Dtd protein (Pelotomaculum thermopropionicum)

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Dtd

D-Tyr-tRNAtyr deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family. (149 aa)

Predicted Functional Partners:

SpoT

0.886

PTH_1043

0.816

GloB-2

0.803

Apt

0.782

ArsR-6

0.689

MMT1

0.559

AspS

0.418

PheA

0.416

PTH_1236

0.411

rny

0.409

Your Current Organism:

Pelotomaculum thermopropionicum

NCBI taxonomy Id: 370438
Other names: P. thermopropionicum SI, Pelotomaculum thermopropionicum SI, Pelotomaculum thermopropionicum str. SI, Pelotomaculum thermopropionicum strain SI

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
Apt	ArsR-6	PTH_1044	PTH_1042	Adenine/guanine phosphoribosyltransferases and related PRPP-binding proteins; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.	Predicted transcriptional regulator.	0.779
Apt	Dtd	PTH_1044	PTH_1046	Adenine/guanine phosphoribosyltransferases and related PRPP-binding proteins; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.	D-Tyr-tRNAtyr deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family.	0.782
Apt	GloB-2	PTH_1044	PTH_1047	Adenine/guanine phosphoribosyltransferases and related PRPP-binding proteins; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.	Zn-dependent hydrolases; Including glyoxylases.	0.741
Apt	MMT1	PTH_1044	PTH_1041	Adenine/guanine phosphoribosyltransferases and related PRPP-binding proteins; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.	Predicted Co/Zn/Cd cation transporters; Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family.	0.607
Apt	PTH_1043	PTH_1044	PTH_1043	Adenine/guanine phosphoribosyltransferases and related PRPP-binding proteins; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.	Hypothetical protein; Containing RecJ, Single-stranded DNA-specific exonuclease domain (COG0608) and HELICc, Helicase superfamily c-terminal domain.	0.833
Apt	PTH_1236	PTH_1044	PTH_1236	Adenine/guanine phosphoribosyltransferases and related PRPP-binding proteins; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.	Hypothetical protein; Containing COG0517and COG0617 domains; Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.	0.506
Apt	SpoT	PTH_1044	PTH_1045	Adenine/guanine phosphoribosyltransferases and related PRPP-binding proteins; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.	Guanosine polyphosphate pyrophosphohydrolases/synthetases; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance.	0.827
ArsR-6	Apt	PTH_1042	PTH_1044	Predicted transcriptional regulator.	Adenine/guanine phosphoribosyltransferases and related PRPP-binding proteins; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.	0.779
ArsR-6	Dtd	PTH_1042	PTH_1046	Predicted transcriptional regulator.	D-Tyr-tRNAtyr deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family.	0.689
ArsR-6	GloB-2	PTH_1042	PTH_1047	Predicted transcriptional regulator.	Zn-dependent hydrolases; Including glyoxylases.	0.637
ArsR-6	MMT1	PTH_1042	PTH_1041	Predicted transcriptional regulator.	Predicted Co/Zn/Cd cation transporters; Belongs to the cation diffusion facilitator (CDF) transporter (TC 2.A.4) family.	0.556
ArsR-6	PTH_1043	PTH_1042	PTH_1043	Predicted transcriptional regulator.	Hypothetical protein; Containing RecJ, Single-stranded DNA-specific exonuclease domain (COG0608) and HELICc, Helicase superfamily c-terminal domain.	0.773
ArsR-6	SpoT	PTH_1042	PTH_1045	Predicted transcriptional regulator.	Guanosine polyphosphate pyrophosphohydrolases/synthetases; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance.	0.734
AspS	Dtd	PTH_1049	PTH_1046	aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.	D-Tyr-tRNAtyr deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family.	0.418
AspS	PTH_1236	PTH_1049	PTH_1236	aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.	Hypothetical protein; Containing COG0517and COG0617 domains; Belongs to the tRNA nucleotidyltransferase/poly(A) polymerase family.	0.414
AspS	PheA	PTH_1049	PTH_0518	aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.	Prephenate dehydratase.	0.484
Dtd	Apt	PTH_1046	PTH_1044	D-Tyr-tRNAtyr deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family.	Adenine/guanine phosphoribosyltransferases and related PRPP-binding proteins; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.	0.782
Dtd	ArsR-6	PTH_1046	PTH_1042	D-Tyr-tRNAtyr deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family.	Predicted transcriptional regulator.	0.689
Dtd	AspS	PTH_1046	PTH_1049	D-Tyr-tRNAtyr deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family.	aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.	0.418
Dtd	GloB-2	PTH_1046	PTH_1047	D-Tyr-tRNAtyr deacylase; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the DTD family.	Zn-dependent hydrolases; Including glyoxylases.	0.803

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