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Conserved domains on  [gi|1537764618|gb|AZN42380|]
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MBL fold metallo-hydrolase [Paenibacillus albus]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869930)

uncharacterized MBL fold metallo-hydrolase similar to Bacillus subtilis YflN

Gene Ontology:  GO:0016787
PubMed:  17597585

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 21-206 3.25e-69

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: 210.93  E-value: 3.25e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  21 PFVIYPTVLWDEQEIILVDTGLPGQVDIIRAAFDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIAHEVAVP 100
Cdd:cd07721     8 LPPVNAYLIEDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPG--APVYAHEREAP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 101 YITGQEPLVKSKSLA-----------EPVHVDVVLHDGDILPYAGGIQVVFTPGHTPDHTSLYHIPSQTLIAGDALTAQD 169
Cdd:cd07721    86 YLEGEKPYPPPVRLGllgllspllpvKPVPVDRTLEDGDTLDLAGGLRVIHTPGHTPGHISLYLEEDGVLIAGDALVTVG 165

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1537764618 170 GVLQSFNPAFTPDPKTAIQSIAKLQALELSSIIAYHG 206
Cdd:cd07721   166 GELVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
 
Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 21-206 3.25e-69

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: 210.93  E-value: 3.25e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  21 PFVIYPTVLWDEQEIILVDTGLPGQVDIIRAAFDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIAHEVAVP 100
Cdd:cd07721     8 LPPVNAYLIEDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPG--APVYAHEREAP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 101 YITGQEPLVKSKSLA-----------EPVHVDVVLHDGDILPYAGGIQVVFTPGHTPDHTSLYHIPSQTLIAGDALTAQD 169
Cdd:cd07721    86 YLEGEKPYPPPVRLGllgllspllpvKPVPVDRTLEDGDTLDLAGGLRVIHTPGHTPGHISLYLEEDGVLIAGDALVTVG 165

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1537764618 170 GVLQSFNPAFTPDPKTAIQSIAKLQALELSSIIAYHG 206
Cdd:cd07721   166 GELVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 13-223 8.04e-38

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 130.97  E-value: 8.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  13 ISMSIQGNPFVIYPTVLWDEQEIILVDTGL-PGQVDIIRAAFDKASipfEKLTKIIITHQDRDHIGSLPELKRLLGdqVQ 91
Cdd:COG0491     4 LPGGTPGAGLGVNSYLIVGGDGAVLIDTGLgPADAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFG--AP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  92 VIAHEVAVPYITGQEPlvKSKSLAEPVHVDVVLHDGDILPYAG-GIQVVFTPGHTPDHTSLYHIPSQTLIAGDALTAQDG 170
Cdd:COG0491    79 VYAHAAEAEALEAPAA--GALFGREPVPPDRTLEDGDTLELGGpGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGV 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1537764618 171 vlqSFNPAFTPDPKTAIQSIAKLQALELSSIIAYHGGVCTDNLQERLQAIISA 223
Cdd:COG0491   157 ---GRPDLPDGDLAQWLASLERLLALPPDLVIPGHGPPTTAEAIDYLEELLAA 206
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 27-205 4.47e-27

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: 102.25  E-value: 4.47e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618   27 TVLWDEQEIILVDTGLPGQVDIIRAAfdkASIPFEKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIAHEVAVPYITGQE 106
Cdd:smart00849   3 YLVRDDGGAILIDTGPGEAEDLLAEL---KKLGPKKIDAIILTHGHPDHIGGLPELLEAPG--APVYAPEGTAELLKDLL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  107 PL-VKSKSLAEPVHVDVVLHDGDILPYAG-GIQVVFTPGHTPDHTSLYHIPSQTLIAGDALTaQDGVLQSFNPAFTPDPK 184
Cdd:smart00849  78 ALlGELGAEAEPAPPDRTLKDGDELDLGGgELEVIHTPGHTPGSIVLYLPEGKILFTGDLLF-AGGDGRTLVDGGDAAAS 156

                          170       180
                   ....*....|....*....|.
gi 1537764618  185 TAIQSIAKLQALELSSIIAYH 205
Cdd:smart00849 157 DALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
19-205 7.38e-17

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 75.87  E-value: 7.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  19 GNPFVIYPTVLWDEQEIILVDTGLPGQVDIIRAAFDKASIPfEKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIAHEVA 98
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLGP-KDIDAVILTHGHFDHIGGLGELAEATD--VPVIVVAEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  99 VPYITGQEPLVKSKSLA-------EPVHVDVVLHDGDILPYAGGIQVVFTPGHTPDHTSLYHIPSQTLIAGDALTAQ--- 168
Cdd:pfam00753  78 ARELLDEELGLAASRLGlpgppvvPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGeig 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1537764618 169 --DGVLQSFNPAFTPDPKTAIQSIAKLQALELSSIIAYH 205
Cdd:pfam00753 158 rlDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 38-196 1.41e-11

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 62.94  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  38 VDTGLPGQVDIIRAA--FDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIAHEVAVPYITGqeplvksksla 115
Cdd:PLN02398   95 EDTGTVGVVDPSEAVpvIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYG--AKVIGSAVDKDRIPG----------- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 116 epvhVDVVLHDGDILPYAGG-IQVVFTPGHTPDHTSLYHIPSQTLIAGDALTAqdgvlQSFNPAFTPDPKTAIQSIAKLQ 194
Cdd:PLN02398  162 ----IDIVLKDGDKWMFAGHeVLVMETPGHTRGHISFYFPGSGAIFTGDTLFS-----LSCGKLFEGTPEQMLSSLQKII 232


