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Conserved domains on  [gi|1011722460|ref|WP_062566266|]
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MULTISPECIES: MBL fold metallo-hydrolase [Pseudoalteromonas]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 581040)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 2-209 1.31e-27

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


The actual alignment was detected with superfamily member cd07721:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 202  Bit Score: 105.00  E-value: 1.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460   2 HIHTLE-GYIQNIYLVEYPDKLMLLDGCCRADVDTVFDYItEQLKRPITDLKLIVVTHMHPDHAGGAHALRKLSGGKIAT 80
Cdd:cd07721     1 GVYQLPlLPPVNAYLIEDDDGLTLIDTGLPGSAKRILKAL-RELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  81 SNAPGQWYRGidgflmhltDIALAWWVAGRLNKKRHNLWYSRHLDADYYLATDATLPGFDDWQALHSPGHTDRDISLYHi 160
Cdd:cd07721    80 HEREAPYLEG---------EKPYPPPVRLGLLGLLSPLLPVKPVPVDRTLEDGDTLDLAGGLRVIHTPGHTPGHISLYL- 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1011722460 161 PSERIYIA-DLLVKVKGQLVPPFPVFY--PKLYLSSLLMLKALQPKRIMFAH 209
Cdd:cd07721   150 EEDGVLIAgDALVTVGGELVPPPPPFTwdMEEALESLRKLAELDPEVLAPGH 201
 
Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 2-209 1.31e-27

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: 105.00  E-value: 1.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460   2 HIHTLE-GYIQNIYLVEYPDKLMLLDGCCRADVDTVFDYItEQLKRPITDLKLIVVTHMHPDHAGGAHALRKLSGGKIAT 80
Cdd:cd07721     1 GVYQLPlLPPVNAYLIEDDDGLTLIDTGLPGSAKRILKAL-RELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  81 SNAPGQWYRGidgflmhltDIALAWWVAGRLNKKRHNLWYSRHLDADYYLATDATLPGFDDWQALHSPGHTDRDISLYHi 160
Cdd:cd07721    80 HEREAPYLEG---------EKPYPPPVRLGLLGLLSPLLPVKPVPVDRTLEDGDTLDLAGGLRVIHTPGHTPGHISLYL- 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1011722460 161 PSERIYIA-DLLVKVKGQLVPPFPVFY--PKLYLSSLLMLKALQPKRIMFAH 209
Cdd:cd07721   150 EEDGVLIAgDALVTVGGELVPPPPPFTwdMEEALESLRKLAELDPEVLAPGH 201
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 12-231 3.99e-22

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: 90.91  E-value: 3.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  12 NIYLVEYPDKLMLLD-GCCRADVDTVFDYITEQLKrpitDLKLIVVTHMHPDHAGGAHALRKLSGGKIatsnapgqwyrg 90
Cdd:COG0491    16 NSYLIVGGDGAVLIDtGLGPADAEALLAALAALGL----DIKAVLLTHLHPDHVGGLAALAEAFGAPV------------ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  91 idgfLMHLTDIALAwwvagrLNKKRHNLWYSRHLDADYYLATDATLP-GFDDWQALHSPGHTDRDISlYHIPSERIYIA- 168
Cdd:COG0491    80 ----YAHAAEAEAL------EAPAAGALFGREPVPPDRTLEDGDTLElGGPGLEVIHTPGHTPGHVS-FYVPDEKVLFTg 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1011722460 169 DLLVkVKGQLVPPFPVFYPKLYLSSLLMLKALQPKRIMFAHSNEVSIDDID-FEQILALVPEKP 231
Cdd:COG0491   149 DALF-SGGVGRPDLPDGDLAQWLASLERLLALPPDLVIPGHGPPTTAEAIDyLEELLAALGERA 211
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 12-209 1.19e-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: 1.19e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460   12 NIYLVEYPDKLMLLDgccrADVDTVFDYITEQLKRPITDLKLIVVTHMHPDHAGGAHALRKLSGGKIATSnapgqwyRGI 91
Cdd:smart00849   1 NSYLVRDDGGAILID----TGPGEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAP-------EGT 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460   92 DGFLMHLTDIALAWWVAGRLNKKRHNLWYSRHLDAdyylatdatlpGFDDWQALHSPGHTDRDISLYhIPSERI-YIADL 170
Cdd:smart00849  70 AELLKDLLALLGELGAEAEPAPPDRTLKDGDELDL-----------GGGELEVIHTPGHTPGSIVLY-LPEGKIlFTGDL 137

