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Conserved domains on  [gi|531683980|gb|EQJ61390|]
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metallo-beta-lactamase superfamily protein [Clostridioides difficile P28]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 581040)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 23-211 5.01e-58

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.


The actual alignment was detected with superfamily member cd07712:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 182  Bit Score: 182.44  E-value: 5.01e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  23 YEKTNCYLLLGKQRALLIDSGLGVADIRKITDQLTALPVTVIATHVHWDHIGSHGSYTDVLVHEREYSWLNGKFPlplgv 102
Cdd:cd07712    6 DDRVNIYLLRGRDRALLIDTGLGIGDLKEYVRTLTDLPLLVVATHGHFDHIGGLHEFEEVYVHPADAEILAAPDN----- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980 103 vkqqlMKEPCSFPGDFHMNAYTVwqghAGIVGDGDILNLGGRHIRVLHTPGHSPGHMCFFDLEREWLYCGDLIYKGVLYC 182
Cdd:cd07712   81 -----FETLTWDAATYSVPPAGP----TLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVYDGPLIM 151

                        170       180       190
                 ....*....|....*....|....*....|.
gi 531683980 183 DYPSTDPQAYLLSVQRLQTLALQ--RLLPAH 211
Cdd:cd07712  152 DLPHSDLDDYLASLEKLSKLPDEfdKVLPGH 182
 
Name Accession Description Interval E-value
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 23-211 5.01e-58

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: 182.44  E-value: 5.01e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  23 YEKTNCYLLLGKQRALLIDSGLGVADIRKITDQLTALPVTVIATHVHWDHIGSHGSYTDVLVHEREYSWLNGKFPlplgv 102
Cdd:cd07712    6 DDRVNIYLLRGRDRALLIDTGLGIGDLKEYVRTLTDLPLLVVATHGHFDHIGGLHEFEEVYVHPADAEILAAPDN----- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980 103 vkqqlMKEPCSFPGDFHMNAYTVwqghAGIVGDGDILNLGGRHIRVLHTPGHSPGHMCFFDLEREWLYCGDLIYKGVLYC 182
Cdd:cd07712   81 -----FETLTWDAATYSVPPAGP----TLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVYDGPLIM 151

                        170       180       190
                 ....*....|....*....|....*....|.
gi 531683980 183 DYPSTDPQAYLLSVQRLQTLALQ--RLLPAH 211
Cdd:cd07712  152 DLPHSDLDDYLASLEKLSKLPDEfdKVLPGH 182
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 26-234 3.10e-37

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: 130.20  E-value: 3.10e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  26 TNCYLLLGKQRALLIDSGLGVADIRKITDQLTAL---PVTVIATHVHWDHIGSHGSYTD-----VLVHEREYSWLNGKFp 97
Cdd:COG0491   15 VNSYLIVGGDGAVLIDTGLGPADAEALLAALAALgldIKAVLLTHLHPDHVGGLAALAEafgapVYAHAAEAEALEAPA- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  98 lplgvvKQQLMKEPCSFPGDFhmnaytvwqghagiVGDGDILNLGGRHIRVLHTPGHSPGHMCFFDLEREWLYCGDLIY- 176
Cdd:COG0491   94 ------AGALFGREPVPPDRT--------------LEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFs 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 531683980 177 KGVLYCDYPSTDPQAYLLSVQRLQTLALQRLLPAHYTIeVGPSLIQETAQAWEELQEK 234
Cdd:COG0491  154 GGVGRPDLPDGDLAQWLASLERLLALPPDLVIPGHGPP-TTAEAIDYLEELLAALGER 210
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 27-211 1.82e-26

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: 101.09  E-value: 1.82e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980    27 NCYLLLGKQRALLIDSGLGVA-DIRKITDQLTALPVT-VIATHVHWDHIGSHGSY-----TDVLVHEREYswlngkfplp 99
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAeDLLAELKKLGPKKIDaIILTHGHPDHIGGLPELleapgAPVYAPEGTA---------- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980   100 lgvvkqQLMKEPCSFPGDFHMNAYTVWQGHagIVGDGDILNLGGRHIRVLHTPGHSPGHMCFFDLEREWLYCGDLIY--- 176
Cdd:smart00849  71 ------ELLKDLLALLGELGAEAEPAPPDR--TLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFagg 142

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 531683980   177 KGVLYCDYPSTDPQAYLLSVQRLQTLALQRLLPAH 211
Cdd:smart00849 143 DGRTLVDGGDAAASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
26-211 1.08e-18

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 81.26  E-value: 1.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980   26 TNCYLLLGKQRALLIDSGLGVADIRKITDQLTAL----PVTVIATHVHWDHIGSHGSYTDVLVHEREYSWLNGKFPLPLG 101
Cdd:pfam00753   6 VNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLgpkdIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  102 VvKQQLMKEPCSFPGDFHMNAYTVWQGHAGIVGdgdilnlGGRHIRVLHTPGHSPGHMCFFDLEREWLYCGDLIY----- 176
Cdd:pfam00753  86 L-GLAASRLGLPGPPVVPLPPDVVLEEGDGILG-------GGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFageig 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 531683980  177 ----KGVLYCDYPSTDPQAYLLSVQRLQTLALQRLLPAH 211
Cdd:pfam00753 158 rldlPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 33-173 2.65e-11

hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione hydrolase, a detoxification enzyme known as glyoxalase II. It follows lactoylglutathione lyase, or glyoxalase I, and acts to remove the toxic metabolite methylglyoxal and related compounds. This protein belongs to the broader metallo-beta-lactamase family (pfam00753). [Cellular processes, Detoxification]


