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Conserved domains on  [gi|1325909070|ref|WP_101782549|]
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MULTISPECIES: MBL fold metallo-hydrolase [Streptococcus]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10865880)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme

CATH:  3.60.15.10
Gene Ontology:  GO:0016787
PubMed:  17597585

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 4-193 5.21e-57

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: 178.63  E-value: 5.21e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070   4 HKTVNPVAYENTYYLEGE-KHLIVVDPG-SHWDAIRQTIETINKPICAILLTHAHYDHIMSLDLVRETFGnPPVYIAESE 81
Cdd:cd06262     1 KRLPVGPLQTNCYLVSDEeGEAILIDPGaGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPG-APVYIHEAD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  82 ASWLYTPVDNLSGLprhdDMVDVVSKPAEHTFVFHEEYQLEEFRFTVLPTPGHSIGGVSLVFPDAHLVLTGDALFRETIG 161
Cdd:cd06262    80 AELLEDPELNLAFF----GGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIG 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1325909070 162 RTDLPTGSMEQLLHSIQTQLFTLP-NYDVYPGH 193
Cdd:cd06262   156 RTDLPGGDPEQLIESIKKLLLLLPdDTVVYPGH 188
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 4-193 5.21e-57

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: 178.63  E-value: 5.21e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070   4 HKTVNPVAYENTYYLEGE-KHLIVVDPG-SHWDAIRQTIETINKPICAILLTHAHYDHIMSLDLVRETFGnPPVYIAESE 81
Cdd:cd06262     1 KRLPVGPLQTNCYLVSDEeGEAILIDPGaGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPG-APVYIHEAD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  82 ASWLYTPVDNLSGLprhdDMVDVVSKPAEHTFVFHEEYQLEEFRFTVLPTPGHSIGGVSLVFPDAHLVLTGDALFRETIG 161
Cdd:cd06262    80 AELLEDPELNLAFF----GGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIG 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1325909070 162 RTDLPTGSMEQLLHSIQTQLFTLP-NYDVYPGH 193
Cdd:cd06262   156 RTDLPGGDPEQLIESIKKLLLLLPdDTVVYPGH 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 14-201 2.68e-44

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: 146.76  E-value: 2.68e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  14 NTYYLEGEKHLIVVDPG---SHWDAIRQTIETINKPICAILLTHAHYDHIMSLDLVRETFGnPPVYIAESEASWLYTPVD 90
Cdd:COG0491    16 NSYLIVGGDGAVLIDTGlgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFG-APVYAHAAEAEALEAPAA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  91 nlsglprhDDMVDVVSKPAEHTFVFHEEYQLEEFRFTVLPTPGHSIGGVSLVFPDAHLVLTGDALFRETIGRTDLPTGSM 170
Cdd:COG0491    95 --------GALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLPDGDL 166

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1325909070 171 EQLLHSIQtQLFTLPNYDVYPGHGSATTIAH 201
Cdd:COG0491   167 AQWLASLE-RLLALPPDLVIPGHGPPTTAEA 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 14-193 1.16e-31

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: 113.42  E-value: 1.16e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070   14 NTYYLEGEKHLIVVDPGSHW-DAIRQTIETIN-KPICAILLTHAHYDHIMSLDLVRETFgNPPVYIAESEASWLYTPVDN 91
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEaEDLLAELKKLGpKKIDAIILTHGHPDHIGGLPELLEAP-GAPVYAPEGTAELLKDLLAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070   92 LSGLPRHDDMVDVVskpaeHTFVFHEEYQLEEFRFTVLPTPGHSIGGVSLVFPDAHLVLTGDALFRETIGRTDLPTG--S 169
Cdd:smart00849  80 LGELGAEAEPAPPD-----RTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGdaA 154

                          170       180
                   ....*....|....*....|....
gi 1325909070  170 MEQLLHSIQTQLFTLPNYdVYPGH 193
Cdd:smart00849 155 ASDALESLLKLLKLLPKL-VVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
14-193 1.20e-31

