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5'-nucleotidase C-terminal domain-containing protein
metallophosphoesterase
This family includes a diverse range of phosphoesterases [1], including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD Swiss:P13457 or yeast MRE11 Swiss:P32829. The most conserved regions in this superfamily centre around the metal chelating residues. [1]. 9685491. Phosphoesterase domains associated with DNA polymerases of. diverse origins.. Aravind L, Koonin EV;. Nucleic Acids Res 1998;26:3746-3752. (from Pfam)
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase
Functions during ribonucleic acid degradation; 2',3'-cyclic nucleotides are first converted to 3'-nucleotide and then cleaved to yield a ribonucleotide and a phosphate
LPXTG cell wall anchor domain-containing protein
This model describes the LPXTG motif-containing region found at the C-terminus of many surface proteins of Streptococcus and Streptomyces species. Cleavage between the Thr and Gly by sortase or a related enzyme leads to covalent anchoring at the new C-terminal Thr to the cell wall. Hits that do not lie at the C-terminus or are not found in Gram-positive bacteria are probably false-positive. A common feature of this proteins containing this domain appears to be a high proportion of charged and zwitterionic residues immediatedly upstream of the LPXTG motif. This model differs from other descriptions of the LPXTG region by including a portion of that upstream charged region.
PRK11907 family protein
heme-binding protein SntA
SntA resembles 2',3'-cyclic nucleotide 2'-phosphodiesterases, but is longer, with an N-terminal signal sequence and a C-terminal LPXTG domain for sortase-mediated anchoring to the streptococcal cell wall.
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