STRINGSTRING
ADZ08357.1 ADZ08357.1 ADZ08378.1 ADZ08378.1 ADZ08381.1 ADZ08381.1 ADZ08382.1 ADZ08382.1 pcn pcn ADZ08961.1 ADZ08961.1 nth nth fen fen ADZ10339.1 ADZ10339.1 ADZ10598.1 ADZ10598.1 ADZ10658.1 ADZ10658.1 ADZ10662.1 ADZ10662.1 lig lig
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
Others
textmining
co-expression
protein homology
Your Input:
ADZ08357.1PFAM: Phosphoesterase, RecJ-like; Phosphoesterase, DHHA1; KEGG: msi:Msm_1193 single-stranded DNA-specific exonuclease. (453 aa)
ADZ08378.1DNA-(apurinic or apyrimidinic site) lyase; PFAM: 8-oxoguanine DNA glycosylase, N-terminal; HhH-GPD domain; KEGG: msi:Msm_1365 3-methyladenine DNA glycosylase/8-oxoguanine DNA glycosylase; SMART: HhH-GPD domain. (328 aa)
ADZ08381.1PFAM: Methylpurine-DNA glycosylase (MPG); TIGRFAM: Methylpurine-DNA glycosylase (MPG); HAMAP: Methylpurine-DNA glycosylase (MPG); KEGG: ccb:Clocel_1348 DNA-3-methyladenine glycosylase; Belongs to the DNA glycosylase MPG family. (202 aa)
ADZ08382.1KEGG: glo:Glov_0058 DNA-3-methyladenine glycosylase I; PFAM: Methyladenine glycosylase. (186 aa)
pcnDNA polymerase sliding clamp; Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication. (244 aa)
ADZ08961.1HhH-GPD family protein; KEGG: mac:MA3207 DNA-3-methyladenine glycosylase II; PFAM: HhH-GPD domain; SMART: HhH-GPD domain. (295 aa)
nthDNA-(apurinic or apyrimidinic site) lyase; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate. (216 aa)
fenFlap structure-specific endonuclease; Structure-specific nuclease with 5'-flap endonuclease and 5'- 3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' cleavage specificity. Cleaves one nucleotide into the double-stranded DNA from the junction in flap DNA, leaving a nick for ligation. Also involved in the base excision repair [...] (328 aa)
ADZ10339.1PFAM: Phosphoesterase, DHHA1; Phosphoesterase, RecJ-like; KEGG: mst:Msp_1189 hypothetical protein. (465 aa)
ADZ10598.1PFAM: DNA ligase, ATP-dependent, central; DNA ligase, ATP-dependent, C-terminal; KEGG: afu:AF1725 DNA ligase, putative. (301 aa)
ADZ10658.1KEGG: msi:Msm_0963 endonuclease IV; PFAM: Xylose isomerase, TIM barrel domain; SMART: Endodeoxyribonuclease IV. (278 aa)
ADZ10662.1TIGRFAM: Exodeoxyribonuclease III xth; AP endonuclease, family 1; KEGG: mmg:MTBMA_c06610 DNA lyase; PFAM: Endonuclease/exonuclease/phosphatase. (257 aa)
ligDNA ligase; DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. (560 aa)
Your Current Organism:
Methanobacterium lacus
NCBI taxonomy Id: 877455
Other names: DSM 24406, JCM 17760, M. lacus, Methanobacterium lacus Borrel et al. 2012, Methanobacterium sp. 17A1, Methanobacterium sp. AL-21, strain 17A1
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