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Conserved domains on  [gi|1403787569|emb|SQE79145|]
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Hydroxyacylglutathione hydrolase [Streptococcus pyogenes]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10865880)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme

Gene Ontology:  GO:0016787
PubMed:  17597585

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 12-194 7.67e-57

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.


:

Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 178.25  E-value: 7.67e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  12 GENTYYLVNDQA-VILIDPGSNGQE-IIAKIKSFEKPLVAILLTHTHYDHIFSLDLVRDAFDhPPVYVSEKEAAWLSSPD 89
Cdd:cd06262     9 QTNCYLVSDEEGeAILIDPGAGALEkILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPG-APVYIHEADAELLEDPE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  90 DNLSGLGRHDdiitVIARPAENFFKLKQPYQLNGFEFTVLPTPGHSWGGVSFVFHSDELVVTGDALFRETIGRTDLPTSN 169
Cdd:cd06262    88 LNLAFFGGGP----LPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDLPGGD 163

                         170       180
                  ....*....|....*....|....*
gi 1403787569 170 FEDLITGIRQELFTLPNHYRVYPGH 194
Cdd:cd06262   164 PEQLIESIKKLLLLLPDDTVVYPGH 188
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 12-194 7.67e-57

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.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 178.25  E-value: 7.67e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  12 GENTYYLVNDQA-VILIDPGSNGQE-IIAKIKSFEKPLVAILLTHTHYDHIFSLDLVRDAFDhPPVYVSEKEAAWLSSPD 89
Cdd:cd06262     9 QTNCYLVSDEEGeAILIDPGAGALEkILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPG-APVYIHEADAELLEDPE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  90 DNLSGLGRHDdiitVIARPAENFFKLKQPYQLNGFEFTVLPTPGHSWGGVSFVFHSDELVVTGDALFRETIGRTDLPTSN 169
Cdd:cd06262    88 LNLAFFGGGP----LPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDLPGGD 163

                         170       180
                  ....*....|....*....|....*
gi 1403787569 170 FEDLITGIRQELFTLPNHYRVYPGH 194
Cdd:cd06262   164 PEQLIESIKKLLLLLPDDTVVYPGH 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 14-199 2.74e-42

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 141.75  E-value: 2.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  14 NTYYLVNDQAVILIDPG---SNGQEIIAKIKSFEKPLVAILLTHTHYDHIFSLDLVRDAFDhPPVYVSEKEAAWLSSPDD 90
Cdd:COG0491    16 NSYLIVGGDGAVLIDTGlgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFG-APVYAHAAEAEALEAPAA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  91 nlsglgrhDDIITVIARPAENFFKLKQPYQLNGFEFTVLPTPGHSWGGVSFVFHSDELVVTGDALFRETIGRTDLPTSNF 170
Cdd:COG0491    95 --------GALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLPDGDL 166

                         170       180
                  ....*....|....*....|....*....
gi 1403787569 171 EDLITGIRqELFTLPNHyRVYPGHGPSTT 199
Cdd:COG0491   167 AQWLASLE-RLLALPPD-LVIPGHGPPTT 193
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 14-194 4.54e-33

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.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 116.88  E-value: 4.54e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569   14 NTYYLVNDQAVILIDPG-SNGQEIIAKIKSF-EKPLVAILLTHTHYDHIFSLDLVRDAFDhPPVYVSEKEAAWLSSPDDN 91
Cdd:smart00849   1 NSYLVRDDGGAILIDTGpGEAEDLLAELKKLgPKKIDAIILTHGHPDHIGGLPELLEAPG-APVYAPEGTAELLKDLLAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569   92 LSGLGRHDDIITVIarpaeNFFKLKQPYQLNGFEFTVLPTPGHSWGGVSFVFHSDELVVTGDALFRETIGRTDLPTSNFE 171
Cdd:smart00849  80 LGELGAEAEPAPPD-----RTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAA 154

                          170       180
                   ....*....|....*....|...
gi 1403787569  172 DLITGIRQELFTLPNHYRVYPGH 194
Cdd:smart00849 155 ASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
14-194 2.19e-26

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 100.52  E-value: 2.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  14 NTYYLVNDQAVILIDPGSNGQEIIAKIKSFE----KPLVAILLTHTHYDHIFSLDLVRDAFDHPPVYVSEKEAAWLSSPD 89
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLLAALglgpKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  90 DNLSGLGRHDDIItVIARPAENFFKLKQPYQLNGFEFTVLPTPGHSWGGVSFVFHSDELVVTGDALFRETIGRTDLPTSN 169
Cdd:pfam00753  87 GLAASRLGLPGPP-VVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPLGG 165

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1403787569 170 FEDLITGIRQELFTL------PNHYRVYPGH 194
Cdd:pfam00753 166 LLVLHPSSAESSLESllklakLKAAVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 13-194 3.83e-08

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 52.54  E-value: 3.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  13 ENTYYLVNDQ---AVILIDPgSNGQEIIAKIKSFEKPLVAILLTHTHYDHIFSLDLVRDAFDhPPVYVSEKEAawlsspd 89
Cdd:PLN02398   86 DNYAYLLHDEdtgTVGVVDP-SEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYG-AKVIGSAVDK------- 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  90 DNLSGLgrhdDIItviarpaenfFKLKQPYQLNGFEFTVLPTPGHSWGGVSFVFHSDELVVTGDALFRETIGRtdLPTSN 169
Cdd:PLN02398  157 DRIPGI----DIV----------LKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGK--LFEGT 220

                         170       180
                  ....*....|....*....|....*
gi 1403787569 170 FEDLITGIrQELFTLPNHYRVYPGH 194
Cdd:PLN02398  221 PEQMLSSL-QKIISLPDDTNIYCGH 244
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 12-194 7.67e-57

