mma_1960 protein (Janthinobacterium sp. Marseille)

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[Homology]

Score

mma_1960

Uncharacterized conserved protein. (255 aa)

Predicted Functional Partners:

mma_1912

0.985

dinP

0.875

dnaE2

0.860

lexA

0.615

mma_3202

0.540

rseB

0.497

mma_1958

0.493

mma_1959

0.493

mma_1961

0.489

mma_1962

0.489

Your Current Organism:

Janthinobacterium sp. Marseille

NCBI taxonomy Id: 375286
Other names: J. sp. Marseille, Minibacterium massiliensis

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
dinP	dnaE2	mma_3585	mma_1913	DNA-damage-inducible protein p; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	DNA polymerase III alpha subunit; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). It is not the major replicative DNA polymerase.	0.470
dinP	lexA	mma_3585	mma_1300	DNA-damage-inducible protein p; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	LexA transcription regulation repressor; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.	0.898
dinP	mma_1960	mma_3585	mma_1960	DNA-damage-inducible protein p; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	Uncharacterized conserved protein.	0.875
dnaE2	dinP	mma_1913	mma_3585	DNA polymerase III alpha subunit; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). It is not the major replicative DNA polymerase.	DNA-damage-inducible protein p; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	0.470
dnaE2	lexA	mma_1913	mma_1300	DNA polymerase III alpha subunit; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). It is not the major replicative DNA polymerase.	LexA transcription regulation repressor; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.	0.448
dnaE2	mma_1912	mma_1913	mma_1912	DNA polymerase III alpha subunit; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). It is not the major replicative DNA polymerase.	Uncharacterized conserved protein.	0.964
dnaE2	mma_1960	mma_1913	mma_1960	DNA polymerase III alpha subunit; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). It is not the major replicative DNA polymerase.	Uncharacterized conserved protein.	0.860
lexA	dinP	mma_1300	mma_3585	LexA transcription regulation repressor; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.	DNA-damage-inducible protein p; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	0.898
lexA	dnaE2	mma_1300	mma_1913	LexA transcription regulation repressor; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.	DNA polymerase III alpha subunit; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). It is not the major replicative DNA polymerase.	0.448
lexA	mma_1912	mma_1300	mma_1912	LexA transcription regulation repressor; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.	Uncharacterized conserved protein.	0.806
lexA	mma_1960	mma_1300	mma_1960	LexA transcription regulation repressor; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.	Uncharacterized conserved protein.	0.615
mma_1912	dnaE2	mma_1912	mma_1913	Uncharacterized conserved protein.	DNA polymerase III alpha subunit; DNA polymerase involved in damage-induced mutagenesis and translesion synthesis (TLS). It is not the major replicative DNA polymerase.	0.964
mma_1912	lexA	mma_1912	mma_1300	Uncharacterized conserved protein.	LexA transcription regulation repressor; Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.	0.806
mma_1912	mma_1960	mma_1912	mma_1960	Uncharacterized conserved protein.	Uncharacterized conserved protein.	0.985
mma_1912	rseB	mma_1912	mma_1364	Uncharacterized conserved protein.	sigma-E factor negative regulatory protein RseB.	0.507
mma_1958	mma_1959	mma_1958	mma_1959	ABC-type transport system involved in resistance to organic solvents, periplasmic component.	Uncharacterized conserved protein.	0.842
mma_1958	mma_1960	mma_1958	mma_1960	ABC-type transport system involved in resistance to organic solvents, periplasmic component.	Uncharacterized conserved protein.	0.493
mma_1959	mma_1958	mma_1959	mma_1958	Uncharacterized conserved protein.	ABC-type transport system involved in resistance to organic solvents, periplasmic component.	0.842
mma_1959	mma_1960	mma_1959	mma_1960	Uncharacterized conserved protein.	Uncharacterized conserved protein.	0.493
mma_1960	dinP	mma_1960	mma_3585	Uncharacterized conserved protein.	DNA-damage-inducible protein p; Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.	0.875