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 Q3ABT5

Entry ID Method Resolution Chain Position Source
AF-Q3ABT5-F1 Predicted AlphaFoldDB

No variants for Q3ABT5

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q3ABT5

No associated diseases with Q3ABT5

6 regional properties for Q3ABT5

Type Name Position InterPro Accession
domain tRNA-binding domain 38 - 148 IPR002547
domain Ferrodoxin-fold anticodon-binding domain 703 - 796 IPR005121
domain B3/B4 tRNA-binding domain 212 - 385 IPR005146
domain tRNA synthetase, B5-domain 400 - 475 IPR005147
domain Phenylalanly tRNA synthetase, tRNA-binding-domain 60 - 147 IPR033714
domain Phenylalanyl tRNA synthetase beta chain, core domain 474 - 689 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
MNISYNWLQE FCEIPYTAQE LGEKLTSVGI AVEKVTYIGN YEKVVVGEVL EVENLPGTEL
70 80 90 100 110 120
FKTKVSTGKE IFEVVTGAKN VFAGFKYPFA LPGAKLPNGI TIEERRIRGV VSQGMLLSAE
130 140 150 160 170 180
ELGLLERKGA EPGLMLLPPE APVGEKIEKV LELDDYLLEL DLTPNRGDCL SVLGVAREVA
190 200 210 220 230 240
ALTGHRLKLA EPELPLDNGS CPVSIEIQNP ELCGRYMGIV IKNVKVGPSP LWLEQRLRKA
250 260 270 280 290 300
GIRPINNIVD VTNYILLEYG QPLHAFDLDK LASPEIIVRN ARAGEKITTL DGVERELTSE
310 320 330 340 350 360
MLVIADREKP IAVAGIMGGQ NTEVDDDTKT VFIEAAWFNP VSVRKTARKL GLRTDASQRF
370 380 390 400 410 420
EKNVDIEGIK RALIKAALMI CELAGGTIQG RYGDVYPKKF TPKVIAVSLS RAEEFLGISL
430 440 450 460 470 480
DAKRVVEILE SLGFRVTIGE KKIFVEVPSY RPDVSLEADI YEEIARYLGY NNFPDTMPIG
490 500 510 520 530 540
ITTTGFSPEY NFEYKVKNLL TALGMQEIIT YSFINPDSYN KLGLSVDEVL TKSVVLLNPL
550 560 570 580 590 600
SIEQSVMRTT LLPGLLDIAK RNENRQQENL LLFEMGNVFE KNGEDLPKET KLIGGIALGY
610 620 630 640 650 660
RYGDWYNKPR KYDFYYVKGI LESLFTSLGI NNFSFSAAKD LPFLHPGKAA RVYLENTEIG
670 680 690 700 710 720
YLGELHPLVQ KKYEFKNTPL VFELNYDLLK TLIPAEKKYT PLSPYPEVKR DIALLVEREI
730 740 750 760 770 780
PAATFIEVIK GLAINTLKNI EIFDVYEGEK LGPNKKSIAI SLTFSSTEKT LSEEEINNFM
790
AQVLKALEAK TGAKLRTF