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.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 178.25  E-value: 7.67e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  12 GENTYYLVNDQA-VILIDPGSNGQE-IIAKIKSFEKPLVAILLTHTHYDHIFSLDLVRDAFDhPPVYVSEKEAAWLSSPD 89
Cdd:cd06262     9 QTNCYLVSDEEGeAILIDPGAGALEkILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPG-APVYIHEADAELLEDPE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  90 DNLSGLGRHDdiitVIARPAENFFKLKQPYQLNGFEFTVLPTPGHSWGGVSFVFHSDELVVTGDALFRETIGRTDLPTSN 169
Cdd:cd06262    88 LNLAFFGGGP----LPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDLPGGD 163

                         170       180
                  ....*....|....*....|....*
gi 1403787569 170 FEDLITGIRQELFTLPNHYRVYPGH 194
Cdd:cd06262   164 PEQLIESIKKLLLLLPDDTVVYPGH 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 14-199 2.74e-42

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 141.75  E-value: 2.74e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  14 NTYYLVNDQAVILIDPG---SNGQEIIAKIKSFEKPLVAILLTHTHYDHIFSLDLVRDAFDhPPVYVSEKEAAWLSSPDD 90
Cdd:COG0491    16 NSYLIVGGDGAVLIDTGlgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFG-APVYAHAAEAEALEAPAA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  91 nlsglgrhDDIITVIARPAENFFKLKQPYQLNGFEFTVLPTPGHSWGGVSFVFHSDELVVTGDALFRETIGRTDLPTSNF 170
Cdd:COG0491    95 --------GALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLPDGDL 166

                         170       180
                  ....*....|....*....|....*....
gi 1403787569 171 EDLITGIRqELFTLPNHyRVYPGHGPSTT 199
Cdd:COG0491   167 AQWLASLE-RLLALPPD-LVIPGHGPPTT 193
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 12-209 1.64e-39

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.


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 134.40  E-value: 1.64e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  12 GENTYyLVNDQA---VILIDPGSNGQEIIAKIKSFEKPLVAILLTHTHYDHIFSLDLVRDAFDhPPVYVSEKEAAWLSSP 88
Cdd:cd16322    10 QENTY-LVADEGggeAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPG-APVYLHPDDLPLYEAA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  89 DDNLSGLGRHDDIITviarPAENFFKLKQPYQLNGFEFTVLPTPGHSWGGVSFVFHSDELVVTGDALFRETIGRTDLPTS 168
Cdd:cd16322    88 DLGAKAFGLGIEPLP----PPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRTDLPGG 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1403787569 169 NFEDLITGIRqELFTLPNHYRVYPGHGPSTTICHEKNANPF 209
Cdd:cd16322   164 DPKAMAASLR-RLLTLPDETRVFPGHGPPTTLGEERRTNPF 203
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 14-194 4.54e-33

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.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 116.88  E-value: 4.54e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569   14 NTYYLVNDQAVILIDPG-SNGQEIIAKIKSF-EKPLVAILLTHTHYDHIFSLDLVRDAFDhPPVYVSEKEAAWLSSPDDN 91
Cdd:smart00849   1 NSYLVRDDGGAILIDTGpGEAEDLLAELKKLgPKKIDAIILTHGHPDHIGGLPELLEAPG-APVYAPEGTAELLKDLLAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569   92 LSGLGRHDDIITVIarpaeNFFKLKQPYQLNGFEFTVLPTPGHSWGGVSFVFHSDELVVTGDALFRETIGRTDLPTSNFE 171
Cdd:smart00849  80 LGELGAEAEPAPPD-----RTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAA 154

                          170       180
                   ....*....|....*....|...
gi 1403787569  172 DLITGIRQELFTLPNHYRVYPGH 194
Cdd:smart00849 155 ASDALESLLKLLKLLPKLVVPGH 177
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 13-194 2.52e-31

Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Salmonella enterica serovar typhimurium YcbL which has type II hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as glyoxalase II) activity, and has a single metal ion binding site, and Thermus thermophilus TTHA1623 which does not have GLX2 activity and has two metal ion binding sites with a glyoxalase II-type metal coordination. 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.


Pssm-ID: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 113.03  E-value: 2.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  13 ENTYYLVNDQ--AVILIDPGSNGQEIIAKIKSFEKPLVAILLTHTHYDHIFSLDLVRDAFDHPPVYVSEKEAAWLSSPDD 90
Cdd:cd07737    11 QNCSLIWCEEtkEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKEDKFLLENLPE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  91 NLSGLGrhddiitviARPAENFFK---LKQPYQLN--GFEFTVLPTPGHSWGGVSFVFHSDELVVTGDALFRETIGRTDL 165
Cdd:cd07737    91 QSQMFG---------FPPAEAFTPdrwLEEGDTVTvgNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTDF 161

                         170       180
                  ....*....|....*....|....*....
gi 1403787569 166 PTSNFEDLITGIRQELFTLPNHYRVYPGH 194
Cdd:cd07737   162 PGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
14-194 2.19e-26

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 100.52  E-value: 2.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  14 NTYYLVNDQAVILIDPGSNGQEIIAKIKSFE----KPLVAILLTHTHYDHIFSLDLVRDAFDHPPVYVSEKEAAWLSSPD 89
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLLAALglgpKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  90 DNLSGLGRHDDIItVIARPAENFFKLKQPYQLNGFEFTVLPTPGHSWGGVSFVFHSDELVVTGDALFRETIGRTDLPTSN 169
Cdd:pfam00753  87 GLAASRLGLPGPP-VVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPLGG 165

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1403787569 170 FEDLITGIRQELFTL------PNHYRVYPGH 194
Cdd:pfam00753 166 LLVLHPSSAESSLESllklakLKAAVIVPGH 196
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 17-194 7.37e-26

Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; Bacillus amyloliquefaciens BaeB may play a role in the synthesis of the antibiotic polyketide bacillaene. 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.


