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Conserved domains on  [gi|22329127|ref|NP_195080|]
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metallo-beta-lactamase family protein [Arabidopsis thaliana]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 11210134)

uncharacterized MBL fold metallo-hydrolase containing a 4Fe-4S single cluster domain

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 147-324 3.84e-94

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: 278.31  E-value: 3.84e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 147 GVFHCGFHSKKSYGATSYLILHREGNILVDSPRYVEKLAGKIEMKGGVRYMFLTHRDDVADHKKWADRFKSTRILHSDDV 226
Cdd:cd07727   1 GVYYCGFHSEKSFGAASYLILRPEGNILVDSPRYSPPLAKRIEALGGIRYIFLTHRDDVADHAKWAERFGAKRIIHEDDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 227 EPSTSDVEL-KLEGSGPWSIYEDVELIHTPGHSEGSVCMFHKSLKALFTGDHVIMTESG--LSILEQYNHGSVPLQLENV 303
Cdd:cd07727  81 NAVTRPDEViVLWGGDPWELDPDLTLIPVPGHTRGSVVLLYKEKGVLFTGDHLAWSRRRgwLSAFRYVCWYSWPEQAESV 160

                       170       180
                ....*....|....*....|.
gi 22329127 304 EKLINLDFNWLIPGHGRRVHF 324
Cdd:cd07727 161 ERLADLDFEWVLPGHGRRVHF 181
Fer4_13 pfam13370
4Fe-4S single cluster domain of Ferredoxin I; Fer4_13 is a ferredoxin I from sulfate-reducing ...
 68-122 2.64e-21

4Fe-4S single cluster domain of Ferredoxin I; Fer4_13 is a ferredoxin I from sulfate-reducing bacteria. Chemical sequence analysis suggests that this characteriztic [4Fe-4S] cluster sulfur environment is widely distributed among ferredoxins.


:

Pssm-ID: 433153 [Multi-domain]  Cd Length: 58  Bit Score: 85.82  E-value: 2.64e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 22329127    68 VD-NTCIDCDTCRWMVPDLFTRVD--NMSAVTKQPTCKEERLNALQALLSCPTGSIRT 122
Cdd:pfam13370   1 VDeDTCIDCGTCRELAPEVFKYDDdgGASFVHDQPVNEEEEDLAEEALDSCPVEAIGT 58
 
Name Accession Description Interval E-value
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 147-324 3.84e-94

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: 278.31  E-value: 3.84e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 147 GVFHCGFHSKKSYGATSYLILHREGNILVDSPRYVEKLAGKIEMKGGVRYMFLTHRDDVADHKKWADRFKSTRILHSDDV 226
Cdd:cd07727   1 GVYYCGFHSEKSFGAASYLILRPEGNILVDSPRYSPPLAKRIEALGGIRYIFLTHRDDVADHAKWAERFGAKRIIHEDDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 227 EPSTSDVEL-KLEGSGPWSIYEDVELIHTPGHSEGSVCMFHKSLKALFTGDHVIMTESG--LSILEQYNHGSVPLQLENV 303
Cdd:cd07727  81 NAVTRPDEViVLWGGDPWELDPDLTLIPVPGHTRGSVVLLYKEKGVLFTGDHLAWSRRRgwLSAFRYVCWYSWPEQAESV 160

                       170       180
                ....*....|....*....|.
gi 22329127 304 EKLINLDFNWLIPGHGRRVHF 324
Cdd:cd07727 161 ERLADLDFEWVLPGHGRRVHF 181
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 160-341 2.62e-25

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: 101.69  E-value: 2.62e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 160 GATSYLILHREGNILVD---SPRYVEKLAGKIEMKGG-VRYMFLTHRDdvADH----KKWADRFKSTRILHSDDVEPSTS 231
Cdd:COG0491  14 GVNSYLIVGGDGAVLIDtglGPADAEALLAALAALGLdIKAVLLTHLH--PDHvgglAALAEAFGAPVYAHAAEAEALEA 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 232 DVELKLEGSGPWSIYE-------------DVELIHTPGHSEGSVCMFHKSLKALFTGDHVIMTESGLSILEqynHGSVPL 298
Cdd:COG0491  92 PAAGALFGREPVPPDRtledgdtlelggpGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLP---DGDLAQ 168

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 22329127 299 QLENVEKLINLDFNWLIPGHGRRVHFKDGDEKAKNLEALVQKH 341
Cdd:COG0491 169 WLASLERLLALPPDLVIPGHGPPTTAEAIDYLEELLAALGERA 211
Fer4_13 pfam13370
4Fe-4S single cluster domain of Ferredoxin I; Fer4_13 is a ferredoxin I from sulfate-reducing ...
 68-122 2.64e-21

4Fe-4S single cluster domain of Ferredoxin I; Fer4_13 is a ferredoxin I from sulfate-reducing bacteria. Chemical sequence analysis suggests that this characteriztic [4Fe-4S] cluster sulfur environment is widely distributed among ferredoxins.


