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 Q8EPH5

Entry ID Method Resolution Chain Position Source
AF-Q8EPH5-F1 Predicted AlphaFoldDB

No variants for Q8EPH5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8EPH5

No associated diseases with Q8EPH5

6 regional properties for Q8EPH5

Type Name Position InterPro Accession
domain tRNA-binding domain 40 - 156 IPR002547
domain Ferrodoxin-fold anticodon-binding domain 717 - 810 IPR005121
domain B3/B4 tRNA-binding domain 222 - 395 IPR005146
domain tRNA synthetase, B5-domain 411 - 486 IPR005147
domain Phenylalanly tRNA synthetase, tRNA-binding-domain 46 - 152 IPR033714
domain Phenylalanyl tRNA synthetase beta chain, core domain 484 - 703 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
MLVSYNWLKN YVNLDAVTPE ELAAKITKSG IEVEGVEYIA EKNENIVVGY VETCEKHPDA
70 80 90 100 110 120
DKLNVTQVSV GEETLQIVCG APNIAKGQKV AVAKPGAVLP GNMKIKKVKL RGVESNGMIC
130 140 150 160 170 180
SLQELGLEEK YIPTDIAEGI FVFPEDEDIE VGSKVDEWLN LTDAVLDLDV LANRPDALSM
190 200 210 220 230 240
LGVAYEVAAV LDQPIELPTK NIDYIDEKVS DQIEINIESK DLNPYYAAFM VKDVVIKPSP
250 260 270 280 290 300
LWMRNYLMAS GIRPINNIVD ITNYVLLEYG QPLHAFDFDR FASNQIVIRR GVEGEVIQTL
310 320 330 340 350 360
DEQERKLTED NLVITNGSEP VALAGVMGGA NSEVTDKTVN VLLEAAYFEA TAVRHTVRQT
370 380 390 400 410 420
GLRSESSTRF EKGIDPNRIV EAGLRACQLM QRYAGGKVLQ GFAEENHLDT KSTKEVKVPL
430 440 450 460 470 480
TQVNQRLGME LTEKDVQSVL NRLKFDFDQD GHTFIVHVPT RRRDITIFED MLEEIIRIHG
490 500 510 520 530 540
YDHLPYTIPQ GWVKSGGLTD KQLLQRKIRE FMMSSGAMET LTYSLTNEQN VKRLVTPNID
550 560 570 580 590 600
LENSYPISLA MPMSEDHKYL RLSIVPELLR ILQHNIARKQ TDLNYFEIGK VFISEEQELT
610 620 630 640 650 660
HQPTEKLHLA GAFTGLWHNH PWQQDKKQVD FFVVKGIIEG LFNYLQLNIS FKQVKMKDMH
670 680 690 700 710 720
PGRCAELNID GENIGFMGQL HPKTANVFDL PETYVFEIDL ESVFEKYINV PSFTDIPRYP
730 740 750 760 770 780
SVSRDIAFIL DTEVFSGEVQ QYIQEIGAPL VKEVSIFDVY QGEHLEDGKK SVAYRLMYQD
790 800 810
PAKTLQDDEV ESSYQQIVEA VNKKFGSYVR S