Pssm-ID: 293833 [Multi-domain]  Cd Length: 174  Bit Score: 98.38  E-value: 7.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  17 YLVNDQA---VILIDPGSNGQEIIAKIKSFEKPLVAILLTHTHYDHI-FSLDLVRDafDHPPVYVSEKEAAWLSSPDDNL 92
Cdd:cd16275    15 YIIIDKAtreAAVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVnLVEPLLAK--YDAPVYMSKEEIDYYGFRCPNL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  93 SGLGRHDDIitviarpaenffklkqpyQLNGFEFTVLPTPGHSWGGVSFVFhSDELvVTGDALFRETIGRTDLPTSNFED 172
Cdd:cd16275    93 IPLEDGDTI------------------KIGDTEITCLLTPGHTPGSMCYLL-GDSL-FTGDTLFIEGCGRCDLPGGDPEE 152

                         170       180
                  ....*....|....*....|..
gi 1403787569 173 LITGIRQELFTLPNHYRVYPGH 194
Cdd:cd16275   153 MYESLQRLKKLPPPNTRVYPGH 174
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 17-194 8.65e-22

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.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 87.52  E-value: 8.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  17 YLVND---QAVILIDPGsNGQEIIAKIKSFEKPLVAILLTHTHYDHIFSLDLVRDAFDHPPVYVSEkeaawlsspDDNLS 93
Cdd:cd07723    12 YLIVDeatGEAAVVDPG-EAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPA---------EDRIP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  94 GLGR---HDDIItviarpaenffklkqpyQLNGFEFTVLPTPGHSWGGVSFVFHSDELVVTGDALFRETIGRTDlpTSNF 170
Cdd:cd07723    82 GLDHpvkDGDEI-----------------KLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGRFF--EGTA 142

                         170       180
                  ....*....|....*....|....
gi 1403787569 171 EDLITGIrQELFTLPNHYRVYPGH 194
Cdd:cd07723   143 EQMYASL-QKLLALPDDTLVYCGH 165
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 14-195 1.07e-21

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.


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 88.05  E-value: 1.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  14 NTYYLVNDQAVILID---PGSnGQEIIAKIKS---FEKPLVAILLTHTHYDHIFSLDLVRDAFDhPPVYVSEKEAAWLSS 87
Cdd:cd07721    12 NAYLIEDDDGLTLIDtglPGS-AKRILKALRElglSPKDIRRILLTHGHIDHIGSLAALKEAPG-APVYAHEREAPYLEG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  88 -----PDDNLSGLGRHDDIITVIARPAENFFKLKQPYQLNGfEFTVLPTPGHSWGGVSFVFHSDELVVTGDALFREtIGR 162
Cdd:cd07721    90 ekpypPPVRLGLLGLLSPLLPVKPVPVDRTLEDGDTLDLAG-GLRVIHTPGHTPGHISLYLEEDGVLIAGDALVTV-GGE 167

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1403787569 163 TDLPTSNF-EDLITGIR--QELFTL-PNHyrVYPGHG 195
Cdd:cd07721   168 LVPPPPPFtWDMEEALEslRKLAELdPEV--LAPGHG 202
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 17-195 1.39e-21

ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; MBL-fold metallo-hydrolase domain; Persulfide dioxygenase (PDO, also known as sulfur dioxygenase, SDO, EC 1.13.11.18) is a non-heme iron-dependent oxygenase which catalyzes the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria. Mutations in ethe1 (the human PDO gene) are responsible for a rare autosomal recessive metabolic disorder called ethylmalonic encephalopathy. Arabidopsis thaliana ETHE1 is essential for embryo and endosperm development. Bacterial ETHE1-type PDOs are also called Type 1 PDOs. Type II PDOs (also called PDOAs), are mainly proteobacterial. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293810 [Multi-domain]  Cd Length: 177  Bit Score: 87.07  E-value: 1.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  17 YLVNDQAV---ILIDPGSNG-QEIIAKIKSFEKPLVAILLTHTHYDHIF-SLDLVRDAfdHPPVYVSEKEAAwlSSPDDN 91
Cdd:cd07724    15 YLVGDPETgeaAVIDPVRDSvDRYLDLAAELGLKITYVLETHVHADHVSgARELAERT--GAPIVIGEGAPA--SFFDRL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  92 LsglgRHDDIItviarpaenffklkqpyQLNGFEFTVLPTPGHSWGGVSFVFHSDELVVTGDALFRETIGRTDLPTSNFE 171
Cdd:cd07724    91 L----KDGDVL-----------------ELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPGEAEG 149

                         170       180
                  ....*....|....*....|....*..
gi 1403787569 172 D---LITGIRQELFTLPNHYRVYPGHG 195
Cdd:cd07724   150 LarqLYDSLQRKLLLLPDETLVYPGHD 176
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 9-194 6.86e-17

uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 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.


Pssm-ID: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 74.97  E-value: 6.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569   9 HIAGENTYYLVN--DQAvILIDPGSNGQEIIAKIKSF-EKPLVAILlTHTHYDHIFSLdlvrDAFDHppVYVSEKEAAWL 85
Cdd:cd07712     4 EEDDRVNIYLLRgrDRA-LLIDTGLGIGDLKEYVRTLtDLPLLVVA-THGHFDHIGGL----HEFEE--VYVHPADAEIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  86 SSPDDNlsgLGRHDDIITVIARPAENFFKLKQPY--QLNGFEFTVLPTPGHSWGGVSFVFHSDELVVTGDALFRETIgRT 163
Cdd:cd07712    76 AAPDNF---ETLTWDAATYSVPPAGPTLPLRDGDviDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVYDGPL-IM 151

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1403787569 164 DLPTSNFEDLITGIRQeLFTLPNHYR-VYPGH 194
Cdd:cd07712   152 DLPHSDLDDYLASLEK-LSKLPDEFDkVLPGH 182
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 12-196 1.03e-15

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.