Pssm-ID: 433153 [Multi-domain]  Cd Length: 58  Bit Score: 85.82  E-value: 2.64e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 22329127    68 VD-NTCIDCDTCRWMVPDLFTRVD--NMSAVTKQPTCKEERLNALQALLSCPTGSIRT 122
Cdd:pfam13370   1 VDeDTCIDCGTCRELAPEVFKYDDdgGASFVHDQPVNEEEEDLAEEALDSCPVEAIGT 58
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 162-318 3.70e-16

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: 75.28  E-value: 3.70e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127    162 TSYLILHREGNILVDS-PRYVEKLAGKIEMKGG--VRYMFLTHRDdvADH----KKWADRFKSTRILHSDDVEPSTSDVE 234
Cdd:smart00849   1 NSYLVRDDGGAILIDTgPGEAEDLLAELKKLGPkkIDAIILTHGH--PDHigglPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127    235 LKLEGSGPWSIYE----------------DVELIHTPGHSEGSVCMFHKSLKALFTGDHVIMTESGLSILEQYnHGSVPL 298
Cdd:smart00849  79 LLGELGAEAEPAPpdrtlkdgdeldlgggELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGG-DAAASD 157

                          170       180
                   ....*....|....*....|
gi 22329127    299 QLENVEKLINLDFNWLIPGH 318
Cdd:smart00849 158 ALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
163-318 6.51e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 69.70  E-value: 6.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127   163 SYLILHREGNILVDS----PRYVEKLAGKIEMKG-GVRYMFLTHRDdvADH----KKWADRFKSTRILHSDDVEPSTSDV 233
Cdd:pfam00753   8 SYLIEGGGGAVLIDTggsaEAALLLLLAALGLGPkDIDAVILTHGH--FDHigglGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127   234 ELKLEGSGPWSIYEDV---------------------ELIHTPGHSEGSVCMFHKSLKALFTGDHV-----IMTESGLSI 287
Cdd:pfam00753  86 LGLAASRLGLPGPPVVplppdvvleegdgilggglglLVTHGPGHGPGHVVVYYGGGKVLFTGDLLfageiGRLDLPLGG 165

                         170       180       190
                  ....*....|....*....|....*....|.
gi 22329127   288 LEQYNHGSVPLQLENVEKLINLDFNWLIPGH 318
Cdd:pfam00753 166 LLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
 
Name Accession Description Interval E-value
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 147-324 3.84e-94

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: 278.31  E-value: 3.84e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 147 GVFHCGFHSKKSYGATSYLILHREGNILVDSPRYVEKLAGKIEMKGGVRYMFLTHRDDVADHKKWADRFKSTRILHSDDV 226
Cdd:cd07727   1 GVYYCGFHSEKSFGAASYLILRPEGNILVDSPRYSPPLAKRIEALGGIRYIFLTHRDDVADHAKWAERFGAKRIIHEDDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 227 EPSTSDVEL-KLEGSGPWSIYEDVELIHTPGHSEGSVCMFHKSLKALFTGDHVIMTESG--LSILEQYNHGSVPLQLENV 303
Cdd:cd07727  81 NAVTRPDEViVLWGGDPWELDPDLTLIPVPGHTRGSVVLLYKEKGVLFTGDHLAWSRRRgwLSAFRYVCWYSWPEQAESV 160

                       170       180
                ....*....|....*....|.
gi 22329127 304 EKLINLDFNWLIPGHGRRVHF 324
Cdd:cd07727 161 ERLADLDFEWVLPGHGRRVHF 181
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 160-341 2.62e-25