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 114.00  E-value: 1.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  14 NTYYLEGEKHLIVVDPGSHWDAIRQTIETI----NKPICAILLTHAHYDHIMSLDLVRETFGNPPVYIAESEASWLYTPV 89
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLLAAlglgPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  90 DNLSGLPRHDDMVDVVSKPaEHTFVFHEEYQLEEFRFTVLPTPGHSIGGVSLVFPDAHLVLTGDALFRETIGRTDLPTGS 169
Cdd:pfam00753  87 GLAASRLGLPGPPVVPLPP-DVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPLGG 165

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1325909070 170 MEQLLHSIQTQ-------LFTLPNYDVYPGH 193
Cdd:pfam00753 166 LLVLHPSSAESslesllkLAKLKAAVIVPGH 196
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 128-207 5.23e-13

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 65.59  E-value: 5.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070 128 VLPTPGHSIGGVSLVF------PDAHLVLTGDALFRETIGRTDLPTGSMEQLLHSIQTQLFTLPNYD-VYPGHG----SA 196
Cdd:PLN02962  119 VRATPGHTAGCVTYVTgegpdqPQPRMAFTGDALLIRGCGRTDFQGGSSDQLYKSVHSQIFTLPKDTlIYPAHDykgfTV 198

                          90
                  ....*....|.
gi 1325909070 197 TTIAHEKTFNP 207
Cdd:PLN02962  199 STVGEEMLYNP 209
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 14-159 1.92e-04

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


Pssm-ID: 273195 [Multi-domain]  Cd Length: 422  Bit Score: 41.57  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  14 NTYYLEGEKHLIVVDPGSHWDAIR-----------QTIETINKPICAILLTHAHYDHIMSLDLVRETFGNPPVYIAESEA 82
Cdd:TIGR00649  15 NMYVVEIDDEIVIFDAGILFPEDEmlgvdgvipdfTYLQENEDKVKGIFITHGHEDHIGAVPYLLHQVGFFPIYGTPLTI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  83 SWLYTPVDNLSGLPRHDDMVDVVSKPAEhtfvFHEEYQLEEFRFTvlptpgHSIG---GVSLVFPDAHLVLTGDALFRET 159
Cdd:TIGR00649  95 ALIKSKIKEHGLNVRTDLLEIHEGEPVE----FGENTAIEFFRIT------HSIPdsvGFALHTPLGYIVYTGDFKFDNT 164
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 4-193 5.21e-57

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: 178.63  E-value: 5.21e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070   4 HKTVNPVAYENTYYLEGE-KHLIVVDPG-SHWDAIRQTIETINKPICAILLTHAHYDHIMSLDLVRETFGnPPVYIAESE 81
Cdd:cd06262     1 KRLPVGPLQTNCYLVSDEeGEAILIDPGaGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPG-APVYIHEAD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  82 ASWLYTPVDNLSGLprhdDMVDVVSKPAEHTFVFHEEYQLEEFRFTVLPTPGHSIGGVSLVFPDAHLVLTGDALFRETIG 161
Cdd:cd06262    80 AELLEDPELNLAFF----GGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIG 155

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1325909070 162 RTDLPTGSMEQLLHSIQTQLFTLP-NYDVYPGH 193
Cdd:cd06262   156 RTDLPGGDPEQLIESIKKLLLLLPdDTVVYPGH 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 14-201 2.68e-44

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: 146.76  E-value: 2.68e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  14 NTYYLEGEKHLIVVDPG---SHWDAIRQTIETINKPICAILLTHAHYDHIMSLDLVRETFGnPPVYIAESEASWLYTPVD 90
Cdd:COG0491    16 NSYLIVGGDGAVLIDTGlgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFG-APVYAHAAEAEALEAPAA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  91 nlsglprhDDMVDVVSKPAEHTFVFHEEYQLEEFRFTVLPTPGHSIGGVSLVFPDAHLVLTGDALFRETIGRTDLPTGSM 170
Cdd:COG0491    95 --------GALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLPDGDL 166

