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 Q04VV0

Entry ID Method Resolution Chain Position Source
AF-Q04VV0-F1 Predicted AlphaFoldDB

No variants for Q04VV0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q04VV0

No associated diseases with Q04VV0

6 regional properties for Q04VV0

Type Name Position InterPro Accession
domain tRNA-binding domain 40 - 149 IPR002547
domain Ferrodoxin-fold anticodon-binding domain 710 - 802 IPR005121
domain B3/B4 tRNA-binding domain 215 - 391 IPR005146
domain tRNA synthetase, B5-domain 407 - 484 IPR005147
domain Phenylalanly tRNA synthetase, tRNA-binding-domain 46 - 148 IPR033714
domain Phenylalanyl tRNA synthetase beta chain, core domain 496 - 693 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
MKLSLDWMND FTPLKEVGLD VILKKIAVSV CEIDGVVPFR PELDFVKIVR IESLDKHPSA
70 80 90 100 110 120
DKLQIAEVFD GSSKSQIVTG ATNVKVGDLV PLAIPGAKLG DREILESELR GVKSSGMFCS
130 140 150 160 170 180
EKELSLSEES SGVWILNGIE GAEIGKTIRS FLYYEDIIFE IDNKSITHRP DLWSHFGFAR
190 200 210 220 230 240
ELASQLRLPI TFNPFESLWN FDLSMKFPRV LENQNAHSYY ASSICEVFVI PSKRKFQSRL
250 260 270 280 290 300
QKCGIRVINN VVDVSNYVML EMGQPTHFFD KRFLESQGGV SLEVSYAKKG ESFALLDETS
310 320 330 340 350 360
PSLEEEILLI RNQGRPVAVA GVMGGKESAV QNNTTEIVME SAVFAREKIR KSIRSTGIRS
370 380 390 400 410 420
DSSVRYEKGL EATTTLPVIR RALNLLKENG CPSLKASEPV GFLHTPHKEV RIHTDIHFIN
430 440 450 460 470 480
TKLGITLSQG DITDILERLH FMVSWKGDRL EALVPKFRHN YDVTIPEDLV EEIGRTRGYD
490 500 510 520 530 540
TIQVTPLLAE IKTPIRNLSR ELERKCKTFF SVGLGYHEVY NYSFQALKEN ELDGDVELSV
550 560 570 580 590 600
KIRNEMPEEQ SVLRNSLISS LLKNIRTNQD RFSEIKIFEF GRAYFNIPEP DNEKKFFSFA
610 620 630 640 650 660
VSFDRKSSES DLGLLEDDFL KVRKEIESFL KYIRIFEYFW DIKPEIFFHP GASLSLIVDS
670 680 690 700 710 720
KQIGNLGYVH PAVLDSFELK KRVIYGSLEF EKLVEIWNTN RNISRFNVPS QFPEAEIDIS
730 740 750 760 770 780
ILIGEKENTN LFTDLVRREK IPELQEGWVY SQFAGGSVPV GKRSVSYRFR LVNYEKTFTQ
790 800
ERIKEISDHL VALAGKNGFV LR