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: 101.69  E-value: 2.62e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 160 GATSYLILHREGNILVD---SPRYVEKLAGKIEMKGG-VRYMFLTHRDdvADH----KKWADRFKSTRILHSDDVEPSTS 231
Cdd:COG0491  14 GVNSYLIVGGDGAVLIDtglGPADAEALLAALAALGLdIKAVLLTHLH--PDHvgglAALAEAFGAPVYAHAAEAEALEA 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 232 DVELKLEGSGPWSIYE-------------DVELIHTPGHSEGSVCMFHKSLKALFTGDHVIMTESGLSILEqynHGSVPL 298
Cdd:COG0491  92 PAAGALFGREPVPPDRtledgdtlelggpGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLP---DGDLAQ 168

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 22329127 299 QLENVEKLINLDFNWLIPGHGRRVHFKDGDEKAKNLEALVQKH 341
Cdd:COG0491 169 WLASLERLLALPPDLVIPGHGPPTTAEAIDYLEELLAALGERA 211
Fer4_13 pfam13370
4Fe-4S single cluster domain of Ferredoxin I; Fer4_13 is a ferredoxin I from sulfate-reducing ...
 68-122 2.64e-21

4Fe-4S single cluster domain of Ferredoxin I; Fer4_13 is a ferredoxin I from sulfate-reducing bacteria. Chemical sequence analysis suggests that this characteriztic [4Fe-4S] cluster sulfur environment is widely distributed among ferredoxins.


Pssm-ID: 433153 [Multi-domain]  Cd Length: 58  Bit Score: 85.82  E-value: 2.64e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 22329127    68 VD-NTCIDCDTCRWMVPDLFTRVD--NMSAVTKQPTCKEERLNALQALLSCPTGSIRT 122
Cdd:pfam13370   1 VDeDTCIDCGTCRELAPEVFKYDDdgGASFVHDQPVNEEEEDLAEEALDSCPVEAIGT 58
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 164-319 2.67e-18

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: 81.88  E-value: 2.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 164 YLILHREGNILVDS--PRYVEKLAGKIEMKGG----VRYMFLTHRDdvADH----KKWADRFKSTRILHSDD-------- 225
Cdd:cd07721  14 YLIEDDDGLTLIDTglPGSAKRILKALRELGLspkdIRRILLTHGH--IDHigslAALKEAPGAPVYAHEREapylegek 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 226 -------------------VEPSTSDVELK----LEGSGPWSIyedvelIHTPGHSEGSVCMFHKSLKALFTGDhVIMTE 282
Cdd:cd07721  92 pypppvrlgllgllspllpVKPVPVDRTLEdgdtLDLAGGLRV------IHTPGHTPGHISLYLEEDGVLIAGD-ALVTV 164

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 22329127 283 SGLSIL--EQYNHgSVPLQLENVEKLINLDFNWLIPGHG 319
Cdd:cd07721 165 GGELVPppPPFTW-DMEEALESLRKLAELDPEVLAPGHG 202
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 162-318 3.70e-16

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: 75.28  E-value: 3.70e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127    162 TSYLILHREGNILVDS-PRYVEKLAGKIEMKGG--VRYMFLTHRDdvADH----KKWADRFKSTRILHSDDVEPSTSDVE 234
Cdd:smart00849   1 NSYLVRDDGGAILIDTgPGEAEDLLAELKKLGPkkIDAIILTHGH--PDHigglPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127    235 LKLEGSGPWSIYE----------------DVELIHTPGHSEGSVCMFHKSLKALFTGDHVIMTESGLSILEQYnHGSVPL 298
Cdd:smart00849  79 LLGELGAEAEPAPpdrtlkdgdeldlgggELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGG-DAAASD 157

                          170       180
                   ....*....|....*....|
gi 22329127    299 QLENVEKLINLDFNWLIPGH 318
Cdd:smart00849 158 ALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
163-318 6.51e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 69.70  E-value: 6.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127   163 SYLILHREGNILVDS----PRYVEKLAGKIEMKG-GVRYMFLTHRDdvADH----KKWADRFKSTRILHSDDVEPSTSDV 233
Cdd:pfam00753   8 SYLIEGGGGAVLIDTggsaEAALLLLLAALGLGPkDIDAVILTHGH--FDHigglGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127   234 ELKLEGSGPWSIYEDV---------------------ELIHTPGHSEGSVCMFHKSLKALFTGDHV-----IMTESGLSI 287
Cdd:pfam00753  86 LGLAASRLGLPGPPVVplppdvvleegdgilggglglLVTHGPGHGPGHVVVYYGGGKVLFTGDLLfageiGRLDLPLGG 165

                         170       180       190
                  ....*....|....*....|....*....|.
gi 22329127   288 LEQYNHGSVPLQLENVEKLINLDFNWLIPGH 318
Cdd:pfam00753 166 LLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 163-322 1.93e-13

