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 Q9WZS9

Entry ID Method Resolution Chain Position Source
AF-Q9WZS9-F1 Predicted AlphaFoldDB

No variants for Q9WZS9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9WZS9

No associated diseases with Q9WZS9

6 regional properties for Q9WZS9

Type Name Position InterPro Accession
domain tRNA-binding domain 39 - 147 IPR002547
domain Ferrodoxin-fold anticodon-binding domain 694 - 787 IPR005121
domain B3/B4 tRNA-binding domain 211 - 384 IPR005146
domain tRNA synthetase, B5-domain 399 - 472 IPR005147
domain Phenylalanly tRNA synthetase, tRNA-binding-domain 45 - 146 IPR033714
domain Phenylalanyl tRNA synthetase beta chain, core domain 474 - 680 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
MRVPESWLRE FVDLDWDIEQ IAERLTFSGT SVEDILRPFN VSGEIITARV IERFDHPASE
70 80 90 100 110 120
KLIVCKVDTG KRIYTVITAD KTVNEGDYVI LALEGATLNN GLKIEPREFK GVISEGMLCS
130 140 150 160 170 180
LEELGLEEKS DRVYRFPDPV ELGVNVVEEY GLNERVLDIE ITPNRPDCLS IIGVARELSA
190 200 210 220 230 240
LSGRPLNKPQ PDVSFVDEDV QFDVEIEDVE GCPRYSARIM KGVTVKDSPL WMKARLVAAG
250 260 270 280 290 300
VRSLNNVVDA TNYVMIELGH PVHAFDLNRL KNKRIVVKSA KGGERVLLLD EKEYELKGGE
310 320 330 340 350 360
VLITDGENVL ALGGIMGGME SGVYDDTRDL VLEVAYFDPV RIRKAAKALG ISSESSYRFE
370 380 390 400 410 420
RGVDPNDVEL VSLRLAELIQ KLAGGYVLRK FWDVYPRKIE PKKVMLRKAR IEKILGTKVE
430 440 450 460 470 480
EPGDILRRLE FQVEDRGDSY EVLVPTFRPD VEREIDLIEE IGRIYGYEKV ESKVISVPAV
490 500 510 520 530 540
NRGWGEKQLF RREISQFMKG MGFDEVVTFS FVDSQKVKKW PLVDREPIAL SNPIASDMDV
550 560 570 580 590 600
MRTSQFYSLI QVLAENFKRQ NRDLKLFEIG KIYFKENGNF REIETLSAMS CGLENPGDYT
610 620 630 640 650 660
DKRSVSFYTI KGVLDELFFR LGVNVVYRAA EIPGLFPTRS ARIYVENREI GFIGMVDPKL
670 680 690 700 710 720
LDEYDVKEDT YFFEIDMELL RKYASKRPAY RPTPRFPAVR RDISFLLPKG FESVKIIELF
730 740 750 760 770 780
KKSGGDLVEE VGVFDIYEGK GIPENMVSVT LYVVFRHPER TLTDEEVNKI FEEMVQKAER
EFGIRRRF