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Conserved domains on  [gi|1052869657|emb|SCJ21995|]
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hydroxyacylglutathione hydrolase [uncultured Flavonifractor sp.]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869773)

uncharacterized MBL fold metallo-hydrolase similar to uncharacterized human metallo-beta-lactamase domain-containing protein 2 (MBLAC2 )

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 20-211 1.03e-75

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: 227.51  E-value: 1.03e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  20 YRHWEETHCYLLNGSERSLLIDTGLGICNIYDQVVRLTQKPVTAVATHIHWDHIGGHRYFPDFYAHEAELDWLHGGFPLS 99
Cdd:cd07712     3 IEEDDRVNIYLLRGRDRALLIDTGLGIGDLKEYVRTLTDLPLLVVATHGHFDHIGGLHEFEEVYVHPADAEILAAPDNFE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 100 PaqiqdmvvdrcdlpEGYDVRTYSLFQGTPTRVLRDGDVIDLGNRRIQVLHTPGHSPGHMCFYEADRGYLFTGDLVYLDT 179
Cdd:cd07712    83 T--------------LTWDAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVYDGP 148

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1052869657 180 LFAYYPSTDPEAYLLSLEKVASL--DVKRVFPGH 211
Cdd:cd07712   149 LIMDLPHSDLDDYLASLEKLSKLpdEFDKVLPGH 182
 
Name Accession Description Interval E-value
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 20-211 1.03e-75

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: 227.51  E-value: 1.03e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  20 YRHWEETHCYLLNGSERSLLIDTGLGICNIYDQVVRLTQKPVTAVATHIHWDHIGGHRYFPDFYAHEAELDWLHGGFPLS 99
Cdd:cd07712     3 IEEDDRVNIYLLRGRDRALLIDTGLGIGDLKEYVRTLTDLPLLVVATHGHFDHIGGLHEFEEVYVHPADAEILAAPDNFE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 100 PaqiqdmvvdrcdlpEGYDVRTYSLFQGTPTRVLRDGDVIDLGNRRIQVLHTPGHSPGHMCFYEADRGYLFTGDLVYLDT 179
Cdd:cd07712    83 T--------------LTWDAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVYDGP 148

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1052869657 180 LFAYYPSTDPEAYLLSLEKVASL--DVKRVFPGH 211
Cdd:cd07712   149 LIMDLPHSDLDDYLASLEKLSKLpdEFDKVLPGH 182
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 26-211 1.38e-41

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 141.37  E-value: 1.38e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  26 THCYLLNGSERSLLIDTGLGICN---IYDQVVRLTQKPVTAVATHIHWDHIGGHRYFPD-----FYAHEAELDWLHGGFP 97
Cdd:COG0491    15 VNSYLIVGGDGAVLIDTGLGPADaeaLLAALAALGLDIKAVLLTHLHPDHVGGLAALAEafgapVYAHAAEAEALEAPAA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  98 LSPAQIQDMVvdrcdlpegydvrtyslfqgtPTRVLRDGDVIDLGNRRIQVLHTPGHSPGHMCFYEADRGYLFTGDLVYL 177
Cdd:COG0491    95 GALFGREPVP---------------------PDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFS 153

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1052869657 178 -DTLFAYYPSTDPEAYLLSLEKVASLDVKRVFPGH 211
Cdd:COG0491   154 gGVGRPDLPDGDLAQWLASLERLLALPPDLVIPGH 188
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 27-211 1.60e-33

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 119.58  E-value: 1.60e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657   27 HCYLLNGSERSLLIDTGLG-ICNIYDQVVRLTQKPVTAV-ATHIHWDHIGGHRYFPDF-----YAHEAELDWLhggfpls 99
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGeAEDLLAELKKLGPKKIDAIiLTHGHPDHIGGLPELLEApgapvYAPEGTAELL------- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  100 paqiqdmvvdrCDLPEGYDVRTYSLFQGTPTRVLRDGDVIDLGNRRIQVLHTPGHSPGHMCFYEADRGYLFTGDLVY--- 176
Cdd:smart00849  74 -----------KDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFagg 142

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1052869657  177 LDTLFAYYPSTDPEAYLLSLEKVASLDVKRVFPGH 211
Cdd:smart00849 143 DGRTLVDGGDAAASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
26-211 3.93e-24

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 95.51  E-value: 3.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  26 THCYLLNGSERSLLIDTGLG---ICNIYDQVVRLTQKPVTAV-ATHIHWDHIGGHRYFPDFYAHEAELDWLHGGFPLSPA 101
Cdd:pfam00753   6 VNSYLIEGGGGAVLIDTGGSaeaALLLLLAALGLGPKDIDAViLTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 102 QIQDMVVDRCDLPEGYDVRtyslfqgtPTRVLRDGDVIDLGNRRIQVLHTPGHSPGHMCFYEADRGYLFTGDLVY----- 176
Cdd:pfam00753  86 LGLAASRLGLPGPPVVPLP--------PDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFageig 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1052869657 177 -----LDTLFAYYPStDPEAYLLSLEKVASLDVKRVFPGH 211
Cdd:pfam00753 158 rldlpLGGLLVLHPS-SAESSLESLLKLAKLKAAVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 66-211 3.44e-14

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 71.03  E-value: 3.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  66 THIHWDHIGGHryfpdfyaheAELDWLHGGFPLSPAqiqdmvVDRCDLPeGYDVrtyslfqgtptrVLRDGDVIDLGNRR 145
Cdd:PLN02398  128 THHHYDHTGGN----------LELKARYGAKVIGSA------VDKDRIP-GIDI------------VLKDGDKWMFAGHE 178

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1052869657 146 IQVLHTPGHSPGHMCFYEADRGYLFTGDLVYLDTLFAYYPSTdPEAYLLSLEKVASL-DVKRVFPGH 211
Cdd:PLN02398  179 VLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGKLFEGT-PEQMLSSLQKIISLpDDTNIYCGH 244
 
Name Accession Description Interval E-value
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 20-211 1.03e-75

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: 227.51  E-value: 1.03e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  20 YRHWEETHCYLLNGSERSLLIDTGLGICNIYDQVVRLTQKPVTAVATHIHWDHIGGHRYFPDFYAHEAELDWLHGGFPLS 99
Cdd:cd07712     3 IEEDDRVNIYLLRGRDRALLIDTGLGIGDLKEYVRTLTDLPLLVVATHGHFDHIGGLHEFEEVYVHPADAEILAAPDNFE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 100 PaqiqdmvvdrcdlpEGYDVRTYSLFQGTPTRVLRDGDVIDLGNRRIQVLHTPGHSPGHMCFYEADRGYLFTGDLVYLDT 179
Cdd:cd07712    83 T--------------LTWDAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVYDGP 148

