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Conserved domains on  [gi|497617566|ref|WP_009931750|]
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MBL fold metallo-hydrolase [Listeria monocytogenes]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869930)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme that may have substrate towards phosphotriesters, esters, and/or lactones

CATH:  3.60.15.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  17597585|12177301|11471246|11513844
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 11-212 1.29e-63

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: 196.67  E-value: 1.29e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  11 QITTFPHLFPVNCYLVLERDGLTLIDTGILAHAKGIISLIHKLK---SPLKRILLTHAHGDHIGGLIAVKAAfPEALVMI 87
Cdd:cd07721    1 GVYQLPLLPPVNAYLIEDDDGLTLIDTGLPGSAKRILKALRELGlspKDIRRILLTHGHIDHIGSLAALKEA-PGAPVYA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  88 GSREKLLVETKEIYAFEAQKPLKGSYSDRLPVRI---DQILKDGDMV---GSLLIIDTPGHTPGSISFFDERNGHLFVGD 161
Cdd:cd07721   80 HEREAPYLEGEKPYPPPVRLGLLGLLSPLLPVKPvpvDRTLEDGDTLdlaGGLRVIHTPGHTPGHISLYLEEDGVLIAGD 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497617566 162 LFQTRGGAaicgekrwLFPFPAMGSWDLPTSIASAENLQLFDVTEIACGHG 212
Cdd:cd07721  160 ALVTVGGE--------LVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
 
Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 11-212 1.29e-63

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: 196.67  E-value: 1.29e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  11 QITTFPHLFPVNCYLVLERDGLTLIDTGILAHAKGIISLIHKLK---SPLKRILLTHAHGDHIGGLIAVKAAfPEALVMI 87
Cdd:cd07721    1 GVYQLPLLPPVNAYLIEDDDGLTLIDTGLPGSAKRILKALRELGlspKDIRRILLTHGHIDHIGSLAALKEA-PGAPVYA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  88 GSREKLLVETKEIYAFEAQKPLKGSYSDRLPVRI---DQILKDGDMV---GSLLIIDTPGHTPGSISFFDERNGHLFVGD 161
Cdd:cd07721   80 HEREAPYLEGEKPYPPPVRLGLLGLLSPLLPVKPvpvDRTLEDGDTLdlaGGLRVIHTPGHTPGHISLYLEEDGVLIAGD 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497617566 162 LFQTRGGAaicgekrwLFPFPAMGSWDLPTSIASAENLQLFDVTEIACGHG 212
Cdd:cd07721  160 ALVTVGGE--------LVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 10-235 1.71e-39

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: 135.59  E-value: 1.71e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  10 WQITT--FPHLFPVNCYLVLERDGLTLIDTGI-LAHAKGIISLIHKLKSPLKRILLTHAHGDHIGGLIAVKAAFpEALVM 86
Cdd:COG0491    2 YVLPGgtPGAGLGVNSYLIVGGDGAVLIDTGLgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAPVY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  87 IGSREkllvetkeiyAFEAQKPLKGSYSDRLPVRIDQILKDGDMV----GSLLIIDTPGHTPGSISFFDERNGHLFVGDL 162
Cdd:COG0491   81 AHAAE----------AEALEAPAAGALFGREPVPPDRTLEDGDTLelggPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDA 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497617566 163 FQTRGgaaicgekrwlFPFPAMGSWDLPTSIASAENLQLFDVTEIACGHGPVKAMADFDLTNVLKRAKEQVTN 235
Cdd:COG0491  151 LFSGG-----------VGRPDLPDGDLAQWLASLERLLALPPDLVIPGHGPPTTAEAIDYLEELLAALGERAN 212
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 22-211 2.82e-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: 108.02  E-value: 2.82e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566    22 NCYLVLERDGLTLIDTGILAHAKGIISLIHKLKSPLKRILLTHAHGDHIGGLIAVKAAfPEALVMIGSREKLLVETKEIY 101
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEA-PGAPVYAPEGTAELLKDLLAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566   102 AFEAqkplkgsYSDRLPVRIDQILKDGDMV----GSLLIIDTPGHTPGSISFFDERNGHLFVGDLFQTRGGAAIcgekrw 177
Cdd:smart00849  80 LGEL-------GAEAEPAPPDRTLKDGDELdlggGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRT------ 146

                          170       180       190
                   ....*....|....*....|....*....|....
gi 497617566   178 lfpFPAMGSWDLPTSIASAENLQLFDVTEIACGH 211
Cdd:smart00849 147 ---LVDGGDAAASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
18-211 4.41e-27

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 102.83  E-value: 4.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566   18 LFPVNCYLVLERDGLTLIDTGILAHAKGIISL--IHKLKSPLKRILLTHAHGDHIGGLIAVKAAFPEALVMIGSREKLLV 95
Cdd:pfam00753   3 PGQVNSYLIEGGGGAVLIDTGGSAEAALLLLLaaLGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566   96 ET-KEIYAFEAQKPLKGSYSDRLPVRIDQILKDGDMVGSLLIIDTPGHTPGSISFFDERNGHLFVGDLFQTRGGAAIcge 174
Cdd:pfam00753  83 DEeLGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRL--- 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 497617566  175 KRWLFPFPAMGSWDLPTSIASAENLQLFDVTEIACGH 211
Cdd:pfam00753 160 DLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 35-211 1.69e-11

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 62.94  E-value: 1.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  35 IDTGIL-----AHAKGIISLIHKLKSPLKRILLTHAHGDHIGGLIAVKAAFpeALVMIGSrekllvetkeiyafeaqkpl 109
Cdd:PLN02398  95 EDTGTVgvvdpSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARY--GAKVIGS-------------------- 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566 110 kGSYSDRLPvRIDQILKDGD--MVG--SLLIIDTPGHTPGSISFFDERNGHLFVGD-LFQTRggaaiCGEkrwLFPfpam 184
Cdd:PLN02398 153 -AVDKDRIP-GIDIVLKDGDkwMFAghEVLVMETPGHTRGHISFYFPGSGAIFTGDtLFSLS-----CGK---LFE---- 218

                        170       180       190
                 ....*....|....*....|....*....|.
gi 497617566 185 GSwdlPTSIASAenLQ----LFDVTEIACGH 211
Cdd:PLN02398 219 GT---PEQMLSS--LQkiisLPDDTNIYCGH 244
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 22-73 6.67e-04

beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and RNase J2, involved in mRNA degradation in a wide range of organism. [Transcription, Degradation of RNA]


Pssm-ID: 273195 [Multi-domain]  Cd Length: 422  Bit Score: 40.41  E-value: 6.67e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497617566   22 NCYLVLERDGLTLIDTGI------LAHAKGII---SLIHKLKSPLKRILLTHAHGDHIGGL 73
Cdd:TIGR00649  15 NMYVVEIDDEIVIFDAGIlfpedeMLGVDGVIpdfTYLQENEDKVKGIFITHGHEDHIGAV 75
 
Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 11-212 1.29e-63

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: 196.67  E-value: 1.29e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  11 QITTFPHLFPVNCYLVLERDGLTLIDTGILAHAKGIISLIHKLK---SPLKRILLTHAHGDHIGGLIAVKAAfPEALVMI 87
Cdd:cd07721    1 GVYQLPLLPPVNAYLIEDDDGLTLIDTGLPGSAKRILKALRELGlspKDIRRILLTHGHIDHIGSLAALKEA-PGAPVYA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  88 GSREKLLVETKEIYAFEAQKPLKGSYSDRLPVRI---DQILKDGDMV---GSLLIIDTPGHTPGSISFFDERNGHLFVGD 161
Cdd:cd07721   80 HEREAPYLEGEKPYPPPVRLGLLGLLSPLLPVKPvpvDRTLEDGDTLdlaGGLRVIHTPGHTPGHISLYLEEDGVLIAGD 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497617566 162 LFQTRGGAaicgekrwLFPFPAMGSWDLPTSIASAENLQLFDVTEIACGHG 212
Cdd:cd07721  160 ALVTVGGE--------LVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 10-235 1.71e-39

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: 135.59  E-value: 1.71e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  10 WQITT--FPHLFPVNCYLVLERDGLTLIDTGI-LAHAKGIISLIHKLKSPLKRILLTHAHGDHIGGLIAVKAAFpEALVM 86
Cdd:COG0491    2 YVLPGgtPGAGLGVNSYLIVGGDGAVLIDTGLgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAPVY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  87 IGSREkllvetkeiyAFEAQKPLKGSYSDRLPVRIDQILKDGDMV----GSLLIIDTPGHTPGSISFFDERNGHLFVGDL 162
Cdd:COG0491   81 AHAAE----------AEALEAPAAGALFGREPVPPDRTLEDGDTLelggPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDA 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497617566 163 FQTRGgaaicgekrwlFPFPAMGSWDLPTSIASAENLQLFDVTEIACGHGPVKAMADFDLTNVLKRAKEQVTN 235
Cdd:COG0491  151 LFSGG-----------VGRPDLPDGDLAQWLASLERLLALPPDLVIPGHGPPTTAEAIDYLEELLAALGERAN 212
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 19-211 7.28e-32

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: 115.08  E-value: 7.28e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  19 FPVNCYLVL-ERDGLTLIDTGILAHAKgIISLIHKLKSPLKRILLTHAHGDHIGGLIAVKAAfPEALVMIGSREK-LLVE 96
Cdd:cd06262    8 LQTNCYLVSdEEGEAILIDPGAGALEK-ILEAIEELGLKIKAILLTHGHFDHIGGLAELKEA-PGAPVYIHEADAeLLED 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  97 TKEIYAFEAQKPLKgsysdrlPVRIDQILKDGDMVG----SLLIIDTPGHTPGSISFFDERNGHLFVGDLfqtrggaaic 172
Cdd:cd06262   86 PELNLAFFGGGPLP-------PPEPDILLEDGDTIElgglELEVIHTPGHTPGSVCFYIEEEGVLFTGDT---------- 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 497617566 173 gekrwLFPfPAMGSWDLPTS-----IASAENL--QLFDVTEIACGH 211
Cdd:cd06262  149 -----LFA-GSIGRTDLPGGdpeqlIESIKKLllLLPDDTVVYPGH 188
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 22-211 2.82e-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: 108.02  E-value: 2.82e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566    22 NCYLVLERDGLTLIDTGILAHAKGIISLIHKLKSPLKRILLTHAHGDHIGGLIAVKAAfPEALVMIGSREKLLVETKEIY 101
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEA-PGAPVYAPEGTAELLKDLLAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566   102 AFEAqkplkgsYSDRLPVRIDQILKDGDMV----GSLLIIDTPGHTPGSISFFDERNGHLFVGDLFQTRGGAAIcgekrw 177
Cdd:smart00849  80 LGEL-------GAEAEPAPPDRTLKDGDELdlggGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRT------ 146

                          170       180       190
                   ....*....|....*....|....*....|....
gi 497617566   178 lfpFPAMGSWDLPTSIASAENLQLFDVTEIACGH 211
Cdd:smart00849 147 ---LVDGGDAAASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
18-211 4.41e-27

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 102.83  E-value: 4.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566   18 LFPVNCYLVLERDGLTLIDTGILAHAKGIISL--IHKLKSPLKRILLTHAHGDHIGGLIAVKAAFPEALVMIGSREKLLV 95
Cdd:pfam00753   3 PGQVNSYLIEGGGGAVLIDTGGSAEAALLLLLaaLGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566   96 ET-KEIYAFEAQKPLKGSYSDRLPVRIDQILKDGDMVGSLLIIDTPGHTPGSISFFDERNGHLFVGDLFQTRGGAAIcge 174
Cdd:pfam00753  83 DEeLGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRL--- 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 497617566  175 KRWLFPFPAMGSWDLPTSIASAENLQLFDVTEIACGH 211
Cdd:pfam00753 160 DLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 20-165 3.79e-22

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: 89.61  E-value: 3.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  20 PVNCYLVLERDGLTLIDTGIlahakGIISLIHKLKSPLKR---ILLTHAHGDHIGGLiavkAAFPEALVMigSREKLLVE 96
Cdd:cd07712    8 RVNIYLLRGRDRALLIDTGL-----GIGDLKEYVRTLTDLpllVVATHGHFDHIGGL----HEFEEVYVH--PADAEILA 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497617566  97 TKEIYAFEAQKPlkGSYSDRLPVRIdQILKDGDMVG----SLLIIDTPGHTPGSISFFDERNGHLFVGDLFQT 165
Cdd:cd07712   77 APDNFETLTWDA--ATYSVPPAGPT-LPLRDGDVIDlgdrQLEVIHTPGHTPGSIALLDRANRLLFSGDVVYD 146
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 10-161 2.39e-21

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: 88.32  E-value: 2.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  10 WQITTFPHLFP--VNCYLVLERDGLTLIDTGILAHAKGIISLIHKLKSPLKR---ILLTHAHGDHIGGLIAVKAAFPEAL 84
Cdd:cd07726    3 YLIDLGFLGFPgrIASYLLDGEGRPALIDTGPSSSVPRLLAALEALGIAPEDvdyIILTHIHLDHAGGAGLLAEALPNAK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  85 VMI---GSR-----EKLLVETKEIY--AFEAQkplkgsYSDRLPVRIDQI--LKDGDMVG----SLLIIDTPGHTPGSIS 148
Cdd:cd07726   83 VYVhprGARhlidpSKLWASARAVYgdEADRL------GGEILPVPEERVivLEDGETLDlggrTLEVIDTPGHAPHHLS 156

                        170
                 ....*....|...
gi 497617566 149 FFDERNGHLFVGD 161
Cdd:cd07726  157 FLDEESDGLFTGD 169
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 17-173 9.35e-21

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: 85.20  E-value: 9.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  17 HLFPVN----CYLVleRDGLT----LIDTGIlahAKGIISLIHKLKSPLKRILLTHAHGDHIGGLIAVKAAFPEAlvmig 88
Cdd:cd07723    1 VPIPALsdnyIYLI--VDEATgeaaVVDPGE---AEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDA----- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  89 srekllvetkEIYafeaqkplkGSYSDRLPvRIDQILKDGDMV----GSLLIIDTPGHTPGSISFFDERNGHLFVGD-LF 163
Cdd:cd07723   71 ----------PVY---------GPAEDRIP-GLDHPVKDGDEIklggLEVKVLHTPGHTLGHICYYVPDEPALFTGDtLF 130

