mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 808357626   3 KRHSTMGQAVDVGKRMNAKHIILTHFSARYPKVPVL 38
Cdd:cd07717  191 TGHSTAKQAAEIAKKAGVKKLVLTHFSARYKDPEEL 226

Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme; this subgroup includes the short form (ELAC1). Only the short form exists in bacteria. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 808357626   3 KRHSTMGQAVDVGKRMNAKHIILTHFSARYPKVPVL 38
Cdd:cd07717  191 TGHSTAKQAAEIAKKAGVKKLVLTHFSARYKDPEEL 226

ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of endonuclease or exonuclease activity, and differs in different species. Member of this family are ribonuclease Z, a tRNA 3-prime endonuclease that processes tRNAs to prepare for addition of CCA. In species where all tRNA sequences already have the CCA tail, such as E. coli, the need for such an enzyme is unclear. Protein similar to the E. coli enzyme, matched by TIGRFAMs model TIGR02649, are designated ribonuclease BN. [Transcription, RNA processing]

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 808357626    5 HSTMGQAVDVGKRMNAKHIILTHFSARYPKVPVLPEYLDK--ENIGVAMDMLRVRF 58
Cdd:TIGR02651 244 HSTAAQAAEIAKEANVKRLILTHISPRYSDEEELLEEAKKifPNTYIAEDFMEIEI 299

Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme; this subgroup includes the short form (ELAC1). Only the short form exists in bacteria. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 808357626   3 KRHSTMGQAVDVGKRMNAKHIILTHFSARYPKVPVL 38
Cdd:cd07717  191 TGHSTAKQAAEIAKKAGVKKLVLTHFSARYKDPEEL 226

ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of endonuclease or exonuclease activity, and differs in different species. Member of this family are ribonuclease Z, a tRNA 3-prime endonuclease that processes tRNAs to prepare for addition of CCA. In species where all tRNA sequences already have the CCA tail, such as E. coli, the need for such an enzyme is unclear. Protein similar to the E. coli enzyme, matched by TIGRFAMs model TIGR02649, are designated ribonuclease BN. [Transcription, RNA processing]

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 808357626    5 HSTMGQAVDVGKRMNAKHIILTHFSARYPKVPVLPEYLDK--ENIGVAMDMLRVRF 58
Cdd:TIGR02651 244 HSTAAQAAEIAKEANVKRLILTHISPRYSDEEELLEEAKKifPNTYIAEDFMEIEI 299

Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism];

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 808357626   5 HSTMGQAVDVGKRMNAKHIILTHFSARYPKvPVLPE-----YLDKENIGVAMDMLRVRF 58
Cdd:COG1235  202 HLSNEEALELLARLGPKRLVLTHLSPDNND-HELDYdeleaALLPAGVEVAYDGMEIEL 259