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1052869657 180 LFAYYPSTDPEAYLLSLEKVASL--DVKRVFPGH 211
Cdd:cd07712   149 LIMDLPHSDLDDYLASLEKLSKLpdEFDKVLPGH 182
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 26-211 1.38e-41

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 141.37  E-value: 1.38e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  26 THCYLLNGSERSLLIDTGLGICN---IYDQVVRLTQKPVTAVATHIHWDHIGGHRYFPD-----FYAHEAELDWLHGGFP 97
Cdd:COG0491    15 VNSYLIVGGDGAVLIDTGLGPADaeaLLAALAALGLDIKAVLLTHLHPDHVGGLAALAEafgapVYAHAAEAEALEAPAA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  98 LSPAQIQDMVvdrcdlpegydvrtyslfqgtPTRVLRDGDVIDLGNRRIQVLHTPGHSPGHMCFYEADRGYLFTGDLVYL 177
Cdd:COG0491    95 GALFGREPVP---------------------PDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFS 153

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1052869657 178 -DTLFAYYPSTDPEAYLLSLEKVASLDVKRVFPGH 211
Cdd:COG0491   154 gGVGRPDLPDGDLAQWLASLERLLALPPDLVIPGH 188
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 25-211 4.60e-35

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: 123.94  E-value: 4.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  25 ETHCYLL-NGSERSLLIDTGLGICN-IYDQVVRLTQKPVTAVATHIHWDHIGGHRYFPD-----FYAHEAELDWLHGGFP 97
Cdd:cd06262     9 QTNCYLVsDEEGEAILIDPGAGALEkILEAIEELGLKIKAILLTHGHFDHIGGLAELKEapgapVYIHEADAELLEDPEL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  98 LSPAQIQDMVVDRcdlpegydvrtyslfqgTPTRVLRDGDVIDLGNRRIQVLHTPGHSPGHMCFYEADRGYLFTGdlvyl 177
Cdd:cd06262    89 NLAFFGGGPLPPP-----------------EPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTG----- 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1052869657 178 DTLFAY------YPSTDPEAYLLSLEKVASL--DVKRVFPGH 211
Cdd:cd06262   147 DTLFAGsigrtdLPGGDPEQLIESIKKLLLLlpDDTVVYPGH 188
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 27-211 1.60e-33

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 119.58  E-value: 1.60e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657   27 HCYLLNGSERSLLIDTGLG-ICNIYDQVVRLTQKPVTAV-ATHIHWDHIGGHRYFPDF-----YAHEAELDWLhggfpls 99
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGeAEDLLAELKKLGPKKIDAIiLTHGHPDHIGGLPELLEApgapvYAPEGTAELL------- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  100 paqiqdmvvdrCDLPEGYDVRTYSLFQGTPTRVLRDGDVIDLGNRRIQVLHTPGHSPGHMCFYEADRGYLFTGDLVY--- 176
Cdd:smart00849  74 -----------KDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFagg 142

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1052869657  177 LDTLFAYYPSTDPEAYLLSLEKVASLDVKRVFPGH 211
Cdd:smart00849 143 DGRTLVDGGDAAASDALESLLKLLKLLPKLVVPGH 177
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 27-211 2.35e-33

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: 119.63  E-value: 2.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  27 HCYLLNGSERSLLIDTGLGIC--NIYDQVVRL--TQKPVTAVA-THIHWDHIGGHRYFPD-----FYAHEAELDWLHGGF 96
Cdd:cd07721    12 NAYLIEDDDGLTLIDTGLPGSakRILKALRELglSPKDIRRILlTHGHIDHIGSLAALKEapgapVYAHEREAPYLEGEK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  97 PLSPAQIQdmvvdrcdLPEGYDVRTYSLFQGTPTRVLRDGDVIDLGNRrIQVLHTPGHSPGHMCFYEADRGYLFTGDLV- 175
Cdd:cd07721    92 PYPPPVRL--------GLLGLLSPLLPVKPVPVDRTLEDGDTLDLAGG-LRVIHTPGHTPGHISLYLEEDGVLIAGDALv 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1052869657 176 ----YLDTLFAYYpSTDPEAYLLSLEKVASLDVKRVFPGH 211
Cdd:cd07721   163 tvggELVPPPPPF-TWDMEEALESLRKLAELDPEVLAPGH 201
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 30-211 3.35e-28

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: 106.50  E-value: 3.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  30 LLNGSERSLLIDTGLGICN---IYDQVVRLTQKPVTAVA-THIHWDHIGGHRYFPD----FYAHEAELDWLHGGfplSPA 101
Cdd:cd16282    19 FIVGDDGVVVIDTGASPRLaraLLAAIRKVTDKPVRYVVnTHYHGDHTLGNAAFADagapIIAHENTREELAAR---GEA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 102 QIQDMVVDRCDLPEGYDVRTyslfqgtPTRVLRDGDVIDLGNRRIQVLHT-PGHSPGHMCFYEADRGYLFTGDLVYLDTL 180
Cdd:cd16282    96 YLELMRRLGGDAMAGTELVL-------PDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEGVLFAGDLVFNGRI 168

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1052869657 181 fAYYPSTDPEAYLLSLEKVASLDVKRVFPGH 211
Cdd:cd16282   169 -PFLPDGSLAGWIAALDRLLALDATVVVPGH 198
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 28-212 1.25e-27

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: 104.30  E-value: 1.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  28 CYLLNGSERSLLIDTGLGICN----IYDQVVRLTQKPV---TAVATHIHWDHIGGHRYFPDfyaheaeldwlhggfplsp 100
Cdd:cd07725    17 VYLLRDGDETTLIDTGLATEEdaeaLWEGLKELGLKPSdidRVLLTHHHPDHIGLAGKLQE------------------- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 101 aqiqdmvVDRCDLpegydvrtYSLfqgtPTRVLRDGDVIDLGNRRIQVLHTPGHSPGHMCFYEADRGYLFTGDLVYLD-- 178
Cdd:cd07725    78 -------KSGATV--------YIL----DVTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLPKit 138

