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dnaA dnaA Sps_00035 Sps_00035 recF recF Sps_00071 Sps_00071 polA polA Sps_00240 Sps_00240 Sps_00496 Sps_00496 Sps_00522 Sps_00522 uvrC uvrC Sps_00626 Sps_00626 Sps_00663 Sps_00663 Sps_00798 Sps_00798 Sps_00863 Sps_00863 uvrB uvrB ruvB ruvB ruvA ruvA ruvC ruvC Sps_01166 Sps_01166 dnaQ dnaQ rnhA rnhA Sps_01307 Sps_01307 Sps_01379 Sps_01379 Sps_01387 Sps_01387 Sps_01645 Sps_01645 topA topA Sps_01671 Sps_01671 topB topB Sps_01833 Sps_01833 sbcD sbcD Sps_01855 Sps_01855 dinG dinG Sps_02003 Sps_02003 Sps_02117 Sps_02117 rnhB rnhB Sps_02227 Sps_02227 Sps_02935 Sps_02935 uvrA uvrA rep rep Sps_03138 Sps_03138 Sps_03223 Sps_03223 Sps_03292 Sps_03292 recG recG Sps_03431 Sps_03431 Sps_03444 Sps_03444 ligA ligA recA recA mutS mutS Sps_04138 Sps_04138 Sps_04227 Sps_04227 Sps_04371 Sps_04371 Sps_04600 Sps_04600 mutL mutL Sps_05174 Sps_05174 rapA rapA priA priA
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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experimentally determined
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dnaAChromosomal replication initiator protein DnaA; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'- TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids. Belongs to the DnaA family. (462 aa)
Sps_00035DNA 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)
recFDNA replication and repair protein RecF; The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP; Belongs to the RecF family. (365 aa)
Sps_00071PFAM: DNA recombination-mediator protein A; TIGRFAM: DNA protecting protein DprA. (331 aa)
polADNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity; Belongs to the DNA polymerase type-A family. (917 aa)
Sps_00240Putative amidophosphoribosyltransferase; PFAM: Phosphoribosyl transferase domain; TIGRFAM: comF family protein. (258 aa)
Sps_00496Hypothetical protein; PFAM: RecX family. (270 aa)
Sps_00522DNA/RNA helicase, superfamily II; 'PFAM: Helicase conserved C-terminal domain; Type III restriction enzyme, res subunit'. (592 aa)
uvrCExcinuclease ABC subunit C; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision. (609 aa)
Sps_00626PFAM: Bacterial dnaA protein; TIGRFAM: DnaA regulatory inactivator Hda; Belongs to the DnaA family. (236 aa)
Sps_00663PFAM: Exonuclease; 'TIGRFAM: exonuclease, DNA polymerase III, epsilon subunit family'. (206 aa)
Sps_00798ATP-dependent DNA helicase, RecQ-like; PFAM: Helicase conserved C-terminal domain; DEAD/DEAH box helicase; 'TIGRFAM: ATP-dependent DNA helicase, RecQ family'. (654 aa)
Sps_00863PFAM: UvrD/REP helicase N-terminal domain. (989 aa)
uvrBExcinuclease ABC subunit B; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB and probably causes local melting of the DNA helix, facilitating insertion of UvrB beta-hairpin between the DNA strands. Then UvrB probes one DNA strand for the presence of a lesion. If a lesion is found the UvrA subunits dissociate [...] (671 aa)
ruvBHolliday junction DNA helicase subunit RuvB; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. (339 aa)
ruvAHolliday junction DNA helicase subunit RuvA; The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. (205 aa)
ruvCHolliday junction endonuclease RuvC; Nuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves the cruciform structure in supercoiled DNA by nicking to strands with the same polarity at sites symmetrically opposed at the junction in the homologous arms and leaves a 5'-terminal phosphate and a 3'-terminal hydroxyl group. (173 aa)
Sps_01166PFAM: Transcriptional regulator; 'TIGRFAM: DNA-binding regulatory protein, YebC/PmpR family'. (248 aa)
dnaQDNA polymerase III, epsilon subunit; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'- 5' exonuclease. (242 aa)
rnhARibonuclease HI; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. (154 aa)
Sps_01307DNA helicase, Rad3; PFAM: Helicase C-terminal domain; DEAD/DEAH box helicase. (644 aa)
Sps_01379PFAM: DNA ligase OB-like domain; ATP dependent DNA ligase domain. (285 aa)
Sps_01387'PFAM: DNA polymerase III, delta subunit'; 'TIGRFAM: DNA polymerase III, delta' subunit'. (304 aa)
Sps_01645DNA internalization-related competence protein ComEC/Rec2; PFAM: Competence protein; Domain of unknown function (DUF4131); Metallo-beta-lactamase superfamily; TIGRFAM: ComEC/Rec2-related protein; DNA internalization-related competence protein ComEC/Rec2. (763 aa)
topADNA topoisomerase I; 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 [...] (919 aa)
Sps_01671'PFAM: DNA polymerase III tau subunit V interacting with alpha; DNA polymerase III subunits gamma and tau domain III; DNA polymerase III, delta subunit'; 'TIGRFAM: DNA polymerase III, delta' subunit; DNA polymerase III, subunit gamma and tau'. (940 aa)
