Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. 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        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691  39 VGEYEVTALFDGYNDLSPALLHGLSGEKVRELLAQHKIDAERMPTAFNAFLVNTGKHLLMIDSGGGHCMAETAGQLVSNM 118
Cdd:cd07720    3 VGDFEVTALSDGTLPLPLDLLLGGAAPEAEAALLAAFLPPDPVETSVNAFLVRTGGRLILVDTGAGGLFGPTAGKLLANL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691 119 NASGYRPEQVDTIFLTHLHLDHVCGLSDAEGKALFPNATVYVPQGEADYWLDPAKEASAPANAREYFAIARNALSAYKAA 198
Cdd:cd07720   83 AAAGIDPEDIDDVLLTHLHPDHIGGLVDAGGKPVFPNAEVHVSEAEWDFWLDDANAAKAPEGAKRFFDAARDRLRPYAAA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691 199 GHlktFVPPASPVPEVQTAYAIGHTPGSTVYRFASQGTAINFIGDLIHAPAVQFPHPEVSIRFDVDPKKAISSRGQEFNA 278
Cdd:cd07720  163 GR---FEDGDEVLPGITAVPAPGHTPGHTGYRIESGGERLLIWGDIVHHPALQFAHPDWTIAFDVDPEQAAATRRRLLDR 239

                        250
                 ....*....|..
gi 779953691 279 LAKDGEWMAAAH 290
Cdd:cd07720  240 AAAEGLLVAGAH 251

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. 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        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691  39 VGEYEVTALFDGYNDLSPALLHGLSGEKVRELLAQHKIDAERMPTAFNAFLVNTGKHLLMIDSGGGHCMAETAGQLVSNM 118
Cdd:cd07720    3 VGDFEVTALSDGTLPLPLDLLLGGAAPEAEAALLAAFLPPDPVETSVNAFLVRTGGRLILVDTGAGGLFGPTAGKLLANL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691 119 NASGYRPEQVDTIFLTHLHLDHVCGLSDAEGKALFPNATVYVPQGEADYWLDPAKEASAPANAREYFAIARNALSAYKAA 198
Cdd:cd07720   83 AAAGIDPEDIDDVLLTHLHPDHIGGLVDAGGKPVFPNAEVHVSEAEWDFWLDDANAAKAPEGAKRFFDAARDRLRPYAAA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691 199 GHlktFVPPASPVPEVQTAYAIGHTPGSTVYRFASQGTAINFIGDLIHAPAVQFPHPEVSIRFDVDPKKAISSRGQEFNA 278
Cdd:cd07720  163 GR---FEDGDEVLPGITAVPAPGHTPGHTGYRIESGGERLLIWGDIVHHPALQFAHPDWTIAFDVDPEQAAATRRRLLDR 239

                        250
                 ....*....|..
gi 779953691 279 LAKDGEWMAAAH 290
Cdd:cd07720  240 AAAEGLLVAGAH 251

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691    86 NAFLVNTGKHLLMIDSGGGhcmaeTAGQLVSNMNASGyrPEQVDTIFLTHLHLDHVCGLsdaEGKALFPNATVYVPQGEA 165
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPG-----EAEDLLAELKKLG--PKKIDAIILTHGHPDHIGGL---PELLEAPGAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691   166 DYWLDPAKEASAPanarEYFAIARNALSAYKAAGHLKTFvppaspVPEVQTAYAIGHTPGSTVYRFASQGTAinFIGDLI 245
Cdd:smart00849  71 ELLKDLLALLGEL----GAEAEPAPPDRTLKDGDELDLG------GGELEVIHTPGHTPGSIVLYLPEGKIL--FTGDLL 138

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 779953691   246 hapavqFPHPEVSIRFDVDPKKAISSRGQEFNALAKDGEWMAAAH 290
Cdd:smart00849 139 ------FAGGDGRTLVDGGDAAASDALESLLKLLKLLPKLVVPGH 177

ribonuclease Z; Reviewed

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 779953691  81 MPTAF---NAFLVNTGKHLLMIDSGgghcmaetAGQLVSnMNASGYRPEQVDTIFLTHLHLDHVCGL 144
Cdd:PRK00055  13 VPTPTrnvSSILLRLGGELFLFDCG--------EGTQRQ-LLKTGIKPRKIDKIFITHLHGDHIFGL 70

guanitoxin biosynthesis MBL fold metallo-hydrolase GntH;