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1325909070 171 EQLLHSIQtQLFTLPNYDVYPGHGSATTIAH 201
Cdd:COG0491   167 AQWLASLE-RLLALPPDLVIPGHGPPTTAEA 196
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 13-208 1.29e-34

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: 121.69  E-value: 1.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  13 ENTYYL--EGEKHLIVVDPGSHWDAIRQTIETINKPICAILLTHAHYDHIMSLDLVRETFGnPPVYIAESEASWLytpvD 90
Cdd:cd16322    11 ENTYLVadEGGGEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPG-APVYLHPDDLPLY----E 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  91 NLSGLPRHDDMVDVVSKPAEHTFVFHEEYQLEEFRFTVLPTPGHSIGGVSLVFPDAHLVLTGDALFRETIGRTDLPTGSM 170
Cdd:cd16322    86 AADLGAKAFGLGIEPLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRTDLPGGDP 165

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1325909070 171 EQLLHSIQTQLFTLPNYDVYPGHGSATTIAHEKTFNPF 208
Cdd:cd16322   166 KAMAASLRRLLTLPDETRVFPGHGPPTTLGEERRTNPF 203
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 14-193 1.16e-31

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: 113.42  E-value: 1.16e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070   14 NTYYLEGEKHLIVVDPGSHW-DAIRQTIETIN-KPICAILLTHAHYDHIMSLDLVRETFgNPPVYIAESEASWLYTPVDN 91
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEaEDLLAELKKLGpKKIDAIILTHGHPDHIGGLPELLEAP-GAPVYAPEGTAELLKDLLAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070   92 LSGLPRHDDMVDVVskpaeHTFVFHEEYQLEEFRFTVLPTPGHSIGGVSLVFPDAHLVLTGDALFRETIGRTDLPTG--S 169
Cdd:smart00849  80 LGELGAEAEPAPPD-----RTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGdaA 154

                          170       180
                   ....*....|....*....|....
gi 1325909070  170 MEQLLHSIQTQLFTLPNYdVYPGH 193
Cdd:smart00849 155 ASDALESLLKLLKLLPKL-VVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
14-193 1.20e-31

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 114.00  E-value: 1.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  14 NTYYLEGEKHLIVVDPGSHWDAIRQTIETI----NKPICAILLTHAHYDHIMSLDLVRETFGNPPVYIAESEASWLYTPV 89
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLLLAAlglgPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  90 DNLSGLPRHDDMVDVVSKPaEHTFVFHEEYQLEEFRFTVLPTPGHSIGGVSLVFPDAHLVLTGDALFRETIGRTDLPTGS 169
Cdd:pfam00753  87 GLAASRLGLPGPPVVPLPP-DVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPLGG 165

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1325909070 170 MEQLLHSIQTQ-------LFTLPNYDVYPGH 193
Cdd:pfam00753 166 LLVLHPSSAESslesllkLAKLKAAVIVPGH 196
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 22-193 2.27e-31

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: 113.03  E-value: 2.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  22 KHLIVVDPGSHWDAIRQTIETINKPICAILLTHAHYDHIMSLDLVRETFGNPPVYIAESEASWLytpvDNLS------GL 95
Cdd:cd07737    22 KEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKEDKFLL----ENLPeqsqmfGF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  96 PrhddmvdvvskPAEhtfVFHEEYQLEE--------FRFTVLPTPGHSIGGVSLVFPDAHLVLTGDALFRETIGRTDLPT 167
Cdd:cd07737    98 P-----------PAE---AFTPDRWLEEgdtvtvgnLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTDFPG 163