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 61.78  E-value: 2.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980   33 GKQRALLIDSGLGvADIRKITDQLTALPVTVIATHVHWDHIGShgsyTDVLVHereyswlngKFPLPL-GVVKQQLmkep 111
Cdd:TIGR03413  18 PDGQAAVVDPGEA-EPVLDALEARGLTLTAILLTHHHHDHVGG----VAELLE---------AFPAPVyGPAEERI---- 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 531683980  112 csfPGdfhmnaytvwQGHagIVGDGDILNLGGRHIRVLHTPGHSPGHMCFFDLEREWLYCGD 173
Cdd:TIGR03413  80 ---PG----------ITH--PVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGD 126
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 36-214 2.25e-09

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 56.37  E-value: 2.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  36 RALLIDSGLGVADIRKITDQlTALPVTVIATHVHWDHIGShgsytdvlvhereyswlngkfplplgvVKQQLMKepcsFP 115
Cdd:PRK10241  23 RCLIVDPGEAEPVLNAIAEN-NWQPEAIFLTHHHHDHVGG---------------------------VKELVEK----FP 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980 116 gdfHMNAY----TVWQGHAGIVGDGDILNLGGRHIRVLHTPGHSPGHMCFFdlEREWLYCGDLIYKGVLYCDYPSTDPQA 191
Cdd:PRK10241  71 ---QIVVYgpqeTQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF--SKPYLFCGDTLFSGGCGRLFEGTASQM 145

                        170       180
                 ....*....|....*....|....*
gi 531683980 192 YlLSVQRLQTLALQRLL-PAH-YTI 214
Cdd:PRK10241 146 Y-QSLKKINALPDDTLIcCAHeYTL 169
 
Name Accession Description Interval E-value
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 23-211 5.01e-58

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: 182.44  E-value: 5.01e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  23 YEKTNCYLLLGKQRALLIDSGLGVADIRKITDQLTALPVTVIATHVHWDHIGSHGSYTDVLVHEREYSWLNGKFPlplgv 102
Cdd:cd07712    6 DDRVNIYLLRGRDRALLIDTGLGIGDLKEYVRTLTDLPLLVVATHGHFDHIGGLHEFEEVYVHPADAEILAAPDN----- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980 103 vkqqlMKEPCSFPGDFHMNAYTVwqghAGIVGDGDILNLGGRHIRVLHTPGHSPGHMCFFDLEREWLYCGDLIYKGVLYC 182
Cdd:cd07712   81 -----FETLTWDAATYSVPPAGP----TLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVYDGPLIM 151

                        170       180       190
                 ....*....|....*....|....*....|.
gi 531683980 183 DYPSTDPQAYLLSVQRLQTLALQ--RLLPAH 211
Cdd:cd07712  152 DLPHSDLDDYLASLEKLSKLPDEfdKVLPGH 182
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 26-234 3.10e-37

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: 130.20  E-value: 3.10e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  26 TNCYLLLGKQRALLIDSGLGVADIRKITDQLTAL---PVTVIATHVHWDHIGSHGSYTD-----VLVHEREYSWLNGKFp 97
Cdd:COG0491   15 VNSYLIVGGDGAVLIDTGLGPADAEALLAALAALgldIKAVLLTHLHPDHVGGLAALAEafgapVYAHAAEAEALEAPA- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  98 lplgvvKQQLMKEPCSFPGDFhmnaytvwqghagiVGDGDILNLGGRHIRVLHTPGHSPGHMCFFDLEREWLYCGDLIY- 176
Cdd:COG0491   94 ------AGALFGREPVPPDRT--------------LEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFs 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 531683980 177 KGVLYCDYPSTDPQAYLLSVQRLQTLALQRLLPAHYTIeVGPSLIQETAQAWEELQEK 234
Cdd:COG0491  154 GGVGRPDLPDGDLAQWLASLERLLALPPDLVIPGHGPP-TTAEAIDYLEELLAALGER 210
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 26-211 5.48e-29

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: 108.14  E-value: 5.48e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  26 TNCYLLLGKQR-ALLIDSGLG-VADIRKITDQLTALPVTVIATHVHWDHIGSHGSYTD-----VLVHEREYSWLNGKFPL 98
Cdd:cd06262   10 TNCYLVSDEEGeAILIDPGAGaLEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEapgapVYIHEADAELLEDPELN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  99 PLGvvkqqLMKEPCSFPGDFHmnaytvwqghagIVGDGDILNLGGRHIRVLHTPGHSPGHMCFFDLEREWLYCGDLIYKG 178
Cdd:cd06262   90 LAF-----FGGGPLPPPEPDI------------LLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAG 152

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 531683980 179 -VLYCDYPSTDPQAYLLSVQRLQTLALQ--RLLPAH 211
Cdd:cd06262  153 sIGRTDLPGGDPEQLIESIKKLLLLLPDdtVVYPGH 188
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 27-211 2.44e-28