                         10        20
                 ....*....|....*....|....*..
gi 779953691 115 VSNMNASGYRPEQVDTIFLTHLHLDHV 141
Cdd:NF041257  55 VANIIALQIPYNLLNKVFITHLHVDHY 81

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. 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        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691  39 VGEYEVTALFDGYNDLSPALLHGLSGEKVRELLAQHKIDAERMPTAFNAFLVNTGKHLLMIDSGGGHCMAETAGQLVSNM 118
Cdd:cd07720    3 VGDFEVTALSDGTLPLPLDLLLGGAAPEAEAALLAAFLPPDPVETSVNAFLVRTGGRLILVDTGAGGLFGPTAGKLLANL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691 119 NASGYRPEQVDTIFLTHLHLDHVCGLSDAEGKALFPNATVYVPQGEADYWLDPAKEASAPANAREYFAIARNALSAYKAA 198
Cdd:cd07720   83 AAAGIDPEDIDDVLLTHLHPDHIGGLVDAGGKPVFPNAEVHVSEAEWDFWLDDANAAKAPEGAKRFFDAARDRLRPYAAA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691 199 GHlktFVPPASPVPEVQTAYAIGHTPGSTVYRFASQGTAINFIGDLIHAPAVQFPHPEVSIRFDVDPKKAISSRGQEFNA 278
Cdd:cd07720  163 GR---FEDGDEVLPGITAVPAPGHTPGHTGYRIESGGERLLIWGDIVHHPALQFAHPDWTIAFDVDPEQAAATRRRLLDR 239

                        250
                 ....*....|..
gi 779953691 279 LAKDGEWMAAAH 290
Cdd:cd07720  240 AAAEGLLVAGAH 251

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691  79 ERMPTAFNAFLVNTGKHLLMIDSGGGhcmAETAGQLVSNMNASGyrpEQVDTIFLTHLHLDHVCGLsdAEGKALFpNATV 158
Cdd:COG0491    9 PGAGLGVNSYLIVGGDGAVLIDTGLG---PADAEALLAALAALG---LDIKAVLLTHLHPDHVGGL--AALAEAF-GAPV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691 159 YVPQGEADYWLDPAKEASAPAnareyfaiarnalsaykaaghlkTFVPPASPV----------PEVQTAYAIGHTPGSTV 228
Cdd:COG0491   80 YAHAAEAEALEAPAAGALFGR-----------------------EPVPPDRTLedgdtlelggPGLEVIHTPGHTPGHVS 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 779953691 229 YRFASQGTAinFIGDLIHAPAVQFPHpevsiRFDVDPKKAISSRgQEFNALakDGEWMAAAH 290
Cdd:COG0491  137 FYVPDEKVL--FTGDALFSGGVGRPD-----LPDGDLAQWLASL-ERLLAL--PPDLVIPGH 188

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691    86 NAFLVNTGKHLLMIDSGGGhcmaeTAGQLVSNMNASGyrPEQVDTIFLTHLHLDHVCGLsdaEGKALFPNATVYVPQGEA 165
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPG-----EAEDLLAELKKLG--PKKIDAIILTHGHPDHIGGL---PELLEAPGAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691   166 DYWLDPAKEASAPanarEYFAIARNALSAYKAAGHLKTFvppaspVPEVQTAYAIGHTPGSTVYRFASQGTAinFIGDLI 245
Cdd:smart00849  71 ELLKDLLALLGEL----GAEAEPAPPDRTLKDGDELDLG------GGELEVIHTPGHTPGSIVLYLPEGKIL--FTGDLL 138

