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Conserved domains on  [gi|2526709325|ref|WP_288069966|]
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MULTISPECIES: MBL fold metallo-hydrolase [Herbaspirillum]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 11422978)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme

CATH:  3.60.15.30
EC:  3.-.-.-
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  17597585|11471246
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 15-226 7.30e-38

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: 133.66  E-value: 7.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  15 LERGWLSSNNVLLFGRDEVAMIDSGYVAHAEQTqtlVRHVLHQRGrERLDVLLNTHLHSDHCGGNAALHAAYGCRIAIPA 94
Cdd:COG0491     8 TPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEA---LLAALAALG-LDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  95 AEDAKVRQWDEDALsyratgQRCPRFVHEQLIRSGDVLSLGDLDWTALAAPGHDPHALLLYCAQEGVLISADALWRNGFG 174
Cdd:COG0491    84 AEAEALEAPAAGAL------FGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2526709325 175 II-FPELDgesgFEEARATLELIRSLDVRTVIPGHGAPFT-EVDDALDKAFSRL 226
Cdd:COG0491   158 RPdLPDGD----LAQWLASLERLLALPPDLVIPGHGPPTTaEAIDYLEELLAAL 207
 
Name Accession Description Interval E-value
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 15-226 7.30e-38

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: 133.66  E-value: 7.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  15 LERGWLSSNNVLLFGRDEVAMIDSGYVAHAEQTqtlVRHVLHQRGrERLDVLLNTHLHSDHCGGNAALHAAYGCRIAIPA 94
Cdd:COG0491     8 TPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEA---LLAALAALG-LDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  95 AEDAKVRQWDEDALsyratgQRCPRFVHEQLIRSGDVLSLGDLDWTALAAPGHDPHALLLYCAQEGVLISADALWRNGFG 174
Cdd:COG0491    84 AEAEALEAPAAGAL------FGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2526709325 175 II-FPELDgesgFEEARATLELIRSLDVRTVIPGHGAPFT-EVDDALDKAFSRL 226
Cdd:COG0491   158 RPdLPDGD----LAQWLASLERLLALPPDLVIPGHGPPTTaEAIDYLEELLAAL 207
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 23-208 1.69e-29

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: 110.72  E-value: 1.69e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325   23 NNVLLFGRDEVAMIDSGyvahaEQTQTLVRHVLHQRGRERLDVLLNTHLHSDHCGGNAALHAAYGCRIAIPAAEDAKVRQ 102
Cdd:smart00849   1 NSYLVRDDGGAILIDTG-----PGEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKD 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  103 WDEDALSYRATGQRCPRFVheqLIRSGDVLSLGDLDWTALAAPGHDPHALLLYCAQEGVLISADALWRNGFGIIFPELDG 182
Cdd:smart00849  76 LLALLGELGAEAEPAPPDR---TLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGD 152

                          170       180
                   ....*....|....*....|....*.
gi 2526709325  183 ESgFEEARATLELIRSLDVRTVIPGH 208
Cdd:smart00849 153 AA-ASDALESLLKLLKLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 13-208 2.14e-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: 110.45  E-value: 2.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  13 HVLERGWLSSNNVLLFGRD-EVAMIDSGYVAHAEQTQTLVRHVLhqrgreRLDVLLNTHLHSDHCGGNAALHAAYGCRIA 91
Cdd:cd06262     1 KRLPVGPLQTNCYLVSDEEgEAILIDPGAGALEKILEAIEELGL------KIKAILLTHGHFDHIGGLAELKEAPGAPVY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  92 IPAAEDAKVRqwDEDALSYRATGQRCPRFVHEQLIRSGDVLSLGDLDWTALAAPGHDPHALLLYCAQEGVLISADALWRN 171
Cdd:cd06262    75 IHEADAELLE--DPELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAG 152

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2526709325 172 GFG-IIFPELDGESGFEEARATLELIRslDVRTVIPGH 208
Cdd:cd06262   153 SIGrTDLPGGDPEQLIESIKKLLLLLP--DDTVVYPGH 188
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
17-208 1.16e-24

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 98.59  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  17 RGWLSSNNVLLFGRDEVAMIDSGYvahAEQTQTLVRHVLHQRGRERLDVLLNTHLHSDHCGGNAALHAAYGCRIAIPAAE 96
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGG---SAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  97 DAKVRQWDEDALSYRATGQRCP--RFVHEQLIRSGDVLSLGDLDWTALAAPGHDPHALLLYCAQEGVLISADALWRNGFG 174
Cdd:pfam00753  78 ARELLDEELGLAASRLGLPGPPvvPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIG 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2526709325 175 IIFPELDGE-----SGFEEARATLELIRSLDVRTVIPGH 208
Cdd:pfam00753 158 RLDLPLGGLlvlhpSSAESSLESLLKLAKLKAAVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 40-208 1.64e-05

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 45.60  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  40 YVAHAEQTQTL----------VRHVLHQRGRErLDVLLNTHLHSDHCGGNAALHAAYGCRIAIPAAedakvrqwDEDals 109
Cdd:PLN02398   90 YLLHDEDTGTVgvvdpseavpVIDALSRKNRN-LTYILNTHHHYDHTGGNLELKARYGAKVIGSAV--------DKD--- 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325 110 yratgqRCPRFvhEQLIRSGDVLSLGDLDWTALAAPGHDPHALLLYCAQEGVLISADALWRNGFGIIFpeldgESGFEEA 189
Cdd:PLN02398  158 ------RIPGI--DIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGKLF-----EGTPEQM 224

                         170       180
                  ....*....|....*....|
gi 2526709325 190 RATLELIRSL-DVRTVIPGH 208
Cdd:PLN02398  225 LSSLQKIISLpDDTNIYCGH 244
 
Name Accession Description Interval E-value
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 15-226 7.30e-38