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: 68.09  E-value: 1.93e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 163 SYLILHREGNILVDS--PRY------VEKLAGKIEMKGGVRYMFLTHRDdvADHKKWADRF--KSTRILHSDDVEPST-- 230
Cdd:cd07725  17 VYLLRDGDETTLIDTglATEedaealWEGLKELGLKPSDIDRVLLTHHH--PDHIGLAGKLqeKSGATVYILDVTPVKdg 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 231 SDVELkleGSGPWSIyedvelIHTPGHSEGSVCMFHKSLKALFTGDHV-IMTESGLSILEQYNHGSVPLQLENVEKLINL 309
Cdd:cd07725  95 DKIDL---GGLRLKV------IETPGHTPGHIVLYDEDRRELFVGDAVlPKITPNVSLWAVRVEDPLGAYLESLDKLEKL 165

                       170
                ....*....|...
gi 22329127 310 DFNWLIPGHGRRV 322
Cdd:cd07725 166 DVDLAYPGHGGPI 178
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 160-319 2.95e-12

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 64.43  E-value: 2.95e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 160 GATSYLILHREGNILVD----SPRYVEKLAGKIEmKGGVRYMFLTHRDdvADHKKWADRFKS----------TRILHSDD 225
Cdd:cd16278  17 GTNTYLLGAPDGVVVIDpgpdDPAHLDALLAALG-GGRVSAILVTHTH--RDHSPGAARLAErtgapvrafgPHRAGGQD 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 226 VEPStSDVELK----LEGSGpWSIyedvELIHTPGHSEGSVCMFHKSLKALFTGDHViMTESGLSI------LEQYnhgs 295
Cdd:cd16278  94 TDFA-PDRPLAdgevIEGGG-LRL----TVLHTPGHTSDHLCFALEDEGALFTGDHV-MGWSTTVIappdgdLGDY---- 162

                       170       180
                ....*....|....*....|....
gi 22329127 296 vplqLENVEKLINLDFNWLIPGHG 319
Cdd:cd16278 163 ----LASLERLLALDDRLLLPGHG 182
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 159-318 4.08e-12

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: 64.23  E-value: 4.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 159 YGATSYLILHREG-NILVD-SPRYVEKLAGKI-EMKGGVRYMFLTHRDdvADH----KKWADRFKSTRILHSDDVEPSTS 231
Cdd:cd06262   8 LQTNCYLVSDEEGeAILIDpGAGALEKILEAIeELGLKIKAILLTHGH--FDHigglAELKEAPGAPVYIHEADAELLED 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 232 DVELKLEGSGPWSIYE-----------------DVELIHTPGHSEGSVCMFHKSLKALFTGDhVIMTES-GLSILEqynH 293
Cdd:cd06262  86 PELNLAFFGGGPLPPPepdilledgdtielgglELEVIHTPGHTPGSVCFYIEEEGVLFTGD-TLFAGSiGRTDLP---G 161

                       170       180
                ....*....|....*....|....*..
gi 22329127 294 GSVPLQLENVEKLINLDFN--WLIPGH 318
Cdd:cd06262 162 GDPEQLIESIKKLLLLLPDdtVVYPGH 188
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 161-320 5.32e-10

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


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 57.98  E-value: 5.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 161 ATSYLILHREGNILVD--SPRYVEKLAGKIEMKG----GVRYMFLTHRDdvADHKKWADRFKSTRILHSDDVEPSTSDVE 234
Cdd:cd07711  22 STVTLIKDGGKNILVDtgTPWDRDLLLKALAEHGlspeDIDYVVLTHGH--PDHIGNLNLFPNATVIVGWDICGDSYDDH 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 235 LkLEGSGPWSIYEDVELIHTPGHSEGSVcmfhkSL--------KALFTGDhVIMTESGL--SILEQYNHGSVPLQLENVE 304
Cdd:cd07711 100 S-LEEGDGYEIDENVEVIPTPGHTPEDV-----SVlvetekkgTVAVAGD-LFEREEDLedPILWDPLSEDPELQEESRK 172

                       170
                ....*....|....*.
gi 22329127 305 KLINLdFNWLIPGHGR 320
Cdd:cd07711 173 RILAL-ADWIIPGHGP 187
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 159-318 9.93e-09

