STRINGSTRING
SES63948.1 SES63948.1 rnhB rnhB recA recA SES69776.1 SES69776.1 lexA lexA recD2 recD2 SES97247.1 SES97247.1 dinB dinB SET16428.1 SET16428.1 SET29294.1 SET29294.1 SET36633.1 SET36633.1 sbcD sbcD SET45864.1 SET45864.1 topB topB SET72253.1 SET72253.1 polA polA
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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
SES63948.1Ribonuclease HI; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. (150 aa)
rnhBRNase HII; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. (203 aa)
recARecA protein; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family. (342 aa)
SES69776.1Stage V sporulation protein K. (324 aa)
lexASOS-response transcriptional repressor, LexA; 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. (208 aa)
recD2ATP-dependent DNA helicase, RecD/TraA family; DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase. Has no activity on blunt DNA or DNA with 3'-overhangs, requires at least 10 bases of 5'-ssDNA for helicase activity; Belongs to the RecD family. RecD-like subfamily. (743 aa)
SES97247.1ATP-dependent DNA helicase, RecQ-like. (604 aa)
dinBDNA polymerase-4; 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. (348 aa)
SET16428.1MutS domain V; Belongs to the DNA mismatch repair MutS family. (603 aa)
SET29294.1D-proline reductase (dithiol) PrdD. (254 aa)
SET36633.1Exonuclease SbcC. (1057 aa)
sbcDExodeoxyribonuclease I subunit D; SbcCD cleaves DNA hairpin structures. These structures can inhibit DNA replication and are intermediates in certain DNA recombination reactions. The complex acts as a 3'->5' double strand exonuclease that can open hairpins. It also has a 5' single-strand endonuclease activity; Belongs to the SbcD family. (427 aa)
SET45864.1LexA DNA binding domain-containing protein. (84 aa)
topBDNA topoisomerase-3; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supe [...] (730 aa)
SET72253.1DNA polymerase III, beta subunit; Confers DNA tethering and processivity to DNA polymerases and other proteins. Acts as a clamp, forming a ring around DNA (a reaction catalyzed by the clamp-loading complex) which diffuses in an ATP- independent manner freely and bidirectionally along dsDNA. Initially characterized for its ability to contact the catalytic subunit of DNA polymerase III (Pol III), a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria; Pol III exhibits 3'-5' exonuclease proofreading activity. The beta chain is required for initiation of [...] (366 aa)
polADNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity. (896 aa)
Your Current Organism:
Natronincola peptidivorans
NCBI taxonomy Id: 426128
Other names: DSM 18979, N. peptidivorans, Natronincola peptidivorans corrig. Zhilina et al. 2009, Natronincola peptidovorans, VKM B-2503, strain Z-7031
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