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1011722460  171 LV-KVKGQLVPPFPVFYPKLYLSSLLMLKALQPKRIMFAH 209
Cdd:smart00849 138 LFaGGDGRTLVDGGDAAASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
6-209 1.71e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 69.70  E-value: 1.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460   6 LEGYIQNIYLVEYPDKLMLLD-GCcraDVDTVFDYITEQLKRPITDLKLIVVTHMHPDHAGGAHALRKLSGGKIATsnAP 84
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDtGG---SAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIV--VA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  85 GQWYRGIDGFLMHLTDIALAWWVAGRLNKKRHNLWysrhldadyylATDATLPGFDDWQALHSPGHTDRDISLYhIPSER 164
Cdd:pfam00753  76 EEARELLDEELGLAASRLGLPGPPVVPLPPDVVLE-----------EGDGILGGGLGLLVTHGPGHGPGHVVVY-YGGGK 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1011722460 165 IYIA-DLL-------VKVKGQLVPPFPVFYPKLYLSSLLMLKALQPKRIMFAH 209
Cdd:pfam00753 144 VLFTgDLLfageigrLDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
 
Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 2-209 1.31e-27

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: 105.00  E-value: 1.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460   2 HIHTLE-GYIQNIYLVEYPDKLMLLDGCCRADVDTVFDYItEQLKRPITDLKLIVVTHMHPDHAGGAHALRKLSGGKIAT 80
Cdd:cd07721     1 GVYQLPlLPPVNAYLIEDDDGLTLIDTGLPGSAKRILKAL-RELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  81 SNAPGQWYRGidgflmhltDIALAWWVAGRLNKKRHNLWYSRHLDADYYLATDATLPGFDDWQALHSPGHTDRDISLYHi 160
Cdd:cd07721    80 HEREAPYLEG---------EKPYPPPVRLGLLGLLSPLLPVKPVPVDRTLEDGDTLDLAGGLRVIHTPGHTPGHISLYL- 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1011722460 161 PSERIYIA-DLLVKVKGQLVPPFPVFY--PKLYLSSLLMLKALQPKRIMFAH 209
Cdd:cd07721   150 EEDGVLIAgDALVTVGGELVPPPPPFTwdMEEALESLRKLAELDPEVLAPGH 201
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 12-231 3.99e-22

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: 90.91  E-value: 3.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  12 NIYLVEYPDKLMLLD-GCCRADVDTVFDYITEQLKrpitDLKLIVVTHMHPDHAGGAHALRKLSGGKIatsnapgqwyrg 90
Cdd:COG0491    16 NSYLIVGGDGAVLIDtGLGPADAEALLAALAALGL----DIKAVLLTHLHPDHVGGLAALAEAFGAPV------------ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  91 idgfLMHLTDIALAwwvagrLNKKRHNLWYSRHLDADYYLATDATLP-GFDDWQALHSPGHTDRDISlYHIPSERIYIA- 168
Cdd:COG0491    80 ----YAHAAEAEAL------EAPAAGALFGREPVPPDRTLEDGDTLElGGPGLEVIHTPGHTPGHVS-FYVPDEKVLFTg 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1011722460 169 DLLVkVKGQLVPPFPVFYPKLYLSSLLMLKALQPKRIMFAHSNEVSIDDID-FEQILALVPEKP 231
Cdd:COG0491   149 DALF-SGGVGRPDLPDGDLAQWLASLERLLALPPDLVIPGHGPPTTAEAIDyLEELLAALGERA 211
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 12-209 1.19e-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: 1.19e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460   12 NIYLVEYPDKLMLLDgccrADVDTVFDYITEQLKRPITDLKLIVVTHMHPDHAGGAHALRKLSGGKIATSnapgqwyRGI 91
Cdd:smart00849   1 NSYLVRDDGGAILID----TGPGEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAP-------EGT 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460   92 DGFLMHLTDIALAWWVAGRLNKKRHNLWYSRHLDAdyylatdatlpGFDDWQALHSPGHTDRDISLYhIPSERI-YIADL 170
Cdd:smart00849  70 AELLKDLLALLGELGAEAEPAPPDRTLKDGDELDL-----------GGGELEVIHTPGHTPGSIVLY-LPEGKIlFTGDL 137