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: 54.17  E-value: 9.93e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 159 YGATSYLILHREGNILVDS-------PRYVEKLAGKIEMkggvryMFLTHR-----------DDVADHKKWADRFKStri 220
Cdd:cd07712   7 DRVNIYLLRGRDRALLIDTglgigdlKEYVRTLTDLPLL------VVATHGhfdhigglhefEEVYVHPADAEILAA--- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 221 lHSDDVEPSTSDVELKLEGSGPWSIYED----------VELIHTPGHSEGSVCMFHKSLKALFTGDHVImteSGlSILEQ 290
Cdd:cd07712  78 -PDNFETLTWDAATYSVPPAGPTLPLRDgdvidlgdrqLEVIHTPGHTPGSIALLDRANRLLFSGDVVY---DG-PLIMD 152

                       170       180       190
                ....*....|....*....|....*....|
gi 22329127 291 YNHGSVPLQLENVEKLINL--DFNWLIPGH 318
Cdd:cd07712 153 LPHSDLDDYLASLEKLSKLpdEFDKVLPGH 182
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 160-319 2.74e-08

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 53.34  E-value: 2.74e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 160 GATSYLILHREGNILVD---SPRYVEKLAGKIEMKGG--VRYMFLTH------------RDDVAD---HKKWADRFKSTR 219
Cdd:cd16282  14 ISNIGFIVGDDGVVVIDtgaSPRLARALLAAIRKVTDkpVRYVVNTHyhgdhtlgnaafADAGAPiiaHENTREELAARG 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 220 ILHSDDVEPSTSDVELKLEGSGPWSIYED----------VELIHT-PGHSEGSVCMFHKSLKALFTGDhvIMTESGLSIL 288
Cdd:cd16282  94 EAYLELMRRLGGDAMAGTELVLPDRTFDDgltldlggrtVELIHLgPAHTPGDLVVWLPEEGVLFAGD--LVFNGRIPFL 171

                       170       180       190
                ....*....|....*....|....*....|.
gi 22329127 289 EqynHGSVPLQLENVEKLINLDFNWLIPGHG 319
Cdd:cd16282 172 P---DGSLAGWIAALDRLLALDATVVVPGHG 199
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 160-319 3.17e-07

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: 49.84  E-value: 3.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 160 GATSYLILHREGNILVDS----PRYVE--KLAGKIEMKGGVRYMFLTHR--------DDVADHKKWADR--FKSTRILHS 223
Cdd:cd07722  17 GTNTYLVGTGKRRILIDTgegrPSYIPllKSVLDSEGNATISDILLTHWhhdhvgglPDVLDLLRGPSPrvYKFPRPEED 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 224 DDVEPSTSDVELKLEGSgpwsIY--EDVEL--IHTPGHSEGSVCMFHKSLKALFTGDHVImtesglsileqyNHGSVPLQ 299
Cdd:cd07722  97 EDPDEDGGDIHDLQDGQ----VFkvEGATLrvIHTPGHTTDHVCFLLEEENALFTGDCVL------------GHGTAVFE 160

                       170       180
                ....*....|....*....|....*
gi 22329127 300 -----LENVEKLINLDFNWLIPGHG 319
Cdd:cd07722 161 dlaayMASLKKLLSLGPGRIYPGHG 185
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 163-276 9.95e-07

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: 48.23  E-value: 9.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 163 SYLILHREGN--ILVDSP------RYVEKLAGKIEmkggvrYMFLTHRDdvADH----KKWADRFKSTRIL-HSDDVEPS 229
Cdd:cd07723  11 IYLIVDEATGeaAVVDPGeaepvlAALEKNGLTLT------AILTTHHH--WDHtggnAELKALFPDAPVYgPAEDRIPG 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 22329127 230 TSDV-----ELKLEGSgpwsiyeDVELIHTPGHSEGSVCMFHKSLKALFTGD 276
Cdd:cd07723  83 LDHPvkdgdEIKLGGL-------EVKVLHTPGHTLGHICYYVPDEPALFTGD 127
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 227-318 3.60e-06

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 47.14  E-value: 3.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 227 EPSTSDVELKlegSGPWSIYE-DVELIHTPGHSEGSVCMFHKSlKALFTGDHVImtesGLSILEQYN---HGSVPLQLEN 302
Cdd:cd07743 110 KPSKVDDIIE---EGELELGGvGLEIIPLPGHSFGQIGILTPD-GVLFAGDALF----GEEVLEKYGipfLYDVEEQLET 181

