match idtarget lengthalignment lengthprobabilityE-valuecoveragematch description
1pfam0937626017997.71.8E-05[                  ----------------------------   ]NurANurA domain. This family includes NurA a nuclease exhibiting both single-stranded endonuclease activity and 5'-3' exonuclease activity on single-stranded and double-stranded DNA from the hyperthermophilic archaeon Sulfolobus acidocaldarius.
2pfam09199842435.926[         ---                                     ]DUF1954Domain of unknown function (DUF1954). Members of this family are found in various staphylococcal toxins, and adopt an OB fold, wherein the domain folds into a five-stranded beta-barrel. The exact manner in which they confer pathogenic properties to the protein has not, as yet, been determined.
3cd144481442622.076[           ----                                  ]CuRO_2_BOD_CotA_likeCupredoxin domain 2 of Bilirubin oxidase (BOD), the bacterial endospore coat component CotA, and similar proteins. Bilirubin oxidase (BOD) catalyzes the oxidation of bilirubin to biliverdin and the four-electron reduction of molecular oxygen to water. CotA protein is an abundant component of the outer coat layer in bacterial endospore coat and is required for spore resistance against hydrogen peroxide and UV light. Also included in this subfamily are phenoxazinone synthase (PHS), which catalyzes the oxidative coupling of substituted o-aminophenols to produce phenoxazinones, and FtsP (also named SufI), which is a component of the cell division apparatus. These proteins are laccase-like multicopper oxidases (MCOs) that are able to couple oxidation of substrates with reduction of dioxygen to water. MCOs are capable of oxidizing a vast range of substrates, varying from aromatic compounds to inorganic compounds such as metals. Although the members of this family have diverse functions, majority of them have three cupredoxin domain repeats. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 2 of 3-domain MCOs has lost the ability to bind copper.
4COG3526993621.178[ -----                                           ]COG3526Predicted selenoprotein, Rdx family
5PRK112533058616.450[          ------------                           ]ldcAL,D-carboxypeptidase A; Provisional
6pfam073721046716.16.2E+02[                                     ---------   ]DUF1491Protein of unknown function (DUF1491). This family consists of several bacterial proteins of around 115 residues in length. Members of this family seem to be found exclusively in the Class Alphaproteobacteria. The function of this family is unknown.
7pfam14383341516.165[                                          --     ]VARLMGLDUF761-associated sequence motif. This family is found frequently at the N-terminus of family DUF3741, pfam12552.
8pfam0449320513015.51.8E+02[                      ------------------------   ]Endonuclease_5Endonuclease V. Endonuclease V is specific for single-stranded DNA or for duplex DNA that contains uracil or that is damaged by a variety of agents.
9pfam084591543613.93.5E+02[                        -----                    ]UvrC_HhH_NUvrC Helix-hairpin-helix N-terminal. This domain is found in the C subunits of the bacterial and archaeal UvrABC system which catalyses nucleotide excision repair in a multi-step process. UvrC catalyses the first incision on the fourth or fifth phosphodiester bond 3' and on the eighth phosphodiester bond 5' from the damage that is to be excised. The domain described here is found to the N-terminus of a helix hairpin helix (pfam00633) motif and also co-occurs with the pfam01541 catalytic domain which is found at the N-terminus of the same proteins.
10pfam067452312513.369[         ----                                    ]KaiCKaiC. This family represents a conserved region within bacterial and archaeal proteins, most of which are hypothetical. More than one copy is sometimes found in each protein. This family includes KaiC, which is one of the Kai proteins among which direct protein-protein association may be a critical process in the generation of circadian rhythms in cyanobacteria.