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: 133.66  E-value: 7.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  15 LERGWLSSNNVLLFGRDEVAMIDSGYVAHAEQTqtlVRHVLHQRGrERLDVLLNTHLHSDHCGGNAALHAAYGCRIAIPA 94
Cdd:COG0491     8 TPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEA---LLAALAALG-LDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  95 AEDAKVRQWDEDALsyratgQRCPRFVHEQLIRSGDVLSLGDLDWTALAAPGHDPHALLLYCAQEGVLISADALWRNGFG 174
Cdd:COG0491    84 AEAEALEAPAAGAL------FGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVG 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2526709325 175 II-FPELDgesgFEEARATLELIRSLDVRTVIPGHGAPFT-EVDDALDKAFSRL 226
Cdd:COG0491   158 RPdLPDGD----LAQWLASLERLLALPPDLVIPGHGPPTTaEAIDYLEELLAAL 207
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 23-208 1.69e-29

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: 110.72  E-value: 1.69e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325   23 NNVLLFGRDEVAMIDSGyvahaEQTQTLVRHVLHQRGRERLDVLLNTHLHSDHCGGNAALHAAYGCRIAIPAAEDAKVRQ 102
Cdd:smart00849   1 NSYLVRDDGGAILIDTG-----PGEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKD 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  103 WDEDALSYRATGQRCPRFVheqLIRSGDVLSLGDLDWTALAAPGHDPHALLLYCAQEGVLISADALWRNGFGIIFPELDG 182
Cdd:smart00849  76 LLALLGELGAEAEPAPPDR---TLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGD 152

                          170       180
                   ....*....|....*....|....*.
gi 2526709325  183 ESgFEEARATLELIRSLDVRTVIPGH 208
Cdd:smart00849 153 AA-ASDALESLLKLLKLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 13-208 2.14e-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: 110.45  E-value: 2.14e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  13 HVLERGWLSSNNVLLFGRD-EVAMIDSGYVAHAEQTQTLVRHVLhqrgreRLDVLLNTHLHSDHCGGNAALHAAYGCRIA 91
Cdd:cd06262     1 KRLPVGPLQTNCYLVSDEEgEAILIDPGAGALEKILEAIEELGL------KIKAILLTHGHFDHIGGLAELKEAPGAPVY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  92 IPAAEDAKVRqwDEDALSYRATGQRCPRFVHEQLIRSGDVLSLGDLDWTALAAPGHDPHALLLYCAQEGVLISADALWRN 171
Cdd:cd06262    75 IHEADAELLE--DPELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAG 152

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2526709325 172 GFG-IIFPELDGESGFEEARATLELIRslDVRTVIPGH 208
Cdd:cd06262   153 SIGrTDLPGGDPEQLIESIKKLLLLLP--DDTVVYPGH 188
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
17-208 1.16e-24

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 98.59  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  17 RGWLSSNNVLLFGRDEVAMIDSGYvahAEQTQTLVRHVLHQRGRERLDVLLNTHLHSDHCGGNAALHAAYGCRIAIPAAE 96
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGG---SAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  97 DAKVRQWDEDALSYRATGQRCP--RFVHEQLIRSGDVLSLGDLDWTALAAPGHDPHALLLYCAQEGVLISADALWRNGFG 174
Cdd:pfam00753  78 ARELLDEELGLAASRLGLPGPPvvPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIG 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2526709325 175 IIFPELDGE-----SGFEEARATLELIRSLDVRTVIPGH 208
Cdd:pfam00753 158 RLDLPLGGLlvlhpSSAESSLESLLKLAKLKAAVIVPGH 196
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 12-209 6.22e-20

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: 85.74  E-value: 6.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  12 LHVLErGWLSSNNVLLFGRDEVAMIDSGYVAHAEQtqtlVRHVLHQRGRERLD---VLLnTHLHSDHCGGNAALHAAYGC 88
Cdd:cd07721     2 VYQLP-LLPPVNAYLIEDDDGLTLIDTGLPGSAKR----ILKALRELGLSPKDirrILL-THGHIDHIGSLAALKEAPGA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  89 RIAI-----PAAEDAKVRQWDEDALSYRATGQRCPRFVHE--QLIRSGDVLSLGDlDWTALAAPGHDP-H-ALLLycAQE 159
Cdd:cd07721    76 PVYAhereaPYLEGEKPYPPPVRLGLLGLLSPLLPVKPVPvdRTLEDGDTLDLAG-GLRVIHTPGHTPgHiSLYL--EED 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2526709325 160 GVLISADALW-RNGFGIIFPELDGESgFEEARATLELIRSLDVRTVIPGHG 209
Cdd:cd07721   153 GVLIAGDALVtVGGELVPPPPPFTWD-MEEALESLRKLAELDPEVLAPGHG 202
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 18-213 1.34e-19

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: 85.09  E-value: 1.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  18 GWLSSNNVLLF--GRDEVAMIDSGyvahaEQTQTLVRHVlhQRGRERLDVLLNTHLHSDHCGGNAALHAAYGCRIAIPAA 95
Cdd:cd16322     7 GPLQENTYLVAdeGGGEAVLVDPG-----DESEKLLARF--GTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  96 EdakVRQWDEDALSYRATGQRCPRFVH-EQLIRSGDVLSLGDLDWTALAAPGHDPHALLLYCAQEGVLISADALWRNGFG 174
Cdd:cd16322    80 D---LPLYEAADLGAKAFGLGIEPLPPpDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIG 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2526709325 175 IIfpELDGESGFEEARATLELIRSLDVRTVIPGHGAPFT 213
Cdd:cd16322   157 RT--DLPGGDPKAMAASLRRLLTLPDETRVFPGHGPPTT 193
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 18-211 1.10e-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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 82.61  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  18 GWLSSNNVLLFGRDEVAMIDSGY-VAHAEQTQTLVRhvlhQRGRERLDVLLNTHLHSDHCGGNAALhAAYGCRIAipAAE 96
Cdd:cd16282    11 GGFISNIGFIVGDDGVVVIDTGAsPRLARALLAAIR----KVTDKPVRYVVNTHYHGDHTLGNAAF-ADAGAPII--AHE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  97 DAKVRQwDEDALSYRATGQRCPRFVHE--------QLIRSGDVLSLGDLDWTALA-APGHDPHALLLYCAQEGVLISADA 167
Cdd:cd16282    84 NTREEL-AARGEAYLELMRRLGGDAMAgtelvlpdRTFDDGLTLDLGGRTVELIHlGPAHTPGDLVVWLPEEGVLFAGDL 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2526709325 168 LWrNGFGIIFPeldgESGFEEARATLELIRSLDVRTVIPGHGAP 211
Cdd:cd16282   163 VF-NGRIPFLP----DGSLAGWIAALDRLLALDATVVVPGHGPV 201
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 25-208 1.20e-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) 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: 82.19  E-value: 1.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  25 VLLFGRDEVAMIDSGyvaHAEQTQTLVRHVLHQRGrERLDVLLNTHLHSDHCGGNAALHAAYGCRIAIPAAEDAKVRQWD 104
Cdd:cd07743    12 VYVFGDKEALLIDSG---LDEDAGRKIRKILEELG-WKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAFIENPL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325 105 -EDALSYRATGQR--CPRFVH------EQLIRSGDvLSLGDLDWTALAAPGHDPHAL-LLYcaQEGVLISADALwrngFG 174
Cdd:cd07743    88 lEPSYLGGAYPPKelRNKFLMakpskvDDIIEEGE-LELGGVGLEIIPLPGHSFGQIgILT--PDGVLFAGDAL----FG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2526709325 175 I-------IFPELDgesgFEEARATLELIRSLDVRTVIPGH 208
Cdd:cd07743   161 EevlekygIPFLYD----VEEQLETLEKLEELDADYYVPGH 197
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 17-215 7.98e-17