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: 106.92  E-value: 2.44e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  27 NCYLLLGKQRALLIDSGLGvADIRKITDQLTAL-----PVT-VIATHVHWDHIGS-------HGsyTDVLVHEREYSWLN 93
Cdd:cd07721   12 NAYLIEDDDGLTLIDTGLP-GSAKRILKALRELglspkDIRrILLTHGHIDHIGSlaalkeaPG--APVYAHEREAPYLE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  94 GKFPLPLGVVKQQLMKEPCSFPGDFHMNAYTVwqghagivGDGDILNLGGRhIRVLHTPGHSPGHMCFFDLEREWLYCGD 173
Cdd:cd07721   89 GEKPYPPPVRLGLLGLLSPLLPVKPVPVDRTL--------EDGDTLDLAGG-LRVIHTPGHTPGHISLYLEEDGVLIAGD 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 531683980 174 LI--YKGVLYCDYP--STDPQAYLLSVQRLQTLALQRLLPAH 211
Cdd:cd07721  160 ALvtVGGELVPPPPpfTWDMEEALESLRKLAELDPEVLAPGH 201
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 27-211 1.82e-26

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: 101.09  E-value: 1.82e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980    27 NCYLLLGKQRALLIDSGLGVA-DIRKITDQLTALPVT-VIATHVHWDHIGSHGSY-----TDVLVHEREYswlngkfplp 99
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAeDLLAELKKLGPKKIDaIILTHGHPDHIGGLPELleapgAPVYAPEGTA---------- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980   100 lgvvkqQLMKEPCSFPGDFHMNAYTVWQGHagIVGDGDILNLGGRHIRVLHTPGHSPGHMCFFDLEREWLYCGDLIY--- 176
Cdd:smart00849  71 ------ELLKDLLALLGELGAEAEPAPPDR--TLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFagg 142

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 531683980   177 KGVLYCDYPSTDPQAYLLSVQRLQTLALQRLLPAH 211
Cdd:smart00849 143 DGRTLVDGGDAAASDALESLLKLLKLLPKLVVPGH 177
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 26-211 3.46e-23

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: 92.75  E-value: 3.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  26 TNCYLLLGKQRALLIDSGLGVADIRK-ITDQLTALPV------TVIATHVHWDHIGshgsytdvlvhereyswLNGKFPL 98
Cdd:cd07725   15 VNVYLLRDGDETTLIDTGLATEEDAEaLWEGLKELGLkpsdidRVLLTHHHPDHIG-----------------LAGKLQE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  99 PLGVVKQQLMKEPcsfpgdfhmnaytvwqghagiVGDGDILNLGGRHIRVLHTPGHSPGHMCFFDLEREWLYCGDLIY-- 176
Cdd:cd07725   78 KSGATVYILDVTP---------------------VKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLpk 136

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 531683980 177 ---KGVLYcDYPSTDP-QAYLLSVQRLQTLALQRLLPAH 211
Cdd:cd07725  137 itpNVSLW-AVRVEDPlGAYLESLDKLEKLDVDLAYPGH 174
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 27-211 1.74e-22

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: 91.26  E-value: 1.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  27 NCYLL--LGKQRALLIDSGLGVADIRKITDQLTALPVTVIATHVHWDHIGS-------HGSytDVLVHEREYSWLNGkfp 97
Cdd:cd16322   12 NTYLVadEGGGEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGvadlrrhPGA--PVYLHPDDLPLYEA--- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  98 lPLGVVKQQLMKEPCSFPGDfhmnaytvwqghaGIVGDGDILNLGGRHIRVLHTPGHSPGHMCFFDLEREWLYCGDLIYK 177
Cdd:cd16322   87 -ADLGAKAFGLGIEPLPPPD-------------RLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQ 152

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 531683980 178 G-VLYCDYPSTDPQAYLLSVQRLQTLALQ-RLLPAH 211
Cdd:cd16322  153 GsIGRTDLPGGDPKAMAASLRRLLTLPDEtRVFPGH 188
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 28-211 2.93e-22

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: 91.01  E-value: 2.93e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  28 CYLLLGKQRALLIDSG--LGVADIRKITDQLTALP--VT-VIATHVHWDHIGSHGSY------TDVLVHER--------- 87
Cdd:cd07726   18 SYLLDGEGRPALIDTGpsSSVPRLLAALEALGIAPedVDyIILTHIHLDHAGGAGLLaealpnAKVYVHPRgarhlidps 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  88 --------------EYSWLNgkfPLPlgvVKQQLMKEpcsfpgdfhmnaytvwqghagiVGDGDILNLGGRHIRVLHTPG 153
Cdd:cd07726   98 klwasaravygdeaDRLGGE---ILP---VPEERVIV----------------------LEDGETLDLGGRTLEVIDTPG 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 531683980 154 HSPGHMCFFDLEREWLYCGD---LIYKGVLYCDYPST-----DPQAYLLSVQRLQTLALQRLLPAH 211
Cdd:cd07726  150 HAPHHLSFLDEESDGLFTGDaagVRYPELDVVGPPSTpppdfDPEAWLESLDRLLSLKPERIYLTH 215
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
26-211 1.08e-18

