UniProtKB - P13922 (DRTS_PLAFK)

BLAST

>sp|P13922|DRTS_PLAFK Bifunctional dihydrofolate reductase-thymidylate synthase OS=Plasmodium falciparum (isolate K1 / Thailand) OX=5839 PE=1 SV=2
MMEQVCDVFDIYAICACCKVESKNEGKKNEVFNNYTFRGLGNKGVLPWKCNSLDMKYFRA
VTTYVNESKYEKLKYKRCKYLNKETVDNVNDMPNSKKLQNVVVMGRTNWESIPKKFKPLS
NRINVILSRTLKKEDFDEDVYIINKVEDLIVLLGKLNYYKCFIIGGSVVYQEFLEKKLIK
KIYFTRINSTYECDVFFPEINENEYQIISVSDVYTSNNTTLDFIIYKKTNNKMLNEQNCI
KGEEKNNDMPLKNDDKDTCHMKKLTEFYKNVDKYKINYENDDDDEEEDDFVYFNFNKEKE
EKNKNSIHPNDFQIYNSLKYKYHPEYQYLNIIYDIMMNGNKQSDRTGVGVLSKFGYIMKF
DLSQYFPLLTTKKLFLRGIIEELLWFIRGETNGNTLLNKNVRIWEANGTREFLDNRKLFH
REVNDLGPIYGFQWRHFGAEYTNMYDNYENKGVDQLKNIINLIKNDPTSRRILLCAWNVK
DLDQMALPPCHILCQFYVFDGKLSCIMYQRSCDLGLGVPFNIASYSIFTHMIAQVCNLQP
AQFIHVLGNAHVYNNHIDSLKIQLNRIPYPFPTLKLNPDIKNIEDFTISDFTIQNYVHHE
KISMDMAA

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History
Entry version 120 (28 Feb 2018)
Sequence version 2 (01 Aug 1990)
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Protein

Bifunctional dihydrofolate reductase-thymidylate synthase

Gene

N/A

Organism

Plasmodium falciparum (isolate K1 / Thailand)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Bifunctional enzyme. Involved in de novo dTMP biosynthesis. Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, DNA precursor synthesis, and for the conversion of dUMP to dTMP.

Miscellaneous

K1 is from a pyrimethamine-resistant strain; FCR3 is a pyrimethamine-sensitive strain.

Catalytic activityⁱ

5,6,7,8-tetrahydrofolate + NADP⁺ = 7,8-dihydrofolate + NADPH.

5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP.

Pathwayⁱ: tetrahydrofolate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate.
Proteins known to be involved in this subpathway in this organism are:

Bifunctional dihydrofolate reductase-thymidylate synthase

This subpathway is part of the pathway tetrahydrofolate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5,6,7,8-tetrahydrofolate from 7,8-dihydrofolate, the pathway tetrahydrofolate biosynthesis and in Cofactor biosynthesis.

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	16	NADP; via amide nitrogen and carbonyl oxygen	1
Binding siteⁱ	31	Substrate; via carbonyl oxygenBy similarity	1
Binding siteⁱ	54	Substrate	1
Binding siteⁱ	108	Substrate	1
Binding siteⁱ	144	NADP; via carbonyl oxygen	1
Binding siteⁱ	164	Substrate; via carbonyl oxygen	1
Binding siteⁱ	170	Substrate	1
Binding siteⁱ	185	SubstrateBy similarity	1
Binding siteⁱ	345	dUMP	1
Active siteⁱ	490	By similarity	1
Binding siteⁱ	491	dUMP	1
Binding siteⁱ	521	dUMP	1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	39 – 45	NADP	7
Nucleotide bindingⁱ	106 – 108	NADP	3
Nucleotide bindingⁱ	128 – 130	NADP	3
Nucleotide bindingⁱ	165 – 172	NADP	8
Nucleotide bindingⁱ	509 – 513	dUMP	5
Nucleotide bindingⁱ	551 – 553	dUMP	3

GO - Molecular functionⁱ

dihydrofolate reductase activity Source: UniProtKB-EC
thymidylate synthase activity Source: UniProtKB-EC

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

dTMP biosynthetic process Source: InterPro
one-carbon metabolic process Source: UniProtKB-KW
tetrahydrofolate biosynthetic process Source: UniProtKB-UniPathway

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Methyltransferase, Multifunctional enzyme, Oxidoreductase, Transferase
Biological process	Nucleotide biosynthesis, One-carbon metabolism
Ligand	NADP

Enzyme and pathway databases

BRENDAⁱ	1.5.1.3 4889 2.1.1.45 4889
SABIO-RKⁱ	P13922
UniPathwayⁱ	UPA00077;UER00158