                         170       180
                  ....*....|....*....|....*..
gi 1325909070 168 GSMEQLLHSIQTQLFTLP-NYDVYPGH 193
Cdd:cd07737   164 GNHAQLIASIKEKLLPLGdDVTFIPGH 190
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 14-194 7.92e-26

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: 98.83  E-value: 7.92e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  14 NTYYLEGEKHLIVVDPG--SHWDAIRQTIETIN---KPICAILLTHAHYDHIMSLDLVRETFGnPPVYIAESEASWLYTP 88
Cdd:cd07721    12 NAYLIEDDDGLTLIDTGlpGSAKRILKALRELGlspKDIRRILLTHGHIDHIGSLAALKEAPG-APVYAHEREAPYLEGE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  89 VDNLSGLPRHDDMVDVVSKPAEHTFVFHE----EYQLEEFRFTVLPTPGHSIGGVSLVFPDAHLVLTGDALFREtIGRTD 164
Cdd:cd07721    91 KPYPPPVRLGLLGLLSPLLPVKPVPVDRTledgDTLDLAGGLRVIHTPGHTPGHISLYLEEDGVLIAGDALVTV-GGELV 169

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1325909070 165 LP----TGSMEQLLHSIQTQLFTLPNYdVYPGHG 194
Cdd:cd07721   170 PPpppfTWDMEEALESLRKLAELDPEV-LAPGHG 202
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 15-195 8.20e-25

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: 95.54  E-value: 8.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  15 TYYL--EGEKHLIVVDPgsHWDAIRQTIETINK---PICAILLTHAHYDHIM-SLDLVRETfgNPPVYIAESeaswlytp 88
Cdd:cd07724    14 SYLVgdPETGEAAVIDP--VRDSVDRYLDLAAElglKITYVLETHVHADHVSgARELAERT--GAPIVIGEG-------- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  89 vdnlsglprhdDMVDVVSKPAEHTFVFHeeyqLEEFRFTVLPTPGHSIGGVSLVFPDAHLVLTGDALFRETIGRTDLP-- 166
Cdd:cd07724    82 -----------APASFFDRLLKDGDVLE----LGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPge 146

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1325909070 167 -TGSMEQLLHSIQTQLFTLP-NYDVYPGHGS 195
Cdd:cd07724   147 aEGLARQLYDSLQRKLLLLPdETLVYPGHDY 177
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 25-193 3.69e-24

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: 93.76  E-value: 3.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  25 IVVDPGshWD--AIRQTIETINKPICAILLTHAHYDHI-MSLDLVRETfgNPPVYIAESEAS-WLYTPvdnlSGLPRHDD 100
Cdd:cd16275    26 AVVDPA--WDieKILAKLNELGLTLTGILLTHSHFDHVnLVEPLLAKY--DAPVYMSKEEIDyYGFRC----PNLIPLED 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070 101 MvdvvskpaehtfvfhEEYQLEEFRFTVLPTPGHSIGGVSLVFPDaHLVlTGDALFRETIGRTDLPTGSMEQLLHSIQtQ 180
Cdd:cd16275    98 G---------------DTIKIGDTEITCLLTPGHTPGSMCYLLGD-SLF-TGDTLFIEGCGRCDLPGGDPEEMYESLQ-R 159

                         170
                  ....*....|....*
gi 1325909070 181 LFTLPNYD--VYPGH 193
Cdd:cd16275   160 LKKLPPPNtrVYPGH 174
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 22-193 3.17e-23

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: 90.98  E-value: 3.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  22 KHLIVVDPGSHwDAIRQTIETINKPICAILLTHAHYDHIMSLDLVRETFGNPPVYiaeseaswlytpvdnlsgLPRHDDm 101
Cdd:cd07723    20 GEAAVVDPGEA-EPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVY------------------GPAEDR- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070 102 VDVVSKPAEHtfvfHEEYQLEEFRFTVLPTPGHSIGGVSLVFPDAHLVLTGDALFRETIGRTDlpTGSMEQLLHSIQtQL 181
Cdd:cd07723    80 IPGLDHPVKD----GDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGRFF--EGTAEQMYASLQ-KL 152