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 71.80  E-value: 1.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  12 GENTYYLVNDQAVILIDPGSNGQEIIAKIKSF-----EKPLVAILLTHTHYDHIFSLDLVRDAFDHPPVYVSEkeaawLS 86
Cdd:cd07722    17 GTNTYLVGTGKRRILIDTGEGRPSYIPLLKSVldsegNATISDILLTHWHHDHVGGLPDVLDLLRGPSPRVYK-----FP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  87 SPDDNLSGLGRHDDIitviarpaeNFFKLKQPYQLNGFEFTVLPTPGHSWGGVSFVFHSDELVVTGDalfreTI---Grt 163
Cdd:cd07722    92 RPEEDEDPDEDGGDI---------HDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGD-----CVlghG-- 155

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1403787569 164 dlpTSNFEDLITGIR--QELFTLPNHyRVYPGHGP 196
Cdd:cd07722   156 ---TAVFEDLAAYMAslKKLLSLGPG-RIYPGHGP 186
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 16-166 1.47e-14

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.


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 69.10  E-value: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  16 YYLVNDQAVILIDPG---SNGQEIIAKIKSFEKPLVAILLTHTHYDHIFSLDLVRDAFdHPPVYVSEKEAAWLSSPDDNL 92
Cdd:cd07743    12 VYVFGDKEALLIDSGldeDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKT-GCKVYAPKIEKAFIENPLLEP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  93 SGLGRhddiitviARPA---ENFFKLKQPYQ-----------LNGFEFTVLPTPGHSWGGVSFVFhSDELVVTGDALF-R 157
Cdd:cd07743    91 SYLGG--------AYPPkelRNKFLMAKPSKvddiieegeleLGGVGLEIIPLPGHSFGQIGILT-PDGVLFAGDALFgE 161


                  ....*....
gi 1403787569 158 ETIGRTDLP 166
Cdd:cd07743   162 EVLEKYGIP 170
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-199 4.84e-14

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.


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 67.98  E-value: 4.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  14 NTYYLVNDQAVILIDPGSN---GQEIIAKIKS-FEKPLVAILLTHTHYDHIFSLDLVRDAfdHPPVYVSEKEAAWLSSPD 89
Cdd:cd16282    16 NIGFIVGDDGVVVIDTGASprlARALLAAIRKvTDKPVRYVVNTHYHGDHTLGNAAFADA--GAPIIAHENTREELAARG 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  90 ----DNLSGLGRHDDIITVIARPAENfFKLKQPYQLNGFEFTVLPT-PGHSWGGVSFVFHSDELVVTGDALFRETIgrTD 164
Cdd:cd16282    94 eaylELMRRLGGDAMAGTELVLPDRT-FDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEGVLFAGDLVFNGRI--PF 170

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1403787569 165 LPTSNFEDLITGIRQELFTLPNHyrVYPGHGPSTT 199
Cdd:cd16282   171 LPDGSLAGWIAALDRLLALDATV--VVPGHGPVGD 203
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 12-153 4.74e-13

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.


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 64.82  E-value: 4.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  12 GENTYYLVNDQAVILIDPGSNGQE----IIAKIKSfeKPLVAILLTHTHYDHIFSLDLVRDAFDhPPVY-VSEKEAA--- 83
Cdd:cd16278    17 GTNTYLLGAPDGVVVIDPGPDDPAhldaLLAALGG--GRVSAILVTHTHRDHSPGAARLAERTG-APVRaFGPHRAGgqd 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  84 WLSSPDDNLsglgRHDDIITViarpaenffklkqpyqlNGFEFTVLPTPGHSWGGVSFVFHSDELVVTGD 153
Cdd:cd16278    94 TDFAPDRPL----ADGEVIEG-----------------GGLRLTVLHTPGHTSDHLCFALEDEGALFTGD 142
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 49-194 1.44e-12

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 64.16  E-value: 1.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  49 AILLTHTHYDHIFSLDLVRDAfdhpPVYVSEKEAAWLSSPdDNLSGLGRHDDIITVIARPAENFFKLKQPYQLNGfEFTV 128
Cdd:cd07729    91 YVILSHLHFDHAGGLDLFPNA----TIIVQRAELEYATGP-DPLAAGYYEDVLALDDDLPGGRVRLVDGDYDLFP-GVTL 164

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1403787569 129 LPTPGHSWGGVSFVFHSDE--LVVTGDAL-FRETIGRTDLP--TSNFEDLITGIR--QELFTLPNHyRVYPGH 194
Cdd:cd07729   165 IPTPGHTPGHQSVLVRLPEgtVLLAGDAAyTYENLEEGRPPgiNYDPEAALASLErlKALAEREGA-RVIPGH 236
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 14-153 1.51e-12

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 64.53  E-value: 1.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  14 NTYYLVNDQAVILIDPGSNGQEIIAKIKSFEKPLVAILLTHTHYDHIFSLDLVRDAFDHP--PVYvsekeaawlsSPDDN 91
Cdd:COG1235    36 SSILVEADGTRLLIDAGPDLREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYGPNpiPVY----------ATPGT 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1403787569  92 LSGLGRHDDIITVIARPAENF--FKLKQPYQLNGFEFTVLPTPGHSWGGVSFVFHSDE--LVVTGD 153
Cdd:COG1235   106 LEALERRFPYLFAPYPGKLEFheIEPGEPFEIGGLTVTPFPVPHDAGDPVGYRIEDGGkkLAYATD 171
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 25-174 1.09e-10

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.


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 59.14  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  25 ILIDPGSNGQ---EIIAKIKSF---EKPLVAILLTHTHYDHIFSLDLVRDAFdHPPVYVSEKEAAWLSSPDDNLSGlGRH 98
Cdd:cd16280    34 ILIDALNNNEaadLIVDGLEKLgldPADIKYILITHGHGDHYGGAAYLKDLY-GAKVVMSEADWDMMEEPPEEGDN-PRW 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1403787569  99 DDIITViarpaENFFKLKQPYQLNGFEFTVLPTPGHSWGGVSFVFHsdelVVTGDALFRE-TIGRTDLPTSNFEDLI 174
Cdd:cd16280   112 GPPPER-----DIVIKDGDTLTLGDTTITVYLTPGHTPGTLSLIFP----VKDGGKTHRAgLWGGTGLNTGPNLERR 179
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 18-197 3.17e-10

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 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.