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1052869657 179 ---TLFAYYPSTDPEAYLLSLEKVASLDVKRVFPGHH 212
Cdd:cd07725   139 pnvSLWAVRVEDPLGAYLESLDKLEKLDVDLAYPGHG 175
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 28-211 2.31e-25

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: 98.96  E-value: 2.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  28 CYLL--NGSERSLLIDTGLGICNIYDQVVRLTQKPVTAVATHIHWDHIGGHRYFPD-----FYAHEAELdwLHGGFPLSP 100
Cdd:cd16322    13 TYLVadEGGGEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRhpgapVYLHPDDL--PLYEAADLG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 101 AQIQDMVVDRcdLPEgydvrtyslfqgtPTRVLRDGDVIDLGNRRIQVLHTPGHSPGHMCFYEADRGYLFTGDLVYLDTL 180
Cdd:cd16322    91 AKAFGLGIEP--LPP-------------PDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSI 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1052869657 181 FAY-YPSTDPEAYLLSLEKVASL-DVKRVFPGH 211
Cdd:cd16322   156 GRTdLPGGDPKAMAASLRRLLTLpDETRVFPGH 188
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 26-211 4.93e-25

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: 98.33  E-value: 4.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  26 THCYLLNGSERSLLIDTG--LGICNIYDQVVRLTQKP--VTAVA-THIHWDHIGGH----RYFPD--FYAHEAELDWLhg 94
Cdd:cd07726    16 IASYLLDGEGRPALIDTGpsSSVPRLLAALEALGIAPedVDYIIlTHIHLDHAGGAgllaEALPNakVYVHPRGARHL-- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  95 gfpLSPAQIQD---MVvdrcdLPEGYDVRTYSLfQGTP---TRVLRDGDVIDLGNRRIQVLHTPGHSPGHMCFYEADRGY 168
Cdd:cd07726    94 ---IDPSKLWAsarAV-----YGDEADRLGGEI-LPVPeerVIVLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESDG 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1052869657 169 LFTGDL--VYLDTLFAYYPST------DPEAYLLSLEKVASLDVKRVFPGH 211
Cdd:cd07726   165 LFTGDAagVRYPELDVVGPPStpppdfDPEAWLESLDRLLSLKPERIYLTH 215
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
26-211 3.93e-24

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 95.51  E-value: 3.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  26 THCYLLNGSERSLLIDTGLG---ICNIYDQVVRLTQKPVTAV-ATHIHWDHIGGHRYFPDFYAHEAELDWLHGGFPLSPA 101
Cdd:pfam00753   6 VNSYLIEGGGGAVLIDTGGSaeaALLLLLAALGLGPKDIDAViLTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 102 QIQDMVVDRCDLPEGYDVRtyslfqgtPTRVLRDGDVIDLGNRRIQVLHTPGHSPGHMCFYEADRGYLFTGDLVY----- 176
Cdd:pfam00753  86 LGLAASRLGLPGPPVVPLP--------PDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFageig 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1052869657 177 -----LDTLFAYYPStDPEAYLLSLEKVASLDVKRVFPGH 211
Cdd:pfam00753 158 rldlpLGGLLVLHPS-SAESSLESLLKLAKLKAAVIVPGH 196
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 12-211 7.54e-24

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: 95.74  E-value: 7.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  12 PDTSILSEYRHWEET-----HCYLLNGSERSLLIDTGLGICNIYDQ---------VVRLTQKPVTA-------------- 63
Cdd:cd07729    13 DKSSLFYYGRGPGEPidlpvYAYLIEHPEGTILVDTGFHPDAADDPgglelafppGVTEEQTLEEQlarlgldpedidyv 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  64 VATHIHWDHIGGHRYFPD--FYAHEAELDWLHGGFPLSPAQIQDMVVDRCDLPEGydvrTYSLFQGtptrvlrDGDVIDl 141
Cdd:cd07729    93 ILSHLHFDHAGGLDLFPNatIIVQRAELEYATGPDPLAAGYYEDVLALDDDLPGG----RVRLVDG-------DYDLFP- 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 142 gnrRIQVLHTPGHSPGHMCFY-EADRG-YLFTGDLVYL------DTLFAyyPSTDPEAYLLSLEKVASL---DVKRVFPG 210
Cdd:cd07729   161 ---GVTLIPTPGHTPGHQSVLvRLPEGtVLLAGDAAYTyenleeGRPPG--INYDPEAALASLERLKALaerEGARVIPG 235


                  .
gi 1052869657 211 H 211
Cdd:cd07729   236 H 236
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 66-211 2.42e-22

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 89.83  E-value: 2.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  66 THIHWDHIGG----HRYFPDF--YAHEAeldwlhggfplspaqiqdmvvDRCDLPegydvrtyslfqgtpTRVLRDGDVI 139
Cdd:cd07723    50 THHHWDHTGGnaelKALFPDApvYGPAE---------------------DRIPGL---------------DHPVKDGDEI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 140 DLGNRRIQVLHTPGHSPGHMCFYEADRGYLFTGdlvylDTLFAyypST-------DPEAYLLSLEKVASLDVK-RVFPGH 211
Cdd:cd07723    94 KLGGLEVKVLHTPGHTLGHICYYVPDEPALFTG-----DTLFS---GGcgrffegTAEQMYASLQKLLALPDDtLVYCGH 165
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 28-211 2.23e-21

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: 87.59  E-value: 2.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  28 CYLL--NGSERSLLIDTGLGICNIYDQVVRLTQKPVTAVATHIHWDHIGG-----HRYFPDFYAHEAELDwlhggfplsp 100
Cdd:cd16275    14 SYIIidKATREAAVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVNLvepllAKYDAPVYMSKEEID---------- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 101 aqiqdmvvdrcdlpegydvrtYSLFQGTPTRVLRDGDVIDLGNRRIQVLHTPGHSPGHMCFYEADRgyLFTGdlvylDTL 180
Cdd:cd16275    84 ---------------------YYGFRCPNLIPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGDS--LFTG-----DTL 135

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1052869657 181 FAY------YPSTDPEAYLLSLEKVASLDVK--RVFPGH 211
Cdd:cd16275   136 FIEgcgrcdLPGGDPEEMYESLQRLKKLPPPntRVYPGH 174
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 129-220 5.03e-21

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: 87.16  E-value: 5.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 129 PTRVLRDGDVIDLGNRRIQVLHTPGHSPGHMCFYEADRGYLFTGDLVyLD--TLFAYYPSTDPEAYLLSLEKVASLDVKR 206
Cdd:cd16278    98 PDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHV-MGwsTTVIAPPDGDLGDYLASLERLLALDDRL 176