                        170
                 ....*....|
gi 497617566 164 qtRGGaaiCG 173
Cdd:cd07723  131 --SGG---CG 135
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 21-221 1.63e-19

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: 83.38  E-value: 1.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  21 VNCYLVLERDGLTLIDTGI-LAHAKGIISLIHKLKS-PLKRILLTHAHGDHIGGLiavkAAFPEALV-MIGSRE--KLLV 95
Cdd:cd16282   15 SNIGFIVGDDGVVVIDTGAsPRLARALLAAIRKVTDkPVRYVVNTHYHGDHTLGN----AAFADAGApIIAHENtrEELA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  96 ETKEIYAFEAQKPLKGSYSD---RLPVRI---DQILKDGDMVgsLLIIDT-PGHTPGSISFFDERNGHLFVGDLFQTRGg 168
Cdd:cd16282   91 ARGEAYLELMRRLGGDAMAGtelVLPDRTfddGLTLDLGGRT--VELIHLgPAHTPGDLVVWLPEEGVLFAGDLVFNGR- 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 497617566 169 aaicgekrwlFPFPAMGSwdLPTSIASAENLQLFDVTEIACGHGPVKAMADFD 221
Cdd:cd16282  168 ----------IPFLPDGS--LAGWIAALDRLLALDATVVVPGHGPVGDKADLR 208
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 19-214 3.27e-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: 82.40  E-value: 3.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  19 FPVNCYLVLERDGLT--LIDTGilAHAKGIISLIHKLKSPLKRILLTHAHGDHIGGLIAVKAAfPEALVMIGSREKLLVE 96
Cdd:cd16322    9 LQENTYLVADEGGGEavLVDPG--DESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRH-PGAPVYLHPDDLPLYE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  97 tkeiyAFEAQKPLKGSYSDRLPvRIDQILKDGDMVG----SLLIIDTPGHTPGSISFFDERNGHLFVGDL-FQtrGGaai 171
Cdd:cd16322   86 -----AADLGAKAFGLGIEPLP-PPDRLLEDGQTLTlgglEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLlFQ--GS--- 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 497617566 172 cgekrwlfpfpaMGSWDLPTSIASAEN------LQLFDVTEIACGHGPV 214
Cdd:cd16322  155 ------------IGRTDLPGGDPKAMAaslrrlLTLPDETRVFPGHGPP 191
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 18-161 8.91e-18

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: 78.11  E-value: 8.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  18 LFPVNCYLVLERDGLTLIDTGiLAHAKGIISLIHKLK------SPLKRILLTHAHGDHIGGLIAVKAAFpEALVMIgsre 91
Cdd:cd07725   12 LGHVNVYLLRDGDETTLIDTG-LATEEDAEALWEGLKelglkpSDIDRVLLTHHHPDHIGLAGKLQEKS-GATVYI---- 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497617566  92 kllvetkeiyafeaqkplkgsysdrLPVRIdqiLKDGDMV----GSLLIIDTPGHTPGSISFFDERNGHLFVGD 161
Cdd:cd07725   86 -------------------------LDVTP---VKDGDKIdlggLRLKVIETPGHTPGHIVLYDEDRRELFVGD 131
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 22-214 1.10e-17

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 77.96  E-value: 1.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  22 NCYLVLERDGLTLIDTGilahaKGIISLIHKLKSPLKR--------ILLTHAHGDHIGGLIAVKAAFPEALVmigsrekl 93
Cdd:cd07722   19 NTYLVGTGKRRILIDTG-----EGRPSYIPLLKSVLDSegnatisdILLTHWHHDHVGGLPDVLDLLRGPSP-------- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  94 lvetkEIYAFEAQKPLKGSYSDRLPVridQILKDGDMV----GSLLIIDTPGHTPGSISFFDERNGHLFVGDlfqtrgga 169
Cdd:cd07722   86 -----RVYKFPRPEEDEDPDEDGGDI---HDLQDGQVFkvegATLRVIHTPGHTTDHVCFLLEEENALFTGD-------- 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 497617566 170 AICGEkrwlfpfpamGSW---DLPTSIASAENLQLFDVTEIACGHGPV 214
Cdd:cd07722  150 CVLGH----------GTAvfeDLAAYMASLKKLLSLGPGRIYPGHGPV 187
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 17-164 1.64e-17

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: 77.59  E-value: 1.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  17 HLFPV-----NCYLVL-ERDGL-TLIDTGilAHAKGIISLIHKLKSPLKRILLTHAHGDHIGGLIAVKAAFPEALVMIGS 89
Cdd:cd07737    2 QIIPVtpfqqNCSLIWcEETKEaAVIDPG--GDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  90 REKLLVEtkeiyAFEAQKPLKGSYSDRlPVRIDQILKDGDMV----GSLLIIDTPGHTPGSISFFDERNGHLFVGD-LFQ 164
Cdd:cd07737   80 EDKFLLE-----NLPEQSQMFGFPPAE-AFTPDRWLEEGDTVtvgnLTLEVLHCPGHTPGHVVFFNRESKLAIVGDvLFK 153
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 21-155 2.78e-17

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: 78.01  E-value: 2.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  21 VNCYLVLERDGLTLIDTGILAHAKG-IISLIHKL---KSPLKRILLTHAHGDHIGGLIAVKAAFPEALVMigSREkllve 96
Cdd:cd16280   22 VSAWAIDTGDGLILIDALNNNEAADlIVDGLEKLgldPADIKYILITHGHGDHYGGAAYLKDLYGAKVVM--SEA----- 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497617566  97 tkEIYAFEAQKPLKGSYSDRLPVRIDQILKDGD--MVG--SLLIIDTPGHTPGSISF-FDERNG 155
Cdd:cd16280   95 --DWDMMEEPPEEGDNPRWGPPPERDIVIKDGDtlTLGdtTITVYLTPGHTPGTLSLiFPVKDG 156
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 20-163 5.28e-16

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 74.51  E-value: 5.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  20 PVNCYLVLERDGLTLIDTG---ILAHAKGiislihKLKSPLK----------RILLTHAHGDHIGGLI--AVKAAFPEAL 84
Cdd:cd07720   48 SVNAFLVRTGGRLILVDTGaggLFGPTAG------KLLANLAaagidpedidDVLLTHLHPDHIGGLVdaGGKPVFPNAE 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  85 VMIGSREkllvetkeiYAF-----------EAQKPLKGSYSDRL-PVRIDQILKDGD-MVGSLLIIDTPGHTPGSISFFD 151
Cdd:cd07720  122 VHVSEAE---------WDFwlddanaakapEGAKRFFDAARDRLrPYAAAGRFEDGDeVLPGITAVPAPGHTPGHTGYRI 192

