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3' exoribonuclease family, domain 2
This family includes 3'-5' exoribonucleases. Ribonuclease PH contains a single copy of this domain, and removes nucleotide residues following the -CCA terminus of tRNA. Polyribonucleotide nucleotidyltransferase (PNPase) contains two tandem copies of the domain. PNPase is involved in mRNA degradation in a 3'-5' direction. The exosome is a 3'-5' exoribonuclease complex that is required for 3' processing of the 5.8S rRNA. Three of its five protein components, Swiss:P46948 Swiss:Q12277 and Swiss:P25359 contain a copy of this domain [1]. Swiss:Q10205, a hypothetical protein from S. pombe appears to belong to an uncharacterised subfamily. This subfamily is found in both eukaryotes and archaebacteria. [1]. 9390555. The exosome: a conserved eukaryotic RNA processing complex. containing multiple 3'-->5' exoribonucleases.. Mitchell P, Petfalski E, Shevchenko A, Mann M, Tollervey D;. Cell 1997;91:457-466. (from Pfam)
non-canonical purine NTP pyrophosphatase
This family consists of the HAM1 protein Swiss:P47119 and hypothetical archaeal bacterial and C. elegans proteins. HAM1 controls 6-N-hydroxylaminopurine (HAP) sensitivity and mutagenesis in S. cerevisiae Swiss:P47119 [1]. The HAM1 protein protects the cell from HAP, either on the level of deoxynucleoside triphosphate or the DNA level by a yet unidentified set of reactions [1]. [1]. 8789257. HAM1, the gene controlling 6-N-hydroxylaminopurine sensitivity. and mutagenesis in the yeast Saccharomyces cerevisiae.. Noskov VN, Staak K, Shcherbakova PV, Kozmin SG, Negishi K, Ono. BC, Hayatsu H, Pavlov YI;. Yeast 1996;12:17-29. (from Pfam)
3' exoribonuclease family, domain 1
ribonuclease PH
This bacterial enzyme, ribonuclease PH, performs the final 3'-trimming and modification of tRNA precursors. This model is restricted absolutely to bacteria. Related families outside the model include proteins described as probable exosome complex exonucleases (rRNA processing) and polyribonucleotide nucleotidyltransferases (mRNA degradation). The most divergent member within the family is RNase PH from Deinococcus radiodurans.
nucleoside-triphosphate diphosphatase
RdgB/HAM1 family non-canonical purine NTP pyrophosphatase
Saccharomyces cerevisiae HAM1 protects against the mutagenic effects of the base analog 6-N-hydroxylaminopurine, which can be a natural product of monooxygenase activity on adenine. Methanococcus jannaschii MJ0226 and E. coli RdgB are also characterized as pyrophosphatases active against non-standard purines NTPs. E. coli RdgB appears to act by intercepting non-canonical deoxyribonucleotide triphosphates from replication precursor pools.[3]
XTP/dITP diphosphatase
Hydrolyzes non-standard nucleotides such as xanthine and inosine
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