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 81.26  E-value: 1.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980   26 TNCYLLLGKQRALLIDSGLGVADIRKITDQLTAL----PVTVIATHVHWDHIGSHGSYTDVLVHEREYSWLNGKFPLPLG 101
Cdd:pfam00753   6 VNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLgpkdIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  102 VvKQQLMKEPCSFPGDFHMNAYTVWQGHAGIVGdgdilnlGGRHIRVLHTPGHSPGHMCFFDLEREWLYCGDLIY----- 176
Cdd:pfam00753  86 L-GLAASRLGLPGPPVVPLPPDVVLEEGDGILG-------GGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFageig 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 531683980  177 ----KGVLYCDYPSTDPQAYLLSVQRLQTLALQRLLPAH 211
Cdd:pfam00753 158 rldlPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 23-211 6.83e-18

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: 78.69  E-value: 6.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  23 YEKTNCYLLLGKQRALLIDSG-LGVADIRKITDQLTALPVTVIA-THVHWDHIGshgsytdvLVHereysWLngkfplpl 100
Cdd:cd16278   15 LDGTNTYLLGAPDGVVVIDPGpDDPAHLDALLAALGGGRVSAILvTHTHRDHSP--------GAA-----RL-------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980 101 gvvkQQLMKEPCSFPGDFHMNAYTVWQGHAGIVGDGDILNLGGRHIRVLHTPGHSPGHMCFFDLEREWLYCGDLIYKG-- 178
Cdd:cd16278   74 ----AERTGAPVRAFGPHRAGGQDTDFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVMGWst 149

                        170       180       190
                 ....*....|....*....|....*....|....
gi 531683980 179 -VLycDYPSTDPQAYLLSVQRLQTLALQRLLPAH 211
Cdd:cd16278  150 tVI--APPDGDLGDYLASLERLLALDDRLLLPGH 181
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 28-211 8.36e-18

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: 79.57  E-value: 8.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  28 CYLLLGKQRALLIDSGL-----------------GVADIRKITDQLTALPVT------VIATHVHWDHIGSHGSYTD--V 82
Cdd:cd07729   34 AYLIEHPEGTILVDTGFhpdaaddpgglelafppGVTEEQTLEEQLARLGLDpedidyVILSHLHFDHAGGLDLFPNatI 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  83 LVHEREYSWLNGKFPLPLGVVKQQLMKEPCSFPGDFHMnaytvwqghagIVGDGDILnlGGrhIRVLHTPGHSPGHMCFF 162
Cdd:cd07729  114 IVQRAELEYATGPDPLAAGYYEDVLALDDDLPGGRVRL-----------VDGDYDLF--PG--VTLIPTPGHTPGHQSVL 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980 163 -DLER-EWLYCGDLIY------KGVLYCdyPSTDPQAYLLSVQRLQTLALQ---RLLPAH 211
Cdd:cd07729  179 vRLPEgTVLLAGDAAYtyenleEGRPPG--INYDPEAALASLERLKALAERegaRVIPGH 236
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 27-198 2.10e-16

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: 74.90  E-value: 2.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  27 NCYLLLGKQ--RALLIDSGlgvADIRKITDQLTALPVTVIA---THVHWDHIGSHG---SYTDVLV---HEREYSWLNGk 95
Cdd:cd07737   12 NCSLIWCEEtkEAAVIDPG---GDADKILQAIEDLGLTLKKillTHGHLDHVGGAAelaEHYGVPIigpHKEDKFLLEN- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  96 fpLPlgvvKQQLMKepcSFPG--DFHMNAYtvwqghagiVGDGDILNLGGRHIRVLHTPGHSPGHMCFFDLEREWLYCGD 173
Cdd:cd07737   88 --LP----EQSQMF---GFPPaeAFTPDRW---------LEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGD 149

                        170       180
                 ....*....|....*....|....*.
gi 531683980 174 LIYKG-VLYCDYPSTDPQAYLLSVQR 198
Cdd:cd07737  150 VLFKGsIGRTDFPGGNHAQLIASIKE 175
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 26-211 2.22e-16

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: 74.49  E-value: 2.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  26 TNCYLL-LGKQRaLLIDSGLG-VADIRKITDQLTALPVT----VIATHVHWDHIG------SHGSYTDVLVHereyswln 93
Cdd:cd07722   18 TNTYLVgTGKRR-ILIDTGEGrPSYIPLLKSVLDSEGNAtisdILLTHWHHDHVGglpdvlDLLRGPSPRVY-------- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  94 gKFPLPLGVvkqqlmKEPCSFPGDFHmnaytvwqghagIVGDGDILNLGGRHIRVLHTPGHSPGHMCFFDLEREWLYCGD 173
Cdd:cd07722   89 -KFPRPEED------EDPDEDGGDIH------------DLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGD 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 531683980 174 LIYKGvlycdypST----DPQAYLLSVQRLQTLALQRLLPAH 211
Cdd:cd07722  150 CVLGH-------GTavfeDLAAYMASLKKLLSLGPGRIYPGH 184
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 27-211 5.31e-16

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: 73.34  E-value: 5.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  27 NCYLLLGK--QRALLIDSGLGVADIRKITDQLTALPVTVIATHVHWDHIGshgsytdvLVHEreyswLNGKFPLPLgvvk 104
Cdd:cd16275   13 YSYIIIDKatREAAVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVN--------LVEP-----LLAKYDAPV---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980 105 qQLMKEPCSFPGDFHMNAYTVwqghagivGDGDILNLGGRHIRVLHTPGHSPGHMCFfdLEREWLYCGDLIY-KGVLYCD 183
Cdd:cd16275   76 -YMSKEEIDYYGFRCPNLIPL--------EDGDTIKIGDTEITCLLTPGHTPGSMCY--LLGDSLFTGDTLFiEGCGRCD 144