                        90
                ....*....|....*.
gi 22329127 303 VEKLINLDFNWLIPGH 318
Cdd:cd07743 182 LEKLEELDADYYVPGH 197
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 163-319 4.12e-06

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: 46.62  E-value: 4.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 163 SYLILHREGN--ILVDS-----PRYVEkLAGKIEMKggVRYMFLTHRDdvADH----KKWADRFKStRILHSDDVEPSTS 231
Cdd:cd07724  14 SYLVGDPETGeaAVIDPvrdsvDRYLD-LAAELGLK--ITYVLETHVH--ADHvsgaRELAERTGA-PIVIGEGAPASFF 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 232 DVELKlEGSgpwSIY---EDVELIHTPGHSEGSVCMFHKSLKALFTGDHVIMTESGLSILEQYNHGSVPLQLENVEKLI- 307
Cdd:cd07724  88 DRLLK-DGD---VLElgnLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPGEAEGLARQLYDSLQRKLl 163

                       170
                ....*....|...
gi 22329127 308 NLDFNWLI-PGHG 319
Cdd:cd07724 164 LLPDETLVyPGHD 176
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 164-319 6.49e-06

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: 46.57  E-value: 6.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 164 YLILHREGN--ILVDSPRYVEKLAGKIEMKGG-VRYMFLTHR--DDV---ADHKKWADrfkSTRILHSDD---------- 225
Cdd:cd16322  14 YLVADEGGGeaVLVDPGDESEKLLARFGTTGLtLLYILLTHAhfDHVggvADLRRHPG---APVYLHPDDlplyeaadlg 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 226 -------VEPSTsDVELKLEGSGPWSIYE-DVELIHTPGHSEGSVCMFHKSLKALFTGDHVIMTESGLSILeqynHGSVP 297
Cdd:cd16322  91 akafglgIEPLP-PPDRLLEDGQTLTLGGlEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRTDL----PGGDP 165

                       170       180
                ....*....|....*....|....
gi 22329127 298 LQL-ENVEKLINL-DFNWLIPGHG 319
Cdd:cd16322 166 KAMaASLRRLLTLpDETRVFPGHG 189
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 250-318 2.54e-04

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: 41.38  E-value: 2.54e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22329127 250 ELIHTPGHSEGSVCMFHKSLKALFTGDhVIMTES-GLSILEQYNHGsvplQLENV--EKLINL--DFNwLIPGH 318
Cdd:cd07737 123 EVLHCPGHTPGHVVFFNRESKLAIVGD-VLFKGSiGRTDFPGGNHA----QLIASikEKLLPLgdDVT-FIPGH 190
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 169-322 1.47e-03

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 39.11  E-value: 1.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 169 REGNILVDSPRYV-EKLAGKIEM--KGGVRYMFLTHrdDVADHKKWADRFKS---TRILHSDDVEpstsdvelKLEGSG- 241
Cdd:cd16276  18 DKGVIVVDAPPSLgENLLAAIRKvtDKPVTHVVYSH--NHADHIGGASIFKDegaTIIAHEATAE--------LLKRNPd 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329127 242 -----PWSIYED----------VELI-HTPGHSEGSVCMFHKSLKALFTGDHVimtesglsileqyNHGSVPLQ------ 299
Cdd:cd16276  88 pkrpvPTVTFDDeytlevggqtLELSyFGPNHGPGNIVIYLPKQKVLMAVDLI-------------NPGWVPFFnfagse 154

                       170       180
                ....*....|....*....|....*...
gi 22329127 300 -----LENVEKLINLDFNWLIPGHGRRV 322
Cdd:cd16276 155 dipgyIEALDELLEYDFDTFVGGHGNRL 182
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 249-276 2.06e-03

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: 38.67  E-value: 2.06e-03
                        10        20
                ....*....|....*....|....*...
gi 22329127 249 VELIHTPGHSEGSVCmFHKSlKALFTGD 276
Cdd:cd16275 108 ITCLLTPGHTPGSMC-YLLG-DSLFTGD 133
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 249-318 7.80e-03

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: 37.09  E-value: 7.80e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22329127 249 VELIHTPGHSEGSVCMFHKSLKALFTGDHVimtesGLSILEQYNHGSVP---------LQLENVEKLINLDFNWLIPGH 318
Cdd:cd07726 142 LEVIDTPGHAPHHLSFLDEESDGLFTGDAA-----GVRYPELDVVGPPStpppdfdpeAWLESLDRLLSLKPERIYLTH 215
 
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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