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: 76.95  E-value: 7.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  17 RGWLSSNNVLLF-GRDEVAMIDSGYvAHAEQTQTLVRHvLHQRGRERLDV--LLNTHLHSDHCGGNAALHAAYGCRIAIP 93
Cdd:cd07725     9 PGPLGHVNVYLLrDGDETTLIDTGL-ATEEDAEALWEG-LKELGLKPSDIdrVLLTHHHPDHIGLAGKLQEKSGATVYIL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  94 aaedakvrqwdedalSYRAtgqrcprfvheqlIRSGDVLSLGDLDWTALAAPGHDPHALLLYCAQEGVLISADALWRNgf 173
Cdd:cd07725    87 ---------------DVTP-------------VKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLPK-- 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2526709325 174 giIFPELDGESGFEEA-----RATLELIRSLDVRTVIPGHGAPFTEV 215
Cdd:cd07725   137 --ITPNVSLWAVRVEDplgayLESLDKLEKLDVDLAYPGHGGPIKDP 181
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 32-208 1.70e-16

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: 75.57  E-value: 1.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  32 EVAMIDSGYVAhaeqtqtLVRHVLHQRGReRLDVLLNTHLHSDHCGGNAALHAAYG-CRIAIPAAEdakvrqwdedalsy 110
Cdd:cd07723    21 EAAVVDPGEAE-------PVLAALEKNGL-TLTAILTTHHHWDHTGGNAELKALFPdAPVYGPAED-------------- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325 111 ratgqRCP---RFVHEqlirsGDVLSLGDLDWTALAAPGHDPHALLLYCAQEGVLISADALWRNGFGIIFpeldgESGFE 187
Cdd:cd07723    79 -----RIPgldHPVKD-----GDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGRFF-----EGTAE 143

                         170       180
                  ....*....|....*....|..
gi 2526709325 188 EARATLELIRSLDVRTVI-PGH 208
Cdd:cd07723   144 QMYASLQKLLALPDDTLVyCGH 165
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 23-211 6.06e-16

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: 74.45  E-value: 6.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  23 NNVLLFGRDEVAMIDSGyVAHAEQTQTLVRHVlhqrGRERLDVLLNTHLHSDHCGGNAALHAAYGCRIAIPAAEDAKVRQ 102
Cdd:cd16278    19 NTYLLGAPDGVVVIDPG-PDDPAHLDALLAAL----GGGRVSAILVTHTHRDHSPGAARLAERTGAPVRAFGPHRAGGQD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325 103 WDedalsyratgqrcprFVHEQLIRSGDVLSLGDLDWTALAAPGHDPHALLLYCAQEGVLISADALWRNGFGIIFPElDG 182
Cdd:cd16278    94 TD---------------FAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVMGWSTTVIAPP-DG 157

                         170       180
                  ....*....|....*....|....*....
gi 2526709325 183 ESGfeEARATLELIRSLDVRTVIPGHGAP 211
Cdd:cd16278   158 DLG--DYLASLERLLALDDRLLLPGHGPP 184
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 14-211 1.68e-13

metallo-beta-lactamases; subclasses B1 and B2 and related proteins; 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. B1 MBls include 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. B2 MBLs have a narrow substrate profile that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis. B2 MBLs include Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I.


Pssm-ID: 293793 [Multi-domain]  Cd Length: 219  Bit Score: 68.34  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  14 VLERGWLSSNNVLLFGRDEVAMIDSGYvaHAEQTQTLVRHVLHQRGRERLDVLlNTHLHSDHCGGNAALHAAYGCRIAIP 93
Cdd:cd07707    13 VTDLGSVPSNGLVYNGSKGLVLVDSTW--TPKTTKELIKEIEKVSQKPVTEVI-NTHFHTDRAGGNAYLKERGAKTVSTA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  94 AAEDAKVRQWDEDALSYRATGQRCPrfvheqliRSGDVLSLGDLDW----------TALAAPGHDPHALLLYCAQEGVLI 163
Cdd:cd07707    90 LTRDLAKSEWAEIVAFTRKGLPEYP--------DLGYELPDGVLDGdfnlqfgkveAFYPGPAHTPDNIVVYFPQENVLY 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2526709325 164 sadalwrnGFGIIFPELDGESGFEEARA---TLELIRSLD--VRTVIPGHGAP 211
Cdd:cd07707   162 --------GGCIIKETDLGNVADADVKEwptSIERLKKRYrnIKAVIPGHGEV 206
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 26-208 4.04e-13

