Q88K22

PR
Gene name
pheT
Protein name
Phenylalanine--tRNA ligase beta subunit
Names
Phenylalanyl-tRNA synthetase beta subunit, PheRS
Species
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
KEGG Pathway
ppu:PP_2470
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)

160-232 (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 Q88K22

Entry ID Method Resolution Chain Position Source
AF-Q88K22-F1 Predicted AlphaFoldDB

No variants for Q88K22

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q88K22

No associated diseases with Q88K22

6 regional properties for Q88K22

Type Name Position InterPro Accession
domain tRNA-binding domain 39 - 147 IPR002547
domain Ferrodoxin-fold anticodon-binding domain 699 - 792 IPR005121
domain B3/B4 tRNA-binding domain 211 - 385 IPR005146
domain tRNA synthetase, B5-domain 401 - 477 IPR005147
domain Phenylalanly tRNA synthetase, tRNA-binding-domain 45 - 146 IPR033714
domain Phenylalanyl tRNA synthetase beta chain, core domain 475 - 683 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
MKFSEQWLRG WVNPQVSRDE LVARLSMAGL EVDSVTPAAG QFSGIVVGEI LATEQHPDAD
70 80 90 100 110 120
KLRVCQVSSG QETFQVVCGA PNARPGIKIP FAMIGAELPG DFKIKKAKLR GVESFGMLCS
130 140 150 160 170 180
AAELQISEEN DGLLELAADA PVGEDIRTYL SLDDASIEIG LTPNRGDCLS IAGLARDVSA
190 200 210 220 230 240
LYDTPVTRPV VPAVAAAHDE VRPVEVSAPA ACPRYLGRVI RNVDLSKPTP LWMVERLRRS
250 260 270 280 290 300
DVRSIDAAVD ITNYVMLELG QPMHAFDLAE INGGIRVRMA EEGEKLVLLD GQEVALRADT
310 320 330 340 350 360
LVIADHTRAL AIAGVMGGEH SGVNTEKTRD LFLESAFFEP ISVAGKARSY GLHTDASHRY
370 380 390 400 410 420
ERGVDSQLAR EAMERATQLL LDIVGGEAGP VVEAVSEQHL PQVAPVTLRA ERITQMLGME
430 440 450 460 470 480
MDPAQVEQLL NALELTTTKS GEGQWTVSVP SHRFDISLEV DLIEELARLY GYNNLPVRYP
490 500 510 520 530 540
QARLAPQGKP ETRGDLPTLR RLLVARGYQE AITYSFIDPK LFELFSPGVE PLLLANPISS
550 560 570 580 590 600
DMAAMRASLW PGLVKALQHN LNRQQDRVRL FESGLRFVGQ LGDLQQQPMI AGVITGSRLP
610 620 630 640 650 660
EGWANGRDGV DFFDVKADVE ALLGYSGALS DFTFSAGKHP ALHPGQTAVI ERDGKLVGYL
670 680 690 700 710 720
GAIHPELAKA LGLDRPVFLF ELVLGDVVEG RLPKFSELSK FPETRRDLAL IAGRDVASSA
730 740 750 760 770 780
VLELIRDNAG EWLTDLRLFD VYQGKGIDPD RKSLAVGLTW QHPSRTLNDD EVNTTLQNIL
790
TSLEQRLNTT LRK