                          90
                  ....*....|....
gi 1052869657 207 VFPGHhslavGPDI 220
Cdd:cd16278   177 LLPGH-----GPPI 185
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 26-220 1.94e-18

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: 80.27  E-value: 1.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  26 THCYLLNGSERSLLIDTGLGICNIYD---QVVR-LTQKPVTAV-ATHIHWDHIGGhryFPDFyaheaeLDWLHGG----- 95
Cdd:cd07722    18 TNTYLVGTGKRRILIDTGEGRPSYIPllkSVLDsEGNATISDIlLTHWHHDHVGG---LPDV------LDLLRGPsprvy 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  96 -FPLSPAQIQDmvvdrcdlpegydvrtysLFQGTPTRVLRDGDVIDLGNRRIQVLHTPGHSPGHMCFYEADRGYLFTGDL 174
Cdd:cd07722    89 kFPRPEEDEDP------------------DEDGGDIHDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGDC 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1052869657 175 VyL---DTLFayypsTDPEAYLLSLEKVASLDVKRVFPGHhslavGPDI 220
Cdd:cd07722   151 V-LghgTAVF-----EDLAAYMASLKKLLSLGPGRIYPGH-----GPVI 188
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 28-211 4.12e-18

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: 79.52  E-value: 4.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  28 CYLLNGSE--RSLLIDTGLGICNIYDQVVRLTQKPVTAVATHIHWDHIGGHRYFPDFYA------HEAELDWLhggfpls 99
Cdd:cd07737    13 CSLIWCEEtkEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGvpiigpHKEDKFLL------- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 100 paqiqDMVVDRCDLPEGYDVRTYslfqgTPTRVLRDGDVIDLGNRRIQVLHTPGHSPGHMCFYEADRGYLFTGdlvylDT 179
Cdd:cd07737    86 -----ENLPEQSQMFGFPPAEAF-----TPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVG-----DV 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1052869657 180 LFAY------YPSTDPEAYLLSL-EKVASL-DVKRVFPGH 211
Cdd:cd07737   151 LFKGsigrtdFPGGNHAQLIASIkEKLLPLgDDVTFIPGH 190
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 11-211 1.40e-17

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: 77.44  E-value: 1.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  11 DPDTSILSeyrhweethcYLLnGSERS---LLIDTGLGICNIYDQVVR---LTqkpVTAVA-THIHWDHIGGHRYFPDfy 83
Cdd:cd07724     7 DPGLGTLS----------YLV-GDPETgeaAVIDPVRDSVDRYLDLAAelgLK---ITYVLeTHVHADHVSGARELAE-- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  84 AHEAELdWLHGGfplspaqiqdmvvdrcDLPEGYDVRtyslfqgtptrvLRDGDVIDLGNRRIQVLHTPGHSPGHMCFYE 163
Cdd:cd07724    71 RTGAPI-VIGEG----------------APASFFDRL------------LKDGDVLELGNLTLEVLHTPGHTPESVSYLV 121

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1052869657 164 ADRGYLFTGDLVYLD----TLFAYYPSTDPEAYLLSLEKVASL--DVKRVFPGH 211
Cdd:cd07724   122 GDPDAVFTGDTLFVGdvgrPDLPGEAEGLARQLYDSLQRKLLLlpDETLVYPGH 175
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 55-213 1.96e-15

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 72.23  E-value: 1.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  55 RLTQKPVTAVA-THIHWDHIGGHRYFPD----FYAHEAELDWLHGgFPLSpaqiqdmvvdrcDLPegydvrtyslfqgTP 129
Cdd:cd16276    40 KVTDKPVTHVVySHNHADHIGGASIFKDegatIIAHEATAELLKR-NPDP------------KRP-------------VP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 130 TRVLRDGDVIDLGNRRIQvLHTPG--HSPGHMCFYEADRGYLFTGDLVYLD--TLFAYYPSTDPEAYLLSLEKVASLDVK 205
Cdd:cd16276    94 TVTFDDEYTLEVGGQTLE-LSYFGpnHGPGNIVIYLPKQKVLMAVDLINPGwvPFFNFAGSEDIPGYIEALDELLEYDFD 172


                  ....*...
gi 1052869657 206 RVFPGHHS 213
Cdd:cd16276   173 TFVGGHGN 180
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 66-211 3.44e-14

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 71.03  E-value: 3.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  66 THIHWDHIGGHryfpdfyaheAELDWLHGGFPLSPAqiqdmvVDRCDLPeGYDVrtyslfqgtptrVLRDGDVIDLGNRR 145
Cdd:PLN02398  128 THHHYDHTGGN----------LELKARYGAKVIGSA------VDKDRIP-GIDI------------VLKDGDKWMFAGHE 178

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1052869657 146 IQVLHTPGHSPGHMCFYEADRGYLFTGDLVYLDTLFAYYPSTdPEAYLLSLEKVASL-DVKRVFPGH 211
Cdd:PLN02398  179 VLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGKLFEGT-PEQMLSSLQKIISLpDDTNIYCGH 244
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 38-211 2.16e-13

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 66.79  E-value: 2.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  38 LLIDTGLGicniyDQVVR--------LTQKPVTAVATHIHWDHIGGHRYFPD-----FYAHEAELDW----------LHG 94
Cdd:cd07743    21 LLIDSGLD-----EDAGRkirkileeLGWKLKAIINTHSHADHIGGNAYLQKktgckVYAPKIEKAFienpllepsyLGG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  95 GFPlspaqiqdmvvdrcdlpegYDVRTYSLFQGTPTRV---LRDGDvIDLGNRRIQVLHTPGHSPGHMCFyEADRGYLFT 171
Cdd:cd07743    96 AYP-------------------PKELRNKFLMAKPSKVddiIEEGE-LELGGVGLEIIPLPGHSFGQIGI-LTPDGVLFA 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1052869657 172 GDLVYLDTLFAYYP---STDPEAYLLSLEKVASLDVKRVFPGH 211
Cdd:cd07743   155 GDALFGEEVLEKYGipfLYDVEEQLETLEKLEELDADYYVPGH 197
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 28-191 1.11e-11

