Q8I5R7

PR
Gene name
proRS
Protein name
Proline--tRNA ligase
Names
PfPRS, Prolyl-tRNA synthetase, PfProRS
Species
Plasmodium falciparum (isolate 3D7)
KEGG Pathway
pfa:PF3D7_1213800
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)

152-277 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

15 structures for Q8I5R7

Entry ID Method Resolution Chain Position Source
4NCX X-ray 185 A A/B 249-746 PDB
4OLF X-ray 290 A A 249-746 PDB
4Q15 X-ray 235 A A/B 249-746 PDB
4TWA X-ray 300 A A/B 254-746 PDB
4WI1 X-ray 165 A A/B 249-746 PDB
4YDQ X-ray 230 A A/B 254-746 PDB
5IFU X-ray 245 A A/B 249-746 PDB
6T7K X-ray 179 A A 249-746 PDB
7F96 X-ray 258 A A 254-746 PDB
7F97 X-ray 239 A A/B/C/D 254-746 PDB
7QB7 X-ray 190 A A 249-746 PDB
7QC1 X-ray 251 A A/D/I 249-746 PDB
7QC2 X-ray 228 A A 249-746 PDB
7V9D X-ray 194 A A 254-746 PDB
AF-Q8I5R7-F1 Predicted AlphaFoldDB

No variants for Q8I5R7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8I5R7

No associated diseases with Q8I5R7

6 regional properties for Q8I5R7

Type Name Position InterPro Accession
domain Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) 351 - 520 IPR002314
domain Anticodon-binding 539 - 629 IPR004154
domain Aminoacyl-tRNA synthetase, class II 283 - 532 IPR006195
domain YbaK/aminoacyl-tRNA synthetase-associated domain 41 - 163 IPR007214
domain Proline-tRNA ligase, class II, C-terminal 662 - 746 IPR016061
domain Prolyl-tRNA synthetase, catalytic domain 261 - 522 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.

3 GO annotations of molecular function

Name Definition
Ala-tRNA(Pro) hydrolase activity Catalysis of the hydrolysis of misacylated Ala-tRNA(Pro).
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).

2 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.
tRNA aminoacylation for protein translation The synthesis of aminoacyl tRNA by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA and the alpha carboxylic acid group of an amino acid, to be used in ribosome-mediated polypeptide synthesis.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNNNTNGEII IPQEYLEKSE CLFKELKELN INFKEVKHGL AATIKDLLEM NLENSTNILK
70 80 90 100 110 120
NLFLKDKKKN YFLICTLNNK TVDLKNLSNI LKTNNLRFVD ENNLNNILNI QPGCLSPLAI
130 140 150 160 170 180
KNDKENIVKL YFDEEIKNMQ EVIIHPLHNY SSLYIKTQDV IKFCESFNHA PEYVQIKEDT
190 200 210 220 230 240
TSKARVDKKE DVQEEMAKNE ELQNNNNNNK NNSNSNNNNN NNNNHIKDTI LKGKLLSNNE
250 260 270 280 290 300
VEDNKSKDSN ILGITSKKIE NFSDWYTQVI VKSELIEYYD ISGCYILRPA AYYIWECVQA
310 320 330 340 350 360
FFNKEIKKLN VENSYFPLFV TKNKLEKEKN HIEGFSPEVA WVTKYGDSNL PEEIAIRPTS
370 380 390 400 410 420
ETIMYSVFPK WIRSYRDLPL KLNQWNTVVR WEFKQPTPFI RTREFLWQEG HTAHKNEEEA
430 440 450 460 470 480
VKLVFDILDL YRRWYEEYLA VPIIKGIKSE GEKFGGANFT STAEAFISEN GRAIQAATSH
490 500 510 520 530 540
YLGTNFAKMF KIEFEDENEV KQYVHQTSWG CTTRSIGIMI MTHGDDKGLV LPPNVSKYKV
550 560 570 580 590 600
VIVPIFYKTT DENAIHSYCK DIEKILKNAQ INCVYDDRAS YSPGYKFNHW ELRGIPIRIE
610 620 630 640 650 660
VGPKDLQNNS CVIVRRDNNE KCNVKKESVL LETQQMLVDI HKNLFLKAKK KLDDSIVQVT
670 680 690 700 710 720
SFSEVMNALN KKKMVLAPWC EDIATEEEIK KETQRLSLNQ TNSETTLSGA MKPLCIPLDQ
730 740
PPMPPNMKCF WSGKPAKRWC LFGRSY