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 779953691   246 hapavqFPHPEVSIRFDVDPKKAISSRGQEFNALAKDGEWMAAAH 290
Cdd:smart00849 139 ------FAGGDGRTLVDGGDAAASDALESLLKLLKLLPKLVVPGH 177

uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Bacillus subtilis yflN protein. 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. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, 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 and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691  80 RMPTAFNAFLVNTGKHLLMIDSGgghcMAETAGQLVSNMNASGYRPEQVDTIFLTHLHLDHVCGLsdAEGKALfPNATVY 159
Cdd:cd07721    6 PLLPPVNAYLIEDDDGLTLIDTG----LPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSL--AALKEA-PGAPVY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691 160 VPQGEADYwldpakeasapanareyfaIARNALSAYKAAGHLKTFVPPASPVPEVQTAYAI------------------G 221
Cdd:cd07721   79 AHEREAPY-------------------LEGEKPYPPPVRLGLLGLLSPLLPVKPVPVDRTLedgdtldlagglrvihtpG 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 779953691 222 HTPGSTVYRFASQGTAInfIGDLI---HAPAVQFPHPevsirFDVDPKKAISS 271
Cdd:cd07721  140 HTPGHISLYLEEDGVLI--AGDALvtvGGELVPPPPP-----FTWDMEEALES 185

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. 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        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691  89 LVNTGKHLLMIDSGGGHCM---------AETA-GQLVSNMNASGYRPEQVDTIFLTHLHLDHVCGLSDAEGKAL---FPN 155
Cdd:cd07728   47 LIQYQGKNYLIDAGIGNGKltekqkrnfGVTEeSSIEESLAELGLTPEDIDYVLMTHLHFDHASGLTKVKGEQLvsvFPN 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691 156 ATVYVPQGEadyWldpaKEASAPaNAReyfaiARNalsAYKA------AGHLKTFVPPASPVPEVQTAYAIGHTPGSTVY 229
Cdd:cd07728  127 ATIYVSEIE---W----EEMRNP-NIR-----SKN---TYWKenwepiEDQVKTFSDEIEIVPGITMIHTGGHSDGHSII 190

                        170       180
                 ....*....|....*....|
gi 779953691 230 RFASQGTAINFIGDLI--HA 247
Cdd:cd07728  191 EIEQGGETAIHMADLMptHA 210

Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691  76 IDAERMPTAFnafLVNTGKHLLMIDSGGGhcmaetagqLVSNMNASGYRPEQVDTIFLTHLHLDHVCGLSDAEGKALFPN 155
Cdd:cd07719   12 PDPDRAGPST---LVVVGGRVYLVDAGSG---------VVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPALLLTAWLAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691 156 A----TVYVPQGEADYWldpakEASAPANAREYFAIARNALSAYKAAG---HLKTFVPPAsPVPEVQ----TAYAIGHTP 224
Cdd:cd07719   80 RktplPVYGPPGTRALV-----DGLLAAYALDIDYRARIGDEGRPDPGalvEVHEIAAGG-VVYEDDgvkvTAFLVDHGP 153

                        170       180
                 ....*....|....*....|....*...
gi 779953691 225 --GSTVYRFASQGTAINFIGDLIHAPAV 250
Cdd:cd07719  154 vpPALAYRFDTPGRSVVFSGDTGPSENL 181

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. 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. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, 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 and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691  74 HKIDAE--RMPTAFNAFLVNTGKHLLMIDSGGGHcmaeTAGQLVSNMNASGYRPEQVDTIFLTHLHLDHVCGLSD-AEgk 150
Cdd:cd07726    3 YLIDLGflGFPGRIASYLLDGEGRPALIDTGPSS----SVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLlAE-- 76

                         90       100
                 ....*....|....*....|....*...
gi 779953691 151 aLFPNATVYVPQGEADYWLDPAK-EASA 177
Cdd:cd07726   77 -ALPNAKVYVHPRGARHLIDPSKlWASA 103