                        170
                 ....*....|....
gi 497617566 152 ERNGH--LFVGDLF 163
Cdd:cd07720  193 ESGGErlLIWGDIV 206
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 25-150 1.10e-15

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: 73.54  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  25 LVLERDGLTLIDTGILAHAKGIISLIHKLKSPLK--RILLT-HAHGDHIGGLIAVKAAfPEALVMIGSREKLLVETKEIy 101
Cdd:cd16315   26 LITGDDGHVLIDSGTEEAAPLVLANIRKLGFDPKdvRWLLSsHEHFDHVGGLAALQRA-TGARVAASAAAAPVLESGKP- 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 497617566 102 afEAQKPLKGSYSDRLPVRIDQILKDGDMV--GSLLI--IDTPGHTPGSISFF 150
Cdd:cd16315  104 --APDDPQAGLHEPFPPVRVDRIVEDGDTValGSLRLtaHATPGHTPGALSWT 154
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 20-163 2.64e-15

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 71.79  E-value: 2.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  20 PVNC-YLVLERDGLTLIDTGI-LAHAKGIISLIHKLKSPLKRILLTHAHGDHIGGliavkAAF----PEALVMIGSREKL 93
Cdd:cd07743    7 PTNIgVYVFGDKEALLIDSGLdEDAGRKIRKILEELGWKLKAIINTHSHADHIGG-----NAYlqkkTGCKVYAPKIEKA 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497617566  94 LVETKEI-----YAFEAQKPLKGSYSDRLPVRIDQILKDGDMVGS---LLIIDTPGHTPGSISFFDErNGHLFVGDLF 163
Cdd:cd07743   82 FIENPLLepsylGGAYPPKELRNKFLMAKPSKVDDIIEEGELELGgvgLEIIPLPGHSFGQIGILTP-DGVLFAGDAL 158
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 21-148 2.76e-15

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: 72.74  E-value: 2.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  21 VNCYLVLERDGLTLIDTGILAHAKGIISLIHKLK---SPLKRILLTHAHGDHIGGLIAVKAAfPEALVMIGSREKLLVE- 96
Cdd:cd16288   22 LASYLITTPQGLILIDTGLESSAPMIKANIRKLGfkpSDIKILLNSHAHLDHAGGLAALKKL-TGAKLMASAEDAALLAs 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 497617566  97 -TKEIYAFEAQKPLkgsysdRLPVRIDQILKDGDMVG----SLLIIDTPGHTPGSIS 148
Cdd:cd16288  101 gGKSDFHYGDDSLA------FPPVKVDRVLKDGDRVTlggtTLTAHLTPGHTRGCTT 151
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 19-148 4.82e-15

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: 71.86  E-value: 4.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  19 FPVNCYLVLERDGLTLIDTGI-----------LAHAKGIISLIHKLKSPLKR----------ILLTHAHGDHIGGLiavk 77
Cdd:cd07729   30 LPVYAYLIEHPEGTILVDTGFhpdaaddpgglELAFPPGVTEEQTLEEQLARlgldpedidyVILSHLHFDHAGGL---- 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497617566  78 AAFPEAlvmigsreKLLVETKEI-YAFEAQKPLKGSYSDRLPV-------RIDQILKDGDMVGSLLIIDTPGHTPGSIS 148
Cdd:cd07729  106 DLFPNA--------TIIVQRAELeYATGPDPLAAGYYEDVLALdddlpggRVRLVDGDYDLFPGVTLIPTPGHTPGHQS 176
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 24-149 2.52e-14

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: 69.88  E-value: 2.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  24 YLVLERDGLTLIDTGILAHAKGIISLIHKLK---SPLKRILLTHAHGDHIGGLIAVKAAfPEALVMIGSREKLLVET--K 98
Cdd:cd07708   25 YLIVTPQGNILIDGDMEQNAPMIKANIKKLGfkfSDTKLILISHAHFDHAGGSAEIKKQ-TGAKVMAGAEDVSLLLSggS 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 497617566  99 EIYAFEaqkplKGSYSDRLPVRIDQILKDGDMV--GSLLIID--TPGHTPGSISF 149
Cdd:cd07708  104 SDFHYA-----NDSSTYFPQSTVDRAVHDGERVtlGGTVLTAhaTPGHTPGCTTW 153
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 23-155 3.46e-14

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: 69.81  E-value: 3.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  23 CYLVLERDGLTLIDTGILAHAKGIISLIHKLK---SPLKRILLTHAHGDHIGGLIAVKAAfPEALVMIGSREKLLVET-- 97
Cdd:cd16308   24 CYLIVTPKGNILINTGLAESVPLIKKNIQALGfkfKDIKILLTTQAHYDHVGAMAAIKQQ-TGAKMMVDEKDAKVLADgg 102

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497617566  98 KEIYAFeaqkplKGSYSDRLPVRIDQILKDGDMVG----SLLIIDTPGHTPGSISF-FDERNG 155
Cdd:cd16308  103 KSDYEM------GGYGSTFAPVKADKLLHDGDTIKlggtKLTLLHHPGHTKGSCSFlFDVKDE 159
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-161 9.91e-14

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 67.13  E-value: 9.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  22 NCYLVLERDGLTLIDTG--ILAHAKGIISLIHKLksPLKRILLTHAHGDHIGGLIAVKAAFPEAlvmigsrekllvetke 99
Cdd:cd16278   19 NTYLLGAPDGVVVIDPGpdDPAHLDALLAALGGG--RVSAILVTHTHRDHSPGAARLAERTGAP---------------- 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497617566 100 IYAFeaqkPLKGSYSDRLPVRIDQILKDGDMV----GSLLIIDTPGHTPGSISFFDERNGHLFVGD 161
Cdd:cd16278   81 VRAF----GPHRAGGQDTDFAPDRPLADGEVIegggLRLTVLHTPGHTSDHLCFALEDEGALFTGD 142
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 24-149 9.97e-13

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: 65.58  E-value: 9.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  24 YLVLERDGLTLIDTGILAHAKGIISLIHKLK---SPLKRILLTHAHGDHIGGLIAVKAAfPEALVMIGSREKLLVETKEI 100
Cdd:cd16309   25 FLITTPEGHILIDGAMPQSTPLIKDNIKKLGfdvKDVKYLLNTHAHFDHAGGLAELKKA-TGAQLVASAADKPLLESGYV 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 497617566 101 YAfEAQKPLKGSysdrlPVRIDQILKDGDMV--GSLLIID--TPGHTPGSISF 149
Cdd:cd16309  104 GS-GDTKNLQFP-----PVRVDRVIGDGDKVtlGGTTLTAhlTPGHSPGCTSW 150
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 40-163 2.50e-12

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: 63.19  E-value: 2.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  40 LAHAKGIISLIHKLKSPLKRILLTHAHGDHIGGLIAVKAAfPEALVMIGSREKllvetkeiyafeaqkplkGSYSDRLpv 119
Cdd:cd07724   32 RDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAER-TGAPIVIGEGAP------------------ASFFDRL-- 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 497617566 120 ridqiLKDGDM--VGSLLI--IDTPGHTPGSISFFDERNGHLFVGD-LF 163
Cdd:cd07724   91 -----LKDGDVleLGNLTLevLHTPGHTPESVSYLVGDPDAVFTGDtLF 134
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 24-149 3.94e-12