                  ..
gi 1537764618 195 AL 196
Cdd:PLN02398  233 SL 234
 
Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 21-206 3.25e-69

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: 210.93  E-value: 3.25e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  21 PFVIYPTVLWDEQEIILVDTGLPGQVDIIRAAFDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIAHEVAVP 100
Cdd:cd07721     8 LPPVNAYLIEDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPG--APVYAHEREAP 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 101 YITGQEPLVKSKSLA-----------EPVHVDVVLHDGDILPYAGGIQVVFTPGHTPDHTSLYHIPSQTLIAGDALTAQD 169
Cdd:cd07721    86 YLEGEKPYPPPVRLGllgllspllpvKPVPVDRTLEDGDTLDLAGGLRVIHTPGHTPGHISLYLEEDGVLIAGDALVTVG 165

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1537764618 170 GVLQSFNPAFTPDPKTAIQSIAKLQALELSSIIAYHG 206
Cdd:cd07721   166 GELVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 13-223 8.04e-38

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 130.97  E-value: 8.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  13 ISMSIQGNPFVIYPTVLWDEQEIILVDTGL-PGQVDIIRAAFDKASipfEKLTKIIITHQDRDHIGSLPELKRLLGdqVQ 91
Cdd:COG0491     4 LPGGTPGAGLGVNSYLIVGGDGAVLIDTGLgPADAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFG--AP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  92 VIAHEVAVPYITGQEPlvKSKSLAEPVHVDVVLHDGDILPYAG-GIQVVFTPGHTPDHTSLYHIPSQTLIAGDALTAQDG 170
Cdd:COG0491    79 VYAHAAEAEALEAPAA--GALFGREPVPPDRTLEDGDTLELGGpGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGV 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1537764618 171 vlqSFNPAFTPDPKTAIQSIAKLQALELSSIIAYHGGVCTDNLQERLQAIISA 223
Cdd:COG0491   157 ---GRPDLPDGDLAQWLASLERLLALPPDLVIPGHGPPTTAEAIDYLEELLAA 206
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 27-205 4.47e-27

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: 102.25  E-value: 4.47e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618   27 TVLWDEQEIILVDTGLPGQVDIIRAAfdkASIPFEKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIAHEVAVPYITGQE 106
Cdd:smart00849   3 YLVRDDGGAILIDTGPGEAEDLLAEL---KKLGPKKIDAIILTHGHPDHIGGLPELLEAPG--APVYAPEGTAELLKDLL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  107 PL-VKSKSLAEPVHVDVVLHDGDILPYAG-GIQVVFTPGHTPDHTSLYHIPSQTLIAGDALTaQDGVLQSFNPAFTPDPK 184
Cdd:smart00849  78 ALlGELGAEAEPAPPDRTLKDGDELDLGGgELEVIHTPGHTPGSIVLYLPEGKILFTGDLLF-AGGDGRTLVDGGDAAAS 156

                          170       180
                   ....*....|....*....|.
gi 1537764618  185 TAIQSIAKLQALELSSIIAYH 205
Cdd:smart00849 157 DALESLLKLLKLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 17-193 4.86e-24

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: 94.66  E-value: 4.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  17 IQGNPFVIYPtvlwDEQEIILVDTGLPGQVDIIRAAFDKasipFEKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIAHE 96
Cdd:cd06262     8 LQTNCYLVSD----EEGEAILIDPGAGALEKILEAIEEL----GLKIKAILLTHGHFDHIGGLAELKEAPG--APVYIHE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  97 VAVPYITGQEPLVKS--KSLAEPVHVDVVLHDGDILPYAG-GIQVVFTPGHTPDHTSLYHIPSQTLIAGDALtAQDGVLQ 173
Cdd:cd06262    78 ADAELLEDPELNLAFfgGGPLPPPEPDILLEDGDTIELGGlELEVIHTPGHTPGSVCFYIEEEGVLFTGDTL-FAGSIGR 156

                         170       180
                  ....*....|....*....|
gi 1537764618 174 SFNPafTPDPKTAIQSIAKL 193
Cdd:cd06262   157 TDLP--GGDPEQLIESIKKL 174
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 18-201 1.04e-21

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 89.09  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  18 QGNPFVIYPTVLWDEQEIILVDTGLPGQVDIIRAAFDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLgDQVQVIAHEV 97
Cdd:cd07726    10 LGFPGRIASYLLDGEGRPALIDTGPSSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLAEAL-PNAKVYVHPR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  98 AVPYITGQEPLVKS----------KSLAEPVHVD----VVLHDGDILPYAG-GIQVVFTPGHTPDHTSLYHIPSQTLIAG 162
Cdd:cd07726    89 GARHLIDPSKLWASaravygdeadRLGGEILPVPeervIVLEDGETLDLGGrTLEVIDTPGHAPHHLSFLDEESDGLFTG 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1537764618 163 DALTAQDGVLQSFNPAFTP----DPKTAIQSIAKLQALELSSI 201
Cdd:cd07726   169 DAAGVRYPELDVVGPPSTPppdfDPEAWLESLDRLLSLKPERI 211
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 31-205 9.64e-19

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 80.65  E-value: 9.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  31 DEQEIILVDTGLPGQVD-IIRAAFDKASIpfeKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIAHEVAVPYItgQEPL- 108
Cdd:cd07743    16 GDKEALLIDSGLDEDAGrKIRKILEELGW---KLKAIINTHSHADHIGGNAYLQKKTG--CKVYAPKIEKAFI--ENPLl 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 109 -------------VKSKSL-AEPVHVDVVLHDGDILPYAGGIQVVFTPGHTPDHTSLYhIPSQTLIAGDALTAQDgVLQS 174
Cdd:cd07743    89 epsylggayppkeLRNKFLmAKPSKVDDIIEEGELELGGVGLEIIPLPGHSFGQIGIL-TPDGVLFAGDALFGEE-VLEK 166

