STRINGSTRING
SES69776.1 SES69776.1 recD2 recD2 SES97247.1 SES97247.1 SET16428.1 SET16428.1 SET29294.1 SET29294.1 SET36633.1 SET36633.1 sbcD sbcD 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
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
Your Input:
SES69776.1Stage V sporulation protein K. (324 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)
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)
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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