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: 62.95  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  28 CYLLNGSERSLLIDTGLGICNiYDQVVRLTQ-------KP--VTAVA-THIHWDHIGG------HRYFPD--FYAHEAEL 89
Cdd:cd07720    51 AFLVRTGGRLILVDTGAGGLF-GPTAGKLLAnlaaagiDPedIDDVLlTHLHPDHIGGlvdaggKPVFPNaeVHVSEAEW 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  90 D-WLHGGF----PLSPAQIQDMVVDRcdlpegydVRTYSlfqgTPTRVLRDGDVIDlGnrrIQVLHTPGHSPGHMCFYEA 164
Cdd:cd07720   130 DfWLDDANaakaPEGAKRFFDAARDR--------LRPYA----AAGRFEDGDEVLP-G---ITAVPAPGHTPGHTGYRIE 193

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1052869657 165 DRGY--LFTGDLVYLDTLFAYYPS------TDPEA 191
Cdd:cd07720   194 SGGErlLIWGDIVHHPALQFAHPDwtiafdVDPEQ 228
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 129-211 4.42e-11

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: 60.96  E-value: 4.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 129 PTRVLRDGDVIDLGNRRIQVLHTPG-HSPGHMCFYEADRGYLFTGDL----VYLDTLFA------------YY-----PS 186
Cdd:cd07709   117 RFVVVKDGDTLDLGKHTLKFIPAPMlHWPDTMVTYDPEDKILFSGDAfgahGASGELFDdevedyleearrYYanimgPF 196

                          90       100
                  ....*....|....*....|....*.
gi 1052869657 187 TdpeAYLLS-LEKVASLDVKRVFPGH 211
Cdd:cd07709   197 S---KQVRKaLEKLEALDIKMIAPSH 219
NorV COG0426
Flavorubredoxin [Energy production and conversion];
131-211 1.15e-09

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 57.92  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 131 RVLRDGDVIDLGNRRIQVLHTPG-HSPGHMCFYEADRGYLFTGDL----VYLDTLFA-------------YY-----PST 187
Cdd:COG0426   121 IVVKEGDTLDLGGHTLQFIPAPMlHWPDTMFTYDPEDKILFSGDAfgshGASDELFDdevdehleeearrYYanimmPFS 200

                          90       100
                  ....*....|....*....|....*
gi 1052869657 188 dpeAYLLS-LEKVASLDVKRVFPGH 211
Cdd:COG0426   201 ---KQVLKaLKKVRGLDIDMIAPSH 222
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 66-211 1.37e-09

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


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 56.89  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  66 THIHWDHIGGHRYFP--DFYAHEAELDWLHGgfPLSPAQIQDMVVDRcDLPEGydVRTYSLFQGTPTRVLRDGDVIDL-G 142
Cdd:cd07730    90 SHLHWDHIGGLSDFPnaRLIVGPGAKEALRP--PGYPSGFLPELLPS-DFEGR--LVRWEEDDFLWVPLGPFPRALDLfG 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 143 NRRIQVLHTPGHSPGHMCFY---EADRGYLFTGDLVYlDTLFAYYPST-----------DPEAYLLSLEKVASLDVK--- 205
Cdd:cd07730   165 DGSLYLVDLPGHAPGHLGLLartTSGTWVFLAGDACH-HRIGLLRPSPllplpdlddgaDREAARETLARLRELDAApdv 243


                  ....*.
gi 1052869657 206 RVFPGH 211
Cdd:cd07730   244 RVVLAH 249
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 66-162 1.65e-09

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 56.44  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  66 THIHWDHIGGHRYF-----PDFYAHEAELDWLHggfplspAQIQDMVVDRCDLPegydvrtyslfqgtPTR--VLRDGDV 138
Cdd:cd16280    68 THGHGDHYGGAAYLkdlygAKVVMSEADWDMME-------EPPEEGDNPRWGPP--------------PERdiVIKDGDT 126

                          90       100
                  ....*....|....*....|....
gi 1052869657 139 IDLGNRRIQVLHTPGHSPGHMCFY 162
Cdd:cd16280   127 LTLGDTTITVYLTPGHTPGTLSLI 150
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 132-211 2.30e-09

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: 55.28  E-value: 2.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 132 VLRDGDVIDLGNRrIQVLHTPGHSPGHMCFYEADRGYLFTGDLVYLD------TLFAYYPSTDPEAYLLSLEKVASLDVK 205
Cdd:cd07727    91 VLWGGDPWELDPD-LTLIPVPGHTRGSVVLLYKEKGVLFTGDHLAWSrrrgwlSAFRYVCWYSWPEQAESVERLADLDFE 169


                  ....*.
gi 1052869657 206 RVFPGH 211
Cdd:cd07727   170 WVLPGH 175
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 64-211 1.20e-08

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: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  64 VATHIHWDHIGGHryfpdfyaheAELDWLHGGFPL-SPAQIQDM---VVDRCDLPEGYDVRtyslFQG-TPTRVLRDGDV 138
Cdd:cd16290    65 LNSHAHFDHAGGI----------AALQRDSGATVAaSPAGAAALrsgGVDPDDPQAGAADP----FPPvAKVRVVADGEV 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 139 IDLGNRRIQVLHTPGHSPGHM------CfyEADRgylfTGDLVYLDTLFAY----YPSTDP------EAYLLSLEKVASL 202
Cdd:cd16290   131 VKLGPLAVTAHATPGHTPGGTswtwrsC--EGGR----CLDIVYADSLTAVsadgFRFSDDahparvAAFRRSIATVAAL 204


                  ....*....
gi 1052869657 203 DVKRVFPGH 211
Cdd:cd16290   205 PCDILISAH 213
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 66-211 2.24e-08

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 53.23  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  66 THIHWDHIGGH----RYFPDFYAHEAELDWLHGgfplspaqiqdmvvdrCdlpegydvrtyslfqgtpTRVLRDGDVIDL 141
Cdd:PLN02469   53 THHHWDHAGGNekikKLVPGIKVYGGSLDNVKG----------------C------------------THPVENGDKLSL 98

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1052869657 142 GNR-RIQVLHTPGHSPGHMCFY----EADRGYLFTGDLVYLDTLFAYYPSTdPEAYLLSLEKV-ASL-DVKRVFPGH 211
Cdd:PLN02469   99 GKDvNILALHTPCHTKGHISYYvtgkEGEDPAVFTGDTLFIAGCGKFFEGT-AEQMYQSLCVTlGSLpKPTQVYCGH 174
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 64-211 3.51e-08