                        170       180       190
                 ....*....|....*....|....*....|
gi 531683980 184 YPSTDPQAYLLSVQRLQTLALQ--RLLPAH 211
Cdd:cd16275  145 LPGGDPEEMYESLQRLKKLPPPntRVYPGH 174
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 27-227 1.10e-15

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: 73.37  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  27 NCYLLLGKQRALLIDSGLGV-------ADIRKITDQLtalPVTVIATHVHWDHIGSHGSYTDVLV----HEREYswlngk 95
Cdd:cd16282   16 NIGFIVGDDGVVVIDTGASPrlarallAAIRKVTDKP---VRYVVNTHYHGDHTLGNAAFADAGApiiaHENTR------ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  96 fplplgvvkqQLMKEpcsfPGDFHMNAYTVWQGHAG----------IVGDGDILNLGGRHIRVLHT-PGHSPGHMCFFDL 164
Cdd:cd16282   87 ----------EELAA----RGEAYLELMRRLGGDAMagtelvlpdrTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLP 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 531683980 165 EREWLYCGDLIYKGVLyCDYPSTDPQAYLLSVQRLQTLALQRLLPAHytievGPSLIQETAQA 227
Cdd:cd16282  153 EEGVLFAGDLVFNGRI-PFLPDGSLAGWIAALDRLLALDATVVVPGH-----GPVGDKADLRA 209
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 28-173 4.25e-14

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: 67.87  E-value: 4.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  28 CYLLL--GKQRALLIDsglgVADIRKITDQLTALPVTVIA---THVHWDHIGshgsytdvlvhereyswlngkfplplGV 102
Cdd:cd07723   11 IYLIVdeATGEAAVVD----PGEAEPVLAALEKNGLTLTAiltTHHHWDHTG--------------------------GN 60

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 531683980 103 VKqqlMKEpcsfpgdfHMNAYTVWQGHAG-------IVGDGDILNLGGRHIRVLHTPGHSPGHMCFFDLEREWLYCGD 173
Cdd:cd07723   61 AE---LKA--------LFPDAPVYGPAEDripgldhPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGD 127
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 33-173 2.65e-11

hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione hydrolase, a detoxification enzyme known as glyoxalase II. It follows lactoylglutathione lyase, or glyoxalase I, and acts to remove the toxic metabolite methylglyoxal and related compounds. This protein belongs to the broader metallo-beta-lactamase family (pfam00753). [Cellular processes, Detoxification]


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 61.78  E-value: 2.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980   33 GKQRALLIDSGLGvADIRKITDQLTALPVTVIATHVHWDHIGShgsyTDVLVHereyswlngKFPLPL-GVVKQQLmkep 111
Cdd:TIGR03413  18 PDGQAAVVDPGEA-EPVLDALEARGLTLTAILLTHHHHDHVGG----VAELLE---------AFPAPVyGPAEERI---- 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 531683980  112 csfPGdfhmnaytvwQGHagIVGDGDILNLGGRHIRVLHTPGHSPGHMCFFDLEREWLYCGD 173
Cdd:TIGR03413  80 ---PG----------ITH--PVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGD 126
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 26-212 2.40e-10

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: 57.79  E-value: 2.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  26 TNCYLLLGKQ--RALLIDSGLGVAD-IRKITDQLTALPVTVIATHVHWDHIGSHGsytdvLVHEReyswlngkfplpLGV 102
Cdd:cd07724   12 TLSYLVGDPEtgEAAVIDPVRDSVDrYLDLAAELGLKITYVLETHVHADHVSGAR-----ELAER------------TGA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980 103 vkQQLMKEPCSFPGDFHMnaytvwqghagiVGDGDILNLGGRHIRVLHTPGHSPGHMCFFDLEREWLYCGD-LIYKGVLY 181
Cdd:cd07724   75 --PIVIGEGAPASFFDRL------------LKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDtLFVGDVGR 140

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 531683980 182 CDYPSTDPQ-AYLL--SVQR-LQTLALQ-RLLPAHY 212
Cdd:cd07724  141 PDLPGEAEGlARQLydSLQRkLLLLPDEtLVYPGHD 176
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-211 2.78e-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) 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: 57.93  E-value: 2.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  14 TYVISEhkhyeKTNC-YLLLGKQRALLIDSGLG---VADIRKITDQLTALPVTVIATHVHWDHIGSHG---SYTDVLV-- 84
Cdd:cd07743    1 TYYIPG-----PTNIgVYVFGDKEALLIDSGLDedaGRKIRKILEELGWKLKAIINTHSHADHIGGNAylqKKTGCKVya 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  85 --HEREY--------SWLNGKFPLPLGVVKQQLMKePCsfpgdfhmnaytvwqgHAGIVGDGDILNLGGRHIRVLHTPGH 154
Cdd:cd07743   76 pkIEKAFienpllepSYLGGAYPPKELRNKFLMAK-PS----------------KVDDIIEEGELELGGVGLEIIPLPGH 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 531683980 155 SPGHMCFFdLEREWLYCGD------LIYK-GVLYCdypsTDPQAYLLSVQRLQTLALQRLLPAH 211
Cdd:cd07743  139 SFGQIGIL-TPDGVLFAGDalfgeeVLEKyGIPFL----YDVEEQLETLEKLEELDADYYVPGH 197
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 36-214 2.25e-09

