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UniProtKB - Q8I5R7 (SYP_PLAF7)
Protein
Proline--tRNA ligase
Gene
proRS
Organism
Plasmodium falciparum (isolate 3D7)
Status
Functioni
Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro) (PubMed:25817387, PubMed:27798837).
Functions in trans to edit the amino acid moiety from incorrectly charged Ala-tRNA(Pro) (PubMed:14663147).
Has no activity on correctly charged Pro-tRNA(Pro) or Ala-tRNA(Ala) (PubMed:14663147).
3 PublicationsCatalytic activityi
- EC:6.1.1.152 Publications
Activity regulationi
Inhibited by the quinazolinone-based compound febrifugine from the Chinese plant Dichroa febrifuga which is used to treat malaria-associated fever (PubMed:25817387, PubMed:27798837). Also inhibited by febrifugine derivatives such as halofuginone (PubMed:25817387, PubMed:27798837).2 Publications
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 390 | L-prolineCombined sources1 Publication | 1 | |
Binding sitei | 480 | L-prolineCombined sources1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 390 – 394 | ATPCombined sources3 Publications | 5 | |
Nucleotide bindingi | 401 – 405 | ATPCombined sources3 Publications | 5 | |
Nucleotide bindingi | 475 – 477 | ATPCombined sources3 Publications | 3 | |
Nucleotide bindingi | 512 – 514 | ATPCombined sources3 Publications | 3 |
GO - Molecular functioni
- Ala-tRNA(Pro) hydrolase activity Source: UniProtKB
- ATP binding Source: UniProtKB-KW
- proline-tRNA ligase activity Source: GeneDB
GO - Biological processi
- prolyl-tRNA aminoacylation Source: GO_Central
- tRNA aminoacylation for protein translation Source: GeneDB
Keywordsi
Molecular function | Aminoacyl-tRNA synthetase, Ligase |
Biological process | Protein biosynthesis |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 6.1.1.15, 4889 |
Names & Taxonomyi
Protein namesi | Recommended name: Proline--tRNA ligase (EC:6.1.1.152 Publications)Short name: PfPRS1 Publication Alternative name(s): Prolyl-tRNA synthetase1 Publication Short name: PfProRS1 Publication |
Gene namesi | Name:proRS1 Publication Synonyms:PRS1 Publication ORF Names:PF3D7_1213800, PFL0670c |
Organismi | Plasmodium falciparum (isolate 3D7) |
Taxonomic identifieri | 36329 [NCBI] |
Taxonomic lineagei | Eukaryota › Sar › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodiidae › Plasmodium › Plasmodium (Laverania) › |
Proteomesi |
|
Organism-specific databases
VEuPathDBi | PlasmoDB:PF3D7_1213800 |
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Other locations
- aminoacyl-tRNA synthetase multienzyme complex Source: GO_Central
- cytoplasm Source: GeneDB
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000392534 | 1 – 746 | Proline--tRNA ligaseAdd BLAST | 746 |
Proteomic databases
PRIDEi | Q8I5R7 |
Expressioni
Developmental stagei
Expressed during the asexual blood stage including at the ring stage and in trophozoites and schizonts (at protein level).1 Publication
Interactioni
Subunit structurei
Homodimer.