Ribonuclease Z; 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. 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. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and 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. 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        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691  87 AFLVNTGKHLLMIDSGGGhcmaeTAGQLVsnmnASGYRPEQVDTIFLTHLHLDHVCGLS--------DAEGKALfpnaTV 158
Cdd:cd16272   19 SYLLETGGTRILLDCGEG-----TVYRLL----KAGVDPDKLDAIFLSHFHLDHIGGLPtllfarryGGRKKPL----TI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691 159 YVPQGEADYWldpakeasapanarEYFAIARNALSaykaAGHLKTFVPPASPVPEVQ-------TAYAIGHTPGSTVYRF 231
Cdd:cd16272   86 YGPKGIKEFL--------------EKLLNFPVEIL----PLGFPLEIEELEEGGEVLelgdlkvEAFPVKHSVESLGYRI 147

                        170
                 ....*....|..
gi 779953691 232 ASQGTAINFIGD 243
Cdd:cd16272  148 EAEGKSIVYSGD 159

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase 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, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, 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 and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Some members of this subgroup are annotated as GumP protein.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 779953691 120 ASGYRPEQVDTIFLTHLHLDHVCGLSDaegkalFPNATVYVPQGEADYWLDPA 172
Cdd:cd07730   76 AGGIDPEDIDAVILSHLHWDHIGGLSD------FPNARLIVGPGAKEALRPPG 122

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. 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. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, 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 and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 779953691  86 NAFLVNTGKHLLMIDSGGGhcMAETAGQLVSNMNASGyrPEQVDTIFLTHLHLDHVCGLSDAEGKALFPNATVY 159
Cdd:cd07722   19 NTYLVGTGKRRILIDTGEG--RPSYIPLLKSVLDSEG--NATISDILLTHWHHDHVGGLPDVLDLLRGPSPRVY 88

metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B3 MBLs include Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Stenotrophomonas Maltophilia L1, and Bradyrhizobium diazoefficiens BJP-1, Serratia marcescens SMB-1, and Pseudomonas Aeruginosa AIM-1. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691  87 AFLVNTGKHLLMIDSGgghcMAETAGQLVSNMNASGYRPEQVDTIFLTHLHLDHvcglsdAEGKALFPNATvyvpqgead 166
Cdd:cd07708   24 AYLIVTPQGNILIDGD----MEQNAPMIKANIKKLGFKFSDTKLILISHAHFDH------AGGSAEIKKQT--------- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691 167 ywldpakEASAPANAREYFAIARNALSAYKAAGHLKTFVPPASPV------------PEVQTAYAI-GHTPGST------ 227
Cdd:cd07708   85 -------GAKVMAGAEDVSLLLSGGSSDFHYANDSSTYFPQSTVDravhdgervtlgGTVLTAHATpGHTPGCTtwtmtl 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691 228 -------------------VYRFASQGTAINFIGDLIHAPAVQ---------FPHPEVsirFDVDPKKAISSRGQEfNAL 279
Cdd:cd07708  158 kdhgkqyqvvfadsltvnpGYRLVDNPTYPKIVEDYRHSFAVVeamrcdillGPHPGV---FDMKNKYVLLSKGQN-NPF 233

                        250
                 ....*....|
gi 779953691 280 AKDGEWMAAA 289
Cdd:cd07708  234 VDPGGCKAYA 243

BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Bradyrhizobium diazoefficiens BJP-1, Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Caulobacter crescentus Mbl1b. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691  87 AFLVNTGKHLLMIDSGgghcMAETAGQLVSNMNASGYRPEQVDTIFLTHLHLDHVCGLsdAEGKAlfpnatvyvpqgead 166
Cdd:cd16288   24 SYLITTPQGLILIDTG----LESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGL--AALKK--------------- 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 779953691 167 ywLDPAKEASAPANAReyfAIARNALSAYKAAGHLKTFvpPASPVPEV-------------QTAYAI-GHTPGSTVY 229
Cdd:cd16288   83 --LTGAKLMASAEDAA---LLASGGKSDFHYGDDSLAF--PPVKVDRVlkdgdrvtlggttLTAHLTpGHTRGCTTW 152

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase 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, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, 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 and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691  87 AFLVNTGKHLLMIDSGGghcMAETAGQLVSNMNASGYRPEQVDTIFLTHLHLDHVCGlsdAEG-KALFpNATVYVPQGEA 165
Cdd:cd16280   24 AWAIDTGDGLILIDALN---NNEAADLIVDGLEKLGLDPADIKYILITHGHGDHYGG---AAYlKDLY-GAKVVMSEADW 96