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1537764618 175 FNPAFTPDPKTAIQSIAKLQALELSSIIAYH 205
Cdd:cd07743   167 YGIPFLYDVEEQLETLEKLEELDADYYVPGH 197
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
19-205 7.38e-17

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 75.87  E-value: 7.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  19 GNPFVIYPTVLWDEQEIILVDTGLPGQVDIIRAAFDKASIPfEKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIAHEVA 98
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLGP-KDIDAVILTHGHFDHIGGLGELAEATD--VPVIVVAEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  99 VPYITGQEPLVKSKSLA-------EPVHVDVVLHDGDILPYAGGIQVVFTPGHTPDHTSLYHIPSQTLIAGDALTAQ--- 168
Cdd:pfam00753  78 ARELLDEELGLAASRLGlpgppvvPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGeig 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1537764618 169 --DGVLQSFNPAFTPDPKTAIQSIAKLQALELSSIIAYH 205
Cdd:pfam00753 158 rlDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 28-211 1.72e-16

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: 74.26  E-value: 1.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  28 VLWDEQEIILVDTGLPGQVDI--IRAAFDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLGdqvqviahevAVPYITGQ 105
Cdd:cd07725    19 LLRDGDETTLIDTGLATEEDAeaLWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSG----------ATVYILDV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 106 EPLvkskslaepvhvdvvlHDGDILPYAG-GIQVVFTPGHTPDHTSLYHIPSQTLIAGDALTAQDGVLQSFNPAFTPDPK 184
Cdd:cd07725    89 TPV----------------KDGDKIDLGGlRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLPKITPNVSLWAVRVEDPL 152

                         170       180
                  ....*....|....*....|....*...
gi 1537764618 185 TA-IQSIAKLQALELSSIIAYHGGVCTD 211
Cdd:cd07725   153 GAyLESLDKLEKLDVDLAYPGHGGPIKD 180
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 24-165 1.80e-15

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: 71.34  E-value: 1.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  24 IYptVLWDE--QEIILVDtglPGQVDIIRAAFDKASIpfeKLTKIIITHQDRDHIGSLPELKRLLGDqVQVIAH-EVAVP 100
Cdd:cd07723    11 IY--LIVDEatGEAAVVD---PGEAEPVLAALEKNGL---TLTAILTTHHHWDHTGGNAELKALFPD-APVYGPaEDRIP 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1537764618 101 yitgqeplvkskslaepvHVDVVLHDGDILPYAGG-IQVVFTPGHTPDHTSlYHIPSQT-LIAGDAL 165
Cdd:cd07723    82 ------------------GLDHPVKDGDEIKLGGLeVKVLHTPGHTLGHIC-YYVPDEPaLFTGDTL 129
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 36-208 1.01e-14

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: 70.81  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  36 ILVDTGLPGQVDIIRAAFDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLGDQVQVIAHEVAVPYITG-QEPLVKSKSL 114
Cdd:cd16288    34 ILIDTGLESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAALKKLTGAKLMASAEDAALLASGGkSDFHYGDDSL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 115 A-EPVHVDVVLHDGDILPYaGGIQVV--FTPGHTPDHTS-----LYHIPSQTLIAGDALTAQDGVLQSFNPAFtPDPKTA 186
Cdd:cd16288   114 AfPPVKVDRVLKDGDRVTL-GGTTLTahLTPGHTRGCTTwtmtvKDDGKVYQVVFADSLTVNPGYKLVGNPTY-PGIAED 191

                         170       180
                  ....*....|....*....|...
gi 1537764618 187 IQ-SIAKLQALELSSIIAYHGGV 208
Cdd:cd16288   192 YRhSFATLRALQCDIFLASHAEY 214
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 36-163 2.05e-14

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: 68.71  E-value: 2.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  36 ILVDTG--LPGQVDIIRAAFDKASIPFekLTKIIITHQDRDHIGSLPELKRLLGDQvQVIAHEvAVPYITGQEPLVKSKS 113
Cdd:cd07722    30 ILIDTGegRPSYIPLLKSVLDSEGNAT--ISDILLTHWHHDHVGGLPDVLDLLRGP-SPRVYK-FPRPEEDEDPDEDGGD 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1537764618 114 LAEpvhvdvvLHDGDILPYAGG-IQVVFTPGHTPDHTSLYHIPSQTLIAGD 163
Cdd:cd07722   106 IHD-------LQDGQVFKVEGAtLRVIHTPGHTTDHVCFLLEEENALFTGD 149
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 27-165 3.23e-14

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: 68.35  E-value: 3.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  27 TVLWDEQ--EIILVDTGlpGQVDIIRAAFDKASIpfeKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIA-HEVAVPYIT 103
Cdd:cd07737    14 SLIWCEEtkEAAVIDPG--GDADKILQAIEDLGL---TLKKILLTHGHLDHVGGAAELAEHYG--VPIIGpHKEDKFLLE 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1537764618 104 GQEPLVKSKSL--AEPVHVDVVLHDGDILPYAGGI-QVVFTPGHTPDHTSLYHIPSQTLIAGDAL 165
Cdd:cd07737    87 NLPEQSQMFGFppAEAFTPDRWLEEGDTVTVGNLTlEVLHCPGHTPGHVVFFNRESKLAIVGDVL 151
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 28-208 7.48e-14