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: 52.94  E-value: 3.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  64 VATHIHWDHIGGhryfpdfyahEAELDWLHGGFPL-SPAQIQdmvVDRCDLPEGYDVRTYSLFQGTP---TRVLRDGDVI 139
Cdd:cd16313    65 LSSHDHWDHAGG----------IAALQKLTGAQVLaSPATVA---VLRSGSMGKDDPQFGGLTPMPPvasVRAVRDGEVV 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 140 DLGNRRIQVLHTPGHSPGHMCFY----EADRgylfTGDLVYLDTLFA-----YYPSTDPEA---YLLSLEKVASLDVKRV 207
Cdd:cd16313   132 KLGPLAVTAHATPGHTTGGTSWTwqscEQGR----CANMVFADSLTAvsadgYRFSAHPAVladVEQSIAAVEKLACDIL 207


                  ....
gi 1052869657 208 FPGH 211
Cdd:cd16313   208 VSAH 211
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-157 4.29e-08

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


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 52.71  E-value: 4.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  28 CYLLNGSERSLLIDTGL--GICNIYDQVVRLTQKPVTA---VATHIHWDHIGGHRYF-----PDFYAHEAELDWLHGGfp 97
Cdd:cd16288    24 SYLITTPQGLILIDTGLesSAPMIKANIRKLGFKPSDIkilLNSHAHLDHAGGLAALkkltgAKLMASAEDAALLASG-- 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  98 lspaqiqdmvvDRCDLPEGYDVRTYSlfQGTPTRVLRDGDVIDLGNRRIQVLHTPGHSPG 157
Cdd:cd16288   102 -----------GKSDFHYGDDSLAFP--PVKVDRVLKDGDRVTLGGTTLTAHLTPGHTRG 148
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 26-222 1.34e-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) 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: 51.09  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  26 THCYLLNGSERSLLIDTGLGICNIYD-------------------------QVVRLTQKP--VT-AVATHIHWDHIGGHR 77
Cdd:cd07742    19 CHCLLVETDDGLVLVDTGFGLADVADpkrrlggpfrrllrprldedetavrQIEALGFDPsdVRhIVLTHLDLDHAGGLA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  78 YFPDfyA----HEAELDWLHGGFPLSPAQiqdmVVDRCDLPEGYDVRTYSlFQGTPTRVLRDGDVIDLGNRRIQVLHTPG 153
Cdd:cd07742    99 DFPH--AtvhvHAAELDAATSPRTRYERR----RYRPQQLAHGPWWVTYA-AGGERWFGFEAVRPLDGLPPEILLVPLPG 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 154 HSPGHMC--FYEADRGYLFTGDlvyldtlfAYY------PSTDPEAYLLSLEKVASLDVKRVFPGHHSLA-----VGPDI 220
Cdd:cd07742   172 HTRGHCGvaVRTGDRWLLHAGD--------AYFhhgeldPLPPPPPPLRLFQRLLAVDRSARLANLARLRelardHGDEV 243


                  ..
gi 1052869657 221 LV 222
Cdd:cd07742   244 EV 245
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 28-224 2.38e-07

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 50.28  E-value: 2.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  28 CYLLNGSERSLLIDTGLGICniyDQVVRLTQKPVTAVA---THIHWDHIGGhryFPDFYAHeaeldWLHGGFPL-SPAQI 103
Cdd:COG1235    37 SILVEADGTRLLIDAGPDLR---EQLLRLGLDPSKIDAillTHEHADHIAG---LDDLRPR-----YGPNPIPVyATPGT 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 104 QDmvvdrcDLPEGYDVRTYSLFQGTPTRVLRDGDVIDLGNRRIQVLHTPgHSPGHMCFY--EADRGYLF----TG----- 172
Cdd:COG1235   106 LE------ALERRFPYLFAPYPGKLEFHEIEPGEPFEIGGLTVTPFPVP-HDAGDPVGYriEDGGKKLAyatdTGyipee 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1052869657 173 --------DLVYLDTLFayypsTDPEAYLLSLEKVA----SLDVKRVFPGHHSLAVGPDILVRM 224
Cdd:COG1235   179 vlellrgaDLLILDATY-----DDPEPGHLSNEEALellaRLGPKRLVLTHLSPDNNDHELDYD 237
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 30-211 2.42e-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) 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: 49.81  E-value: 2.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  30 LLNGSERSLLIDTGLGICNIYDQV--VRLTQKPVTAV-ATHIHWDHIGG----HRYFPD--FYAHEAELDWLH----GGF 96
Cdd:cd07739    20 LIYGETEAVLVDAQFTRADAERLAdwIKASGKTLTTIyITHGHPDHYFGlevlLEAFPDakVVATPAVVAHIKaqlePKL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  97 PLSPAQIQDMVVDRCDLPEGYDvrtyslfqgtptrvlrdGDVIDLGNRRIQVLHTPGHSP-GHMCFYEADRGYLFTGDLV 175
Cdd:cd07739   100 AFWGPLLGGNAPARLVVPEPLD-----------------GDTLTLEGHPLEIVGVGGGDTdDTTYLWIPSLKTVVAGDVV 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1052869657 176 YLDTlfayYP----STDPE---AYLLSLEKVASLDVKRVFPGH 211
Cdd:cd07739   163 YNGV----HVwladATTPElraAWLAALDKIEALNPETVVPGH 201
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 59-202 2.99e-07

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 50.21  E-value: 2.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  59 KPVTAVATHIHWDHIGGHR----YFPDFYAHeaeldwlhggfplSPAQIQDmvvdrcdlpegydvrtyslfQGTpTRVLR 134
Cdd:PRK10241   45 QPEAIFLTHHHHDHVGGVKelveKFPQIVVY-------------GPQETQD--------------------KGT-TQVVK 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052869657 135 DGDVIDLGNRRIQVLHTPGHSPGHMCFYEadRGYLFTGdlvylDTLFA-----YYPSTdPEAYLLSLEKVASL 202
Cdd:PRK10241   91 DGETAFVLGHEFSVFATPGHTLGHICYFS--KPYLFCG-----DTLFSggcgrLFEGT-ASQMYQSLKKINAL 155
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 56-212 3.11e-07