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: 67.13  E-value: 4.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  26 LLFGRDEVAMIDSGYVAHAEQTQTLVRhvLHQRGRERLDVLLNTHLHSDHCGGNAAL-HAAYGCRIAI-PAAED------ 97
Cdd:cd07726    20 LLDGEGRPALIDTGPSSSVPRLLAALE--ALGIAPEDVDYIILTHIHLDHAGGAGLLaEALPNAKVYVhPRGARhlidps 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  98 ------AKVRQWDEDALSYRatgqrcPRFVHEQLIRS---GDVLSLGDLDWTALAAPGHDPHALLLYCAQEGVLISADAl 168
Cdd:cd07726    98 klwasaRAVYGDEADRLGGE------ILPVPEERVIVledGETLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDA- 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2526709325 169 wrngFGIIFPELDGESGF---------EEARATLELIRSLDVRTVIPGH 208
Cdd:cd07726   171 ----AGVRYPELDVVGPPstpppdfdpEAWLESLDRLLSLKPERIYLTH 215
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 54-208 1.47e-12

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: 65.27  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  54 VLHQRGRErLDVLLNTHLHSDHCGGNAALHAAYGCRIAIPAAEDAkvrQWDE--DALSYRATGQRCPRFVHEQLIRSGDV 131
Cdd:cd07737    39 AIEDLGLT-LKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKEDK---FLLEnlPEQSQMFGFPPAEAFTPDRWLEEGDT 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325 132 LSLGDLDWTALAAPGHDPHALLLYCAQEGVLISADALWRNGFGII-FPELDGEsgfeearatlELIRSL---------DV 201
Cdd:cd07737   115 VTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTdFPGGNHA----------QLIASIkekllplgdDV 184


                  ....*..
gi 2526709325 202 rTVIPGH 208
Cdd:cd07737   185 -TFIPGH 190
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-222 6.41e-12

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: 64.53  E-value: 6.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  35 MIDSGYVAHAEQT-----QTL------VRHVLHqrgrerldvllnTHLHSDHCGGNAALHAAYGCRIAIpAAEDAKVRQW 103
Cdd:cd16280    35 LIDALNNNEAADLivdglEKLgldpadIKYILI------------THGHGDHYGGAAYLKDLYGAKVVM-SEADWDMMEE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325 104 DEDALSYRATGQRCPRFVHeqlIRSGDVLSLGDLDWTALAAPGHDPHAL-LLYCAQEGVLISADALWrNGFGIIFpeLDG 182
Cdd:cd16280   102 PPEEGDNPRWGPPPERDIV---IKDGDTLTLGDTTITVYLTPGHTPGTLsLIFPVKDGGKTHRAGLW-GGTGLNT--GPN 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2526709325 183 ESGFEEARATLELIRSL----DVRTVIPGHgaPFTevDDALDKA 222
Cdd:cd16280   176 LERREQYIASLERFKKIaeeaGVDVFLSNH--PFQ--DGSLEKR 215
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 26-208 1.30e-10

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: 59.56  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  26 LLFGRDEVAMIDSGY--VAHAEQTQTLvrhvlhqrgrERLDVL-LNTHLHSDHCGGN-----AALHAAygcRIAIPAAED 97
Cdd:cd07712    13 LLRGRDRALLIDTGLgiGDLKEYVRTL----------TDLPLLvVATHGHFDHIGGLhefeeVYVHPA---DAEILAAPD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  98 akvrqwDEDALSYRATGQRCPRFVHEQLIRSGDVLSLGDLDWTALAAPGHDPHALLLYCAQEGVLISADALwrnGFGIIF 177
Cdd:cd07712    80 ------NFETLTWDAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVV---YDGPLI 150

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2526709325 178 PELDGeSGFEEARATLELIRSL--DVRTVIPGH 208
Cdd:cd07712   151 MDLPH-SDLDDYLASLEKLSKLpdEFDKVLPGH 182
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 25-167 1.68e-10

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: 60.26  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  25 VLLFGRDEVAMIDSGYVAHAEQTQTLVRHVLHQRGRERLDVLLNTHLHSDHCGGNAALHAAYGCR---IAIPAAEDAKVR 101
Cdd:COG2333    15 LIRTPDGKTILIDTGPRPSFDAGERVVLPYLRALGIRRLDLLVLTHPDADHIGGLAAVLEAFPVGrvlVSGPPDTSETYE 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526709325 102 QWDEDALSYRATGQRCprfvheqliRSGDVLSLGDLDWTALAAPGHDPHA---------LLLYCAQEGVLISADA 167
Cdd:COG2333    95 RLLEALKEKGIPVRPC---------RAGDTWQLGGVRFEVLWPPEDLLEGsdennnslvLRLTYGGFSFLLTGDA 160
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 62-210 4.04e-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: 4.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  62 RLDVLLNTHLHSDHCGGNAALHAAYGCRIAIPAAEDAKvrqwdedalsyratgqrcprFVHEqLIRSGDVLSLGDLDWTA 141
Cdd:cd07724    48 KITYVLETHVHADHVSGARELAERTGAPIVIGEGAPAS--------------------FFDR-LLKDGDVLELGNLTLEV 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526709325 142 LAAPGHDPHALLLYCAQEGVLISADALWRNGFGII-FPELDGESgfeeARA---TL-ELIRSLDVRTVI-PGHGA 210
Cdd:cd07724   107 LHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPdLPGEAEGL----ARQlydSLqRKLLLLPDETLVyPGHDY 177
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 6-221 8.76e-10

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: 57.88  E-value: 8.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325   6 LRLPPSLHVLERGwLSSNNVLLFGrDEVAMIDSGYVAHAEQTQTLVRHVLhqrGRERLDVLLNTHLHSDHCGGNAALHAA 85
Cdd:cd07709    17 LRLFEGEYPTPRG-TSYNSYLIKD-EKTALIDTVKEPFFDEFLENLEEVI---DPRKIDYIVVNHQEPDHSGSLPELLEL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  86 YGcriaipaaeDAKVrqwdedalsyrATGQRCPRFVHEQL---------IRSGDVLSLGDLDWTALAAPG-HDPHALLLY 155
Cdd:cd07709    92 AP---------NAKI-----------VCSKKAARFLKHFYpgiderfvvVKDGDTLDLGKHTLKFIPAPMlHWPDTMVTY 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325 156 CAQEGVLISADAlwrngFG--IIFPEL--DGESGFEEA----------------RATLELIRSLDVRTVIPGHGAPF-TE 214
Cdd:cd07709   152 DPEDKILFSGDA-----FGahGASGELfdDEVEDYLEEarryyanimgpfskqvRKALEKLEALDIKMIAPSHGPIWrKD 226


