P47525

PR
Gene name
proS
Protein name
Proline--tRNA ligase
Names
Prolyl-tRNA synthetase, ProRS
Species
Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37) (Mycoplasmoides genitalium)
KEGG Pathway
mge:MG_283
EC number
6.1.1.15: 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)

228-297 (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 P47525

Entry ID Method Resolution Chain Position Source
AF-P47525-F1 Predicted AlphaFoldDB

No variants for P47525

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P47525

No associated diseases with P47525

4 regional properties for P47525

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 116 - 282 IPR002314
domain Aminoacyl-tRNA synthetase, class II 78 - 295 IPR006195
domain Proline-tRNA ligase, class II, C-terminal 418 - 483 IPR016061
domain Prolyl-tRNA synthetase, catalytic domain 7 - 285 IPR033721

Functions

Description
EC Number 6.1.1.15 Ligases forming aminoacyl-tRNA and related compounds
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
aminoacyl-tRNA synthetase multienzyme complex A multienzyme complex found in all multicellular eukaryotes composed of eight proteins with aminoacyl-tRNA synthetase activities (abbreviated as: ArgRS, AspRS, GluProRS, GlnRS, IleRS, LeuRS, LysRS, MetRS where RS is the enzyme, preceded by the amino acid it uses as a substrate) as well as three non-synthetase proteins (p43, p38, and p18) with diverse functions. Several of these subunits are known dimers, so the total polypeptide count in the multisynthetase complex is at least fifteen. All of the enzymes in this assembly catalyze the same reaction, the covalent attachment of an amino acid to either the 2'- or 3'-hydroxyl of the 3'-terminal adenosine of tRNA, but using different substrates.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
proline-tRNA ligase activity Catalysis of the reaction: ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).

1 GO annotations of biological process

Name Definition
prolyl-tRNA aminoacylation The process of coupling proline to prolyl-tRNA, catalyzed by prolyl-tRNA synthetase. The prolyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a methionine-accetping tRNA.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTKKTQDLTS WYDQLLVKAK LICHGEVKGT VCFLNNSWGL WMEIQQLYND AIANKNQLSA
70 80 90 100 110 120
IALTKFQPTT SFCYQVFQVQ LPTLSFYSEY QKEKTHIKGF NPELFLINQV GQKQLNDPLV
130 140 150 160 170 180
LRPTSEIAFC NLWKKQELSY HDLPLIYNQW TQVFRAEKNT RPFLRNSEFY WQETHGLFVD
190 200 210 220 230 240
QSQSEQAAIS FWNLYQDLII NKLCIPAFVG LKSESEKFAG AKNTWTIEAI MPDGQSLQCA
250 260 270 280 290 300
TSHDLGDTFT KSFTISYQSK TNQKMTPSSF SCGMSTRILG AIFLTHSDDY GLVLPWYLAS
310 320 330 340 350 360
KQVKLYLFDK NNNPKTRALA FLVKDFLEKL KIRFSFIEIN NQLGKQLLKG EIEGIPLQMI
370 380 390 400 410 420
VDNEKTINIF NRLTRLKTSL TFANLQTEFV NLVNNYHTEM YRKANDLVEQ KLARVQTLKE
430 440 450 460 470 480
IEQAFKNKKA VLCTVKLTGE LEQHLKTKYQ VSVRCVFKKS DVTQNCPFTN QPCFDSVLIA
RAY