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 67.13  E-value: 7.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  28 VLWDEQEIILVDTG--LPGQVDIIRAAfdkasIPFEKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIAHevaVPYITGq 105
Cdd:cd16278    22 LLGAPDGVVVIDPGpdDPAHLDALLAA-----LGGGRVSAILVTHTHRDHSPGAARLAERTG--APVRAF---GPHRAG- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 106 eplvkskSLAEPVHVDVVLHDGDILPYAG-GIQVVFTPGHTPDHTSLYHIPSQTLIAGDA--------LTAQDGVLQSFn 176
Cdd:cd16278    91 -------GQDTDFAPDRPLADGEVIEGGGlRLTVLHTPGHTSDHLCFALEDEGALFTGDHvmgwsttvIAPPDGDLGDY- 162

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1537764618 177 paftpdpktaIQSIAKLQALELSSIIAYHGGV 208
Cdd:cd16278   163 ----------LASLERLLALDDRLLLPGHGPP 184
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 33-219 1.59e-13

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: 67.57  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  33 QEIILVDTGLPGQVDIIRAAFDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLGDQVQVIAHEVAVPYITGQE--PLVK 110
Cdd:cd07708    31 QGNILIDGDMEQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAEIKKQTGAKVMAGAEDVSLLLSGGSSdfHYAN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 111 SKSLAEP-VHVDVVLHDGDILPyAGGIQVV--FTPGHTPDHTSL------YHIPSQTLIAgDALTAQDGVLQSFNPAFTP 181
Cdd:cd07708   111 DSSTYFPqSTVDRAVHDGERVT-LGGTVLTahATPGHTPGCTTWtmtlkdHGKQYQVVFA-DSLTVNPGYRLVDNPTYPK 188

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1537764618 182 DPKTAIQSIAKLQALELSSIIAYHGGVctDNLQERLQA 219
Cdd:cd07708   189 IVEDYRHSFAVVEAMRCDILLGPHPGV--FDMKNKYVL 224
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 36-150 5.31e-13

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


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 66.34  E-value: 5.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  36 ILVDTGLPGQVDIIRAAFDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLGDQVQVIAHEVAVPYITGQEPLV--KSKS 113
Cdd:cd16308    34 ILINTGLAESVPLIKKNIQALGFKFKDIKILLTTQAHYDHVGAMAAIKQQTGAKMMVDEKDAKVLADGGKSDYEmgGYGS 113

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1537764618 114 LAEPVHVDVVLHDGDILPYaGGIQVVFT--PGHTPDHTS 150
Cdd:cd16308   114 TFAPVKADKLLHDGDTIKL-GGTKLTLLhhPGHTKGSCS 151
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 36-196 1.97e-12

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: 63.42  E-value: 1.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  36 ILVDTGLpGQVDIIRAAfdkasipfEKLTK----IIITHQDRDHIGSLPELKRllgdqvqVIAHEVAVPYITGQEPLVKS 111
Cdd:cd07712    21 LLIDTGL-GIGDLKEYV--------RTLTDlpllVVATHGHFDHIGGLHEFEE-------VYVHPADAEILAAPDNFETL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 112 KSLAEPVHVDVV-----LHDGDILPyAGG--IQVVFTPGHTPDHTSLYHIPSQTLIAGDALtaQDGVLQSFNPAFTPDpk 184
Cdd:cd07712    85 TWDAATYSVPPAgptlpLRDGDVID-LGDrqLEVIHTPGHTPGSIALLDRANRLLFSGDVV--YDGPLIMDLPHSDLD-- 159

                         170
                  ....*....|..
gi 1537764618 185 TAIQSIAKLQAL 196
Cdd:cd07712   160 DYLASLEKLSKL 171
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 27-193 2.17e-12

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


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 63.37  E-value: 2.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  27 TVLWDEQEIILVDTGLPGQVDIIRAAFDKASIPFEKLTKIIITHQDRDHIGSLPelkrlLGDQVQVIAHEVAVPYITGQE 106
Cdd:cd07711    25 TLIKDGGKNILVDTGTPWDRDLLLKALAEHGLSPEDIDYVVLTHGHPDHIGNLN-----LFPNATVIVGWDICGDSYDDH 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 107 PLVKSkslaEPVHVDvvlhdgdilpyaGGIQVVFTPGHTPDHTSL--YHIPSQT-LIAGDAL-TAQDGVLQSFNPAFTPD 182
Cdd:cd07711   100 SLEEG----DGYEID------------ENVEVIPTPGHTPEDVSVlvETEKKGTvAVAGDLFeREEDLEDPILWDPLSED 163

                         170
                  ....*....|.
gi 1537764618 183 PKTAIQSIAKL 193
Cdd:cd07711   164 PELQEESRKRI 174
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 38-196 1.41e-11

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 62.94  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  38 VDTGLPGQVDIIRAA--FDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIAHEVAVPYITGqeplvksksla 115
Cdd:PLN02398   95 EDTGTVGVVDPSEAVpvIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYG--AKVIGSAVDKDRIPG----------- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 116 epvhVDVVLHDGDILPYAGG-IQVVFTPGHTPDHTSLYHIPSQTLIAGDALTAqdgvlQSFNPAFTPDPKTAIQSIAKLQ 194
Cdd:PLN02398  162 ----IDIVLKDGDKWMFAGHeVLVMETPGHTRGHISFYFPGSGAIFTGDTLFS-----LSCGKLFEGTPEQMLSSLQKII 232


                  ..
gi 1537764618 195 AL 196
Cdd:PLN02398  233 SL 234
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 28-165 1.44e-11