                  ....*..
gi 2526709325 215 VDDALDK 221
Cdd:cd07709   227 PGEIIDL 233
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 62-208 3.09e-09

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: 55.24  E-value: 3.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  62 RLDVLLNTHLHSDHCGGNAALHAAYGCRIAIPAAEdakvrqwdedalsYRATGQRCPRFVheqLIRSGDVLSLGDLDWTA 141
Cdd:cd16275    47 TLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEE-------------IDYYGFRCPNLI---PLEDGDTIKIGDTEITC 110

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526709325 142 LAAPGHDP--HALLLycaqEGVLISADALWRNGFGII-FPELDGESGFEearaTLELIRSL---DVRtVIPGH 208
Cdd:cd16275   111 LLTPGHTPgsMCYLL----GDSLFTGDTLFIEGCGRCdLPGGDPEEMYE----SLQRLKKLpppNTR-VYPGH 174
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 61-225 8.34e-09

Janthinobacterium lividum THIN-B 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 THIN-B-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: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 55.38  E-value: 8.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  61 ERLDVLLNTHLHSDHCGGNAALHAAYGCRIAIPAAEDAKVR---------QWDEDALSYratgqrCPRFVHEQLIRSGDV 131
Cdd:cd16312    59 EDVKLILNSHAHWDHAGGIAALQKASGATVAASAHGAQVLQsgtngkddpQYQAKPVVH------VAKVAKVKEVGEGDT 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325 132 LSLGDLDWTALAAPGHDPHALL---LYCAQEGVL--ISADAL-------WRNGFGIIFPelDGESGFeeaRATLELIRSL 199
Cdd:cd16312   133 LKVGPLRLTAHMTPGHTPGGTTwtwTSCEGQRCLdvVYADSLnpyssgdFYYTGKGGYP--DISASF---RASIAKVAAL 207

                         170       180
                  ....*....|....*....|....*.
gi 2526709325 200 DVRTVIPGHgaPFTEvdDALDKAFSR 225
Cdd:cd16312   208 PCDIIIAVH--PGFT--DVLDKAKRR 229
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 35-149 1.75e-08

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: 54.25  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  35 MIDSGYvahaEQTQTLVRHVLHQRGRERLDV--LLNTHLHSDHCGGNAALHAAYGCRIAIPAAEdakVRQWDEDALSYRA 112
Cdd:cd16288    35 LIDTGL----ESSAPMIKANIRKLGFKPSDIkiLLNSHAHLDHAGGLAALKKLTGAKLMASAED---AALLASGGKSDFH 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2526709325 113 TGQRCPRF--VH-EQLIRSGDVLSLGDLDWTALAAPGHDP 149
Cdd:cd16288   108 YGDDSLAFppVKvDRVLKDGDRVTLGGTTLTAHLTPGHTR 147
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 25-152 4.03e-08

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: 53.12  E-value: 4.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  25 VLLFGRDEVAMIDSGYVAHAEqtqtLVRHVLHQRGRERLDV--LLNTHLHSDHCGGNAALHAAYGCRI-AIPAAedAKVr 101
Cdd:cd16315    25 ILITGDDGHVLIDSGTEEAAP----LVLANIRKLGFDPKDVrwLLSSHEHFDHVGGLAALQRATGARVaASAAA--APV- 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526709325 102 qwdedalsyRATGQRCP----RFVHE--------QLIRSGDVLSLGDLDWTALAAPGHDPHAL 152
Cdd:cd16315    98 ---------LESGKPAPddpqAGLHEpfppvrvdRIVEDGDTVALGSLRLTAHATPGHTPGAL 151
NorV COG0426
Flavorubredoxin [Energy production and conversion];
6-221 6.45e-08

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 53.30  E-value: 6.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325   6 LRLPPSLHVLERGwLSSNNVLLFGrDEVAMIDSGyvaHAEQTQTLVRHVLHQRGRERLDVLLNTHLHSDHCGGNAALHAA 85
Cdd:COG0426    19 RRLFEGEYPTPRG-TTYNSYLIVD-EKTALIDTV---GESFFEEFLENLSKVIDPKKIDYIIVNHQEPDHSGSLPELLEL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  86 YgcriaiPaaeDAKV---RQWdEDALsyratgqrcPRFVHE-----QLIRSGDVLSLGDLDWTALAAPG-HDPHALLLYC 156
Cdd:COG0426    94 A------P---NAKIvcsKKA-ARFL---------PHFYGIpdfrfIVVKEGDTLDLGGHTLQFIPAPMlHWPDTMFTYD 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325 157 AQEGVLISADAlwrngFGIIFP-------ELDGESgFEEAR---------------ATLELIRSLDVRTVIPGHGAPFTE 214
Cdd:COG0426   155 PEDKILFSGDA-----FGSHGAsdelfddEVDEHL-EEEARryyanimmpfskqvlKALKKVRGLDIDMIAPSHGPIWRG 228


                  ....*...
gi 2526709325 215 -VDDALDK 221
Cdd:COG0426   229 nPKEILDW 236
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 66-149 8.75e-08

Bradyrhizobium diazoefficiens BJP-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 BJP-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: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 52.10  E-value: 8.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  66 LLNTHLHSDHCGGNAALHAAYGCRIAIPAA-----EDAKVRQWDEDALSYratgqrcPRFVHEQLIRSGDVLSLGDLDWT 140
Cdd:cd16309    64 LLNTHAHFDHAGGLAELKKATGAQLVASAAdkpllESGYVGSGDTKNLQF-------PPVRVDRVIGDGDKVTLGGTTLT 136


                  ....*....
gi 2526709325 141 ALAAPGHDP 149
Cdd:cd16309   137 AHLTPGHSP 145
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 64-149 1.73e-07

AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Pseudomonas Aeruginosa AIM-1, Serratia marcescens SMB-1, Erythrobacter vulgaris EVM-1, and Janthinobacterium lividum THIN-B. 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 AIM-1-,SMB-1-, EVM-1-, THIN-B-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: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 51.19  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  64 DV--LLNTHLHSDHCGGNAALHAAYGCRIAIPAAEDAKVRQWDEDALSYRATG-QRCPRFVHEQLIRSGDVLSLGDLDWT 140
Cdd:cd16290    60 DVklILNSHAHFDHAGGIAALQRDSGATVAASPAGAAALRSGGVDPDDPQAGAaDPFPPVAKVRVVADGEVVKLGPLAVT 139


                  ....*....
gi 2526709325 141 ALAAPGHDP 149
Cdd:cd16290   140 AHATPGHTP 148
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 35-147 8.61e-07

SMB-1, THIN-B 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 SMB-1- and THIN-B-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: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 49.09  E-value: 8.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  35 MIDSGYVAHAEQTQTLVRhvlhQRGRERLDV--LLNTHLHSDHCGGNAALHAAYGCRIAIPAAEDAKVR--QWDEDALSY 110
Cdd:cd16313    35 LIDGGFPKSPEQIAASIR----QLGFKLEDVkyILSSHDHWDHAGGIAALQKLTGAQVLASPATVAVLRsgSMGKDDPQF 110

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2526709325 111 RATgQRCPRFVHEQLIRSGDVLSLGDLDWTALAAPGH 147
Cdd:cd16313   111 GGL-TPMPPVASVRAVRDGEVVKLGPLAVTAHATPGH 146
CphS_ImiS-like_MBL-B2 cd16287
metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas ...
 10-212 1.81e-06

metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I. 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. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis.


Pssm-ID: 293845  Cd Length: 226  Bit Score: 48.19  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  10 PSLHVLERGWLSSNNVLLFGRDEVAMIDSGYVAH-AEQTQTLVRHVlhqrGRERLDVLLNTHLHSDHCGGNAALHAAYGC 88
Cdd:cd16287     9 PLYIVEDKEYVQENSMVYIGTDGITIIGATWTPEtAETLYKEIRKV----SPLPINEVINTNYHTDRAGGNAYWKTLGAK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  89 RIAIPAAEDAKVRQWDEDALSYRATGQRCPR--FVHEQLIRSGD-VLSLGDLDwTALAAPGHDPHALLLYCAQEGVLISa 165
Cdd:cd16287    85 IVATQMTYDLQKSQWGSIVNFTRQGNNKYPNleKSLPDTVFPGDfNLQNGSIR-AMYLGEAHTKDGIFVYFPAERVLYG- 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2526709325 166 dalwrngfGIIFPELDGESGFEEARA---TLELIRSLD------VRTVIPGHGAPF 212
Cdd:cd16287   163 --------NCILKENLGNMSFANRTEypkTLEKLKGLIeqgelkVDSIIAGHDTPI 210
SPM-1-like_MBL-B1-B2-like cd16286
Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; ...
 2-209 2.47e-06

Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; MBL-fold metallo-hydrolase domain; SPM-1 was first identified in a Pseudomonas aeruginosa strain from a paediatric leukaemia patient and is a major clinical problem. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs are most closely related to each other. SPM-1 appears to be a hybrid B1/B2 MBL.


Pssm-ID: 293844 [Multi-domain]  Cd Length: 236  Bit Score: 47.91  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325   2 NTSALRLPPSLHVLERGWLSSNNVLL--FGRDEVAMIDSGYVAHAeqTQTLVRHVLHQRGRERLdVLLNTHLHSDHCGGN 79
Cdd:cd16286     6 NLTAREIDPDVFVITHRDPWSSNVLVvkMLDGTVVIVDSPYTNLA--TQTVLDWIAKTMGPRKV-VAINTHFHLDGTGGN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  80 AALH----AAYGCRIAIP--AAEDAKVRQW-----DEDALSYRATGQRCPRFVHEQLIRSGDVLSLGD-LDWTALAAPGH 147
Cdd:cd16286    83 EALKkrgiPTWGSDLTKQllLERGKADRIKaaeflKNEDLKRRIESSPPVPPDNVFDLKEGKVFSFGNeLVEVSFPGPAH 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526709325 148 DPHALLLYCAQEGVLISAdALWRNGFGIIFpelDGESGFEEARATLELIRSLDVRTVIPGHG 209
Cdd:cd16286   163 APDNVVVYFPERKILFGG-CMIKPGKELGN---LGDANMKAWPDSVRRLKKFDAKIVIPGHG 220
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 64-212 2.81e-06

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: 46.81  E-value: 2.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  64 DVLLNTHLHSDHCGgNAALHaaygcriaipaaEDAKVRQ-WDEDALSYRATGqrcprfvheqlIRSGDVLSLGDlDWTAL 142
Cdd:cd07711    62 DYVVLTHGHPDHIG-NLNLF------------PNATVIVgWDICGDSYDDHS-----------LEEGDGYEIDE-NVEVI 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526709325 143 AAPGHDPH--ALLLYCAQEG-VLISADALWRNGFGIIFPELDGESGFEE-ARATLELIRSL-DVrtVIPGHGAPF 212
Cdd:cd07711   117 PTPGHTPEdvSVLVETEKKGtVAVAGDLFEREEDLEDPILWDPLSEDPElQEESRKRILALaDW--IIPGHGPPF 189
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 63-149 3.17e-06

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


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 47.54  E-value: 3.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  63 LDVLLNTHLHSDHCGGNAALHAAYGCRIAIPAAEDAKVRQW------DEDALSYRATGQRCPRFVHEqlirsGDVLSLGD 136
Cdd:cd07708    61 TKLILISHAHFDHAGGSAEIKKQTGAKVMAGAEDVSLLLSGgssdfhYANDSSTYFPQSTVDRAVHD-----GERVTLGG 135