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 56.37  E-value: 2.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  36 RALLIDSGLGVADIRKITDQlTALPVTVIATHVHWDHIGShgsytdvlvhereyswlngkfplplgvVKQQLMKepcsFP 115
Cdd:PRK10241  23 RCLIVDPGEAEPVLNAIAEN-NWQPEAIFLTHHHHDHVGG---------------------------VKELVEK----FP 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980 116 gdfHMNAY----TVWQGHAGIVGDGDILNLGGRHIRVLHTPGHSPGHMCFFdlEREWLYCGDLIYKGVLYCDYPSTDPQA 191
Cdd:PRK10241  71 ---QIVVYgpqeTQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF--SKPYLFCGDTLFSGGCGRLFEGTASQM 145

                        170       180
                 ....*....|....*....|....*
gi 531683980 192 YlLSVQRLQTLALQRLL-PAH-YTI 214
Cdd:PRK10241 146 Y-QSLKKINALPDDTLIcCAHeYTL 169
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 36-211 2.70e-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) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 56.12  E-value: 2.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  36 RALLIDSGLGVADIRkitdqltalpvTVIATHVHWDHIGSHGSY--TDVLVHEREYSWLNGKfPLPLGVVKQqlmkepcS 113
Cdd:cd07730   71 AEQLAAGGIDPEDID-----------AVILSHLHWDHIGGLSDFpnARLIVGPGAKEALRPP-GYPSGFLPE-------L 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980 114 FPGDFHMNAYTV------WQGHAG------IVGDGDILnlggrhirVLHTPGHSPGHMCFF--DLEREWLY-CGD----- 173
Cdd:cd07730  132 LPSDFEGRLVRWeeddflWVPLGPfpraldLFGDGSLY--------LVDLPGHAPGHLGLLarTTSGTWVFlAGDachhr 203

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 531683980 174 -LIYKGV----LYCDYPSTDPQAYLLSVQRLQTLALQ---RLLPAH 211
Cdd:cd07730  204 iGLLRPSpllpLPDLDDGADREAARETLARLRELDAApdvRVVLAH 249
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 27-161 4.56e-08

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: 52.55  E-value: 4.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  27 NCYLLLGKQRALLIDSGLGVADIR---KITDQLTALPV------TVIATHVHWDHIGshGSYTD----------VLVHER 87
Cdd:cd07720   50 NAFLVRTGGRLILVDTGAGGLFGPtagKLLANLAAAGIdpedidDVLLTHLHPDHIG--GLVDAggkpvfpnaeVHVSEA 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 531683980  88 EYS-WLNGKFplplgvvKQQLMKEPCSFPGDFHmNAYTVWQGHAGIVGDGDIlnLGGrhIRVLHTPGHSPGHMCF 161
Cdd:cd07720  128 EWDfWLDDAN-------AAKAPEGAKRFFDAAR-DRLRPYAAAGRFEDGDEV--LPG--ITAVPAPGHTPGHTGY 190
NorV COG0426
Flavorubredoxin [Energy production and conversion];
26-174 7.52e-08

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 52.53  E-value: 7.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  26 TNCYLLLGKQRALlIDSG------------LGVADIRKITdqltalpvTVIATHVHWDHIGS----HGSYTDVLVHereY 89
Cdd:COG0426   34 YNSYLIVDEKTAL-IDTVgesffeeflenlSKVIDPKKID--------YIIVNHQEPDHSGSlpelLELAPNAKIV---C 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  90 SWLNGKFplplgvVKQQLmkepCSFPGDFHmnaytvwqghagIVGDGDILNLGGRHIRVLHTPG-HSPGHMCFFDLEREW 168
Cdd:COG0426  102 SKKAARF------LPHFY----GIPDFRFI------------VVKEGDTLDLGGHTLQFIPAPMlHWPDTMFTYDPEDKI 159


                 ....*.
gi 531683980 169 LYCGDL 174
Cdd:COG0426  160 LFSGDA 165
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 132-188 1.06e-07

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. 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. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 51.33  E-value: 1.06e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 531683980 132 IVGDGDILNLGGRHIRVLHTPG-HSPGHMCFFDLEREWLYCGDLIykGVLYCDYPSTD 188
Cdd:cd07709  120 VVKDGDTLDLGKHTLKFIPAPMlHWPDTMVTYDPEDKILFSGDAF--GAHGASGELFD 175
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 28-175 4.11e-06

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: 46.36  E-value: 4.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  28 CYLLLGKQRALLIDSGLGVADIRKIT-----------DQLTALPVT------VIATHVHWDHIGSHGSYTD--------- 81
Cdd:cd16277   15 SWLVRTPGRTILVDTGIGNDKPRPGPpafhnlntpylERLAAAGVRpedvdyVLCTHLHVDHVGWNTRLVDgrwvptfpn 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  82 --VLVHEREYSWLngkfplplgvvkqqlmkEPCSFPGDFHMNAYT------VWQGHAGIVGDGDILnlgGRHIRVLHTPG 153
Cdd:cd16277   95 arYLFSRAEYDHW-----------------SSPDAGGPPNRGVFEdsvlpvIEAGLADLVDDDHEI---LDGIRLEPTPG 154