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: 64.01  E-value: 3.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  24 YLVLERDGLTLIDTGILAHAKGIISLIHKLK---SPLKRILLTHAHGDHIGGLIAVKAAfpealvmigSREKLLVETKEI 100
Cdd:cd16310   25 YLITSNHGAILLDGGLEENAALIEQNIKALGfklSDIKIIINTHAHYDHAGGLAQLKAD---------TGAKLWASRGDR 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566 101 YAFEAQKPLKGSYSDRL---PVRIDQILKDGD--------MVGSLliidTPGHTPGSISF 149
Cdd:cd16310   96 PALEAGKHIGDNITQPApfpAVKVDRILGDGEkiklgditLTATL----TPGHTKGCTTW 151
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 10-155 7.15e-12

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: 62.91  E-value: 7.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  10 WQITTFPhlfpVNCYLVLERDGLTLIDTGILAHAKGIISLIHKL---KSPLKRILLTHAHGDHIGGLIAVKAAfpealvm 86
Cdd:cd16289   15 WYIGTES----LTALLVKTPDGAVLLDGGMPQAADMLLDNMRALgvaPGDLKLILHSHAHADHAGPLAALKRA------- 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497617566  87 IGSREKLLVETKEIYAFEAQKPLKgsYSDRL---PVRIDQILKDGDMV--GSLLIID--TPGHTPGSISFF--DERNG 155
Cdd:cd16289   84 TGARVAANAESAVLLARGGSDDIH--FGDGItfpPVQADRIVMDGEVVtlGGVTFTAhfTPGHTPGSTSWTwtDTRDG 159
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 22-213 9.97e-12

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: 61.83  E-value: 9.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  22 NCYLVLERDGLTLIDTGILAHAKGIISLI--HKLKSP-LKRILLTHAHGDHIGGLiavkAAFPEALVMIGSrekllVETK 98
Cdd:cd07711   23 TVTLIKDGGKNILVDTGTPWDRDLLLKALaeHGLSPEdIDYVVLTHGHPDHIGNL----NLFPNATVIVGW-----DICG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  99 EIYafeaqkpLKGSYSDRLPVRIDQILKdgdmvgsllIIDTPGHTPGSISFF--DERNGHLFV-GDLFQTRGGAaicgEK 175
Cdd:cd07711   94 DSY-------DDHSLEEGDGYEIDENVE---------VIPTPGHTPEDVSVLveTEKKGTVAVaGDLFEREEDL----ED 153

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 497617566 176 RWLFPfpaMGSWDLPTSIASAEN-LQLFDVteIACGHGP 213
Cdd:cd07711  154 PILWD---PLSEDPELQEESRKRiLALADW--IIPGHGP 187
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 43-163 1.20e-11

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: 61.01  E-value: 1.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  43 AKGIISLIHKLKSPLKRILLTHAHGDHIGGLIAVKAAFPEALVMigSREkllvetkEIYAFEAQKPlkgsysdRLpvrid 122
Cdd:cd16275   34 IEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYM--SKE-------EIDYYGFRCP-------NL----- 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 497617566 123 QILKDGD--MVGSLLI--IDTPGHTPGSISFFdeRNGHLFVGD-LF 163
Cdd:cd16275   93 IPLEDGDtiKIGDTEItcLLTPGHTPGSMCYL--LGDSLFTGDtLF 136
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 35-211 1.69e-11

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 62.94  E-value: 1.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  35 IDTGIL-----AHAKGIISLIHKLKSPLKRILLTHAHGDHIGGLIAVKAAFpeALVMIGSrekllvetkeiyafeaqkpl 109
Cdd:PLN02398  95 EDTGTVgvvdpSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARY--GAKVIGS-------------------- 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566 110 kGSYSDRLPvRIDQILKDGD--MVG--SLLIIDTPGHTPGSISFFDERNGHLFVGD-LFQTRggaaiCGEkrwLFPfpam 184
Cdd:PLN02398 153 -AVDKDRIP-GIDIVLKDGDkwMFAghEVLVMETPGHTRGHISFYFPGSGAIFTGDtLFSLS-----CGK---LFE---- 218

                        170       180       190
                 ....*....|....*....|....*....|.
gi 497617566 185 GSwdlPTSIASAenLQ----LFDVTEIACGH 211
Cdd:PLN02398 219 GT---PEQMLSS--LQkiisLPDDTNIYCGH 244
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 58-203 4.92e-11

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: 60.74  E-value: 4.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  58 KRILLTHAHGDHIGGLiavkAAFPEALVMIGSREKLLVETKEIYAFEAQKPLKGSYSDRLPVRIDQILKD---------- 127
Cdd:cd07730   85 DAVILSHLHWDHIGGL----SDFPNARLIVGPGAKEALRPPGYPSGFLPELLPSDFEGRLVRWEEDDFLWvplgpfpral 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566 128 ---GDmvGSLLIIDTPGHTPGSIS-FFDERNGH--LFVGDLFQTRGGAAICGEKRWLFPFPAMGswDLPTSIASAENLQL 201
Cdd:cd07730  161 dlfGD--GSLYLVDLPGHAPGHLGlLARTTSGTwvFLAGDACHHRIGLLRPSPLLPLPDLDDGA--DREAARETLARLRE 236


                 ..
gi 497617566 202 FD 203
Cdd:cd07730  237 LD 238
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 ...
 25-148 8.86e-09

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: 54.28  E-value: 8.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  25 LVLERDGLTLIDTGILAHAKGIISLIHKLK---SPLKRILLTHAHGDHIGGLIAVKAAfPEALVMIGSREKLLVETKEIy 101
Cdd:cd16290   26 LITSPQGLILIDGALPQSAPQIEANIRALGfrlEDVKLILNSHAHFDHAGGIAALQRD-SGATVAASPAGAAALRSGGV- 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497617566 102 afEAQKPLKGSYSDRLPVRIDQILKDGDMV--GSLLIID--TPGHTPGSIS 148
Cdd:cd16290  104 --DPDDPQAGAADPFPPVAKVRVVADGEVVklGPLAVTAhaTPGHTPGGTS 152
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 19-83 1.15e-08

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 53.27  E-value: 1.15e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497617566  19 FPVNCYLVL-ERDGLtLIDTGI-LAHAKGIISLIHKLKSPLKRILLTHAHGDHIGGLIAVKAAFPEA 83
Cdd:cd07739   14 FPVTSTLIYgETEAV-LVDAQFtRADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAFPDA 79
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 1-214 1.22e-08