                         170
                  ....*....|....
gi 1325909070 182 FTLPNyD--VYPGH 193
Cdd:cd07723   153 LALPD-DtlVYCGH 165
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-196 1.04e-16

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: 74.45  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  14 NTYYLEGEKHLIVVDPG----SHWDAIRQTIEtiNKPICAILLTHAHYDHIMSLDLVRETFGnPPVYiaeseaswlytpv 89
Cdd:cd16278    19 NTYLLGAPDGVVVIDPGpddpAHLDALLAALG--GGRVSAILVTHTHRDHSPGAARLAERTG-APVR------------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  90 dnlsGLPRHDDMVDVVSKPAEHTFVFHEEYQLEEFRFTVLPTPGHSIGGVSLVFPDAHLVLTGDALFREtiGRT--DLPT 167
Cdd:cd16278    83 ----AFGPHRAGGQDTDFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVMGW--STTviAPPD 156

                         170       180
                  ....*....|....*....|....*....
gi 1325909070 168 GSMEQLLHSIQtQLFTLPNYDVYPGHGSA 196
Cdd:cd16278   157 GDLGDYLASLE-RLLALDDRLLLPGHGPP 184
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 16-193 1.58e-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) 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: 68.71  E-value: 1.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  16 YYLEGEKHLIVVDPG---SHWDAIRQTIETINKPICAILLTHAHYDHIMSLDLVRETFGNpPVYIAESEAS--------- 83
Cdd:cd07743    12 VYVFGDKEALLIDSGldeDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGC-KVYAPKIEKAfienpllep 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  84 ---WLYTPVDNLSG--LPRHDDMVDVVSKPaehtfvfhEEYQLEEFRFTVLPTPGHSIGGVSLVFPDAhlVL-TGDALF- 156
Cdd:cd07743    91 sylGGAYPPKELRNkfLMAKPSKVDDIIEE--------GELELGGVGLEIIPLPGHSFGQIGILTPDG--VLfAGDALFg 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1325909070 157 RETIGRTDLPtgsmeqLLHSIQTQLFTLP-----NYDVY-PGH 193
Cdd:cd07743   161 EEVLEKYGIP------FLYDVEEQLETLEkleelDADYYvPGH 197
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 17-194 1.22e-13

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: 66.45  E-value: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  17 YLEGEKHLIVVDPGSHWD--AIRQTIETIN-KP--ICAILLTHAHYDHIMSLDLvretFGNPPVYIAESEASWLYTPvdn 91
Cdd:cd07711    26 LIKDGGKNILVDTGTPWDrdLLLKALAEHGlSPedIDYVVLTHGHPDHIGNLNL----FPNATVIVGWDICGDSYDD--- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  92 lsglprhddmvdvvskpaeHTFVFHEEYQLEEFRfTVLPTPGHSIGGVSLVFPDAHL---VLTGDALFRE--TIGRTDLP 166
Cdd:cd07711    99 -------------------HSLEEGDGYEIDENV-EVIPTPGHTPEDVSVLVETEKKgtvAVAGDLFEREedLEDPILWD 158

                         170       180       190
                  ....*....|....*....|....*....|
gi 1325909070 167 TGS--MEQLLHSIQtQLFTLPNYdVYPGHG 194
Cdd:cd07711   159 PLSedPELQEESRK-RILALADW-IIPGHG 186
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 14-193 2.61e-13