2 PublicationsProtein-protein interaction databases
DIPi | DIP-61496N |
STRINGi | 5833.PFL0670c |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q8I5R7 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 223 | Required for editing of incorrectly charged tRNA1 PublicationAdd BLAST | 223 | |
Regioni | 181 – 226 | DisorderedSequence analysisAdd BLAST | 46 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 181 – 198 | Basic and acidic residuesSequence analysisAdd BLAST | 18 | |
Compositional biasi | 199 – 226 | Polar residuesSequence analysisAdd BLAST | 28 |
Domaini
Consists of four domains: the N-terminal editing domain, the N-terminal catalytic domain, the anticodon-binding domain and the C-terminal extension (Probable). The first domain (about residues 1-163) is required for editing of incorrectly charged tRNA (PubMed:14663147). When it is deleted the enzyme shows pronounced misacylation of tRNA(Pro) with alanine (PubMed:14663147).1 Publication1 Publication
Sequence similaritiesi
Phylogenomic databases
HOGENOMi | CLU_001882_4_1_1 |
InParanoidi | Q8I5R7 |
OMAi | EVYWVTH |
PhylomeDBi | Q8I5R7 |
Family and domain databases
CDDi | cd00778, ProRS_core_arch_euk, 1 hit |
Gene3Di | 3.30.110.30, 1 hit 3.30.930.10, 1 hit 3.40.50.800, 1 hit 3.90.960.10, 1 hit |
HAMAPi | MF_01571, Pro_tRNA_synth_type3, 1 hit |
InterProi | View protein in InterPro IPR002314, aa-tRNA-synt_IIb IPR006195, aa-tRNA-synth_II IPR045864, aa-tRNA-synth_II/BPL/LPL IPR004154, Anticodon-bd IPR036621, Anticodon-bd_dom_sf IPR002316, Pro-tRNA-ligase_IIa IPR004499, Pro-tRNA-ligase_IIa_arc-type IPR016061, Pro-tRNA_ligase_II_C IPR017449, Pro-tRNA_synth_II IPR033721, ProRS_core_arch_euk IPR036754, YbaK/aa-tRNA-synt-asso_dom_sf IPR007214, YbaK/aa-tRNA-synth-assoc-dom |
PANTHERi | PTHR43382, PTHR43382, 1 hit |
Pfami | View protein in Pfam PF03129, HGTP_anticodon, 1 hit PF09180, ProRS-C_1, 1 hit PF00587, tRNA-synt_2b, 1 hit PF04073, tRNA_edit, 1 hit |
PRINTSi | PR01046, TRNASYNTHPRO |
SMARTi | View protein in SMART SM00946, ProRS-C_1, 1 hit |
SUPFAMi | SSF55681, SSF55681, 1 hit SSF55826, SSF55826, 1 hit SSF64586, SSF64586, 1 hit |
TIGRFAMsi | TIGR00408, proS_fam_I, 1 hit |
PROSITEi | View protein in PROSITE PS50862, AA_TRNA_LIGASE_II, 1 hit |
i Sequence
Sequence statusi: Complete.
Q8I5R7-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MNNNTNGEII IPQEYLEKSE CLFKELKELN INFKEVKHGL AATIKDLLEM
60 70 80 90 100
NLENSTNILK NLFLKDKKKN YFLICTLNNK TVDLKNLSNI LKTNNLRFVD
110 120 130 140 150
ENNLNNILNI QPGCLSPLAI KNDKENIVKL YFDEEIKNMQ EVIIHPLHNY
160 170 180 190 200
SSLYIKTQDV IKFCESFNHA PEYVQIKEDT TSKARVDKKE DVQEEMAKNE
210 220 230 240 250
ELQNNNNNNK NNSNSNNNNN NNNNHIKDTI LKGKLLSNNE VEDNKSKDSN
260 270 280 290 300
ILGITSKKIE NFSDWYTQVI VKSELIEYYD ISGCYILRPA AYYIWECVQA
310 320 330 340 350
FFNKEIKKLN VENSYFPLFV TKNKLEKEKN HIEGFSPEVA WVTKYGDSNL
360 370 380 390 400
PEEIAIRPTS ETIMYSVFPK WIRSYRDLPL KLNQWNTVVR WEFKQPTPFI
410 420 430 440 450
RTREFLWQEG HTAHKNEEEA VKLVFDILDL YRRWYEEYLA VPIIKGIKSE
460 470 480 490 500
GEKFGGANFT STAEAFISEN GRAIQAATSH YLGTNFAKMF KIEFEDENEV
510 520 530 540 550
KQYVHQTSWG CTTRSIGIMI MTHGDDKGLV LPPNVSKYKV VIVPIFYKTT
560 570 580 590 600
DENAIHSYCK DIEKILKNAQ INCVYDDRAS YSPGYKFNHW ELRGIPIRIE
610 620 630 640 650