                         90
                 ....*....|....
gi 779953691 166 DYWLDPAKEASAPA 179
Cdd:cd16280   97 DMMEEPPEEGDNPR 110

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. 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        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691  87 AFLVNTGKHLLMIDSGGGhcMAETAGQLVSNMNASGYRpeQVDTIFLTHLHLDHVCGLSDAEGKalFPNATVYVPQGEAD 166
Cdd:cd07731   12 AILIQTPGKTILIDTGPR--DSFGEDVVVPYLKARGIK--KLDYLILTHPDADHIGGLDAVLKN--FPVKEVYMPGVTHT 85

                         90
                 ....*....|....*...
gi 779953691 167 -----YWLDPAKEASAPA 179
Cdd:cd07731   86 tktyeDLLDAIKEKGIPV 103

uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 and related proteins. 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. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691  82 PTAFNAFLVNT--GKHLLMIDSGGGhcmaetAGQLVSNMNASGYRpeqVDTIFLTHLHLDHVCGLSDAegkALFPNATVY 159
Cdd:cd16322    8 PLQENTYLVADegGGEAVLVDPGDE------SEKLLARFGTTGLT---LLYILLTHAHFDHVGGVADL---RRHPGAPVY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691 160 VPQGEADYWLDPAKEAsapanAREYFAIarnalsaykaaghlKTFVPPASPVPEVQTAYAI----------GHTPGSTVY 229
Cdd:cd16322   76 LHPDDLPLYEAADLGA-----KAFGLGI--------------EPLPPPDRLLEDGQTLTLGglefkvlhtpGHSPGHVCF 136

                        170
                 ....*....|....*.
gi 779953691 230 RFASQGTAinFIGDLI 245
Cdd:cd16322  137 YVEEEGLL--FSGDLL 150

uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YycJ protein. 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. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, 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 and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 779953691  86 NAFLVNTGKHLLMIDSGgghcmaETAGQLVSNMNASGYRPEQVDTIFLTHLHLDHVCGL 144
Cdd:cd07733   10 NCTYLETEDGKLLIDAG------LSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGL 62

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase 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) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, 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 and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691  88 FLVNTGKHLLMIDSGGGHCMAetagqlvsnMNASGYRPEQVDTIFLTHLHLDHVCGLSDAEGKALFPNA-----TVYVPQ 162
Cdd:cd07740   19 FHVASEAGRFLIDCGASSLIA---------LKRAGIDPNAIDAIFITHLHGDHFGGLPFFLLDAQFVAKrtrplTIAGPP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 779953691 163 GEADyWLDPAKEASAPANAREyfaIARNALSAYKAAGHLKTFVPPASPvpevqTAYAIGHTPGSTVYRF--ASQGTAINF 240
Cdd:cd07740   90 GLRE-RLRRAMEALFPGSSKV---PRRFDLEVIELEPGEPTTLGGVTV-----TAFPVVHPSGALPLALrlEAAGRVLAY 160

                 ...
gi 779953691 241 IGD 243
Cdd:cd07740  161 SGD 163

Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General function prediction only];

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 779953691  87 AFLVNTGKHLLMIDSGgghcMAETAGQL-VSNMNASGYRPEQVDTIFLTHLHLDHvCGL 144
Cdd:COG1782   16 CHLLETGESRILLDCG----LFQGGREErERNNDAFPFDPEELDAVVLTHAHLDH-SGL 69

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs 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 779953691 127 QVDTIFLTHLHLDHVCGLsdAEGKALFPNATVYVPQGE 164
Cdd:cd07723   43 TLTAILTTHHHWDHTGGN--AELKALFPDAPVYGPAED 78

RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure and biogenesis];

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 779953691  86 NAFLVNTGKHLLMIDSGgghcMAEtaGQLVSNMNASGYRPEQVDTIFLTHLHLDHvCGL 144
Cdd:COG1236   15 SCYLLETGGTRILIDCG----LFQ--GGKERNWPPFPFRPSDVDAVVLTHAHLDH-SGA 66

Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of L1- and Pom-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).