pepQ1 protein (Methanosarcina acetivorans) - STRING interaction network

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Score

pepQ1

Xaa-Pro dipeptidase (cobalt-dependent). (388 aa)

Predicted Functional Partners:

map

0.909

hisC

0.823

hisC-2

0.823

aspB

0.683

gatA

0.671

pepN

0.616

adk

0.574

rpiA

0.565

phoA

0.515

ahpC

0.501

Your Current Organism:

Methanosarcina acetivorans

NCBI taxonomy Id: 188937
Other names: M. acetivorans C2A, Methanosarcina acetivorans C2A, Methanosarcina acetivorans str. C2A

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
adk	map	MA_1096	MA_0212	Adenylate kinase; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism; Belongs to the adenylate kinase family.	Methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val); Belongs to the peptidase M24A family. Methionine aminopeptidase archaeal type 2 subfamily.	0.922
adk	pepQ1	MA_1096	MA_4232	Adenylate kinase; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism; Belongs to the adenylate kinase family.	Xaa-Pro dipeptidase (cobalt-dependent).	0.574
ahpC	pepQ1	MA_4103	MA_4232	Peroxiredoxin (alkyl hydroperoxide reductase); Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.	Xaa-Pro dipeptidase (cobalt-dependent).	0.501
aspB	hisC	MA_1819	MA_0118	Aspartate aminotransferase.	Histidinol-phosphate aminotransferase.	0.952
aspB	hisC-2	MA_1819	MA_0942	Aspartate aminotransferase.	Histidinol-phosphate aminotransferase.	0.535
aspB	map	MA_1819	MA_0212	Aspartate aminotransferase.	Methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val); Belongs to the peptidase M24A family. Methionine aminopeptidase archaeal type 2 subfamily.	0.623
aspB	pepN	MA_1819	MA_1605	Aspartate aminotransferase.	Membrane alanine aminopeptidase.	0.825
aspB	pepQ1	MA_1819	MA_4232	Aspartate aminotransferase.	Xaa-Pro dipeptidase (cobalt-dependent).	0.683
gatA	pepQ1	MA_4523	MA_4232	glutamyl-tRNA (Gln) amidotransferase, subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln).	Xaa-Pro dipeptidase (cobalt-dependent).	0.671
hisC	aspB	MA_0118	MA_1819	Histidinol-phosphate aminotransferase.	Aspartate aminotransferase.	0.952
hisC	map	MA_0118	MA_0212	Histidinol-phosphate aminotransferase.	Methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val); Belongs to the peptidase M24A family. Methionine aminopeptidase archaeal type 2 subfamily.	0.908
hisC	pepQ1	MA_0118	MA_4232	Histidinol-phosphate aminotransferase.	Xaa-Pro dipeptidase (cobalt-dependent).	0.823
hisC-2	aspB	MA_0942	MA_1819	Histidinol-phosphate aminotransferase.	Aspartate aminotransferase.	0.535
hisC-2	map	MA_0942	MA_0212	Histidinol-phosphate aminotransferase.	Methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val); Belongs to the peptidase M24A family. Methionine aminopeptidase archaeal type 2 subfamily.	0.832
hisC-2	pepQ1	MA_0942	MA_4232	Histidinol-phosphate aminotransferase.	Xaa-Pro dipeptidase (cobalt-dependent).	0.823
map	adk	MA_0212	MA_1096	Methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val); Belongs to the peptidase M24A family. Methionine aminopeptidase archaeal type 2 subfamily.	Adenylate kinase; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism; Belongs to the adenylate kinase family.	0.922
map	aspB	MA_0212	MA_1819	Methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val); Belongs to the peptidase M24A family. Methionine aminopeptidase archaeal type 2 subfamily.	Aspartate aminotransferase.	0.623
map	hisC	MA_0212	MA_0118	Methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val); Belongs to the peptidase M24A family. Methionine aminopeptidase archaeal type 2 subfamily.	Histidinol-phosphate aminotransferase.	0.908
map	hisC-2	MA_0212	MA_0942	Methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val); Belongs to the peptidase M24A family. Methionine aminopeptidase archaeal type 2 subfamily.	Histidinol-phosphate aminotransferase.	0.832
map	pepN	MA_0212	MA_1605	Methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val); Belongs to the peptidase M24A family. Methionine aminopeptidase archaeal type 2 subfamily.	Membrane alanine aminopeptidase.	0.570