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: 49.81  E-value: 3.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  56 LTQKPVTAVA-THIHWDHIGGHRYF--------PDFYAHEAELDWLHG-----------------GFPLSPAQIQDMvvd 109
Cdd:cd07710    52 TGDKPVKAIIyTHSHPDHFGGAGGFveeedsgkVPIIAPEGFMEEAVSenvlagnamsrraayqfGALLPKGEKGQV--- 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 110 rcDLPEGYDVR--TYSLFqgTPTRVL-RDGDVIDLGNRRIQVLHTPGHSPGHMCFYEADRGYLFTGDLVYlDTLFAYY-- 184
Cdd:cd07710   129 --GAGLGPGLStgTVGFI--PPTITItETGETLTIDGVELEFQHAPGEAPDEMMVWLPDYKVLFCADNVY-HTFPNLYtl 203

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1052869657 185 ---PSTDPEAYLLSLEKVASLDVKRVFPGHH 212
Cdd:cd07710   204 rgaKYRDALAWAKSLDEAISLKAEVLFPSHT 234
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 30-203 7.54e-07

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: 48.88  E-value: 7.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  30 LLNGSERSLLIDTGL--GICNIYDQVVRLTQKPVTA---VATHIHWDHIGGHryfpdfyaheAELDWLHGG-FPLSPAQI 103
Cdd:cd16315    26 LITGDDGHVLIDSGTeeAAPLVLANIRKLGFDPKDVrwlLSSHEHFDHVGGL----------AALQRATGArVAASAAAA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 104 QDMvvdRCDLPEGYDVRTYSLFQGTPTRV---LRDGDVIDLGNRRIQVLHTPGHSPGHM------CFYEADRgylftgDL 174
Cdd:cd16315    96 PVL---ESGKPAPDDPQAGLHEPFPPVRVdriVEDGDTVALGSLRLTAHATPGHTPGALswtwrsCEGADCR------TI 166

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1052869657 175 VYLDTLFA-----YYPSTDPE---AYLLSLEKVASLD 203
Cdd:cd16315   167 VYADSLSPvsadgYRFSDHPDyvaAYRAGLAKVAALP 203
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 28-161 1.14e-06

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


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 48.23  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  28 CYLLNGSERSLLIDTGLGicniydQVVRLTQKPVTAV-----------ATHIHWDHIGGHRYFPD-----FYAHEAELDW 91
Cdd:cd16308    24 CYLIVTPKGNILINTGLA------ESVPLIKKNIQALgfkfkdikillTTQAHYDHVGAMAAIKQqtgakMMVDEKDAKV 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  92 LHGGfplspaqiqdmvvDRCDLPEGYDVRTYSLFqgTPTRVLRDGDVIDLGNRRIQVLHTPGHSPGHMCF 161
Cdd:cd16308    98 LADG-------------GKSDYEMGGYGSTFAPV--KADKLLHDGDTIKLGGTKLTLLHHPGHTKGSCSF 152
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 24-174 1.38e-06

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 47.90  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  24 EETHCYLLNGSERSLLIDTGLG---------ICNIYDQVV--RLTQ---KP--VTAVA-THIHWDHIG------GHRYFP 80
Cdd:cd16277    11 ELIHSWLVRTPGRTILVDTGIGndkprpgppAFHNLNTPYleRLAAagvRPedVDYVLcTHLHVDHVGwntrlvDGRWVP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  81 DF-----YAHEAELDWL---HGGFPLSPAQIQDMVvdrcdLPegydvrtysLFQGTPTRVLRDGDVIDLGnrrIQVLHTP 152
Cdd:cd16277    91 TFpnaryLFSRAEYDHWsspDAGGPPNRGVFEDSV-----LP---------VIEAGLADLVDDDHEILDG---IRLEPTP 153

                         170       180
                  ....*....|....*....|....*
gi 1052869657 153 GHSPGHMCfYEADRG---YLFTGDL 174
Cdd:cd16277   154 GHTPGHVS-VELESGgerALFTGDV 177
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 28-211 8.92e-06

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 44.88  E-value: 8.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  28 CYLLNGSERSLLIDTGLGicNIYDQVVR-LTQKPVTA------VATHIHWDHIGGHRYFPD--FYAHEAELDWLHGGFPL 98
Cdd:cd07711    24 VTLIKDGGKNILVDTGTP--WDRDLLLKaLAEHGLSPedidyvVLTHGHPDHIGNLNLFPNatVIVGWDICGDSYDDHSL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  99 SPaqiqdmvvdrcdlpegydvrtyslfqgtptrvlRDGDVIDLGnrrIQVLHTPGHSPGHMCF--YEADRG-YLFTGDL- 174
Cdd:cd07711   102 EE---------------------------------GDGYEIDEN---VEVIPTPGHTPEDVSVlvETEKKGtVAVAGDLf 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1052869657 175 -----VYLDTLFAYYpSTDPEAYLLSLEKVASLdVKRVFPGH 211
Cdd:cd07711   146 ereedLEDPILWDPL-SEDPELQEESRKRILAL-ADWIIPGH 185
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
28-188 9.55e-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: 9.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  28 CYLLNGSERSLLIDTGLGIcniYDQVVRLTQKP--VTAVA-THIHWDHIGG---HRYFPDFYAHEAELDwLHGgfplsPA 101
Cdd:COG1234    21 SYLLEAGGERLLIDCGEGT---QRQLLRAGLDPrdIDAIFiTHLHGDHIAGlpgLLSTRSLAGREKPLT-IYG-----PP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 102 QIQDMV---VDRCDLPEGYDVRtyslfqgtpTRVLRDGDVIDLGNRRIQVLHTPgHSPGH--MCFYEADRGYLFTGDLVY 176
Cdd:COG1234    92 GTKEFLealLKASGTDLDFPLE---------FHEIEPGEVFEIGGFTVTAFPLD-HPVPAygYRFEEPGRSLVYSGDTRP 161

                         170
                  ....*....|..
gi 1052869657 177 LDTLFAYYPSTD 188
Cdd:COG1234   162 CEALVELAKGAD 173
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 29-157 3.79e-05

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: 43.69  E-value: 3.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  29 YLLNGSERSLLIDTGL--GICNIYDQVVRLTQKPVTA---VATHIHWDHIGG-----HRYFPDFYAHEAELDWLHGGFpl 98
Cdd:cd07708    25 YLIVTPQGNILIDGDMeqNAPMIKANIKKLGFKFSDTkliLISHAHFDHAGGsaeikKQTGAKVMAGAEDVSLLLSGG-- 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1052869657  99 spaqiqdmvvdRCDLPEGYDVRTYsLFQGTPTRVLRDGDVIDLGNRRIQVLHTPGHSPG 157
Cdd:cd07708   103 -----------SSDFHYANDSSTY-FPQSTVDRAVHDGERVTLGGTVLTAHATPGHTPG 149
SPM-1-like_MBL-B1-B2-like cd16286
Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; ...
 6-211 7.08e-05