Protein family/group databases

MoonProtⁱ	P13922

MoonProtⁱ

P13922

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Bifunctional dihydrofolate reductase-thymidylate synthase Short name: DHFR-TS Including the following 2 domains: Dihydrofolate reductase (EC:1.5.1.3) Thymidylate synthase (EC:2.1.1.45)
Organismⁱ	Plasmodium falciparum (isolate K1 / Thailand)
Taxonomic identifierⁱ	5839 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodiidae › Plasmodium › Plasmodium (Laverania) › Plasmodium falciparum

Pathology & Biotechⁱ

Chemistry databases

ChEMBLⁱ	CHEMBL1939
Drug and drug target database More...DrugBankⁱ	DB01131 Proguanil DB00205 Pyrimethamine DB01299 Sulfadoxine

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000186349	1 – 608	Bifunctional dihydrofolate reductase-thymidylate synthaseAdd BLAST		608

Proteomic databases

PRIDEⁱ	P13922

PRIDEⁱ

P13922

Interactionⁱ

Subunit structureⁱ

Homodimer.1 Publication

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	5 – 8	Combined sources	4
Beta strandⁱ	11 – 20	Combined sources	10
Turnⁱ	23 – 25	Combined sources	3
Helixⁱ	27 – 29	Combined sources	3
Helixⁱ	34 – 36	Combined sources	3
Beta strandⁱ	37 – 42	Combined sources	6
Beta strandⁱ	47 – 49	Combined sources	3
Helixⁱ	52 – 63	Combined sources	12
Helixⁱ	67 – 81	Combined sources	15
Beta strandⁱ	101 – 105	Combined sources	5
Helixⁱ	106 – 111	Combined sources	6
Helixⁱ	114 – 116	Combined sources	3
Beta strandⁱ	122 – 127	Combined sources	6
Helixⁱ	133 – 135	Combined sources	3
Beta strandⁱ	141 – 145	Combined sources	5
Helixⁱ	146 – 155	Combined sources	10
Beta strandⁱ	161 – 163	Combined sources	3
Helixⁱ	167 – 175	Combined sources	9
Beta strandⁱ	180 – 191	Combined sources	12
Beta strandⁱ	194 – 196	Combined sources	3
Turnⁱ	202 – 204	Combined sources	3
Beta strandⁱ	205 – 210	Combined sources	6
Beta strandⁱ	214 – 216	Combined sources	3
Beta strandⁱ	219 – 228	Combined sources	10
Helixⁱ	285 – 293	Combined sources	9
Turnⁱ	294 – 296	Combined sources	3
Helixⁱ	304 – 307	Combined sources	4
Helixⁱ	309 – 312	Combined sources	4
Helixⁱ	313 – 317	Combined sources	5
Beta strandⁱ	319 – 321	Combined sources	3
Helixⁱ	325 – 338	Combined sources	14
Beta strandⁱ	340 – 342	Combined sources	3
Turnⁱ	346 – 348	Combined sources	3
Beta strandⁱ	350 – 361	Combined sources	12
Turnⁱ	362 – 364	Combined sources	3
Beta strandⁱ	370 – 372	Combined sources	3
Helixⁱ	377 – 387	Combined sources	11
Helixⁱ	393 – 397	Combined sources	5
Turnⁱ	398 – 400	Combined sources	3
Turnⁱ	403 – 405	Combined sources	3
Helixⁱ	406 – 408	Combined sources	3
Helixⁱ	410 – 415	Combined sources	6
Helixⁱ	430 – 436	Combined sources	7
Helixⁱ	455 – 465	Combined sources	11
Beta strandⁱ	473 – 475	Combined sources	3
Helixⁱ	479 – 484	Combined sources	6
Beta strandⁱ	485 – 487	Combined sources	3
Beta strandⁱ	490 – 499	Combined sources	10
Beta strandⁱ	502 – 513	Combined sources	12
Turnⁱ	514 – 516	Combined sources	3
Helixⁱ	517 – 535	Combined sources	19
Beta strandⁱ	539 – 553	Combined sources	15
Helixⁱ	554 – 556	Combined sources	3
Helixⁱ	557 – 563	Combined sources	7
Beta strandⁱ	573 – 576	Combined sources	4
Helixⁱ	583 – 585	Combined sources	3
Helixⁱ	588 – 590	Combined sources	3
Beta strandⁱ	591 – 594	Combined sources	4

Show more details

3D structure databases

ProteinModelPortalⁱ	P13922
SMRⁱ	P13922
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P13922

EvolutionaryTraceⁱ

P13922

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	10 – 228	DHFRAdd BLAST		219

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	14 – 15	Substrate binding		2
Regionⁱ	322 – 608	Thymidylate synthaseAdd BLAST		287