                          90
                  ....*....|...
gi 2526709325 137 LDWTALAAPGHDP 149
Cdd:cd07708   136 TVLTAHATPGHTP 148
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 25-148 3.42e-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: 46.74  E-value: 3.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  25 VLLFGRDEVAMIDSGYVAHAEQtQTLVRHvLHQRGRERLDVLLNTHLHSDHCGGNAALHAAYGC-RIAIPAAEDAKV--R 101
Cdd:cd07731    13 ILIQTPGKTILIDTGPRDSFGE-DVVVPY-LKARGIKKLDYLILTHPDADHIGGLDAVLKNFPVkEVYMPGVTHTTKtyE 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2526709325 102 QWDEDALSYRATGQRCprfvheqliRSGDVLSLGDLDWTALAAPGHD 148
Cdd:cd07731    91 DLLDAIKEKGIPVTPC---------KAGDRWQLGGVSFEVLSPPKDD 128
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 61-208 5.92e-06

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: 46.44  E-value: 5.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  61 ERLDVLLNTHLHSDHCGGNAA------------LHAAYGcriaiPAAEDAKVRQWDEDALSYRATGQrcPRFVheqlirS 128
Cdd:cd07729    87 EDIDYVILSHLHFDHAGGLDLfpnatiivqraeLEYATG-----PDPLAAGYYEDVLALDDDLPGGR--VRLV------D 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325 129 GDVLSLGDLdwTALAAPGHDP-H-ALLLYCAQEGVLISADA--LWRNGFGIIFPELDGesGFEEARATLELIRSL---DV 201
Cdd:cd07729   154 GDYDLFPGV--TLIPTPGHTPgHqSVLVRLPEGTVLLAGDAayTYENLEEGRPPGINY--DPEAALASLERLKALaerEG 229


                  ....*..
gi 2526709325 202 RTVIPGH 208
Cdd:cd07729   230 ARVIPGH 236
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 21-160 1.06e-05

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: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  21 SSNNVLLFGRDEVAMIDSGYVAHAeqTQTLvrhvLHQRGR--ERLDVLLNTHLHSDHCGGNAALHAAYGCRIAIPAAeda 98
Cdd:cd07733     8 KGNCTYLETEDGKLLIDAGLSGRK--ITGR----LAEIGRdpEDIDAILVTHEHADHIKGLGVLARKYNVPIYATAG--- 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526709325  99 kvrqwdedalSYRATGQ-RCPRFVHE-QLIRSGDVLSLGDLDWTALAAPgHDPHALLLYCAQEG 160
Cdd:cd07733    79 ----------TLRAMERkVGLIDVDQkQIFEPGETFSIGDFDVESFGVS-HDAADPVGYRFEEG 131
CphA_ImiS-like_MBL-B2 cd16306
Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and related metallo-beta-lactamases, ...
 19-211 1.51e-05

Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and related metallo-beta-lactamases, subclass B2; 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. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis.


Pssm-ID: 293864  Cd Length: 222  Bit Score: 45.32  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  19 WLSSNNVLLFGRDEVAMIDSGYVAH-AEQTQTLVRHVlhqrGRERLDVLLNTHLHSDHCGGNAALHAAyGCRI-AIPAAE 96
Cdd:cd16306    18 YVQENSMVYFGAKGVTVVGATWTPDtARELHKLIKRV----SRKPVLEVINTNYHTDRAGGNAYWKSI-GAKVvSTRQTR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  97 DAKVRQWDEDALSYRatgQRCPRF-----VHEQLIRSGDVLSLGDLDWTALAAPGHDPHALLLYCAQEGVLIsadalwrn 171
Cdd:cd16306    93 DLMKSDWAEIVAFTR---KGLPEYpdlplVLPNVVHDGDFTLQEGKVRAFYLGPAHTPDGIFVYFPDEQVLY-------- 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2526709325 172 GFGIIFPELdGESGFEEARA---TLELIRS--LDVRTVIPGHGAP 211
Cdd:cd16306   162 GNCILKEKL-GNLSFADVKAypqTLERLKAmkLPIKTVIGGHDSP 205
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 72-212 1.60e-05

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: 44.49  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  72 HSDHCGGNAALHAAYGCRIAIPAAEdakvRQWDedalsyratgqrcPRFVHEQLIRSGDVLSLGDlDWTALAAPGHDPHA 151
Cdd:cd07727    55 HRDDVADHAKWAERFGAKRIIHEDD----VNAV-------------TRPDEVIVLWGGDPWELDP-DLTLIPVPGHTRGS 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526709325 152 LLLYCAQEGVLISADALW---RNGFGIIFPELDGESgFEEARATLELIRSLDVRTVIPGHGAPF 212
Cdd:cd07727   117 VVLLYKEKGVLFTGDHLAwsrRRGWLSAFRYVCWYS-WPEQAESVERLADLDFEWVLPGHGRRV 179
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 11-211 1.63e-05

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: 44.97  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  11 SLHVLERGWLSSNNVLLFGRDEVAMIDSGYvaHAEQTQTLVrHVLHQRGRERLDVLLNTHLHSDHCGGNAALHAAygcri 90
Cdd:cd16285    15 SLAEFNGGAVPSNGLIVIDGKGLVLIDTPW--TEAQTATLL-DWIEKKLGKPVTAAISTHSHDDRTGGIKALNAR----- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  91 AIPAAEDAKVRQwdedalsyRATGQRCPRFVHEqlIRSGDVLSLGDLDwTALAAPGHDPHALLLYCAQEGVLI------S 164
Cdd:cd16285    87 GIPTYATALTNE--------LAKKEGKPVPTHS--LKGALTLGFGPLE-VFYPGPGHTPDNIVVWLPKSKILFggclvkS 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2526709325 165 ADAlwrNGFGIIfpeldGESGFEEARATLELIRSL--DVRTVIPGHGAP 211
Cdd:cd16285   156 ASA---TSLGNV-----GDADVEAWPKSIENLKAKypEARMVVPGHGAP 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 40-208 1.64e-05