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: 60.88  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  28 VLWDEQ--EIILVDTGLpGQVDIIRAAFDKASIpfeKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIAHEvavpyitgq 105
Cdd:cd07724    16 LVGDPEtgEAAVIDPVR-DSVDRYLDLAAELGL---KITYVLETHVHADHVSGARELAERTG--APIVIGE--------- 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1537764618 106 eplvksksLAEPVHVDVVLHDGDILpYAGG--IQVVFTPGHTPDHTSLYHIPSQTLIAGDAL 165
Cdd:cd07724    81 --------GAPASFFDRLLKDGDVL-ELGNltLEVLHTPGHTPESVSYLVGDPDAVFTGDTL 133
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 36-197 4.82e-11

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: 60.31  E-value: 4.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  36 ILVDTGLPGQVdIIRAAFDKASIPF-------------------EKLTKIIITHQDRDHIGSLPELKRllgdqVQVIAHE 96
Cdd:cd07729    44 ILVDTGFHPDA-ADDPGGLELAFPPgvteeqtleeqlarlgldpEDIDYVILSHLHFDHAGGLDLFPN-----ATIIVQR 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  97 VAVPYITGQEPLVKSKSLAEPVHVD------VVLHDGDIlPYAGGIQVVFTPGHTPDHTSLY-HIPSQT-LIAGDALTAQ 168
Cdd:cd07729   118 AELEYATGPDPLAAGYYEDVLALDDdlpggrVRLVDGDY-DLFPGVTLIPTPGHTPGHQSVLvRLPEGTvLLAGDAAYTY 196

                         170       180
                  ....*....|....*....|....*....
gi 1537764618 169 DGVLQSFNPAFTPDPKTAIQSIAKLQALE 197
Cdd:cd07729   197 ENLEEGRPPGINYDPEAALASLERLKALA 225
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 13-189 5.36e-11

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


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 60.64  E-value: 5.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  13 ISMSIqgNPFVIYptvlwDEQEIILVDTGLPGQVDI----IRAAFDKASIPFEKLTKIIITHQDRDHIGSL-PELKRLLG 87
Cdd:cd07720    45 VETSV--NAFLVR-----TGGRLILVDTGAGGLFGPtagkLLANLAAAGIDPEDIDDVLLTHLHPDHIGGLvDAGGKPVF 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  88 DQVQVIAHEVAVPYITGQEPLVKSKSLAEPVHVDV------------VLHDGDILPyagGIQVVFTPGHTPDHTSlYHIP 155
Cdd:cd07720   118 PNAEVHVSEAEWDFWLDDANAAKAPEGAKRFFDAArdrlrpyaaagrFEDGDEVLP---GITAVPAPGHTPGHTG-YRIE 193

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1537764618 156 SQT---LIAGDALTAQdgVLQSFNPAFTP----DPKTAIQS 189
Cdd:cd07720   194 SGGerlLIWGDIVHHP--ALQFAHPDWTIafdvDPEQAAAT 232
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 36-150 5.81e-11

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: 60.58  E-value: 5.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  36 ILVDTGLPGQVDIIRAAFDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIAHEVAVPYI----TGQEPlvKS 111
Cdd:cd16309    34 ILIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAELKKATG--AQLVASAADKPLLesgyVGSGD--TK 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1537764618 112 KSLAEPVHVDVVLHDGDILPYAG-GIQVVFTPGHTPDHTS 150
Cdd:cd16309   110 NLQFPPVRVDRVIGDGDKVTLGGtTLTAHLTPGHSPGCTS 149
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 28-165 2.36e-10

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: 58.13  E-value: 2.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  28 VLWDEQ--EIILVDTGLPGQvDIIRAAFDKASipfeKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIAHEVAVPYITGQ 105
Cdd:cd16322    15 LVADEGggEAVLVDPGDESE-KLLARFGTTGL----TLLYILLTHAHFDHVGGVADLRRHPG--APVYLHPDDLPLYEAA 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1537764618 106 EPLVKSKSLA--EPVHVDVVLHDGDILPYAG-GIQVVFTPGHTPDHTSLYhIPSQT-LIAGDAL 165
Cdd:cd16322    88 DLGAKAFGLGiePLPPPDRLLEDGQTLTLGGlEFKVLHTPGHSPGHVCFY-VEEEGlLFSGDLL 150
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 36-219 3.62e-10

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: 58.13  E-value: 3.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  36 ILVDTGLPGQVDIIRAAFDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIAHEVAVPYI-TGQ----EPLVK 110
Cdd:cd16315    34 VLIDSGTEEAAPLVLANIRKLGFDPKDVRWLLSSHEHFDHVGGLAALQRATG--ARVAASAAAAPVLeSGKpapdDPQAG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 111 SKSLAEPVHVDVVLHDGDIL--------PYAggiqvvfTPGHTPDHTSlYHIPS------QTLIAGDALTA--QDGVLQS 174
Cdd:cd16315   112 LHEPFPPVRVDRIVEDGDTValgslrltAHA-------TPGHTPGALS-WTWRScegadcRTIVYADSLSPvsADGYRFS 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1537764618 175 FNPAFTPDPKTaiqSIAKLQALELSSIIAYHGGvcTDNLQERLQA 219
Cdd:cd16315   184 DHPDYVAAYRA---GLAKVAALPCDILLTPHPS--ASDMFERLSG 223
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 36-205 1.16e-09

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: 56.79  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  36 ILVDTGLPGQVDIIRAAFDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIAHEVAVPYI-TGQ----EPLVK 110
Cdd:cd16313    34 ILIDGGFPKSPEQIAASIRQLGFKLEDVKYILSSHDHWDHAGGIAALQKLTG--AQVLASPATVAVLrSGSmgkdDPQFG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 111 SKSLAEPVHVDVVLHDGDIL---PYAggIQVVFTPGHTPDHTSLYHIPSQ-----TLIAGDALTA--QDGVLQSFNPAFT 180
Cdd:cd16313   112 GLTPMPPVASVRAVRDGEVVklgPLA--VTAHATPGHTTGGTSWTWQSCEqgrcaNMVFADSLTAvsADGYRFSAHPAVL 189