Sequence similaritiesⁱ

In the N-terminal section; belongs to the dihydrofolate reductase family.Curated

In the C-terminal section; belongs to the thymidylate synthase family.Curated

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00209 DHFR, 1 hit cd00351 TS_Pyrimidine_HMase, 1 hit
Gene3Dⁱ	3.30.572.10, 1 hit 3.40.430.10, 1 hit
HAMAPⁱ	MF_00008 Thymidy_synth_bact, 1 hit
InterProⁱ	View protein in InterPro IPR024072 DHFR-like_dom_sf IPR012262 DHFR-TS IPR017925 DHFR_CS IPR001796 DHFR_dom IPR023451 Thymidate_synth/dCMP_Mease IPR036926 Thymidate_synth/dCMP_Mease_sf IPR000398 Thymidylate_synthase IPR020940 Thymidylate_synthase_AS
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00186 DHFR_1, 1 hit PF00303 Thymidylat_synt, 1 hit
PIRSFⁱ	PIRSF000389 DHFR-TS, 1 hit
PRINTSⁱ	PR00108 THYMDSNTHASE
SUPFAMⁱ	SSF53597 SSF53597, 1 hit SSF55831 SSF55831, 1 hit
TIGRFAMsⁱ	TIGR03284 thym_sym, 1 hit
PROSITEⁱ	View protein in PROSITE PS00075 DHFR_1, 1 hit PS51330 DHFR_2, 1 hit PS00091 THYMIDYLATE_SYNTHASE, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P13922-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MMEQVCDVFD IYAICACCKV ESKNEGKKNE VFNNYTFRGL GNKGVLPWKC 
        60         70         80         90        100
NSLDMKYFRA VTTYVNESKY EKLKYKRCKY LNKETVDNVN DMPNSKKLQN 
       110        120        130        140        150
VVVMGRTNWE SIPKKFKPLS NRINVILSRT LKKEDFDEDV YIINKVEDLI 
       160        170        180        190        200
VLLGKLNYYK CFIIGGSVVY QEFLEKKLIK KIYFTRINST YECDVFFPEI 
       210        220        230        240        250
NENEYQIISV SDVYTSNNTT LDFIIYKKTN NKMLNEQNCI KGEEKNNDMP 
       260        270        280        290        300
LKNDDKDTCH MKKLTEFYKN VDKYKINYEN DDDDEEEDDF VYFNFNKEKE 
       310        320        330        340        350
EKNKNSIHPN DFQIYNSLKY KYHPEYQYLN IIYDIMMNGN KQSDRTGVGV 
       360        370        380        390        400
LSKFGYIMKF DLSQYFPLLT TKKLFLRGII EELLWFIRGE TNGNTLLNKN 
       410        420        430        440        450
VRIWEANGTR EFLDNRKLFH REVNDLGPIY GFQWRHFGAE YTNMYDNYEN 
       460        470        480        490        500
KGVDQLKNII NLIKNDPTSR RILLCAWNVK DLDQMALPPC HILCQFYVFD 
       510        520        530        540        550
GKLSCIMYQR SCDLGLGVPF NIASYSIFTH MIAQVCNLQP AQFIHVLGNA 
       560        570        580        590        600
HVYNNHIDSL KIQLNRIPYP FPTLKLNPDI KNIEDFTISD FTIQNYVHHE 

KISMDMAA

Length:608

Mass (Da):71,817

Last modified:August 1, 1990 - v2

Checksum:ⁱ7727EEB4A3946996

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱ	16	A → V in strain: Isolate Palo-Alto.	1
Natural variantⁱ	51	N → I.	1
Natural variantⁱ	59	R → C in strain: Isolate FCR-3, Isolate Gambia and Isolate Palo-Alto.	1
Natural variantⁱ	108	N → T in strain: Isolate FCR-3, Isolate Gambia and Isolate Palo-Alto.	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M22159 Genomic DNA Translation: AAA29580.1 J04643 Genomic DNA Translation: AAA29586.1 J03772 Genomic DNA Translation: AAB59212.1 J03028 Genomic DNA Translation: AAA29585.1
PIRⁱ	A39975 RDZQK1

Protein	Similar proteins		Species	Score	Length	Source
P13922	Bifunctional dihydrofolate reductase-thymidylate synthase		PLAFA		608	UniRef100_P13922
Bifunctional dihydrofolate reductase-thymidylate synthase (Fragment)		PLAFA		596
Bifunctional dihydrofolate reductase-thymidylate synthase (Fragment)		PLAFA		594
Bifunctional dihydrofolate reductase-thymidylate synthase (Fragment)		PLAFA		593
Bifunctional dihydrofolate reductase-thymidylate synthase (Fragment)		PLAFA		592
+28