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


Pssm-ID: 293844 [Multi-domain]  Cd Length: 236  Bit Score: 42.90  E-value: 7.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657   6 TLDQIDPDTSILSEYRHWEETHCYLLNGSERSLLID---TGLGICNIYDQVVR-LTQKPVTAVATHIHWDHIGGHRYFpd 81
Cdd:cd16286     8 TAREIDPDVFVITHRDPWSSNVLVVKMLDGTVVIVDspyTNLATQTVLDWIAKtMGPRKVVAINTHFHLDGTGGNEAL-- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  82 fyaheaeldwLHGGFPLSPAQIQDMVV------DRCDLPEGYDVRTY-SLFQGTPTRV------LRDGDVIDLGNRRIQV 148
Cdd:cd16286    86 ----------KKRGIPTWGSDLTKQLLlergkaDRIKAAEFLKNEDLkRRIESSPPVPpdnvfdLKEGKVFSFGNELVEV 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1052869657 149 LHT-PGHSPGHMCFYEADRGYLFTGDLVYLDTLFAYYPSTDPEAYLLSLEKVASLDVKRVFPGH 211
Cdd:cd16286   156 SFPgPAHAPDNVVVYFPERKILFGGCMIKPGKELGNLGDANMKAWPDSVRRLKKFDAKIVIPGH 219
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 36-174 7.30e-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: 7.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  36 RSLLIDTG-LGICNIYDQVVR--LTQKPVT----AVATHIHWDHIGGhryfpdfyaheaeLDWLHGGFPlsPAQIQDMVV 108
Cdd:COG2333    22 KTILIDTGpRPSFDAGERVVLpyLRALGIRrldlLVLTHPDADHIGG-------------LAAVLEAFP--VGRVLVSGP 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052869657 109 DRcDLPEGYDVRTYSLFQGTPTRVLRDGDVIDLGNRRIQVLHTPGHSPGH---------MCFYEADRGYLFTGDL 174
Cdd:COG2333    87 PD-TSETYERLLEALKEKGIPVRPCRAGDTWQLGGVRFEVLWPPEDLLEGsdennnslvLRLTYGGFSFLLTGDA 160
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 29-157 9.76e-05

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: 42.47  E-value: 9.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  29 YLLNGSERSLLIDTGL--GICNIYDQVVRLTQKPVTA---VATHIHWDHIGGHryfpdfyaheAELDWLHGgfplspAQI 103
Cdd:cd16309    25 FLITTPEGHILIDGAMpqSTPLIKDNIKKLGFDVKDVkylLNTHAHFDHAGGL----------AELKKATG------AQL 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1052869657 104 QDMVVDRCDLPEGY----DVRTYSLFQGTPTRVLRDGDVIDLGNRRIQVLHTPGHSPG 157
Cdd:cd16309    89 VASAADKPLLESGYvgsgDTKNLQFPPVRVDRVIGDGDKVTLGGTTLTAHLTPGHSPG 146
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 131-182 6.74e-04

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: 39.80  E-value: 6.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1052869657 131 RVLRDGDVIDLGNRRIQVLHTPGHSPGHMCFYEADRGYLFTGDLVYLDTLFA 182
Cdd:cd16289   121 RIVMDGEVVTLGGVTFTAHFTPGHTPGSTSWTWTDTRDGKPVRIAYADSLSA 172
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 14-75 7.45e-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: 39.17  E-value: 7.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1052869657  14 TSILSEYRHweeTHCYLLNGSERSLLIDTGLGICNIYDQVVRLTQKPVTAVATHIHWDHIGG 75
Cdd:cd16272     8 GAVPSLTRN---TSSYLLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGG 66
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 64-248 8.46e-04

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: 39.59  E-value: 8.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  64 VATHIHWDHIGGHryfpdfyaheAELDWLHGGF-PLSPAQIQDMVVDRCdlpeGYDVRTYSLFQGTP----TRVLRDGDV 138
Cdd:cd16311    65 LNSHGHIDHAGGL----------AELQRRSGALvAASPSAALDLASGEV----GPDDPQYHALPKYPpvkdMRLARDGGQ 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657 139 IDLGNRRIQVLHTPGHSPGHMCFY----EADRGYlftgDLVYLDTLFAYypSTDPEAYLLSLE-KVASLDVKRVFPGHHS 213
Cdd:cd16311   131 FNVGPVSLTAHATPGHTPGGLSWTwqscDGPRCL----NMVYADSQNAV--SRPGFKFSASSEyPNAVADLRRSFETLEK 204

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1052869657 214 LAVgpDILVRMRDAFRQLKSEGRLHHGSGTYAYGD 248
Cdd:cd16311   205 LPC--DVLISAHPEASQLWERLEASDRSARPALVD 237
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 26-97 3.30e-03

MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain; Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 37.48  E-value: 3.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052869657  26 THCYLLNGSERSLLIDTGLGICNIYDQVV-RLTQKPVTAVATHIHWDHIGGHRYFPDFYAHEAELDwLHGGFP 97
Cdd:cd07715    23 TSCVEVRAGGELLILDAGTGIRELGNELMkEGPPGEAHLLLSHTHWDHIQGFPFFAPAYDPGNRIH-IYGPHK 94
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 28-174 8.92e-03

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 37.09  E-value: 8.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  28 CYLLNGSERSLLIDTGLGICNIYDQVVRLTQKPVT---AVATHIHWDHIG-GHRYFPDF-----YAHEA--EL------D 90
Cdd:COG1236    16 CYLLETGGTRILIDCGLFQGGKERNWPPFPFRPSDvdaVVLTHAHLDHSGaLPLLVKEGfrgpiYATPAtaDLarillgD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052869657  91 WLHggfplspaqIQDMVVDRCDLPEGYDV-RTYSLFQGtptrvLRDGDVIDLGNRRIQvLHTPGHSPGHMCFYEADRGY- 168
Cdd:COG1236    96 SAK---------IQEEEAEAEPLYTEEDAeRALELFQT-----VDYGEPFEIGGVRVT-FHPAGHILGSAQVELEVGGKr 160


                  ....*..
gi 1052869657 169 -LFTGDL 174
Cdd:COG1236   161 iVFSGDY 167
 
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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