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: 53.65  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566   1 MKITTKHSY-----WQITTFPHLFPV------NCYLVLErDGLTLIDTGILAHAKGIISLIHKLKSP--LKRILLTHAHG 67
Cdd:cd07709    1 VEIADDIYWvgvndWDLRLFEGEYPTprgtsyNSYLIKD-EKTALIDTVKEPFFDEFLENLEEVIDPrkIDYIVVNHQEP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  68 DHIGGLIAVKAAFPEALVmIGSR--EKLLvetKEIYafeaqkplkgsysDRLPVRIdQILKDGDMV--GS--LLIIDTPG 141
Cdd:cd07709   80 DHSGSLPELLELAPNAKI-VCSKkaARFL---KHFY-------------PGIDERF-VVVKDGDTLdlGKhtLKFIPAPM 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566 142 -HTPGSISFFDERNGHLFVGDLFqtrgGAAICGEKR----WLFPFPAM----GSWDLPTS---IASAENLQLFDVTEIAC 209
Cdd:cd07709  142 lHWPDTMVTYDPEDKILFSGDAF----GAHGASGELfddeVEDYLEEArryyANIMGPFSkqvRKALEKLEALDIKMIAP 217


                 ....*
gi 497617566 210 GHGPV 214
Cdd:cd07709  218 SHGPI 222
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 60-173 1.75e-08

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 53.29  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  60 ILLTHAHGDHIGGLIAVKAAFPEaLVMIGSRekllvETKEiyafeaqkplKGsysdrlpvrIDQILKDGDMVGSL----L 135
Cdd:PRK10241  49 IFLTHHHHDHVGGVKELVEKFPQ-IVVYGPQ-----ETQD----------KG---------TTQVVKDGETAFVLghefS 103

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 497617566 136 IIDTPGHTPGSISFFDERngHLFVGD-LFQtrGGaaiCG 173
Cdd:PRK10241 104 VFATPGHTLGHICYFSKP--YLFCGDtLFS--GG---CG 135
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 21-163 1.21e-07

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 50.60  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  21 VNCYLVlERDGLT-LIDTGILAHAK-GIISLIHKLKSP-LKR-------------ILLTHAHGDHIG-------GliAVK 77
Cdd:cd16277   13 IHSWLV-RTPGRTiLVDTGIGNDKPrPGPPAFHNLNTPyLERlaaagvrpedvdyVLCTHLHVDHVGwntrlvdG--RWV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  78 AAFPEALVMIGSREkllvetkeiYAF-----EAQKPLKGSYSDR-LPVrIDQIL-----KDGDMVGSLLIIDTPGHTPGS 146
Cdd:cd16277   90 PTFPNARYLFSRAE---------YDHwsspdAGGPPNRGVFEDSvLPV-IEAGLadlvdDDHEILDGIRLEPTPGHTPGH 159

                        170
                 ....*....|....*....
gi 497617566 147 ISFFDERNGH--LFVGDLF 163
Cdd:cd16277  160 VSVELESGGEraLFTGDVM 178
VIM_type_MBL-B1 cd16303
VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona ...
 14-100 2.20e-07

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: 49.86  E-value: 2.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  14 TFP-HLFPVNCYLVLERDGLTLIDT--GILAHAKgIISLIHK-LKSPLKRILLTHAHGDHIGGLIAVKAAFPEALVMIGS 89
Cdd:cd16303   20 SFDgAVYPSNGLIVRDGDELLLIDTawGAKNTAA-LLAEIEKqIGLPVTRAVSTHFHDDRVGGVDVLRAAGVATYASPST 98

                         90
                 ....*....|.
gi 497617566  90 REKLLVETKEI 100
Cdd:cd16303   99 RRLAEAEGNEI 109
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 25-149 4.23e-07

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: 49.60  E-value: 4.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  25 LVLERDGLTLIDTGILAHAKGIISLIHKLK---SPLKRILLTHAHGDHIGGLIAVKaAFPEALVMIGSREKLLVETKEIY 101
Cdd:cd16311   26 LVTSPQGHVLVDGGLPESAPKIIANIEALGfriEDVKLILNSHGHIDHAGGLAELQ-RRSGALVAASPSAALDLASGEVG 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 497617566 102 AFEAQKPLKGSYSdrlPVRIDQILKDGDM--VGSLLIID--TPGHTPGSISF 149
Cdd:cd16311  105 PDDPQYHALPKYP---PVKDMRLARDGGQfnVGPVSLTAhaTPGHTPGGLSW 153
NorV COG0426
Flavorubredoxin [Energy production and conversion];
10-177 5.28e-07

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 49.44  E-value: 5.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  10 WQITTFPHLFPV------NCYLVLErDGLTLIDTGILAHAKGIISLIHKLKSP--LKRILLTHAHGDHIGGLIAVKAAFP 81
Cdd:COG0426   17 WDRRLFEGEYPTprgttyNSYLIVD-EKTALIDTVGESFFEEFLENLSKVIDPkkIDYIIVNHQEPDHSGSLPELLELAP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  82 EALVmIGSR--EKLLvetKEIYafeaqkplkGSYSDRLpvridQILKDGDMV--GS--LLIIDTPG-HTPGSISFFDERN 154
Cdd:COG0426   96 NAKI-VCSKkaARFL---PHFY---------GIPDFRF-----IVVKEGDTLdlGGhtLQFIPAPMlHWPDTMFTYDPED 157

                        170       180
                 ....*....|....*....|...
gi 497617566 155 GHLFVGDLFqtrgGAAICGEKRW 177
Cdd:COG0426  158 KILFSGDAF----GSHGASDELF 176
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 19-214 1.60e-06

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: 47.54  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  19 FPVNCYLVLERDGLTLIDTGILAH-AKGIISLIHK-LKSPLKRILLTHAHGDHIGGLIAVKAAFPEALVMIGSREKLLVE 96
Cdd:cd07707   19 VPSNGLVYNGSKGLVLVDSTWTPKtTKELIKEIEKvSQKPVTEVINTHFHTDRAGGNAYLKERGAKTVSTALTRDLAKSE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  97 TKEIYAFEAQkpLKGSYSDRLPVRIDQILkDGDMVGSLLIIDT----PGHTPGSISFFDERNGHLFvgdlfqtrGGAAIC 172
Cdd:cd07707   99 WAEIVAFTRK--GLPEYPDLGYELPDGVL-DGDFNLQFGKVEAfypgPAHTPDNIVVYFPQENVLY--------GGCIIK 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 497617566 173 GEKRWLFPFPAMGSWdlPTSIasaENLQLFD--VTEIACGHGPV 214
Cdd:cd07707  168 ETDLGNVADADVKEW--PTSI---ERLKKRYrnIKAVIPGHGEV 206
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 22-73 2.84e-06

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 46.81  E-value: 2.84e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 497617566  22 NCYLVLERDGLTLIDTGIlahakGIISLIHKLK---SPLKRILLTHAHGDHIGGL 73
Cdd:COG1235   36 SSILVEADGTRLLIDAGP-----DLREQLLRLGldpSKIDAILLTHEHADHIAGL 85
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 22-73 3.23e-06

uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YycJ protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 45.72  E-value: 3.23e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 497617566  22 NCYLVLERDGLTLIDTGIlaHAKGIISLIHKL-KSP--LKRILLTHAHGDHIGGL 73
Cdd:cd07733   10 NCTYLETEDGKLLIDAGL--SGRKITGRLAEIgRDPedIDAILVTHEHADHIKGL 62
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 23-91 4.21e-06