topBDNA topoisomerase III; 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 su [...] (649 aa)
Sps_01833ATPase involved in DNA repair; 'PFAM: AAA domain; Putative exonuclease SbcCD, C subunit'; TIGRFAM: exonuclease SbcC. (1018 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. (381 aa)
Sps_01855'PFAM: DNA polymerase family B; DNA polymerase family B, exonuclease domain'. (811 aa)
dinGDNA helicase, Rad3; DNA-dependent ATPase and 5'-3' DNA helicase. (701 aa)
Sps_02003Ribonuclease HI; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. (255 aa)
Sps_02117PFAM: Bacterial DNA polymerase III alpha subunit; PHP domain; OB-fold nucleic acid binding domain; Helix-hairpin-helix motif; TIGRFAM: DNA-directed DNA polymerase III (polc). (1157 aa)
rnhBRNase HII; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids. (218 aa)
Sps_02227'PFAM: 5'-3' exonuclease, C-terminal SAM fold; 5'-3' exonuclease, N-terminal resolvase-like domain'. (252 aa)
Sps_02935Single-strand binding protein; Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. (238 aa)
uvrAExcinuclease ABC subunit A; The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrA is an ATPase and a DNA-binding protein. A damage recognition complex composed of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. When the presence of a lesion has been verified by UvrB, the UvrA molecules dissociate. (944 aa)
repATP-dependent DNA helicase Rep; Rep helicase is a single-stranded DNA-dependent ATPase involved in DNA replication; it can initiate unwinding at a nick in the DNA. It binds to the single-stranded DNA and acts in a progressive fashion along the DNA in the 3' to 5' direction. (670 aa)
Sps_03138PFAM: UvrD-like helicase C-terminal domain; UvrD/REP helicase N-terminal domain; TIGRFAM: DNA helicase II. (721 aa)
Sps_03223Mg chelatase-related protein; 'PFAM: Magnesium chelatase, subunit ChlI; Subunit ChlI of Mg-chelatase'; TIGRFAM: Mg chelatase-related protein. (507 aa)
Sps_03292ATP-dependent DNA helicase RecQ; PFAM: Helicase conserved C-terminal domain; RQC domain; HRDC domain; DEAD/DEAH box helicase; 'TIGRFAM: ATP-dependent DNA helicase RecQ; ATP-dependent DNA helicase, RecQ family'. (608 aa)
recGATP-dependent DNA helicase RecG; Critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with a 3'- to 5'- polarity. Unwinds branched duplex DNA (Y- DNA); Belongs to the helicase family. RecG subfamily. (706 aa)
Sps_03431PFAM: Exonuclease; 'TIGRFAM: exonuclease, DNA polymerase III, epsilon subunit family'. (227 aa)
Sps_03444TIGRFAM: tape measure domain. (970 aa)
ligADNA ligase, NAD-dependent; DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. (682 aa)
recAProtein RecA; 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. (352 aa)
mutSDNA mismatch repair protein MutS; This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. (855 aa)
Sps_04138PFAM: Calcineurin-like phosphoesterase. (371 aa)
Sps_04227DNA repair protein RadA; PFAM: Subunit ChlI of Mg-chelatase; AAA domain; TIGRFAM: DNA repair protein RadA. (457 aa)
Sps_04371DNA polymerase III, delta subunit; 'PFAM: Processivity clamp loader gamma complex DNA pol III C-term; DNA polymerase III, delta subunit'; 'TIGRFAM: DNA polymerase III, delta subunit'. (346 aa)
Sps_04600'PFAM: DNA polymerase III chi subunit, HolC'. (156 aa)
mutLDNA mismatch repair protein MutL; This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex. (621 aa)
Sps_05174Primary replicative DNA helicase; Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins. Belongs to the helicase family. DnaB subfamily. (468 aa)
rapADNA/RNA helicase, superfamily II, SNF2 family; Transcription regulator that activates transcription by stimulating RNA polymerase (RNAP) recycling in case of stress conditions such as supercoiled DNA or high salt concentrations. Probably acts by releasing the RNAP, when it is trapped or immobilized on tightly supercoiled DNA. Does not activate transcription on linear DNA. Probably not involved in DNA repair; Belongs to the SNF2/RAD54 helicase family. RapA subfamily. (968 aa)
priAReplication restart DNA helicase PriA; Involved in the restart of stalled replication forks. Recognizes and binds the arrested nascent DNA chain at stalled replication forks. It can open the DNA duplex, via its helicase activity, and promote assembly of the primosome and loading of the major replicative helicase DnaB onto DNA; Belongs to the helicase family. PriA subfamily. (731 aa)
Your Current Organism:
Shewanella psychrophila
NCBI taxonomy Id: 225848
Other names: CGMCC 1.6159, JCM 13876, S. psychrophila, Shewanella psychrophila Xiao et al. 2007 emend. Thorell et al. 2019, Shewanella sp. WP2, strain WP2
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