                         170       180
                  ....*....|....*....|....*
gi 1537764618 181 PDPKtaiQSIAKLQALELSSIIAYH 205
Cdd:cd16313   190 ADVE---QSIAAVEKLACDILVSAH 211
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 36-150 2.79e-09

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: 55.59  E-value: 2.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  36 ILVDTGLPGQVDIIRAAFDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLGDQVQVIAHEVAVPYITGQEPLVKSKSLA 115
Cdd:cd16289    34 VLLDGGMPQAADMLLDNMRALGVAPGDLKLILHSHAHADHAGPLAALKRATGARVAANAESAVLLARGGSDDIHFGDGIT 113

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1537764618 116 -EPVHVDVVLHDGDILPyAGGIQVV--FTPGHTPDHTS 150
Cdd:cd16289   114 fPPVQADRIVMDGEVVT-LGGVTFTahFTPGHTPGSTS 150
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-152 4.79e-09

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 54.90  E-value: 4.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  35 IILVDTGLPGQ-VDIIRAAFDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIAHEVAVPYITGQEPLVKSKS 113
Cdd:cd16280    33 LILIDALNNNEaADLIVDGLEKLGLDPADIKYILITHGHGDHYGGAAYLKDLYG--AKVVMSEADWDMMEEPPEEGDNPR 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1537764618 114 LAEPVHVDVVLHDGDILPYaGG--IQVVFTPGHTPDHTSLY 152
Cdd:cd16280   111 WGPPPERDIVIKDGDTLTL-GDttITVYLTPGHTPGTLSLI 150
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 36-145 1.11e-08

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


Pssm-ID: 293865  Cd Length: 255  Bit Score: 53.99  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  36 ILVDTGLPGQVDIIRAAFDKASIPFEKlTKI-IITHQDRDHIGSLPELKRLLGDQVQVIAHEVAVPYITGQEPLV---KS 111
Cdd:cd16307    34 ILINSNLESSVPQIKASIEKLGFKFSD-TKIlLISHAHFDHAAGSALIKRETHAKYMVMDGDVDVVESGGKSDFFygnDP 112

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1537764618 112 KSLAEPVHVDVVLHDGDILPYAGGIQVV-FTPGHT 145
Cdd:cd16307   113 STYFPPAHVDKVLHDGEQVELGGTVLTAhLTAGHT 147
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 20-167 1.49e-08

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 53.26  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  20 NPFVIyptvlwDEQEIILVDTGLPGQVDIIRAAFDKAsIPFEKLTKIIITHQDRDHIGSLPELKRLLGDqVQVIAHEVAV 99
Cdd:cd07709    33 NSYLI------KDEKTALIDTVKEPFFDEFLENLEEV-IDPRKIDYIVVNHQEPDHSGSLPELLELAPN-AKIVCSKKAA 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1537764618 100 PYITGQEPLVKSKSlaepvhvdVVLHDGDILPyAGG--IQVVFTPG-HTPDHTSLYHIPSQTLIAGDALTA 167
Cdd:cd07709   105 RFLKHFYPGIDERF--------VVVKDGDTLD-LGKhtLKFIPAPMlHWPDTMVTYDPEDKILFSGDAFGA 166
NorV COG0426
Flavorubredoxin [Energy production and conversion];
12-164 2.63e-08

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 53.30  E-value: 2.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  12 EISMSIQG----NPFVIyptvlwDEQEIILVDTGLPGQVDIIRAAFDKAsIPFEKLTKIIITHQDRDHIGSLPELKRLLg 87
Cdd:COG0426    23 EGEYPTPRgttyNSYLI------VDEKTALIDTVGESFFEEFLENLSKV-IDPKKIDYIIVNHQEPDHSGSLPELLELA- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  88 DQVQVIAHEVAVPYITGQEPLVKSKSlaepvhvdVVLHDGDILPYaGGIQVVF--TPG-HTPDHTSLYHIPSQTLIAGDA 164
Cdd:COG0426    95 PNAKIVCSKKAARFLPHFYGIPDFRF--------IVVKEGDTLDL-GGHTLQFipAPMlHWPDTMFTYDPEDKILFSGDA 165
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 33-150 3.15e-08

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: 52.45  E-value: 3.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  33 QEIILVDTGLPGQVDIIRAAFDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIAHEVAVPYITGQEPL---V 109
Cdd:cd16310    31 HGAILLDGGLEENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQLKADTG--AKLWASRGDRPALEAGKHIgdnI 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1537764618 110 KSKSLAEPVHVDVVLHDGDILPYaGGIQVV--FTPGHTPDHTS 150
Cdd:cd16310   109 TQPAPFPAVKVDRILGDGEKIKL-GDITLTatLTPGHTKGCTT 150
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 32-211 5.07e-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: 51.41  E-value: 5.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  32 EQEIILVDTGL-PGQVDIIRAAFdkASIPFEKLTKIIITHQDRDHIGSLPELKrllGDQVQVIAHEVAVPYI--TGQEPL 108
Cdd:cd16282    23 DDGVVVIDTGAsPRLARALLAAI--RKVTDKPVRYVVNTHYHGDHTLGNAAFA---DAGAPIIAHENTREELaaRGEAYL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 109 VKSKSLA-------EPVHVDVVLHDGDILpYAGGIQVV---FTPGHTPDHTSLYHIPSQTLIAGDALtaqdgvlqsFNPA 178
Cdd:cd16282    98 ELMRRLGgdamagtELVLPDRTFDDGLTL-DLGGRTVElihLGPAHTPGDLVVWLPEEGVLFAGDLV---------FNGR 167