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1011722460  171 LV-KVKGQLVPPFPVFYPKLYLSSLLMLKALQPKRIMFAH 209
Cdd:smart00849 138 LFaGGDGRTLVDGGDAAASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
6-209 1.71e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 69.70  E-value: 1.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460   6 LEGYIQNIYLVEYPDKLMLLD-GCcraDVDTVFDYITEQLKRPITDLKLIVVTHMHPDHAGGAHALRKLSGGKIATsnAP 84
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDtGG---SAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIV--VA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  85 GQWYRGIDGFLMHLTDIALAWWVAGRLNKKRHNLWysrhldadyylATDATLPGFDDWQALHSPGHTDRDISLYhIPSER 164
Cdd:pfam00753  76 EEARELLDEELGLAASRLGLPGPPVVPLPPDVVLE-----------EGDGILGGGLGLLVTHGPGHGPGHVVVY-YGGGK 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1011722460 165 IYIA-DLL-------VKVKGQLVPPFPVFYPKLYLSSLLMLKALQPKRIMFAH 209
Cdd:pfam00753 144 VLFTgDLLfageigrLDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 2-209 5.26e-13

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: 65.38  E-value: 5.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460   2 HIHTLEGYIQNIYLVEYPDKLMLLdgccradVDT---VFDYITEQLKRPITDLKLIVVTHMHPDHAGGAHALRKLSGGKI 78
Cdd:cd06262     1 KRLPVGPLQTNCYLVSDEEGEAIL-------IDPgagALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  79 AtsnapgqwyrgidgflMHLTDiaLAWWVAGRLNKKRHNLWYSRHLDADYYLATDATL-PGFDDWQALHSPGHTDRDISL 157
Cdd:cd06262    74 Y----------------IHEAD--AELLEDPELNLAFFGGGPLPPPEPDILLEDGDTIeLGGLELEVIHTPGHTPGSVCF 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1011722460 158 YhIPSERIYIA-DLLVKvKGQLVPPFPVFYPKLYLSSLLMLKALQPK--RIMFAH 209
Cdd:cd06262   136 Y-IEEEGVLFTgDTLFA-GSIGRTDLPGGDPEQLIESIKKLLLLLPDdtVVYPGH 188
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 14-209 2.06e-11

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: 61.74  E-value: 2.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  14 YLVEYPDKLMLLDGCCRADVDTVFDyITEQLKRPITDLKLIVVTHMHPDHAGGAHAL-RKLSGGKIATsnAPgqwyRGID 92
Cdd:cd07726    19 YLLDGEGRPALIDTGPSSSVPRLLA-ALEALGIAPEDVDYIILTHIHLDHAGGAGLLaEALPNAKVYV--HP----RGAR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  93 gflmHLTD----IALAWWVAGrlnKKRHNLWYS-RHLDADYYLATD--ATLP-GFDDWQALHSPGHTDRDISLYHIPSER 164
Cdd:cd07726    92 ----HLIDpsklWASARAVYG---DEADRLGGEiLPVPEERVIVLEdgETLDlGGRTLEVIDTPGHAPHHLSFLDEESDG 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1011722460 165 IYIAD-------LLVKVKGQLVPPfPVFYPKLYLSSLLMLKALQPKRIMFAH 209
Cdd:cd07726   165 LFTGDaagvrypELDVVGPPSTPP-PDFDPEAWLESLDRLLSLKPERIYLTH 215
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 12-214 1.74e-10

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: 58.46  E-value: 1.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  12 NIYLVEYPDKLMLLDG--CCRADVDTVFDYITEqLKRPITDLKLIVVTHMHPDHAGGAHALRKLSGGKIATSN----APG 85
Cdd:cd07725    16 NVYLLRDGDETTLIDTglATEEDAEALWEGLKE-LGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGATVYILDvtpvKDG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  86 QWYRGidgflmhltdialawwvagrlnkkrhnlwysrhldadyylatdatlpGFDDWQALHSPGHTDRDISLYHIPSERI 165
Cdd:cd07725    95 DKIDL-----------------------------------------------GGLRLKVIETPGHTPGHIVLYDEDRREL 127

