Q3JBZ7

PR
Gene name
pheT
Protein name
Phenylalanine--tRNA ligase beta subunit
Names
Phenylalanyl-tRNA synthetase beta subunit, PheRS
Species
Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / JCM 30415 / NCIMB 11848 / C-107)
KEGG Pathway
noc:Noc_1145
EC number
6.1.1.20: Ligases forming aminoacyl-tRNA and related compounds
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

151-229 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q3JBZ7

Entry ID Method Resolution Chain Position Source
AF-Q3JBZ7-F1 Predicted AlphaFoldDB

No variants for Q3JBZ7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q3JBZ7

No associated diseases with Q3JBZ7

6 regional properties for Q3JBZ7

Type Name Position InterPro Accession
domain tRNA-binding domain 39 - 148 IPR002547
domain Ferrodoxin-fold anticodon-binding domain 699 - 792 IPR005121
domain B3/B4 tRNA-binding domain 212 - 385 IPR005146
domain tRNA synthetase, B5-domain 401 - 476 IPR005147
domain Phenylalanly tRNA synthetase, tRNA-binding-domain 45 - 147 IPR033714
domain Phenylalanyl tRNA synthetase beta chain, core domain 474 - 687 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
MKFSEAWLRT WVDPDISRET LVERLTLAGL EVESTEPVAA PFKGVKAARI VAVEPHPSAP
70 80 90 100 110 120
RLQVCQVDIG SGSLLTVVCG APNARAGLWA PLAIIGAQLP AGIRIELAKL QGVESFGMLC
130 140 150 160 170 180
SAAELGLAEQ SAGLLELPEG DFPGVDLHEF LQFDDISIEV DLTPNRSDCL SVAGIAREVG
190 200 210 220 230 240
VLTQSPVTEP AIEPVTAQIG DIFPVTVTAP AACPRYLGRV LRGVNPQTQT PWWLRERLRR
250 260 270 280 290 300
SGIRSLGLVV DVTNYVMLEL GQPMHAFDLE RLKGGIQVRY GQADEALTLL DGTHLRLDEE
310 320 330 340 350 360
TLIIADQQRA LALAGIMGGE ESGINNQTRH LFLESAFFNP SVIAGRARFY GLHTDSSHRF
370 380 390 400 410 420
ERGVDPELPR RAMERATALL LEIAGGQAGP VIEVADSSQL PPQATIILRK ARIHRVLGVE
430 440 450 460 470 480
IAESRITEQL TRLGLKVERI EEGWEVKVPS FRFDLALEVD LIEELGRLYG YDRLPSTRPV
490 500 510 520 530 540
GQIQPVLKTE AGAFIDRIRQ VLVDRDYQEA ITYSFVDQEL QQLLDPEGSP LVLNNPISTD
550 560 570 580 590 600
MAVMRTTLWT GLVQALQYNS YRQQERIRFF EYGLTFNGQL ADLKQERTIA GLISGASYPE
610 620 630 640 650 660
QWGLVGRPAD FFDLKGDVEA ILSLVGEQRN CFEFMAASHP ALHPGQSAQI LREGQAVGWL
670 680 690 700 710 720
GALHPWLESK LDLSSRAYLF SLQLEAVERG SLPVFQSLSK FPAIRRDIAF LVNANIPVQV
730 740 750 760 770 780
VFDCLKGCES DILKEFQLFD VYTGKGIDPD KKSLALKLIL QHPSYTLTDD RVNIFIERVM
790
ALLVTELGAI IRE