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1537764618 179 FTP----DPKTAIQSIAKLQALELSSIIAYHGGVCTD 211
Cdd:cd16282   168 IPFlpdgSLAGWIAALDRLLALDATVVVPGHGPVGDK 204
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 32-165 1.82e-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: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 47.11  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  32 EQEIILVDTGL-PGQ----VDIIRAaFDKasipfeKLTKIIITHQDRDHIGSLPELKRLLGDqVQVIAHEVAVPYITGQ- 105
Cdd:cd07739    24 ETEAVLVDAQFtRADaerlADWIKA-SGK------TLTTIYITHGHPDHYFGLEVLLEAFPD-AKVVATPAVVAHIKAQl 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1537764618 106 ------------EPLVKSKSLAEPVHVDVVLHDGDIlpyaggIQVVFTPGHTPDHTSLYHIPSQ-TLIAGDAL 165
Cdd:cd07739    96 epklafwgpllgGNAPARLVVPEPLDGDTLTLEGHP------LEIVGVGGGDTDDTTYLWIPSLkTVVAGDVV 162
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 66-209 4.91e-06

uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YmaE and Nostoc all1228 proteins.Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 45.26  E-value: 4.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  66 IIITHqdRDHIGSLPELKRLLGdqVQVIAHEVAVPYITGqeplvkskslaePVHVdVVLHDGDILPYAGGIQVVFTPGHT 145
Cdd:cd07727    51 IFLTH--RDDVADHAKWAERFG--AKRIIHEDDVNAVTR------------PDEV-IVLWGGDPWELDPDLTLIPVPGHT 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1537764618 146 PDHTSLYHIPSQTLIAGD--ALTAQDGVLQSFNPAFTPDPKTAIQSIAKLQALELSSIIAYHGGVC 209
Cdd:cd07727   114 RGSVVLLYKEKGVLFTGDhlAWSRRRGWLSAFRYVCWYSWPEQAESVERLADLDFEWVLPGHGRRV 179
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 116-189 9.52e-06

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 45.21  E-value: 9.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 116 EPVH----VDVVLHDGDILPyagGIQVVFTPGHTPDHTSLyHIPSQT---LIAGDALTAQdgvLQ----SFNPAFTPDPK 184
Cdd:cd16277   126 LPVIeaglADLVDDDHEILD---GIRLEPTPGHTPGHVSV-ELESGGeraLFTGDVMHHP---IQvarpDWSSVFDEDPA 198


                  ....*
gi 1537764618 185 TAIQS 189
Cdd:cd16277   199 QAAAT 203
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 49-165 1.51e-05

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: 44.06  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  49 IRAAFDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLGDQVQVIAHEVAVPYItgqeplvKSKSLaepvhvdVVLHDGD 128
Cdd:cd16275    34 IEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDYYGF-------RCPNL-------IPLEDGD 99

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1537764618 129 ILPyAGG--IQVVFTPGHTPDHTSlYHIpSQTLIAGDAL 165
Cdd:cd16275   100 TIK-IGDteITCLLTPGHTPGSMC-YLL-GDSLFTGDTL 135
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 36-150 4.88e-05

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


Pssm-ID: 293869  Cd Length: 257  Bit Score: 43.05  E-value: 4.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  36 ILVDTGLPGQVDIIRAAFDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLGDQVQV---IAHEVAVPYITGQEPLVKSK 112
Cdd:cd16311    34 VLVDGGLPESAPKIIANIEALGFRIEDVKLILNSHGHIDHAGGLAELQRRSGALVAAspsAALDLASGEVGPDDPQYHAL 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1537764618 113 SLAEPVHVDVVLHDGDILPyAGGIQVV--FTPGHTPDHTS 150
Cdd:cd16311   114 PKYPPVKDMRLARDGGQFN-VGPVSLTahATPGHTPGGLS 152
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 36-150 8.61e-05

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


Pssm-ID: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 42.57  E-value: 8.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  36 ILVDTGLPGQVDIIRAAFDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLGdqVQVIAHEVAVPYITG-----QEPLVK 110
Cdd:cd16314    34 ILIDGGTDKAAPLIEANIRALGFRPEDVRYIVSSHEHFDHAGGIARLQRATG--APVVAREPAATTLERgrsdrSDPQFL 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1537764618 111 SKSLAEPVHVDVVLHDGDIL---PYAggIQVVFTPGHTPDHTS 150
Cdd:cd16314   112 VVEKFPPVASVQRIGDGEVLrvgPLA--LTAHATPGHTPGGTS 152
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 33-207 9.45e-05

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: 42.28  E-value: 9.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  33 QEIILVDTGLPGQVDIIRAAFDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLGDQVQVIAHEVAV--PYITGQE-PLV 109
Cdd:cd16312    31 QGHVLLDGALPQSAPLIIANIEALGFRIEDVKLILNSHAHWDHAGGIAALQKASGATVAASAHGAQVlqSGTNGKDdPQY 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 110 KSKSLAEPVHVDVV--LHDGDILPYAG-GIQVVFTPGHTPDHTSLYHIPSQ-----TLIAGDALTA-QDGVLQSFNPAFT 180
Cdd:cd16312   111 QAKPVVHVAKVAKVkeVGEGDTLKVGPlRLTAHMTPGHTPGGTTWTWTSCEgqrclDVVYADSLNPySSGDFYYTGKGGY 190

                         170       180
                  ....*....|....*....|....*...
gi 1537764618 181 PDPKTAI-QSIAKLQALELSSIIAYHGG 207
Cdd:cd16312   191 PDISASFrASIAKVAALPCDIIIAVHPG 218
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 32-82 9.67e-05