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1011722460 166 YIAD-LLVKVKgqlvpPFPVFYPKL-------YLSSLLMLKALQPKRIMFAHSNEVS 214
Cdd:cd07725   128 FVGDaVLPKIT-----PNVSLWAVRvedplgaYLESLDKLEKLDVDLAYPGHGGPIK 179
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 4-209 3.36e-09

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: 54.85  E-value: 3.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460   4 HTLEGyiQNIYLVEYPDKLMLLD---GCcRADVDTVFDYITEQLKRPITDlklIVVTHMHPDHAGGAHALRKLSGG---- 76
Cdd:cd07722    13 FTLQG--TNTYLVGTGKRRILIDtgeGR-PSYIPLLKSVLDSEGNATISD---ILLTHWHHDHVGGLPDVLDLLRGpspr 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  77 --KIATSNAPGQWYRGIDGFlmhltdialawwvagrlnkkrHNLwysrhLDADYYLATDATLpgfddwQALHSPGHTDRD 154
Cdd:cd07722    87 vyKFPRPEEDEDPDEDGGDI---------------------HDL-----QDGQVFKVEGATL------RVIHTPGHTTDH 134

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1011722460 155 ISLYhIPSER-IYIADLlvkVKGQLVPPFPVFYPklYLSSLLMLKALQPKRIMFAH 209
Cdd:cd07722   135 VCFL-LEEENaLFTGDC---VLGHGTAVFEDLAA--YMASLKKLLSLGPGRIYPGH 184
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 33-209 5.48e-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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 54.49  E-value: 5.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  33 VDTVFDY-ITEQLK---RPITDL--KLIVVTHMHPDHAGGAHALRKLSGGKIATSNAPgqwyrgidgflMHLTDIALAWW 106
Cdd:cd16282    29 IDTGASPrLARALLaaiRKVTDKpvRYVVNTHYHGDHTLGNAAFADAGAPIIAHENTR-----------EELAARGEAYL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460 107 VAGrlnkkrhnlwysRHLDADYYLATDATLP--GFDDWQALH-----------SPGHTDRDISLyHIPSERIYIA-DLLV 172
Cdd:cd16282    98 ELM------------RRLGGDAMAGTELVLPdrTFDDGLTLDlggrtvelihlGPAHTPGDLVV-WLPEEGVLFAgDLVF 164

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1011722460 173 KvkgQLVPPFPVFYPKLYLSSLLMLKALQPKRIMFAH 209
Cdd:cd16282   165 N---GRIPFLPDGSLAGWIAALDRLLALDATVVVPGH 198
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 14-79 2.02e-08

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: 53.32  E-value: 2.02e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1011722460  14 YLVEYPDKLMLLDGCCRADVDTVFDYItEQLKRPITDLKLIVVTHMHPDHAGGAHALRKLSGGKIA 79
Cdd:cd07708    25 YLIVTPQGNILIDGDMEQNAPMIKANI-KKLGFKFSDTKLILISHAHFDHAGGSAEIKKQTGAKVM 89
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 14-151 4.27e-08

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: 52.22  E-value: 4.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  14 YLVEYPDKLMLLDGCCRADV--------------DTVFDYITEQLKR----PiTDLKLIVVTHMHPDHAGGAHALRklsg 75
Cdd:cd07729    35 YLIEHPEGTILVDTGFHPDAaddpgglelafppgVTEEQTLEEQLARlgldP-EDIDYVILSHLHFDHAGGLDLFP---- 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1011722460  76 gkiatsNAPgqwyrgidgFLMHLTDIALAWWVAGRLNKKRHNLWYSRHLDADYYLAT---DATLpgFDDWQALHSPGHT 151
Cdd:cd07729   110 ------NAT---------IIVQRAELEYATGPDPLAAGYYEDVLALDDDLPGGRVRLvdgDYDL--FPGVTLIPTPGHT 171
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 14-81 1.97e-07