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 57.21  E-value: 3.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  18 LVNDQ-AVILIDPGS--NGQEIIAKIKSFE-KP--LVAILLTHTHYDHIFSLDLVRDAfdhpPVYVSEKEAAWLSSPDDN 91
Cdd:cd07711    26 LIKDGgKNILVDTGTpwDRDLLLKALAEHGlSPedIDYVVLTHGHPDHIGNLNLFPNA----TVIVGWDICGDSYDDHSL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  92 LSGLGRH-DDIITVIarpaenffklkqpyqlngfeftvlPTPGHSWGGVSFVFHSDEL---VVTGDALFRE---TIGRTD 164
Cdd:cd07711   102 EEGDGYEiDENVEVI------------------------PTPGHTPEDVSVLVETEKKgtvAVAGDLFEREedlEDPILW 157

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1403787569 165 LPTSNFEDLITGIRQELFTLPNHyrVYPGHGPS 197
Cdd:cd07711   158 DPLSEDPELQEESRKRILALADW--IIPGHGPP 188
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 21-156 3.77e-09

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.


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 54.43  E-value: 3.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  21 DQAVILIDPG---SNGQEIIAKIKSFEKPLVAILLTHTHYDHIFSLDLVRDAFD------HPPVY------VSEKEAAWL 85
Cdd:cd07739    24 ETEAVLVDAQftrADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAFPdakvvaTPAVVahikaqLEPKLAFWG 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1403787569  86 SSPDDNLSglgrhDDIITVIARPAENFfklkqpyQLNGFEFTVLPTPGHSWGGVSFVF-HSDELVVTGDALF 156
Cdd:cd07739   104 PLLGGNAP-----ARLVVPEPLDGDTL-------TLEGHPLEIVGVGGGDTDDTTYLWiPSLKTVVAGDVVY 163
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 14-195 3.97e-09

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 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.


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 53.84  E-value: 3.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  14 NTYYLVNDQAVILIDPGSNGQEIIAKIKSFEKPLVA-------ILLTHTHYDHIfsldlvrdafdhppvyvsekeaawls 86
Cdd:cd07725    16 NVYLLRDGDETTLIDTGLATEEDAEALWEGLKELGLkpsdidrVLLTHHHPDHI-------------------------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  87 spddNLSGLGRHDDIITVIArPAENFFKLKQPYQLNGFEFTVLPTPGHSWGGVSFVFHSDELVVTGDALF-RETIGRTDL 165
Cdd:cd07725    70 ----GLAGKLQEKSGATVYI-LDVTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLpKITPNVSLW 144

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1403787569 166 PTSNFEDLITGIR--QELFTLPnHYRVYPGHG 195
Cdd:cd07725   145 AVRVEDPLGAYLEslDKLEKLD-VDLAYPGHG 175
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 13-194 3.83e-08

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 52.54  E-value: 3.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  13 ENTYYLVNDQ---AVILIDPgSNGQEIIAKIKSFEKPLVAILLTHTHYDHIFSLDLVRDAFDhPPVYVSEKEAawlsspd 89
Cdd:PLN02398   86 DNYAYLLHDEdtgTVGVVDP-SEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYG-AKVIGSAVDK------- 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  90 DNLSGLgrhdDIItviarpaenfFKLKQPYQLNGFEFTVLPTPGHSWGGVSFVFHSDELVVTGDALFRETIGRtdLPTSN 169
Cdd:PLN02398  157 DRIPGI----DIV----------LKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGK--LFEGT 220

                         170       180
                  ....*....|....*....|....*
gi 1403787569 170 FEDLITGIrQELFTLPNHYRVYPGH 194
Cdd:PLN02398  221 PEQMLSSL-QKIISLPDDTNIYCGH 244
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 18-162 5.58e-08

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 51.36  E-value: 5.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  18 LVNDQA-VILIDPGsNGQEIIAKIKSFEKPLVAILLTHTHYDHIFSLDLVRDAFDHPPVYVSEKEaawlsspddnlsglg 96
Cdd:PRK10241   17 LNDEAGrCLIVDPG-EAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQET--------------- 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1403787569  97 rHDDIITVIARPAENFFKLkqpyqlnGFEFTVLPTPGHSWGGVSfvFHSDELVVTGDALFRETIGR 162
Cdd:PRK10241   81 -QDKGTTQVVKDGETAFVL-------GHEFSVFATPGHTLGHIC--YFSKPYLFCGDTLFSGGCGR 136
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
16-160 7.39e-08

Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 50.96  E-value: 7.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  16 YYLVNDQAVILIDPGSNGQEIIAKIK-SFEKpLVAILLTHTHYDHIFSLDLVRDAF-----DHP-PVYVSEKEAAWLssp 88
Cdd:COG1234    22 YLLEAGGERLLIDCGEGTQRQLLRAGlDPRD-IDAIFITHLHGDHIAGLPGLLSTRslagrEKPlTIYGPPGTKEFL--- 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1403787569  89 dDNLSGLGRHDDIITVIARPaenfFKLKQPYQLNGFEFTVLPTPgHSWGGVSFVFHSDE--LVVTGDALFRETI 160
Cdd:COG1234    98 -EALLKASGTDLDFPLEFHE----IEPGEVFEIGGFTVTAFPLD-HPVPAYGYRFEEPGrsLVYSGDTRPCEAL 165
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 128-194 9.09e-08

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 50.95  E-value: 9.09e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1403787569 128 VLPTPGHSWGGVSFVFH------SDELVVTGDALFRETIGRTDLPTSNFEDLITGIRQELFTLPNHYRVYPGH 194
Cdd:PLN02962  119 VRATPGHTAGCVTYVTGegpdqpQPRMAFTGDALLIRGCGRTDFQGGSSDQLYKSVHSQIFTLPKDTLIYPAH 191
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 49-156 2.54e-07

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.