VGPKDLQNNS CVIVRRDNNE KCNVKKESVL LETQQMLVDI HKNLFLKAKK
660 670 680 690 700
KLDDSIVQVT SFSEVMNALN KKKMVLAPWC EDIATEEEIK KETQRLSLNQ
710 720 730 740
TNSETTLSGA MKPLCIPLDQ PPMPPNMKCF WSGKPAKRWC LFGRSY
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | LN999947 Genomic DNA Translation: CZT99299.1 |
RefSeqi | XP_001350543.1, XM_001350507.1 |
Genome annotation databases
EnsemblProtistsi | CZT99299; CZT99299; PF3D7_1213800 |
GeneIDi | 811187 |
KEGGi | pfa:PF3D7_1213800 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | LN999947 Genomic DNA Translation: CZT99299.1 |
RefSeqi | XP_001350543.1, XM_001350507.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4NCX | X-ray | 1.85 | A/B | 249-746 | [»] | |
4OLF | X-ray | 2.90 | A | 249-746 | [»] | |
4Q15 | X-ray | 2.35 | A/B | 249-746 | [»] | |
4TWA | X-ray | 3.00 | A/B | 254-746 | [»] | |
4WI1 | X-ray | 1.65 | A/B | 249-746 | [»] | |
4YDQ | X-ray | 2.30 | A/B | 254-746 | [»] | |
5IFU | X-ray | 2.45 | A/B | 249-746 | [»] | |
6T7K | X-ray | 1.79 | A | 249-746 | [»] | |
SMRi | Q8I5R7 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
DIPi | DIP-61496N |
STRINGi | 5833.PFL0670c |
Chemistry databases
ChEMBLi | CHEMBL3301560 |
Proteomic databases
PRIDEi | Q8I5R7 |
Genome annotation databases
EnsemblProtistsi | CZT99299; CZT99299; PF3D7_1213800 |
GeneIDi | 811187 |
KEGGi | pfa:PF3D7_1213800 |
Organism-specific databases
VEuPathDBi | PlasmoDB:PF3D7_1213800 |
Phylogenomic databases
HOGENOMi | CLU_001882_4_1_1 |
InParanoidi | Q8I5R7 |
OMAi | EVYWVTH |
PhylomeDBi | Q8I5R7 |
Enzyme and pathway databases
BRENDAi | 6.1.1.15, 4889 |
Family and domain databases
CDDi | cd00778, ProRS_core_arch_euk, 1 hit |
Gene3Di | 3.30.110.30, 1 hit 3.30.930.10, 1 hit 3.40.50.800, 1 hit 3.90.960.10, 1 hit |
HAMAPi | MF_01571, Pro_tRNA_synth_type3, 1 hit |
InterProi | View protein in InterPro IPR002314, aa-tRNA-synt_IIb IPR006195, aa-tRNA-synth_II IPR045864, aa-tRNA-synth_II/BPL/LPL IPR004154, Anticodon-bd IPR036621, Anticodon-bd_dom_sf IPR002316, Pro-tRNA-ligase_IIa IPR004499, Pro-tRNA-ligase_IIa_arc-type IPR016061, Pro-tRNA_ligase_II_C IPR017449, Pro-tRNA_synth_II IPR033721, ProRS_core_arch_euk IPR036754, YbaK/aa-tRNA-synt-asso_dom_sf IPR007214, YbaK/aa-tRNA-synth-assoc-dom |
PANTHERi | PTHR43382, PTHR43382, 1 hit |
Pfami | View protein in Pfam PF03129, HGTP_anticodon, 1 hit PF09180, ProRS-C_1, 1 hit PF00587, tRNA-synt_2b, 1 hit PF04073, tRNA_edit, 1 hit |
PRINTSi | PR01046, TRNASYNTHPRO |
SMARTi | View protein in SMART SM00946, ProRS-C_1, 1 hit |
SUPFAMi | SSF55681, SSF55681, 1 hit SSF55826, SSF55826, 1 hit SSF64586, SSF64586, 1 hit |
TIGRFAMsi | TIGR00408, proS_fam_I, 1 hit |
PROSITEi | View protein in PROSITE PS50862, AA_TRNA_LIGASE_II, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | SYP_PLAF7 | |
Accessioni | Q8I5R7Primary (citable) accession number: Q8I5R7 Secondary accession number(s): A0A144A0G8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 23, 2010 |
Last sequence update: | March 1, 2003 | |
Last modified: | February 23, 2022 | |
This is version 124 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Aminoacyl-tRNA synthetases
List of aminoacyl-tRNA synthetase entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families