                        170       180
                 ....*....|....*....|....*
gi 531683980 154 HSPGHMCfFDLE---REWLYCGDLI 175
Cdd:cd16277  155 HTPGHVS-VELEsggERALFTGDVM 178
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 37-211 8.90e-06

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: 45.65  E-value: 8.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  37 ALLIDS----GLGVADIRKItdqltalpvtvIATHVHWDHIGshGSY-------TDVLVHEREYSWLNgkfplplgvvKQ 105
Cdd:cd16280   46 DLIVDGleklGLDPADIKYI-----------LITHGHGDHYG--GAAylkdlygAKVVMSEADWDMME----------EP 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980 106 QLMKEPCSFPGDFHMNAYtvwqghagiVGDGDILNLGGRHIRVLHTPGHSPGHMCF-FDLERewlycGDLIYKGVLY--- 181
Cdd:cd16280  103 PEEGDNPRWGPPPERDIV---------IKDGDTLTLGDTTITVYLTPGHTPGTLSLiFPVKD-----GGKTHRAGLWggt 168

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 531683980 182 ---CDYPSTDPQAYLLSVQRLQTLALQR----LLPAH 211
Cdd:cd16280  169 glnTGPNLERREQYIASLERFKKIAEEAgvdvFLSNH 205
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 28-206 1.99e-05

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: 44.54  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  28 CYLLLGKQRALLIDSGLGVADIR----------------KITDQLTAL-----------PVT-VIATHVHWDHIGSHGSY 79
Cdd:cd07742   21 CLLVETDDGLVLVDTGFGLADVAdpkrrlggpfrrllrpRLDEDETAVrqiealgfdpsDVRhIVLTHLDLDHAGGLADF 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  80 TD--VLVHEREYSWLN--GKFPLPLGVVKQQLMKEPcsfpgDFHMNAYT--VWQGHAGiVGDGDILNLGgrhIRVLHTPG 153
Cdd:cd07742  101 PHatVHVHAAELDAATspRTRYERRRYRPQQLAHGP-----WWVTYAAGgeRWFGFEA-VRPLDGLPPE---ILLVPLPG 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 531683980 154 HSPGHMC--FFDLEREWLYCGDLIY-KGVLYCDYP------------STDPQAYLLSVQRLQTLALQR 206
Cdd:cd07742  172 HTRGHCGvaVRTGDRWLLHAGDAYFhHGELDPLPPpppplrlfqrllAVDRSARLANLARLRELARDH 239
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 27-175 2.44e-05

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: 43.73  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  27 NCYLLLGKQRALLIDSGlGVADIRKITDQLTALPVT------VIATHVHWDHIGShgsytdvlvhereyswlngkfpLPL 100
Cdd:cd07711   23 TVTLIKDGGKNILVDTG-TPWDRDLLLKALAEHGLSpedidyVVLTHGHPDHIGN----------------------LNL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980 101 gvvkqqlmkepcsFPGDFHMNAYTVWQGHagiVGDGDILNLGGR----HIRVLHTPGHSPGHMCFF---DLEREWLYCGD 173
Cdd:cd07711   80 -------------FPNATVIVGWDICGDS---YDDHSLEEGDGYeideNVEVIPTPGHTPEDVSVLvetEKKGTVAVAGD 143


                 ..
gi 531683980 174 LI 175
Cdd:cd07711  144 LF 145
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 28-161 4.18e-05

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: 43.61  E-value: 4.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  28 CYLLLGKQRALLIDSGLGVAD--IRKITDQL----TALPVtVIATHVHWDHIGSHGSY-----TDVLVHEREYSWL--NG 94
Cdd:cd16308   24 CYLIVTPKGNILINTGLAESVplIKKNIQALgfkfKDIKI-LLTTQAHYDHVGAMAAIkqqtgAKMMVDEKDAKVLadGG 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 531683980  95 KfplplgvvkqqlmkepcsfpGDFHMNAY-------TVWQghagIVGDGDILNLGGRHIRVLHTPGHSPGHMCF 161
Cdd:cd16308  103 K--------------------SDYEMGGYgstfapvKADK----LLHDGDTIKLGGTKLTLLHHPGHTKGSCSF 152
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 135-236 5.63e-05

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 43.68  E-value: 5.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980 135 DGDILNLGGRHIRVLHTPGHSPGHMCFFDLEREWLYCGDLIYKgvLYCD--YPSTdPQAYLLSVQRLQTLALQ-RLLPAH 211
Cdd:PLN02398 168 DGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFS--LSCGklFEGT-PEQMLSSLQKIISLPDDtNIYCGH 244

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 531683980 212 -YT---------IEVGPSLIQETAQAWEELQEKGL 236
Cdd:PLN02398 245 eYTlsnskfalsIEPNNEVLQSYAAHVAHLRSKGL 279
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 62-162 6.45e-05

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 43.21  E-value: 6.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  62 TVIATHVHWDHIGSHGSYTDVLVHEREYswlngkfplplGVVKQQLmkEPCSFPgdfhmnaytvwqghagiVGDGDILNL 141
Cdd:PLN02469  49 LVLTTHHHWDHAGGNEKIKKLVPGIKVY-----------GGSLDNV--KGCTHP-----------------VENGDKLSL 98