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 49.47  E-value: 2.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  49 AILLTHTHYDHIFSL--DLVRDAFDHPPVYVSEKEAA-WLSspDDNLSGLGRHDDIITVIAR----PAENFFKLKQPYQ- 120
Cdd:cd07720    94 DVLLTHLHPDHIGGLvdAGGKPVFPNAEVHVSEAEWDfWLD--DANAAKAPEGAKRFFDAARdrlrPYAAAGRFEDGDEv 171

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1403787569 121 LNGfeFTVLPTPGHSWGGVSFVFHS--DELVVTGDALF 156
Cdd:cd07720   172 LPG--ITAVPAPGHTPGHTGYRIESggERLLIWGDIVH 207
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 25-153 3.91e-07

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 48.46  E-value: 3.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  25 ILIDPGSN--GQE--IIAKIKSFEKPLVAILLTHTHYDHIFSLDLVRdAFDHPPVYVSEKEAAWLSspddnlsglgRHDD 100
Cdd:pfam12706   3 ILIDPGPDlrQQAlpALQPGRLRDDPIDAVLLTHDHYDHLAGLLDLR-EGRPRPLYAPLGVLAHLR----------RNFP 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1403787569 101 IITVIARPAENFFKLK--QPYQLNGFEFTVLPTPGHSWGGVSFVFHSDE---LVVTGD 153
Cdd:pfam12706  72 YLFLLEHYGVRVHEIDwgESFTVGDGGLTVTATPARHGSPRGLDPNPGDtlgFRIEGP 129
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 9-145 3.66e-06

Erythrobacter vulgaris EVM-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 EVM-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).


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 46.19  E-value: 3.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569   9 HIAGeNTYY----------LVNDQAVILIDPGSN--GQEIIAKIKS--FEKPLVAILLT-HTHYDHIFSLDLVRDAfDHP 73
Cdd:cd16315     9 RIFG-NTYYvgtcgisailITGDDGHVLIDSGTEeaAPLVLANIRKlgFDPKDVRWLLSsHEHFDHVGGLAALQRA-TGA 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1403787569  74 PVYVSEKEAAWLSS----PDDNLSGLgrHDDIitviaRPAENFFKLK--QPYQLNGFEFTVLPTPGHSWGGVSFVFHS 145
Cdd:cd16315    87 RVAASAAAAPVLESgkpaPDDPQAGL--HEPF-----PPVRVDRIVEdgDTVALGSLRLTAHATPGHTPGALSWTWRS 157
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 15-154 3.66e-06

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.


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 45.95  E-value: 3.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  15 TYYLVNDQAVILIDPGSN-----GQEIIAKIKSFEKPLVAILLTHTHYDHIFSLDLVRDAFDHPPVYVSEKEAAWLSSP- 88
Cdd:cd07726    18 SYLLDGEGRPALIDTGPSssvprLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLAEALPNAKVYVHPRGARHLIDPs 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1403787569  89 -----------DDNLSGLGrhdDIITViarPAENFFKLK--QPYQLNGFEFTVLPTPGHSWGGVSFVFHSDELVVTGDA 154
Cdd:cd07726    98 klwasaravygDEADRLGG---EILPV---PEERVIVLEdgETLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDA 170
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 24-154 3.78e-06

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.


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 45.59  E-value: 3.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  24 VILIDPGSN----GQEIIAKIKSFE-KPLVAILLTHTHYDHIFSLDLVRDAFDHPPVYVSEKEAAwlSSPDDNLSGLGRH 98
Cdd:cd07731    21 TILIDTGPRdsfgEDVVVPYLKARGiKKLDYLILTHPDADHIGGLDAVLKNFPVKEVYMPGVTHT--TKTYEDLLDAIKE 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  99 DDIITVIARPAENFfklkqpyQLNGFEFTVL-PTPGH-------------SWGGVSFVFhsdelvvTGDA 154
Cdd:cd07731    99 KGIPVTPCKAGDRW-------QLGGVSFEVLsPPKDDyddlnnnscvlrlTYGGTSFLL-------TGDA 154
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 24-80 5.02e-06

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. 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.


Pssm-ID: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 45.57  E-value: 5.02e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1403787569  24 VILIDPGSN---GQEIIAKIKSF--EKPLVAILLTHTHYDHIFSLDLVRDAFDH--PPVYVSEK 80
Cdd:cd07710    29 LIIIDTLESaeaAKAALELFRKHtgDKPVKAIIYTHSHPDHFGGAGGFVEEEDSgkVPIIAPEG 92
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 14-146 6.25e-06

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.


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 44.56  E-value: 6.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  14 NTYYLVNDQAVILIDPGSNGQEIIAKIKSFE-KP--LVAILLTHTHYDHIFSLDLVRDAFDhPPVYVSEKeaawlsspdd 90
Cdd:cd07733    10 NCTYLETEDGKLLIDAGLSGRKITGRLAEIGrDPedIDAILVTHEHADHIKGLGVLARKYN-VPIYATAG---------- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1403787569  91 NLSGLGRHDDIITViarPAENFFKLKQPYQLNGFEFTVLPTPGHSWGGVSFVFHSD 146
Cdd:cd07733    79 TLRAMERKVGLIDV---DQKQIFEPGETFSIGDFDVESFGVSHDAADPVGYRFEEG 131
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 10-143 8.30e-06

Elizabethkingia meningoseptica GOB-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 GOB-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).