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 45.60  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  40 YVAHAEQTQTL----------VRHVLHQRGRErLDVLLNTHLHSDHCGGNAALHAAYGCRIAIPAAedakvrqwDEDals 109
Cdd:PLN02398   90 YLLHDEDTGTVgvvdpseavpVIDALSRKNRN-LTYILNTHHHYDHTGGNLELKARYGAKVIGSAV--------DKD--- 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325 110 yratgqRCPRFvhEQLIRSGDVLSLGDLDWTALAAPGHDPHALLLYCAQEGVLISADALWRNGFGIIFpeldgESGFEEA 189
Cdd:PLN02398  158 ------RIPGI--DIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGKLF-----EGTPEQM 224

                         170       180
                  ....*....|....*....|
gi 2526709325 190 RATLELIRSL-DVRTVIPGH 208
Cdd:PLN02398  225 LSSLQKIISLpDDTNIYCGH 244
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 61-152 2.93e-05

Janthinobacterium lividum THIN-B2 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 THIN-B2-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: 293869  Cd Length: 257  Bit Score: 44.59  E-value: 2.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  61 ERLDVLLNTHLHSDHCGGNAALHAAYGCRIAI--PAAEDAKVRQWDEDALSYRATgQRCPRFVHEQLIRSGDVLSLGDLD 138
Cdd:cd16311    59 EDVKLILNSHGHIDHAGGLAELQRRSGALVAAspSAALDLASGEVGPDDPQYHAL-PKYPPVKDMRLARDGGQFNVGPVS 137

                          90
                  ....*....|....
gi 2526709325 139 WTALAAPGHDPHAL 152
Cdd:cd16311   138 LTAHATPGHTPGGL 151
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 61-152 4.94e-05

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


Pssm-ID: 293847  Cd Length: 239  Bit Score: 44.04  E-value: 4.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  61 ERLDVLLNTHLHSDHCGGNAALHAAYGCRIAIPAAEDAKVRQWDEDALSYrATGQRCPRFVHEQLIRSGDVLSLGDLDWT 140
Cdd:cd16289    59 GDLKLILHSHAHADHAGPLAALKRATGARVAANAESAVLLARGGSDDIHF-GDGITFPPVQADRIVMDGEVVTLGGVTFT 137

                          90
                  ....*....|..
gi 2526709325 141 ALAAPGHDPHAL 152
Cdd:cd16289   138 AHFTPGHTPGST 149
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 63-151 6.55e-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: 6.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  63 LDVLLNTHLHSDHCGGNAALHAAYGCRIAIPAAeDAKVRQwDEDALSYRATGQRcPRFV---HEQLIRSGDVLSLGDLDW 139
Cdd:cd16308    61 IKILLTTQAHYDHVGAMAAIKQQTGAKMMVDEK-DAKVLA-DGGKSDYEMGGYG-STFApvkADKLLHDGDTIKLGGTKL 137

                          90
                  ....*....|..
gi 2526709325 140 TALAAPGHDPHA 151
Cdd:cd16308   138 TLLHHPGHTKGS 149
VIM_type_MBL-B1 cd16303
VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona ...
 22-211 2.25e-04

VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona integron-encoded metallo-beta-lactamase)-type MBLs are integron-associated and are widely distributed acquired MBLs. MBLs (class B of the Ambler beta-lactamase classification) 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 VIM-type 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: 293861 [Multi-domain]  Cd Length: 218  Bit Score: 41.77  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  22 SNNVLLFGRDEVAMIDSGYvaHAEQTQTLVRHVLHQRGrerLDVL--LNTHLHSDHCGGNAALHAAYGCRIAIPAAEDAK 99
Cdd:cd16303    28 SNGLIVRDGDELLLIDTAW--GAKNTAALLAEIEKQIG---LPVTraVSTHFHDDRVGGVDVLRAAGVATYASPSTRRLA 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325 100 VRQwdedalsyratGQRCPRFVHEQLIRSGDVLSLGDLDwTALAAPGHDPHALLLYCAQEGVLISADALWrngfgiifpE 179
Cdd:cd16303   103 EAE-----------GNEIPTHSLEGLSSSGDAVRFGPVE-LFYPGAAHSTDNLVVYVPSARVLYGGCAVR---------E 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2526709325 180 LDGESGFEEARATL----ELIRSL-----DVRTVIPGHGAP 211
Cdd:cd16303   162 LSSTSAGNVADADLaewpTSIERIqkhypEAEFVIPGHGLP 202
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 65-149 2.47e-04

Caulobacter crescentus Mbl1b 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 Mbl1b-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: 293868  Cd Length: 252  Bit Score: 41.67  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  65 VLLNTHLHSDHCGGNAALHAAYGCRIAI-----PAAEDAKVRQWDE-DALSYRAtgqrcprfVH-EQLIRSGDVLSLGDL 137
Cdd:cd16310    63 IIINTHAHYDHAGGLAQLKADTGAKLWAsrgdrPALEAGKHIGDNItQPAPFPA--------VKvDRILGDGEKIKLGDI 134

                          90
                  ....*....|..
gi 2526709325 138 DWTALAAPGHDP 149
Cdd:cd16310   135 TLTATLTPGHTK 146
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 51-208 4.61e-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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 41.10  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325  51 VRHVLHQRGR--ERLDVLLNTHLHSDHCGG-----NAALHAAYGcriAIPAAEDAKVRQWDEDAL-----SYRATGQRCP 118
Cdd:cd07730    70 VAEQLAAGGIdpEDIDAVILSHLHWDHIGGlsdfpNARLIVGPG---AKEALRPPGYPSGFLPELlpsdfEGRLVRWEED 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526709325 119 RFVHEQLI---RSGDVlsLGDLDWTALAAPGHDP-HALLLYCAQEG--VLISADALW------RNGFGIIFPELDGESGF 186
Cdd:cd07730   147 DFLWVPLGpfpRALDL--FGDGSLYLVDLPGHAPgHLGLLARTTSGtwVFLAGDACHhrigllRPSPLLPLPDLDDGADR 224

                         170       180
                  ....*....|....*....|....*
gi 2526709325 187 EEARATLELIRSLDVR---TVIPGH 208
Cdd:cd07730   225 EAARETLARLRELDAApdvRVVLAH 249
 
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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