match idtarget lengthalignment lengthprobabilityE-valuecoveragematch description
1COG32648355462.88.1[                ----------------                 ]MscKSmall-conductance mechanosensitive channel
2pfam06169764142.538[          ------------                           ]DUF982Protein of unknown function (DUF982). This family consists of several hypothetical proteins from Rhizobium meliloti, Rhizobium loti and Agrobacterium tumefaciens. The function of this family is unknown. Structural modelling suggests this domain may bind nucleic acids.
3PRK131285183242.118[         -----------                             ]PRK13128D-aminopeptidase; Reviewed
4pfam08383352840.818[           ---------                             ]Maf_NMaf N-terminal region. This region is found in various leucine zipper transcription factors of the Maf family. These are implicated in the regulation of insulin gene expression, in erythroid differentiation, and in differentiation of the neuroretina.
5COG11555883435.026[        ------------                             ]NtpAArchaeal/vacuolar-type H+-ATPase catalytic subunit A/Vma1
6pfam03861561529.746[                -----                            ]ANTARANTAR domain. ANTAR (AmiR and NasR transcription antitermination regulators) is an RNA-binding domain found in bacterial transcription antitermination regulatory proteins. The majority of the domain consists of a coiled-coil.
7pfam009242024727.184[                 --------------                  ]MS_channelMechanosensitive ion channel. Two members of this protein family from M. jannaschii have been functionally characterized. Both proteins form mechanosensitive (MS) ion channels upon reconstitution into liposomes and functional examination by the patch-clamp technique. Therefore this family are likely to also be MS channel proteins.
8cd011343693625.427[        -------------                            ]V_A-ATPase_AV/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. The Vacuolar (V-type) ATPase is found in the membranes of vacuoles, the golgi apparatus and in other coated vesicles in eukaryotes. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.
9PRK137631802024.350[              ------                             ]PRK13763putative RNA-processing protein; Provisional
10TIGR036651721923.054[              ------                             ]arCOG04150arCOG04150 universal archaeal KH domain protein. This family of proteins is universal among the 41 archaeal genomes analyzed, and is not observed outside of the archaea. The proteins contain a single KH domain (pfam00013) which is likely to confer the ability to bind RNA.
11TIGR015452104622.964[                             ------------------  ]YfhB_g-proteohaloacid dehalogenase superfamily, subfamily IF hydrolase, YfhB. This model describes a clade of sequences limited to the gamma proteobacteria. This group is a member of the haloacid dehalogenase (HAD) superfamily of aspartate-dependent hydrolases and all of the conserved catalytic motifs are present. Although structurally similar to subfamily IA in that the variable domain is predicted to consist of five consecutive alpha helices (by PSI-PRED), it is sufficiently divergent to warrant being regarded as a separate sub-family (IF). The gene name comes from the E. coli gene. There is currently no information regarding the function of this gene.
12cd14807982822.71.2E+02[          -----------                            ]RAP_D2Domain 2 of receptor-associated protein (RAP). This subfamily is the N-terminal domain (D2) of receptor-associated protein, RAP, an antagonist and a specialized chaperone in the endoplasmic reticulum that binds tightly to members of the low-density lipoprotein (LDL) receptor family and prevents them from associating with other ligands. D2, along with RAP domain 1 (D1), is essential for blocking low-density lipoprotein receptor-related protein (LRP) from binding of certain ligands, such as alpha2-macroglobulin; D1 and D2 each bind LRP weakly but the tandem D1D2 binds much more tightly to the second and the fourth ligand-binding clusters present on LRP, suggesting the avidity effects arising from amino acid residues contributed from each domain. Also, RAP has regions that interact weakly with heparin, one located in D2 and two located in D3. The double module of complement type repeats, CR56, of LRP binds many ligands including alpha2-macroglobulin, which promotes the catabolism of the Abeta-peptide implicated in Alzheimer's disease.
13pfam012652392822.344[                              -----------        ]Cyto_heme_lyaseCytochrome c/c1 heme lyase.
14pfam09105612321.089[            --------                             ]SelB-wing_1Elongation factor SelB, winged helix. Members of this family adopt a winged-helix fold, with an alpha/beta structure consisting of three alpha-helices and a twisted three-stranded antiparallel beta-sheet, with an alpha-beta-alpha-alpha-beta-beta connectivity. They are involved in both DNA and RNA binding.