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 46.46  E-value: 4.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  23 CYLVLERDGLTLIDTGI----LAHAKGIIS--LIHKLK--------------------SPLKRILLTHAHGDHIGGLiav 76
Cdd:cd07742   21 CLLVETDDGLVLVDTGFgladVADPKRRLGgpFRRLLRprldedetavrqiealgfdpSDVRHIVLTHLDLDHAGGL--- 97

                         90
                 ....*....|....*
gi 497617566  77 kAAFPEALVMIGSRE 91
Cdd:cd07742   98 -ADFPHATVHVHAAE 111
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 24-145 5.16e-06

Fluoribacter gormanii FEZ-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 FEZ-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: 293865  Cd Length: 255  Bit Score: 46.28  E-value: 5.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  24 YLVLERDGLTLIDTGILAHAKGIISLIHKLK---SPLKRILLTHAHGDHIGGLIAVKAAfPEALVMIGSREKLLVETKEI 100
Cdd:cd16307   25 YLITTPRGNILINSNLESSVPQIKASIEKLGfkfSDTKILLISHAHFDHAAGSALIKRE-THAKYMVMDGDVDVVESGGK 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 497617566 101 YAFEAQKPLKGSYSdrlPVRIDQILKDGDMV---GSLLIID-TPGHTPG 145
Cdd:cd16307  104 SDFFYGNDPSTYFP---PAHVDKVLHDGEQVelgGTVLTAHlTAGHTKG 149
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 22-94 8.68e-06

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 45.57  E-value: 8.68e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497617566  22 NCYLVLERDGLTLIDTGI-LAHAKGIISLI--HKLKSPLKRILLTHAHGDHIGGLIAVKAAFPEALVMIGSREKLL 94
Cdd:cd07710   19 NMTFIEGDTGLIIIDTLEsAEAAKAALELFrkHTGDKPVKAIIYTHSHPDHFGGAGGFVEEEDSGKVPIIAPEGFM 94
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 129-212 9.22e-06

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: 44.88  E-value: 9.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566 129 DMVGSLLIIDTPGHTPGSISFFDERNGHLFVGD-LFQTRggaaicgEKRWLFPFPAMGSWDLPTSIASAENLQLFDVTEI 207
Cdd:cd07727   99 ELDPDLTLIPVPGHTRGSVVLLYKEKGVLFTGDhLAWSR-------RRGWLSAFRYVCWYSWPEQAESVERLADLDFEWV 171


                 ....*
gi 497617566 208 ACGHG 212
Cdd:cd07727  172 LPGHG 176
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
20-161 9.27e-06

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 45.57  E-value: 9.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  20 PVNCYLVLERDGLTLIDTGIlahakGIISLIHKLK---SPLKRILLTHAHGDHIGGLIAVKaafpEALVMIGSREKLLV- 95
Cdd:COG1234   18 ATSSYLLEAGGERLLIDCGE-----GTQRQLLRAGldpRDIDAIFITHLHGDHIAGLPGLL----STRSLAGREKPLTIy 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497617566  96 ---ETKEiyAFEAQkpLKGSYSD-RLPVRIdQILKDGD--MVGSLLI--IDTPgHTPGSISF-FDERNGHL-FVGD 161
Cdd:COG1234   89 gppGTKE--FLEAL--LKASGTDlDFPLEF-HEIEPGEvfEIGGFTVtaFPLD-HPVPAYGYrFEEPGRSLvYSGD 158
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 34-88 1.13e-05

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: 44.43  E-value: 1.13e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 497617566  34 LIDTGILAHAKG--IISLIHKLK-SPLKRILLTHAHGDHIGGLIAVKAAFPEALVMIG 88
Cdd:cd07731   23 LIDTGPRDSFGEdvVVPYLKARGiKKLDYLILTHPDADHIGGLDAVLKNFPVKEVYMP 80
NDM_FIM-like_MBL-B1 cd16300
NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase ...
 10-228 1.48e-05

NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the ISCR-mediated MBLs NDM-1 (NDM (New Delhi metallo-beta-lactamase) and FIM-1 (Florence imipenemase). MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293858  Cd Length: 214  Bit Score: 44.43  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  10 WQITTFPHL-----FPVNCYLVLERDGLTLIDTG--------ILAHAKGIISLihklksPLKRILLTHAHGDHIGGLIAV 76
Cdd:cd16300   11 WMHTSYLDMpgfgaVPSNGLIVRDGDRVLLVDTAwtddqtaqILNWAKQELNL------PVRLAVVTHAHQDKMGGMDAL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  77 KAA----FPEALVMIGSREKLLVETKEIYAFEAQkplkGSYSDRLPVRidqILKDGdmvgslliidtPGHTPGSISFFDE 152
Cdd:cd16300   85 HAAgiatYANALSNQLAPQEGLVPAQHSLTFAAE----PSTAPNFPLK---VFYPG-----------PGHTRDNIVVGID 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497617566 153 RNGHLFVGDLFQTrGGAAICGEkrwlfpfpaMGSWDLPTSIASAENL-QLF-DVTEIACGHGPVKAMADFDLTNVLKR 228
Cdd:cd16300  147 GTGIAFGGCLIRP-SKATSLGN---------LADADTEHWAASARAFgAAFpDASMIVPSHGAPDGRAAITHTARLAD 214
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 19-77 2.89e-05

Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Bacillus cereus Beta-lactamase 2, also called BcII. 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. BcII is a chromosome-encoded B1 MBL. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293862 [Multi-domain]  Cd Length: 212  Bit Score: 43.81  E-value: 2.89e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497617566  19 FPVNCYLVLERDGLTLIDTG-ILAHAKGIISLI-HKLKSPLKRILLTHAHGDHIGGLIAVK 77
Cdd:cd16304   24 VPSNGLIVETSKGVVLIDTPwDDEQTEELLDWIkKKLKKPVTLAIVTHAHDDRIGGIKALQ 84
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 25-149 4.24e-05

Pseudomonas Aeruginosa AIM-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 AIM-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: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 43.34  E-value: 4.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  25 LVLERDGLTLIDTGILAHAKGIISLIHKL---KSPLKRILLTHAHGDHIGGLIAVKAAFPEALVmigSREKllvetkeiy 101
Cdd:cd16314   26 LVTSDAGHILIDGGTDKAAPLIEANIRALgfrPEDVRYIVSSHEHFDHAGGIARLQRATGAPVV---AREP--------- 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497617566 102 afeAQKPLKGSYSDR-----------LPVRIDQILKDGDM--VGSLLII--DTPGHTPGSISF 149
Cdd:cd16314   94 ---AATTLERGRSDRsdpqflvvekfPPVASVQRIGDGEVlrVGPLALTahATPGHTPGGTSW 153
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 34-88 5.57e-05

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: 42.92  E-value: 5.57e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  34 LIDTG----ILAHAKGIISLIHKLK-SPLKRILLTHAHGDHIGGLIAVKAAFPEALVMIG 88
Cdd:COG2333   25 LIDTGprpsFDAGERVVLPYLRALGiRRLDLLVLTHPDADHIGGLAAVLEAFPVGRVLVS 84
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 46-163 1.57e-04