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 45.15  E-value: 8.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  10 IAGeNTYY----------LVNDQAVILIDPGSNGQEIIAKiKSFE------KPLVAILLTHTHYDHIFSLDLVRDAfDHP 73
Cdd:cd16308    10 IAG-NLYYvgtydlacylIVTPKGNILINTGLAESVPLIK-KNIQalgfkfKDIKILLTTQAHYDHVGAMAAIKQQ-TGA 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1403787569  74 PVYVSEKEAAWLSS---PDDNLSGLGRHDDIITviarpAENFFKLKQPYQLNGFEFTVLPTPGHSWGGVSFVF 143
Cdd:cd16308    87 KMMVDEKDAKVLADggkSDYEMGGYGSTFAPVK-----ADKLLHDGDTIKLGGTKLTLLHHPGHTKGSCSFLF 154
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 1-156 9.30e-06

L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 44.91  E-value: 9.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569   1 MKIYKtINHiageNTYYLVNDQAVILIDPGSNGQEIIAKIKSFE----KPLVAILLTHTHYDHifsLDLVRDAF---DHP 73
Cdd:COG2220     4 MKITW-LGH----ATFLIETGGKRILIDPVFSGRASPVNPLPLDpedlPKIDAVLVTHDHYDH---LDDATLRAlkrTGA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  74 PVYVSEKEAAWLSSpddnlSGLGRhddiitviARPAENFfklkQPYQLNGFEFTVlpTPGHSWGG---------VSFVFH 144
Cdd:COG2220    76 TVVAPLGVAAWLRA-----WGFPR--------VTELDWG----ESVELGGLTVTA--VPARHSSGrpdrngglwVGFVIE 136

                         170
                  ....*....|....
gi 1403787569 145 SDELVV--TGDALF 156
Cdd:COG2220   137 TDGKTIyhAGDTGY 150
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 17-130 4.26e-05

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; 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 named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 42.46  E-value: 4.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  17 YLVNDQAVILIDPGSN--GQEIIAKIKSFEkplvAILLTHTHYDHIFSLDLVRDAF----DHPPVYVSEKEAAWLSSPDD 90
Cdd:cd16279    39 LIETGGKNILIDTGPDfrQQALRAGIRKLD----AVLLTHAHADHIHGLDDLRPFNrlqqRPIPVYASEETLDDLKRRFP 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1403787569  91 NLSGLGRHDDiitvIARPAENFFKLKQPYQLNGFEFTVLP 130
Cdd:cd16279   115 YFFAATGGGG----VPKLDLHIIEPDEPFTIGGLEITPLP 150
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 11-169 6.62e-05

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 42.87  E-value: 6.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  11 AGENT---YYLVNDQAVILIDPGSNGQEIIAKIKSFE---KPLVAILLTHTHYDHIFSL-DLVRDAFdHPPVYVSE---- 79
Cdd:COG1236     9 AGEVTgscYLLETGGTRILIDCGLFQGGKERNWPPFPfrpSDVDAVVLTHAHLDHSGALpLLVKEGF-RGPIYATPatad 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  80 ------KEAAWLSSPDDNLSGLGRHDDIITVIA--RPAEnffkLKQPYQLNGFEFTVLPTpGHSWGGVSFVFHSDE--LV 149
Cdd:COG1236    88 larillGDSAKIQEEEAEAEPLYTEEDAERALElfQTVD----YGEPFEIGGVRVTFHPA-GHILGSAQVELEVGGkrIV 162

                         170       180
                  ....*....|....*....|
gi 1403787569 150 VTGDalfretIGRTDLPTSN 169
Cdd:COG1236   163 FSGD------YGREDDPLLA 176
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 17-146 7.87e-05

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. 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.


Pssm-ID: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 41.84  E-value: 7.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  17 YLVNDQAVILIDPGSN--GQEIiakiksFEKPLVAILLTHTHYDHIFSL-DLVRDAFDHPPVYvsekeaawlsSPDDNLS 93
Cdd:cd07736    41 LIEVDGERILLDAGLTdlAERF------PPGSIDAILLTHFHMDHVQGLfHLRWGVGDPIPVY----------GPPDPQG 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1403787569  94 --GLGRHDDIITViaRPAENFFklkQPYQLNGFEFTVLPTpGHSWGGVSFVFHSD 146
Cdd:cd07736   105 caDLFKHPGILDF--QPLVAPF---QSFELGGLKITPLPL-NHSKPTFGYLLESG 153
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-92 1.68e-04

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.


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 41.03  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  14 NTYYLVNDQAVILID-PGSNGQEIIAKIKSF-EKPLVAILLTHTHYDHIFSLDLVRdafDHPPVYVSEKEAA-WLS-SPD 89
Cdd:cd16276    11 QSMFLVTDKGVIVVDaPPSLGENLLAAIRKVtDKPVTHVVYSHNHADHIGGASIFK---DEGATIIAHEATAeLLKrNPD 87


                  ...
gi 1403787569  90 DNL 92
Cdd:cd16276    88 PKR 90
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 50-167 2.70e-04

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.


Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 40.69  E-value: 2.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  50 ILLTHTHYDHIFSLDlvrDaFDHPPVYVSEKEAAWLSSPddNLSGLGR--------HDDIITVIARPAENFFKLKQPYQL 121
Cdd:cd07742    84 IVLTHLDLDHAGGLA---D-FPHATVHVHAAELDAATSP--RTRYERRryrpqqlaHGPWWVTYAAGGERWFGFEAVRPL 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1403787569 122 NGFEFTVL--PTPGHSWGGVSFVFHSDE--LVVTGDALF-RETIGRTDLPT 167
Cdd:cd07742   158 DGLPPEILlvPLPGHTRGHCGVAVRTGDrwLLHAGDAYFhHGELDPLPPPP 208
PRK02113 PRK02113
MBL fold metallo-hydrolase;
21-79 7.46e-04

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 39.38  E-value: 7.46e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1403787569  21 DQAVILID--PGSNGQEIIAKIKSFEkplvAILLTHTHYDHIFSLDLVRD--AFDHPPVYVSE 79
Cdd:PRK02113   43 EGARILIDcgPDFREQMLRLPFGKID----AVLITHEHYDHVGGLDDLRPfcRFGEVPIYAEQ 101
PRK00055 PRK00055
ribonuclease Z; Reviewed
 17-63 1.28e-03