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: 50.78  E-value: 1.97e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1011722460  14 YLVEYPDKLMLLDGCCRADVDTVFDYItEQLKRPITDLKLIVVTHMHPDHAGGAHALRKLSGGKIATS 81
Cdd:cd16288    25 YLITTPQGLILIDTGLESSAPMIKANI-RKLGFKPSDIKILLNSHAHLDHAGGLAALKKLTGAKLMAS 91
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 ...
 15-83 2.85e-07

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


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 50.04  E-value: 2.85e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1011722460  15 LVEYPDKLMLLDGCCRADVDTVFDYItEQLKRPITDLKLIVVTHMHPDHAGGAHALRKLSGGKIATSNA 83
Cdd:cd16290    26 LITSPQGLILIDGALPQSAPQIEANI-RALGFRLEDVKLILNSHAHFDHAGGIAALQRDSGATVAASPA 93
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 15-83 6.25e-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: 6.25e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1011722460  15 LVEYPDKLMLLDGCCRADVDTVFDYItEQLKRPITDLKLIVVTHMHPDHAGGAHALRKLSGGKIATSNA 83
Cdd:cd16315    26 LITGDDGHVLIDSGTEEAAPLVLANI-RKLGFDPKDVRWLLSSHEHFDHVGGLAALQRATGARVAASAA 93
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 3-173 2.19e-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: 46.96  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460   3 IHTLEGYIQNIYLVEYPDKlmllDGCCRadVDTVFDyiTEQLKRPI----TDLKLIVVTHMHPDHAGGAHALRKLSGGKI 78
Cdd:cd16322     3 PFTLGPLQENTYLVADEGG----GEAVL--VDPGDE--SEKLLARFgttgLTLLYILLTHAHFDHVGGVADLRRHPGAPV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  79 AtsnapgqwyrgidgflMHLTDIALawWVAGRLNKKRHNLWYSRHLDADYYLATDATLP-GFDDWQALHSPGHTDRDISL 157
Cdd:cd16322    75 Y----------------LHPDDLPL--YEAADLGAKAFGLGIEPLPPPDRLLEDGQTLTlGGLEFKVLHTPGHSPGHVCF 136

                         170
                  ....*....|....*..
gi 1011722460 158 YhIPSERIYIA-DLLVK 173
Cdd:cd16322   137 Y-VEEEGLLFSgDLLFQ 152
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 13-83 3.73e-06

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: 46.71  E-value: 3.73e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1011722460  13 IYLVEYPDKLMLLDGCCRADVDTVFDYItEQLKRPITDLKLIVVTHMHPDHAGGAHALRKLSGGKIATSNA 83
Cdd:cd16309    24 VFLITTPEGHILIDGAMPQSTPLIKDNI-KKLGFDVKDVKYLLNTHAHFDHAGGLAELKKATGAQLVASAA 93
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 15-86 4.27e-06

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


Pssm-ID: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 46.52  E-value: 4.27e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1011722460  15 LVEYPDKLMLLDGCCRADVDTVFDYItEQLKRPITDLKLIVVTHMHPDHAGGAHALRKLSGGKIATSNAPGQ 86
Cdd:cd16312    26 LVTSPQGHVLLDGALPQSAPLIIANI-EALGFRIEDVKLILNSHAHWDHAGGIAALQKASGATVAASAHGAQ 96
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 15-87 6.04e-06

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: 46.13  E-value: 6.04e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1011722460  15 LVEYPDKLMLLDGCCRADVDTVFDYItEQLKRPITDLKLIVVTHMHPDHAGGAHALRKLSGGKIATSNAPGQW 87
Cdd:cd16311    26 LVTSPQGHVLVDGGLPESAPKIIANI-EALGFRIEDVKLILNSHGHIDHAGGLAELQRRSGALVAASPSAALD 97
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 15-81 6.72e-06

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: 45.96  E-value: 6.72e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1011722460  15 LVEYPDKLMLLDGCCRADVDTVFDYITEQLKRPiTDLKLIVVTHMHPDHAGGAHALRKLSGGKIATS 81
Cdd:cd16289    26 LVKTPDGAVLLDGGMPQAADMLLDNMRALGVAP-GDLKLILHSHAHADHAGPLAALKRATGARVAAN 91
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 53-151 9.37e-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: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 44.79  E-value: 9.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  53 LIVVTHMHPDHAGGAHALRKLSGgkiatsnAPgqwyrgIDGFLMHLTDIALAWWVAGRLnkkrhnlwysrhldadyyLAT 132
Cdd:cd16278    56 AILVTHTHRDHSPGAARLAERTG-------AP------VRAFGPHRAGGQDTDFAPDRP------------------LAD 104