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 41.67  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  46 IISLIHKLKSPLKRILLTHAHGDHIGGLIAVKAAFPEALVMIGSREKLLVETKEIyafeaqkplkgSYSDRLPVRIDQil 125
Cdd:PLN02469  36 VLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSLDNVKGCTHPV-----------ENGDKLSLGKDV-- 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 497617566 126 kdgdmvgSLLIIDTPGHTPGSISFF----DERNGHLFVGD-LF 163
Cdd:PLN02469 103 -------NILALHTPCHTKGHISYYvtgkEGEDPAVFTGDtLF 138
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 23-75 1.64e-04

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


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 41.09  E-value: 1.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 497617566  23 CYLVLERDGLTLIDTGILAHAKgiISLIHKLKSPLKRILLTHAHGDHIGGLIA 75
Cdd:cd16272   19 SYLLETGGTRILLDCGEGTVYR--LLKAGVDPDKLDAIFLSHFHLDHIGGLPT 69
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 10-73 1.67e-04

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: 41.50  E-value: 1.67e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  10 WQITTFPH----LFPVNCYLVLERDGLTLIDTGIL-AHAKGIISLIHK-LKSPLKRILLTHAHGDHIGGL 73
Cdd:cd16285   11 WVHTSLAEfnggAVPSNGLIVIDGKGLVLIDTPWTeAQTATLLDWIEKkLGKPVTAAISTHSHDDRTGGI 80
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 34-73 1.87e-04

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 41.14  E-value: 1.87e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 497617566   34 LIDTG--ILAHAKGIISLIHKLKSPLKRILLTHAHGDHIGGL 73
Cdd:pfam12706   4 LIDPGpdLRQQALPALQPGRLRDDPIDAVLLTHDHYDHLAGL 45
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-162 3.56e-04

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293839  Cd Length: 252  Bit Score: 40.56  E-value: 3.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  22 NCYLVLERDGLTLIDTGILA-HA---KGIISLI--HKLKSPLKR----------ILLTHAHGDHIGGLIA------VKAA 79
Cdd:cd16281   44 RCLLIETGGRNILIDTGIGDkQDpkfRSIYVQHseHSLLKSLARlglspeditdVILTHLHFDHCGGATRadddglVELL 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  80 FPEALVMIGSRekllvetkeiyAFE-AQKPL---KGSYsdrLPVRIDQI-------LKDG--DMVG---SLLIIDtpGHT 143
Cdd:cd16281  124 FPNATYWVQKR-----------HWEwALNPNpreRASF---LPENIEPLeesgrlkLIDGsdAELGpgiRFHLSD--GHT 187

                        170       180
                 ....*....|....*....|.
gi 497617566 144 PGSISFFDERNGH--LFVGDL 162
Cdd:cd16281  188 PGQMLPEISTPGGtvVFAADL 208
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 22-73 3.64e-04

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry. Some members of this subgroup are named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 40.15  E-value: 3.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 497617566  22 NCYLVLERDGLT-LIDTG------ILAHakGIislihklkSPLKRILLTHAHGDHIGGL 73
Cdd:cd16279   35 RSSILIETGGKNiLIDTGpdfrqqALRA--GI--------RKLDAVLLTHAHADHIHGL 83
PRK00055 PRK00055
ribonuclease Z; Reviewed
 21-76 5.19e-04

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 40.16  E-value: 5.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 497617566  21 VNCYLVLERDGLTLIDTGilahaKG-IISLIH-KLK-SPLKRILLTHAHGDHIGGLIAV 76
Cdd:PRK00055  20 VSSILLRLGGELFLFDCG-----EGtQRQLLKtGIKpRKIDKIFITHLHGDHIFGLPGL 73
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 22-73 6.67e-04

beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and RNase J2, involved in mRNA degradation in a wide range of organism. [Transcription, Degradation of RNA]


Pssm-ID: 273195 [Multi-domain]  Cd Length: 422  Bit Score: 40.41  E-value: 6.67e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497617566   22 NCYLVLERDGLTLIDTGI------LAHAKGII---SLIHKLKSPLKRILLTHAHGDHIGGL 73
Cdd:TIGR00649  15 NMYVVEIDDEIVIFDAGIlfpedeMLGVDGVIpdfTYLQENEDKVKGIFITHGHEDHIGAV 75
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 25-149 6.85e-04

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: 39.85  E-value: 6.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  25 LVLERDGLTLIDTGILAHAKGIISLIHKLK---SPLKRILLTHAHGDHIGGlIAVKAAFPEALVMIGSREkllVETKEIY 101
Cdd:cd16313   26 LITSPQGHILIDGGFPKSPEQIAASIRQLGfklEDVKYILSSHDHWDHAGG-IAALQKLTGAQVLASPAT---VAVLRSG 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 497617566 102 AFEAQKPLKGSYSDRLPVRIDQILKDGDMV--GSLLIID--TPGHTPGSISF 149
Cdd:cd16313  102 SMGKDDPQFGGLTPMPPVASVRAVRDGEVVklGPLAVTAhaTPGHTTGGTSW 153
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
22-73 1.87e-03

mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 38.89  E-value: 1.87e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497617566  22 NCYLVLERDGLTLIDTGIL---AHAKGI------ISLIHKLKSPLKRILLTHAHGDHIGGL 73
Cdd:COG0595   20 NMYVYEYDDDIIIVDCGLKfpeDEMPGVdlvipdISYLEENKDKIKGIVLTHGHEDHIGAL 80
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 23-102 1.96e-03

class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. 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: 293821  Cd Length: 259  Bit Score: 38.35  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497617566  23 CYLV--LERDGLTLID--TGILA---------HAKGIISLIHKLKSPLKRILLTHAHGDHIGGLIavkaafpealVMIGS 89
Cdd:cd07735   19 SFLLdpAGSDGDILLDagTGVGAlsleemfndILFPSQKAAYELYQRIRHYLITHAHLDHIAGLP----------LLSPN 88

                         90
                 ....*....|...
gi 497617566  90 REKLLVETKEIYA 102
Cdd:cd07735   89 DGGQRGSPKTIYG 101
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 22-73 2.85e-03

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. 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: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 37.77  E-value: 2.85e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497617566  22 NCYlVLERDG-LTLIDTGIL---AHAKGI------ISLIHKLKSPLKRILLTHAHGDHIGGL 73
Cdd:cd07714   12 NMY-VVEYDDdIIIIDCGLKfpdEDMPGVdyiipdFSYLEENKDKIKGIFITHGHEDHIGAL 72
PRK11539 PRK11539
ComEC family competence protein; Provisional
 26-85 3.07e-03

ComEC family competence protein; Provisional


Pssm-ID: 236924 [Multi-domain]  Cd Length: 755  Bit Score: 38.44  E-value: 3.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497617566  26 VLERDGLTLI-DTGIL-----AHAKGIISLIHKLKSPLKRILLTHAHGDHIGGLIAVKAAFPEALV 85
Cdd:PRK11539 515 VIERNGKAILyDTGNAwptgdSAQQVIIPWLRWHGLTPEGIILSHEHLDHRGGLASLLHAWPMAWI 580
 
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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