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recD2 recD2 sbcD sbcD DFI_05700 DFI_05700 polA polA DFI_05295 DFI_05295 uvrA uvrA DFI_03530 DFI_03530 dnaG dnaG DFI_01215 DFI_01215 DFI_00985 DFI_00985 DFI_00060 DFI_00060 DFI_00010 DFI_00010 dnaA dnaA DFI_13225 DFI_13225 uvrB uvrB dnaX dnaX GCA_000419625_01410 GCA_000419625_01410 GCA_000419625_01411 GCA_000419625_01411 DFI_10765 DFI_10765 DFI_10505 DFI_10505 gyrA gyrA DFI_08600 DFI_08600 DFI_07260 DFI_07260 uvrC uvrC mutM mutM topA-2 topA-2 DFI_15475 DFI_15475 dinB dinB DFI_17065 DFI_17065 DFI_17070 DFI_17070
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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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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
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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
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recD2ATP-dependent RecD-like DNA helicase; 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. (714 aa)
sbcDNuclease SbcCD 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. (399 aa)
DFI_05700Chromosome segregation protein SMC. (911 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. (936 aa)
DFI_05295DNA helicase. (738 aa)
uvrAUvrABC system protein 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. (1040 aa)
DFI_03530DNA polymerase III subunit epsilon. (203 aa)
dnaGDNA primase; RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. (588 aa)
DFI_01215DNA polymerase III. (323 aa)
DFI_00985DNA polymerase III subunit alpha. (1335 aa)
DFI_00060Single-stranded DNA-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. (296 aa)
DFI_00010Beta sliding clamp; 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 replication a [...] (362 aa)
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. (451 aa)
DFI_13225Replicative DNA helicase; Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity. Belongs to the helicase family. DnaB subfamily. (448 aa)
uvrBUvrABC system protein 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 and [...] (671 aa)
dnaXDNA polymerase III subunit gamma/tau; DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. (790 aa)
GCA_000419625_01410annotation not available (349 aa)
GCA_000419625_01411annotation not available (1620 aa)
DFI_10765DNA polymerase III subunit epsilon. (183 aa)
DFI_10505DNA helicase. (709 aa)
gyrADNA gyrase subunit A; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. (811 aa)
DFI_08600DNA topoisomerase (ATP-hydrolyzing). (679 aa)
DFI_07260DNA polymerase III subunit delta. (300 aa)
uvrCUvrABC system protein 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. (617 aa)
mutMFormamidopyrimidine-DNA glycosylase; Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. (275 aa)
topA-2DNA topoisomerase 1; 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 [...] (676 aa)
DFI_15475Excinuclease ABC subunit A. (843 aa)
dinBDNA polymerase IV; 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. (356 aa)
DFI_17065DNA polymerase. (762 aa)
DFI_17070Daunorubicin resistance protein DrrC. (797 aa)
Your Current Organism:
Deinococcus ficus
NCBI taxonomy Id: 317577
Other names: CCUG 51391, CIP 108832, D. ficus, DSM 17424 [[Deinococcus mumbaiensis Shashidhar and Bandekar 2006]], DSM 19119, Deinococcus ficus Lai et al. 2006 emend. Kampfer 2009, Deinococcus mumbaiensis, Deinococcus mumbaiensis Shashidhar and Bandekar 2006, Deinococcus sp. 2009, Deinococcus sp. CC-FR2-10, Deinococcus sp. UK, MTCC 7297 [[Deinococcus mumbaiensis Shashidhar and Bandekar 2006]], strain CC-FR2-10, strain CON-1 [[Deinococcus mumbaiensis Shashidhar and Bandekar 2006]]
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