                          90       100
                  ....*....|....*....|.
gi 1011722460 133 DATLPGfDDW--QALHSPGHT 151
Cdd:cd16278   105 GEVIEG-GGLrlTVLHTPGHT 124
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 15-83 1.59e-05

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: 44.85  E-value: 1.59e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1011722460  15 LVEYPDKLMLLDGCCRADVDTVFDYItEQLKRPITDLKLIVVTHMHPDHAGGAHALRKLSGGKIATSNA 83
Cdd:cd16313    26 LITSPQGHILIDGGFPKSPEQIAASI-RQLGFKLEDVKYILSSHDHWDHAGGIAALQKLTGAQVLASPA 93
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 50-83 1.72e-05

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 44.88  E-value: 1.72e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1011722460  50 DLKLIVVTHMHPDHAGGAHALRKLSGGKIATSNA 83
Cdd:cd16280    61 DIKYILITHGHGDHYGGAAYLKDLYGAKVVMSEA 94
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 41-173 1.94e-05

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: 44.08  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  41 TEQLKRPITDLKL----IVVTHMHPDHAGGAHALRKLSGGKIATSnapgqwyrgidgflmHLTDialAWWVAGrLNK--K 114
Cdd:cd07737    33 ADKILQAIEDLGLtlkkILLTHGHLDHVGGAAELAEHYGVPIIGP---------------HKED---KFLLEN-LPEqsQ 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460 115 RHNLWYSRHLDADYYLATDATL-PGFDDWQALHSPGHTDRDISLYHIPSERIYIADLLVK 173
Cdd:cd07737    94 MFGFPPAEAFTPDRWLEEGDTVtVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFK 153
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 4-68 4.31e-05

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: 43.00  E-value: 4.31e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1011722460   4 HTLEGYIQNIYLVEYPDKLMLLD---GCCRADvdtvfDYIteqlkRPITDLKLIVV-THMHPDHAGGAH 68
Cdd:cd07712     2 FIEEDDRVNIYLLRGRDRALLIDtglGIGDLK-----EYV-----RTLTDLPLLVVaTHGHFDHIGGLH 60
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 15-84 6.98e-05

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 42.12  E-value: 6.98e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1011722460  15 LVEYPDKLMLLDGCCRADV--DTVFDYIteqLKRPITDLKLIVVTHMHPDHAGGA-HALRKLSGGKIATSNAP 84
Cdd:cd07731    14 LIQTPGKTILIDTGPRDSFgeDVVVPYL---KARGIKKLDYLILTHPDADHIGGLdAVLKNFPVKEVYMPGVT 83
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 51-209 7.52e-05

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 42.52  E-value: 7.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  51 LKLIVVTHMHPDHAGGAHALRKLSGGKIATSnapgqwyrGID-GFLMHlTDIALAWWVAGRLNKKRHNLWY-SRHLDADY 128
Cdd:cd07743    46 LKAIINTHSHADHIGGNAYLQKKTGCKVYAP--------KIEkAFIEN-PLLEPSYLGGAYPPKELRNKFLmAKPSKVDD 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460 129 YLATDATLPGFDDWQALHSPGHTDRDISLYhIPSERIYIADLLV------KVkgqlvpPFPVFY-PKLYLSSLLMLKALQ 201
Cdd:cd07743   117 IIEEGELELGGVGLEIIPLPGHSFGQIGIL-TPDGVLFAGDALFgeevleKY------GIPFLYdVEEQLETLEKLEELD 189


                  ....*...
gi 1011722460 202 PKRIMFAH 209
Cdd:cd07743   190 ADYYVPGH 197
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 14-81 1.29e-04

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


Pssm-ID: 293868  Cd Length: 252  Bit Score: 42.05  E-value: 1.29e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1011722460  14 YLVEYPDKLMLLDGCCRADVDTVFDYITeQLKRPITDLKLIVVTHMHPDHAGGAHALRKLSGGKIATS 81
Cdd:cd16310    25 YLITSNHGAILLDGGLEENAALIEQNIK-ALGFKLSDIKIIINTHAHYDHAGGLAQLKADTGAKLWAS 91
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 12-151 1.43e-04

