Q9JVA0

PR
Gene name
pheT (NMA0937)
Protein name
Phenylalanine--tRNA ligase beta subunit
Names
Phenylalanyl-tRNA synthetase beta subunit, PheRS
Species
Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 / Z2491)
KEGG Pathway
nma:NMA0937
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)

449-519 (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 Q9JVA0

Entry ID Method Resolution Chain Position Source
AF-Q9JVA0-F1 Predicted AlphaFoldDB

No variants for Q9JVA0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9JVA0

No associated diseases with Q9JVA0

6 regional properties for Q9JVA0

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
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
MQFSYSWLKT QADTELSSDK LEHLLTMSGL EVEEAETAAP AFAGVVIAEV KSVEKHPDAD
70 80 90 100 110 120
RLNVTRVDVG TGELVQIVCG APNVKAGIKV PCSLPGAVLP GNFKIKPTKM RGVVSNGMLC
130 140 150 160 170 180
STDELGLPDD GVNGLHILPE DAPVGTNIRE YLDLDDTLFT LKITPNRADC LSVKGIAREV
190 200 210 220 230 240
SALTGCAFRQ PEIRKMPSEG GKTRAVKIDA PADCGRFISR VIENVNAKAA TPDWMKQRLE
250 260 270 280 290 300
RSGIRSISVL VDIGNYVMLE IGQPMHVFDA DKLSGSLHIR RAREGETLEC LNEKTVSLSE
310 320 330 340 350 360
NTLVVADEKG ALSLAGLMGG AASAVSDGTQ NIVLEAAWFA PEIIAGKSRQ YGFGSDSSFR
370 380 390 400 410 420
FERGVDYRLQ ADAIERATEL VLQICGGAAG EMVEAQGELP EVKQVGLRLG RLKTVLGVDI
430 440 450 460 470 480
PSEQVETILQ HLGLQPEKTA EGFRVTAPSF RFDIEIEADL IEEIGRVYGY ENIPDDYTSG
490 500 510 520 530 540
RLKMLELPET RRPRFAVYNE MAARGYREVV SYAFVNEQWE QDFAANADPI RLQNPLAAQY
550 560 570 580 590 600
AVMRSTLIGG LVEILQNNLN RKQNRVRVFE IARVFGKGSD GRFVQNERIG GLWYGAAMPE
610 620 630 640 650 660
QWGGKTRNAD FYDIKADVEN LLKNKAVEFV KTGYPALHPG RAANIVSDGK VIGFVGELHP
670 680 690 700 710 720
KWLQKYDLPQ APLVFEIDMA AVLECGKTRY RAVSKFQPVR RDLAFVMPEA MSHDDLLLVL
730 740 750 760 770 780
KGAANKLVQE ISVFDVYRGM GLPEGMKSVA VKVILQDMEN TLTDEAVEPL IGKLIGAATA
AGARLRS