dtd protein (Clostridium saccharoperbutylacetonicum)

Nodes:

Network nodes represent proteins

splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.

Node Color

colored nodes:
query proteins and first shell of interactors

white nodes:
second shell of interactors

Node Content

empty nodes:
proteins of unknown 3D structure

filled nodes:
a 3D structure is known or predicted

Edges:

Edges represent protein-protein associations

associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.

Knowledge-based Evidence

from curated databases

textmining

Assay-based Predictions

experimentally determined

co-expression

Genomic Predictions

gene neighborhood

gene co-occurrence

gene fusions

Your Input:

Neighborhood

Gene Fusion

Co-occurrence

Co-expression

Experiments

Databases

Textmining

[Homology]

Score

dtd

D-tyrosyl-tRNA(Tyr) 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:

AQR95073.1

0.813

relA_2

0.796

aspS

0.627

hemZ

0.586

rny_4

0.579

mutS_2

0.566

apt

0.540

spoT

0.503

relA_1

0.499

hisS_2

0.472

Your Current Organism:

Clostridium saccharoperbutylacetonicum

NCBI taxonomy Id: 36745
Other names: ATCC 27021, C. saccharoperbutylacetonicum, Clostridium saccharoperbutylacetonicum Keis et al. 2001, DSM 14923, NCIMB 12606, strain N1-4 (HMT)

Export your current network:

... as a bitmap image:

download

file format is 'PNG': portable network graphic

... as a high-resolution bitmap:

download

same PNG format, but at higher resolution

... as a vector graphic:

download

SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc

... as short tabular text output:

download

TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)

... as tabular text output:

download

TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)

... as an XML summary:

download

structured XML interaction data, according to the 'PSI-MI' data standard

... protein node degrees:

download

node degree of proteins in your network (given the current score cut-off)

... network coordinates:

download

a flat-file format describing the coordinates and colors of nodes in the network

... protein sequences:

download

MFA: multi-fasta format - containing the aminoacid sequences in the network

... protein annotations:

download

a tab-delimited file describing the names, domains and descriptions of proteins in your network

... functional annotations:

download

a tab-delimited file containing all known functional terms of proteins in your network

Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
AQR95073.1	apt	CLSAP_23870	CLSAP_23840	Putative metallo-hydrolase.	Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.	0.523
AQR95073.1	aspS	CLSAP_23870	CLSAP_23900	Putative metallo-hydrolase.	aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.	0.499
AQR95073.1	dtd	CLSAP_23870	CLSAP_23860	Putative metallo-hydrolase.	D-tyrosyl-tRNA(Tyr) 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.	0.813
AQR95073.1	hemZ	CLSAP_23870	CLSAP_23880	Putative metallo-hydrolase.	Oxygen-independent coproporphyrinogen-III oxidase-like protein HemZ.	0.607
AQR95073.1	hisS_2	CLSAP_23870	CLSAP_23890	Putative metallo-hydrolase.	histidine--tRNA ligase.	0.427
AQR95073.1	relA_2	CLSAP_23870	CLSAP_23850	Putative metallo-hydrolase.	GTP pyrophosphokinase; 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.	0.685
apt	AQR95073.1	CLSAP_23840	CLSAP_23870	Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.	Putative metallo-hydrolase.	0.523
apt	aspS	CLSAP_23840	CLSAP_23900	Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.	aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.	0.459
apt	dtd	CLSAP_23840	CLSAP_23860	Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.	D-tyrosyl-tRNA(Tyr) 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.	0.540
apt	hemZ	CLSAP_23840	CLSAP_23880	Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.	Oxygen-independent coproporphyrinogen-III oxidase-like protein HemZ.	0.505
apt	relA_2	CLSAP_23840	CLSAP_23850	Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.	GTP pyrophosphokinase; 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.	0.640
aspS	AQR95073.1	CLSAP_23900	CLSAP_23870	aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.	Putative metallo-hydrolase.	0.499
aspS	apt	CLSAP_23900	CLSAP_23840	aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.	Adenine phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.	0.459
aspS	dtd	CLSAP_23900	CLSAP_23860	aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.	D-tyrosyl-tRNA(Tyr) 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.	0.627
aspS	hemZ	CLSAP_23900	CLSAP_23880	aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.	Oxygen-independent coproporphyrinogen-III oxidase-like protein HemZ.	0.489
aspS	hisS_2	CLSAP_23900	CLSAP_23890	aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.	histidine--tRNA ligase.	0.914
aspS	relA_2	CLSAP_23900	CLSAP_23850	aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.	GTP pyrophosphokinase; 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.	0.449
dtd	AQR95073.1	CLSAP_23860	CLSAP_23870	D-tyrosyl-tRNA(Tyr) 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.	Putative metallo-hydrolase.	0.813
dtd	apt	CLSAP_23860	CLSAP_23840	D-tyrosyl-tRNA(Tyr) 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 phosphoribosyltransferase; Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.	0.540
dtd	aspS	CLSAP_23860	CLSAP_23900	D-tyrosyl-tRNA(Tyr) 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.	aspartate--tRNA ligase; Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp). Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.	0.627

page 1 of 3

Server load: medium (52%) [HD]

Permalink

Network

Neighborhood

Experiments

Co-occurrence

Databases

Co-expression

Textmining

Fusion

© STRING Consortium 2026

Credits

Access

Info

About