Protein	Similar proteins		Species	Score	Length	Source
P13922	Bifunctional dihydrofolate reductase-thymidylate synthase		PLAFA		608	UniRef90_P13922
Bifunctional dihydrofolate reductase-thymidylate synthase		PLARE		610
Bifunctional dihydrofolate reductase-thymidylate synthase		PLAFO		608
Bifunctional dihydrofolate reductase-thymidylate synthase		PLAF7		608
Bifunctional dihydrofolate reductase-thymidylate synthase		Plasmodium falciparum IGH-CR14		607
+171

Protein	Similar proteins		Species	Score	Length	Source
P13922	Bifunctional dihydrofolate reductase-thymidylate synthase (Fragment)		PLAVN		182	UniRef50_P13922
Bifunctional dihydrofolate reductase-thymidylate synthase		PLACH		583
Bifunctional dihydrofolate reductase-thymidylate synthase	)	PLAVI		623
Bifunctional dihydrofolate reductase-thymidylate synthase		PLABA		587
Bifunctional dihydrofolate reductase-thymidylate synthase		PLAFA		608
+368

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M22159 Genomic DNA Translation: AAA29580.1 J04643 Genomic DNA Translation: AAA29586.1 J03772 Genomic DNA Translation: AAB59212.1 J03028 Genomic DNA Translation: AAA29585.1
PIRⁱ	A39975 RDZQK1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1J3I	X-ray	2.33	A/B	1-280	[»]
				C/D	281-608	[»]
	1J3J	X-ray	2.30	A/B	1-280	[»]
				C/D	281-608	[»]
	1J3K	X-ray	2.10	A/B	1-280	[»]
				C/D	281-608	[»]
	3DG8	X-ray	2.58	A/B	1-280	[»]
				C/D	281-608	[»]
	3DGA	X-ray	2.70	A/B	1-280	[»]
				C/D	281-608	[»]
ProteinModelPortalⁱ	P13922
SMRⁱ	P13922
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Chemistry databases

ChEMBLⁱ	CHEMBL1939
DrugBankⁱ	DB01131 Proguanil DB00205 Pyrimethamine DB01299 Sulfadoxine

Protein family/group databases

MoonProtⁱ	P13922

MoonProtⁱ

P13922

Proteomic databases

PRIDEⁱ	P13922

PRIDEⁱ

P13922

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Enzyme and pathway databases

UniPathwayⁱ	UPA00077;UER00158
BRENDAⁱ	1.5.1.3 4889 2.1.1.45 4889
SABIO-RKⁱ	P13922

Miscellaneous databases

EvolutionaryTraceⁱ	P13922

EvolutionaryTraceⁱ

P13922

Family and domain databases

CDDⁱ	cd00209 DHFR, 1 hit cd00351 TS_Pyrimidine_HMase, 1 hit
Gene3Dⁱ	3.30.572.10, 1 hit 3.40.430.10, 1 hit
HAMAPⁱ	MF_00008 Thymidy_synth_bact, 1 hit
InterProⁱ	View protein in InterPro IPR024072 DHFR-like_dom_sf IPR012262 DHFR-TS IPR017925 DHFR_CS IPR001796 DHFR_dom IPR023451 Thymidate_synth/dCMP_Mease IPR036926 Thymidate_synth/dCMP_Mease_sf IPR000398 Thymidylate_synthase IPR020940 Thymidylate_synthase_AS
Pfamⁱ	View protein in Pfam PF00186 DHFR_1, 1 hit PF00303 Thymidylat_synt, 1 hit
PIRSFⁱ	PIRSF000389 DHFR-TS, 1 hit
PRINTSⁱ	PR00108 THYMDSNTHASE
SUPFAMⁱ	SSF53597 SSF53597, 1 hit SSF55831 SSF55831, 1 hit
TIGRFAMsⁱ	TIGR03284 thym_sym, 1 hit
PROSITEⁱ	View protein in PROSITE PS00075 DHFR_1, 1 hit PS51330 DHFR_2, 1 hit PS00091 THYMIDYLATE_SYNTHASE, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	DRTS_PLAFK
Accessionⁱ	P13922Primary (citable) accession number: P13922 Secondary accession number(s): Q27734
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
	Last sequence update:	August 1, 1990
	Last modified:	February 28, 2018
	This is version 120 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)

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UniParc

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Supporting data

UniProtKB - P13922 (DRTS_PLAFK)

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Bifunctional dihydrofolate reductase-thymidylate synthase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: tetrahydrofolate biosynthesis

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Family and domain databases

Natural variant

Sequence databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Chemistry databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

Pathwayⁱ: tetrahydrofolate biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