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 42.15  E-value: 9.67e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1537764618  32 EQEIILVDTGLPGQVD----IIRAAFDKASIpfEKLTKIIITHQDRDHIGSLPEL 82
Cdd:COG2333    20 DGKTILIDTGPRPSFDagerVVLPYLRALGI--RRLDLLVLTHPDADHIGGLAAV 72
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 32-82 5.30e-04

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: 39.42  E-value: 5.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1537764618  32 EQEIILVDTG--LPGQVDIIraafdkasIPF------EKLTKIIITHQDRDHIGSLPEL 82
Cdd:cd07731    18 PGKTILIDTGprDSFGEDVV--------VPYlkargiKKLDYLILTHPDADHIGGLDAV 68
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 27-82 7.31e-04

Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 39.42  E-value: 7.31e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1537764618  27 TVLWDEQEIILVDTGlPGQVdiirAAFDKASIPFEKLTKIIITHQDRDHIGSLPEL 82
Cdd:cd07719    21 TLVVVGGRVYLVDAG-SGVV----RRLAQAGLPLGDLDAVFLTHLHSDHVADLPAL 71
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 31-202 1.61e-03

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 38.65  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  31 DEQEIILVDtglPGQVD-IIRAAFDKASIPfeklTKIIITHQDRDHIGSLPELkrllgdqvqvIAHevaVPYITGQEPL- 108
Cdd:PRK10241   20 EAGRCLIVD---PGEAEpVLNAIAENNWQP----EAIFLTHHHHDHVGGVKEL----------VEK---FPQIVVYGPQe 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 109 VKSKSlaepvhVDVVLHDGDILPYAGGIQVVF-TPGHTPDHTSLYHIPsqTLIAGDAL-TAQDGVLqsfnpaFTPDPKTA 186
Cdd:PRK10241   80 TQDKG------TTQVVKDGETAFVLGHEFSVFaTPGHTLGHICYFSKP--YLFCGDTLfSGGCGRL------FEGTASQM 145

                         170
                  ....*....|....*.
gi 1537764618 187 IQSIAKLQALELSSII 202
Cdd:PRK10241  146 YQSLKKINALPDDTLI 161
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 27-96 1.64e-03

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 38.72  E-value: 1.64e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1537764618  27 TVLWDEQEIILVDTGlPGqvdiIRAAFDKASIPFEKLTKIIITHQDRDHIGSLPELKRLLG-DQVQVIAHE 96
Cdd:COG1235    38 ILVEADGTRLLIDAG-PD----LREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYGpNPIPVYATP 103
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 36-223 3.40e-03

L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 37.59  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  36 ILVDtglPGQVDIIrAAFDKASIPFEKLTK---IIITHQDRDHIGsLPELKRLLGDQVQVIAHEVAVPYITGQEplvksk 112
Cdd:COG2220    23 ILID---PVFSGRA-SPVNPLPLDPEDLPKidaVLVTHDHYDHLD-DATLRALKRTGATVVAPLGVAAWLRAWG------ 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 113 slAEPVHvdvVLHDGDILPYaGGIQVVFTPG-HTPDHTS---------LYHIPSQTL-IAGDALTAQD--GVLQSFNP-- 177
Cdd:COG2220    92 --FPRVT---ELDWGESVEL-GGLTVTAVPArHSSGRPDrngglwvgfVIETDGKTIyHAGDTGYFPEmkEIGERFPIdv 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1537764618 178 AFTP--------DPKTAIQSIAKLQAlelSSIIAYHGGVCTDNLQERLQAIISA 223
Cdd:COG2220   166 ALLPigaypftmGPEEAAEAARDLKP---KVVIPIHYGTFPLLDEDPLERFAAA 216
CphS_ImiS-like_MBL-B2 cd16287
metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas ...
 117-200 6.23e-03

metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis.


Pssm-ID: 293845  Cd Length: 226  Bit Score: 36.64  E-value: 6.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 117 PVHVDVVLHDGDILPYAGGIQVVFT-PGHTPDHTSLYHIPSQTLIAGDALTAQDGVLqSFnpaftPDPKTAIQSIAKLQA 195
Cdd:cd16287   117 EKSLPDTVFPGDFNLQNGSIRAMYLgEAHTKDGIFVYFPAERVLYGNCILKENLGNM-SF-----ANRTEYPKTLEKLKG 190


                  ....*
gi 1537764618 196 LELSS 200
Cdd:cd16287   191 LIEQG 195
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 32-207 7.99e-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: 36.02  E-value: 7.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618  32 EQEIILVDTgLPGQVDIIRAAFDKasIPFEKLTKIIITHQDRDHIGSLPELKrllGDQVQVIAHEvavpyITGQEpLVKS 111
Cdd:cd16276    18 DKGVIVVDA-PPSLGENLLAAIRK--VTDKPVTHVVYSHNHADHIGGASIFK---DEGATIIAHE-----ATAEL-LKRN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537764618 112 KSLAEPVHvDVVLHDGDILpYAGG--IQVVFT-PGHTPDHTSLYhIPSQ-TLIAGDALTAqdGVLQSFNPAFTPDPKTAI 187
Cdd:cd16276    86 PDPKRPVP-TVTFDDEYTL-EVGGqtLELSYFgPNHGPGNIVIY-LPKQkVLMAVDLINP--GWVPFFNFAGSEDIPGYI 160

                         170       180
                  ....*....|....*....|
gi 1537764618 188 QSIAKLQALELSSIIAYHGG 207
Cdd:cd16276   161 EALDELLEYDFDTFVGGHGN 180
 
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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