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 38.62  E-value: 1.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1403787569  17 YLVN-DQAVILIDPGSNGQE--IIAKIKSfeKPLVAILLTHTHYDHIFSL 63
Cdd:PRK00055   23 ILLRlGGELFLFDCGEGTQRqlLKTGIKP--RKIDKIFITHLHGDHIFGL 70
NorV COG0426
Flavorubredoxin [Energy production and conversion];
15-80 1.39e-03

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 38.66  E-value: 1.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1403787569  15 TY--YLVNDQAVILIDPGSNG--QEIIAKIKSFEKP--LVAILLTHTHYDHIFSLDLVRDAFDHPPVYVSEK 80
Cdd:COG0426    33 TYnsYLIVDEKTALIDTVGESffEEFLENLSKVIDPkkIDYIIVNHQEPDHSGSLPELLELAPNAKIVCSKK 104
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 17-153 1.70e-03

uncharacterized bacterial subgroup of Ribonuclease Z, short form; 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. Members of this bacterial subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 37.81  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  17 YLV-NDQAVILIDPGSnG-----QEIIAkiksFEKpLVAILLTHTHYDHIfsLDL------VRDAFDHP-----PVYVSE 79
Cdd:cd07716    21 YLLeADGFRILLDCGS-GvlsrlQRYID----PED-LDAVVLSHLHPDHC--ADLgvlqyaRRYHPRGArkpplPLYGPA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  80 KEAAWLSSpddnLSGLGRHDDIITViaRPAEnffklkqPYQLNGFEFTVLPTPgH---------SWGGVSFVFhsdelvv 150
Cdd:cd07716    93 GPAERLAA----LYGLEDVFDFHPI--EPGE-------PLEIGPFTITFFRTV-HpvpcyamriEDGGKVLVY------- 151


                  ...
gi 1403787569 151 TGD 153
Cdd:cd07716   152 TGD 154
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 12-60 2.20e-03

MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain; Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. 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.


Pssm-ID: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 37.86  E-value: 2.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1403787569  12 GENT--YYLVNDQAVILIDPGSN----GQEIIAKIKSFEkplVAILLTHTHYDHI 60
Cdd:cd07715    20 GGNTscVEVRAGGELLILDAGTGirelGNELMKEGPPGE---AHLLLSHTHWDHI 71
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 50-155 3.91e-03

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.


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 37.12  E-value: 3.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  50 ILLTHTHYDHI-FSLDLVRDA----FDHPPVYVSEKEAAWLSSPDDNLSGLGRH--DDIITVI-ARPAENFFklkQPYQL 121
Cdd:cd16277    67 VLCTHLHVDHVgWNTRLVDGRwvptFPNARYLFSRAEYDHWSSPDAGGPPNRGVfeDSVLPVIeAGLADLVD---DDHEI 143

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1403787569 122 NGfEFTVLPTPGHSWGGVSFVFHS--DELVVTGDAL 155
Cdd:cd16277   144 LD-GIRLEPTPGHTPGHVSVELESggERALFTGDVM 178
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 16-63 4.22e-03

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.


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 36.86  E-value: 4.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1403787569  16 YYLVNDQAVILIDPGSNGQEIIAKIKSFEKPLVAILLTHTHYDHIFSL 63
Cdd:cd16272    20 YLLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGL 67
IND_BlaB-like_MBL-B1 cd16299
IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 1-58 9.16e-03

IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded metallo-beta-lactamases Chryseobacterium indologenes IND-1, IND-2, and IND-7, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB, Chryseobacterium gleum CGB-1, and Empedobacter brevis EBR-1. 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 MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293857  Cd Length: 212  Bit Score: 35.88  E-value: 9.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1403787569   1 MKIYKTINHIAG----ENTYYLVNDQAVILID---PGSNGQEIIAKIKS-FEKPLVAILLTHTHYD 58
Cdd:cd16299    10 LYIYTTYNEFNGvkysANAMYLVTKKGVILFDtpwDKDQYQPLLDSIRKkHNLPVIAVIATHSHED 75
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 21-154 9.61e-03

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 35.99  E-value: 9.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  21 DQAVILID-----PGSNGQEIIAK------IKSFEkplvAILLTHTHYDHIFSLDLVRDAFdhpPVyvsekEAAWLSSPD 89
Cdd:COG2333    20 DGKTILIDtgprpSFDAGERVVLPylralgIRRLD----LLVLTHPDADHIGGLAAVLEAF---PV-----GRVLVSGPP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  90 DNLSGLgrhDDIITVIARPAENFFKLK--QPYQLNGFEFTVL-PTPGH---------------SWGGVSFVFhsdelvvT 151
Cdd:COG2333    88 DTSETY---ERLLEALKEKGIPVRPCRagDTWQLGGVRFEVLwPPEDLlegsdennnslvlrlTYGGFSFLL-------T 157


                  ...
gi 1403787569 152 GDA 154
Cdd:COG2333   158 GDA 160
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 14-150 9.87e-03

metallo-beta-lactamases, subclass B1; 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 B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. Includes chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1.


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 35.72  E-value: 9.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1403787569  14 NTYYLVNDQAVILIDPG---SNGQEIIAKI-KSFEKPLVAILLTHTHYDHIFSLDLVRDAfdHPPVYVSEKEAAWLSSPD 89
Cdd:cd16285    27 NGLIVIDGKGLVLIDTPwteAQTATLLDWIeKKLGKPVTAAISTHSHDDRTGGIKALNAR--GIPTYATALTNELAKKEG 104

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1403787569  90 DnlsglgrhddiitviaRPAENFFKLKQPYQLNGFEfTVLPTPGHSwggvsfvfhSDELVV 150
Cdd:cd16285   105 K----------------PVPTHSLKGALTLGFGPLE-VFYPGPGHT---------PDNIVV 139
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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