Exonuclease-Endonuclease-Phosphatase domain; uncharacterized family 1. This family of uncharacterized proteins belongs to a superfamily that includes the catalytic domain (exonuclease/endonuclease/phosphatase, EEP, domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds. Their substrates range from nucleic acids to phospholipids and perhaps, proteins.

Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function prediction only].

DOMON-like type 9 carbohydrate binding module of xylanases. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. The CBM9 domain frequently occurs in tandem repeats; members found in this subfamily typically co-occur with glycosyl hydrolase family 10 domains and are annotated as endo-1,4-beta-xylanases. CBM9 from Thermotoga maritima xylanase 10A is reported to have specificity for polysaccharide reducing ends.

Carbohydrate family 9 binding domain-like. CBM9_1 is a C-terminal domain on bacterial xylanase proteins, and it is tandemly repeated in a number of family-members. The CBM9 module binds to amorphous and crystalline cellulose and a range of soluble di- and monosaccharides as well as to cello- and xylo- oligomers of different degrees of polymerization. Comparison of the glucose and cellobiose complexes during crystallisation reveals surprising differences in binding of these two substrates by CBM9-2. Cellobiose was found to bind in a distinct orientation from glucose, while still maintaining optimal stacking and electrostatic interactions with the reducing end sugar.

Exonuclease-Endonuclease-Phosphatase (EEP) domain superfamily. This large superfamily includes the catalytic domain (exonuclease/endonuclease/phosphatase or EEP domain) of a diverse set of proteins including the ExoIII family of apurinic/apyrimidinic (AP) endonucleases, inositol polyphosphate 5-phosphatases (INPP5), neutral sphingomyelinases (nSMases), deadenylases (such as the vertebrate circadian-clock regulated nocturnin), bacterial cytolethal distending toxin B (CdtB), deoxyribonuclease 1 (DNase1), the endonuclease domain of the non-LTR retrotransposon LINE-1, and related domains. These diverse enzymes share a common catalytic mechanism of cleaving phosphodiester bonds; their substrates range from nucleic acids to phospholipids and perhaps proteins.

Bacteroidesthetaiotaomicron VPI-5482 mannosyl-6-phosphatase Bt3783 [Bacteroides thetaiotaomicron VPI-5482],4C1R_B Bacteroides thetaiotaomicron VPI-5482 mannosyl-6-phosphatase Bt3783 [Bacteroides thetaiotaomicron VPI-5482],4C1R_C Bacteroides thetaiotaomicron VPI-5482 mannosyl-6-phosphatase Bt3783 [Bacteroides thetaiotaomicron VPI-5482],4C1R_D Bacteroides thetaiotaomicron VPI-5482 mannosyl-6-phosphatase Bt3783 [Bacteroides thetaiotaomicron VPI-5482]

ChainA, Putative endonuclease/exonuclease/phosphatase family protein [Phocaeicola vulgatus ATCC 8482]

CrystalStructure of endonuclease/exonuclease/phosphatase family protein from Bacteroides thetaiotaomicron, Northeast Structural Genomics Consortium Target BtR318A [Bacteroides thetaiotaomicron],3MPR_B Crystal Structure of endonuclease/exonuclease/phosphatase family protein from Bacteroides thetaiotaomicron, Northeast Structural Genomics Consortium Target BtR318A [Bacteroides thetaiotaomicron],3MPR_C Crystal Structure of endonuclease/exonuclease/phosphatase family protein from Bacteroides thetaiotaomicron, Northeast Structural Genomics Consortium Target BtR318A [Bacteroides thetaiotaomicron],3MPR_D Crystal Structure of endonuclease/exonuclease/phosphatase family protein from Bacteroides thetaiotaomicron, Northeast Structural Genomics Consortium Target BtR318A [Bacteroides thetaiotaomicron]

Thecrystal structure of a functionally unknown conserved protein from Enterococcus faecalis V583 [Enterococcus faecalis],3L1W_B The crystal structure of a functionally unknown conserved protein from Enterococcus faecalis V583 [Enterococcus faecalis],3L1W_C The crystal structure of a functionally unknown conserved protein from Enterococcus faecalis V583 [Enterococcus faecalis],3L1W_D The crystal structure of a functionally unknown conserved protein from Enterococcus faecalis V583 [Enterococcus faecalis],3L1W_E The crystal structure of a functionally unknown conserved protein from Enterococcus faecalis V583 [Enterococcus faecalis],3L1W_F The crystal structure of a functionally unknown conserved protein from Enterococcus faecalis V583 [Enterococcus faecalis]