                         90       100
                 ....*....|....*....|..
gi 531683980 142 GGR-HIRVLHTPGHSPGHMCFF 162
Cdd:PLN02469  99 GKDvNILALHTPCHTKGHISYY 120
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 26-73 1.44e-04

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 42.19  E-value: 1.44e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 531683980  26 TNCYLLLGKQRALLIDSGLgvaDIRKITDQLTALPVTVIA---THVHWDHI 73
Cdd:COG1235   35 RSSILVEADGTRLLIDAGP---DLREQLLRLGLDPSKIDAillTHEHADHI 82
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 49-211 4.01e-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: 40.26  E-value: 4.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  49 IRKITDQltalPVT-VIATHVHWDHIGSHGSYTD----VLVHEREYSWLNgKFPLPLGVVKQQlmkepcsfpgdfhmnay 123
Cdd:cd16276   38 IRKVTDK----PVThVVYSHNHADHIGGASIFKDegatIIAHEATAELLK-RNPDPKRPVPTV----------------- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980 124 tVWQGHagivgdgDILNLGGRHIrVLHTPG--HSPGHMCFFDLEREWLYCGDLIYKG--VLYCDYPSTDPQAYLLSVQRL 199
Cdd:cd16276   96 -TFDDE-------YTLEVGGQTL-ELSYFGpnHGPGNIVIYLPKQKVLMAVDLINPGwvPFFNFAGSEDIPGYIEALDEL 166

                        170
                 ....*....|..
gi 531683980 200 QTLALQRLLPAH 211
Cdd:cd16276  167 LEYDFDTFVGGH 178
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 25-74 6.19e-04

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: 39.17  E-value: 6.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 531683980  25 KTNCYLLLGKQRALLIDSGLGvadIRKITDQLTALPVT------VIATHVHWDHIG 74
Cdd:cd07733    8 KGNCTYLETEDGKLLIDAGLS---GRKITGRLAEIGRDpedidaILVTHEHADHIK 60
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-157 1.32e-03

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


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 39.23  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 531683980  28 CYLLLGKQRALLIDSGLG------VADIRKITDQLTALPVtVIATHVHWDHIGSHG------------SYTDVLVHEREY 89
Cdd:cd16288   24 SYLITTPQGLILIDTGLEssapmiKANIRKLGFKPSDIKI-LLNSHAHLDHAGGLAalkkltgaklmaSAEDAALLASGG 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 531683980  90 SwlngkfplplgvvkqqlmkepcsfpGDFHMN----AYTvwQGHA-GIVGDGDILNLGGRHIRVLHTPGHSPG 157
Cdd:cd16288  103 K-------------------------SDFHYGddslAFP--PVKVdRVLKDGDRVTLGGTTLTAHLTPGHTRG 148
SoxH_rel_PQQ_2 TIGR04559
quinoprotein relay system zinc metallohydrolase 2; By homology, members are Zn ...
 33-73 2.23e-03

quinoprotein relay system zinc metallohydrolase 2; By homology, members are Zn metallohydrolases in the same family as the SoxH protein associated with sulfate metabolism, Bacillus cereus beta-lactamase II (see PDB:1bc2), and, more distantly, hydroxyacylglutathione hydrolase (glyoxalase II). All members occur in genomes with both PQQ biosynthesis and a PQQ-dependent (quinoprotein) dehydrogenase that has a motif of two consecutive Cys residues (see TIGR03075). The Cys-Cys motif is associated with electron transfer by specialized cytochromes such as c551. All these genomes also include a fusion protein (TIGR04557) whose domains resemble SoxY and SoxZ from thiosulfate oxidation. A conserved Cys in this fusion protein aligns to the Cys residue in SoxY that carries sulfur cycle intermediates. In many genomes, the genes for PQQ biosynthesis enzymes, PQQ-dependent enzymes, their associated cytochromes, and members of this family are clustered. Note that one to three closely related Zn metallohydrolases may occur; this family represents a specific clade among them. Some members of this family have a short additional N-terminal domain with four conserved Cys residues. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275352  Cd Length: 283  Bit Score: 38.72  E-value: 2.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 531683980   33 GKQRALLIDSGLGVAD-------IRKITDqltaLPV-TVIATHVHWDHI 73
Cdd:TIGR04559  37 GEDAVAVIDTGGSRAEgeallaaIRQRTD----LPIrYVINTHVHPDHI 81
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 146-211 2.62e-03

uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YmaE and Nostoc all1228 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. 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: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 37.56  E-value: 2.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 531683980 146 IRVLHTPGHSPGHMCFFDLEREWLYCGDLIY----KGVL-----YCDYpSTDPQAYllSVQRLQTLALQRLLPAH 211
Cdd:cd07727  104 LTLIPVPGHTRGSVVLLYKEKGVLFTGDHLAwsrrRGWLsafryVCWY-SWPEQAE--SVERLADLDFEWVLPGH 175
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 26-73 4.05e-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: 37.48  E-value: 4.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 531683980  26 TNCYLLLGKQRALLIDSGLGvadIRKITDQL----TALPVTVIATHVHWDHI 73
Cdd:cd07715   23 TSCVEVRAGGELLILDAGTG---IRELGNELmkegPPGEAHLLLSHTHWDHI 71
 
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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