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: 42.15  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  12 NIYLVEYPDKLMLLDGCCRADVDTVFDYITEQLK----RP--ITDlklIVVTHMHPDHAGGahALRKlsGGKIATSNApg 85
Cdd:cd07720    50 NAFLVRTGGRLILVDTGAGGLFGPTAGKLLANLAaagiDPedIDD---VLLTHLHPDHIGG--LVDA--GGKPVFPNA-- 120

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1011722460  86 QWYrgidgflMHLTDiaLAWWV------AGRLNKKRHNLWYSRHL----DADYYLATDATLPGFddwQALHSPGHT 151
Cdd:cd07720   121 EVH-------VSEAE--WDFWLddanaaKAPEGAKRFFDAARDRLrpyaAAGRFEDGDEVLPGI---TAVPAPGHT 184
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 14-77 2.61e-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: 40.71  E-value: 2.61e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  14 YLVEYPDKLMLLD---GCCRAdvdtvfdyiTEQLKRPITDLKLIVVTHMHPDHAGGAHAL---RKLSGGK 77
Cdd:cd16272    20 YLLETGGTRILLDcgeGTVYR---------LLKAGVDPDKLDAIFLSHFHLDHIGGLPTLlfaRRYGGRK 80
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 15-72 3.30e-04

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: 41.00  E-value: 3.30e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  15 LVEYPD-KLMLLDGCCRADVDTVFDYITEQLK-RPITDLKLIVVTHMHPDHAGGAHALRK 72
Cdd:COG2333    15 LIRTPDgKTILIDTGPRPSFDAGERVVLPYLRaLGIRRLDLLVLTHPDADHIGGLAAVLE 74
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 31-76 5.50e-04

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: 39.37  E-value: 5.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1011722460  31 ADVDTVFDYITEQLKRpitdLKLIVVTHMHPDHAGGAHALRKLSGG 76
Cdd:cd07723    28 GEAEPVLAALEKNGLT----LTAILTTHHHWDHTGGNAELKALFPD 69
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
14-77 1.67e-03

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 38.64  E-value: 1.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1011722460  14 YLVEYPDKLMLLD---GCcradvdtvfdyiTEQLKR---PITDLKLIVVTHMHPDHAGGAHAL---RKLSGGK 77
Cdd:COG1234    22 YLLEAGGERLLIDcgeGT------------QRQLLRaglDPRDIDAIFITHLHGDHIAGLPGLlstRSLAGRE 82
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 30-81 4.13e-03

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: 36.99  E-value: 4.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1011722460  30 RADVDTVFDYITEQlkrpitDLKLIVV--THMHPDHAGGAHALRKLSGGKIATS 81
Cdd:cd07724    32 RDSVDRYLDLAAEL------GLKITYVleTHVHADHVSGARELAERTGAPIVIG 79
NorV COG0426
Flavorubredoxin [Energy production and conversion];
12-95 5.95e-03

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 37.50  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  12 NIYLVEYpDKLMLLDGCCRADVDTVFDYITEQLkrPITDLKLIVVTHMHPDHAGGAHALRKL-SGGKIATSNapgQWYRG 90
Cdd:COG0426    35 NSYLIVD-EKTALIDTVGESFFEEFLENLSKVI--DPKKIDYIIVNHQEPDHSGSLPELLELaPNAKIVCSK---KAARF 108


                  ....*
gi 1011722460  91 IDGFL 95
Cdd:COG0426   109 LPHFY 113
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 12-100 6.21e-03

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: 37.08  E-value: 6.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011722460  12 NIYLVEYpDKLMLLDGCCRADVDTVFDYITEQLkrPITDLKLIVVTHMHPDHAGGAHALRKL-SGGKIATSNApgqWYRG 90
Cdd:cd07709    33 NSYLIKD-EKTALIDTVKEPFFDEFLENLEEVI--DPRKIDYIVVNHQEPDHSGSLPELLELaPNAKIVCSKK---AARF 106

                          90
                  ....*....|
gi 1011722460  91 IDGFLMHLTD 100
Cdd:cd07709   107 LKHFYPGIDE 116
 
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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