500 510 520 530 540
APLGIKPLPE SKVSLRRLKL HLVSRGYQEA ITYTFVDQKV LSLLTPEEDT ITLANPIASD
550 560 570 580 590 600
MAAMRTTLWA GLLQTALYNQ NRQQNRIRLF ESGLRFLKRG GQIQQDPMLA GLIMGASMPE
610 620 630 640 650 660
GWESKKRTVD FYDVKGDLES LLEIPGCNLS FRSAQHPALH PGQTAEVLKD GQPIGVLGAL
670 680 690 700 710 720
HPRIAKTLNL NGPLYLFELC LNSIADGQVP SFKGVSRFPE IRRDLAIVID EQTPYADVAL
730 740 750 760 770 780
AIAQSAGEWR VHHELFDVYH GESVGADKKS LAISIVWRHP ERTLRDEEIT EAFDNVVKEL
GNRFGASLRS