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: 65.34  E-value: 2.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  14 NTYYLEGEKHLIVVDPGSHWDAIRQTIETI-NKPICAILlTHAHYDHIMSLDLVREtfgnppVYIAESEASWLYTPvDNL 92
Cdd:cd07712    10 NIYLLRGRDRALLIDTGLGIGDLKEYVRTLtDLPLLVVA-THGHFDHIGGLHEFEE------VYVHPADAEILAAP-DNF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  93 SGLPRHDDMVDVVSKPAEHTFVFHEEYQLEEFRFTVLPTPGHSIGGVSLVFPDAHLVLTGDALFRETIgRTDLPTGSMEQ 172
Cdd:cd07712    82 ETLTWDAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVYDGPL-IMDLPHSDLDD 160

                         170       180
                  ....*....|....*....|...
gi 1325909070 173 LLHSIQtQLFTLPNY--DVYPGH 193
Cdd:cd07712   161 YLASLE-KLSKLPDEfdKVLPGH 182
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-200 3.10e-13

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 65.66  E-value: 3.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  14 NTYYLEGEKHLIVVDPGS---HWDAIRQTIETI-NKPICAILLTHAHYDHimsldlvreTFGN-------PPVY------ 76
Cdd:cd16282    16 NIGFIVGDDGVVVIDTGAsprLARALLAAIRKVtDKPVRYVVNTHYHGDH---------TLGNaafadagAPIIahentr 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  77 --IAESEASWLytpvDNLSGLPRhDDMVDVVSKPAEHTFVFHEEYQL--EEFRFTVLPtPGHSIGGVSLVFPDAHLVLTG 152
Cdd:cd16282    87 eeLAARGEAYL----ELMRRLGG-DAMAGTELVLPDRTFDDGLTLDLggRTVELIHLG-PAHTPGDLVVWLPEEGVLFAG 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1325909070 153 DALFRETIgrTDLPTGSMEQLLHSIQTQLFTLPNYdVYPGHGSATTIA 200
Cdd:cd16282   161 DLVFNGRI--PFLPDGSLAGWIAALDRLLALDATV-VVPGHGPVGDKA 205
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 16-193 4.41e-13

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: 65.70  E-value: 4.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  16 YYLEGEKHLIVVDPGSHWDAIRQT--IETINKPIC---------------------AILLTHAHYDHIMSLDLvretFGN 72
Cdd:cd07729    35 YLIEHPEGTILVDTGFHPDAADDPggLELAFPPGVteeqtleeqlarlgldpedidYVILSHLHFDHAGGLDL----FPN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  73 PPVYIAESEASWLYTPvDNLSGLPRHDDMVDVVSKPAEHTFVFHEEYQLEEfRFTVLPTPGHSIGGVSLVF--PDAHLVL 150
Cdd:cd07729   111 ATIIVQRAELEYATGP-DPLAAGYYEDVLALDDDLPGGRVRLVDGDYDLFP-GVTLIPTPGHTPGHQSVLVrlPEGTVLL 188

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1325909070 151 TGDAL-FRETIGRTDLP--TGSMEQLLHSIQT--QLFTLPNYDVYPGH 193
Cdd:cd07729   189 AGDAAyTYENLEEGRPPgiNYDPEAALASLERlkALAEREGARVIPGH 236
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 128-207 5.23e-13

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 65.59  E-value: 5.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070 128 VLPTPGHSIGGVSLVF------PDAHLVLTGDALFRETIGRTDLPTGSMEQLLHSIQTQLFTLPNYD-VYPGHG----SA 196
Cdd:PLN02962  119 VRATPGHTAGCVTYVTgegpdqPQPRMAFTGDALLIRGCGRTDFQGGSSDQLYKSVHSQIFTLPKDTlIYPAHDykgfTV 198

                          90
                  ....*....|.
gi 1325909070 197 TTIAHEKTFNP 207
Cdd:PLN02962  199 STVGEEMLYNP 209
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 14-143 1.71e-11

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 61.45  E-value: 1.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  14 NTYYLEGEKHLIVVDPGShwdAIRQTIETIN---KPICAILLTHAHYDHIMSLDLVRETFGNPPVYIaeseaswlYTPVD 90
Cdd:COG1235    36 SSILVEADGTRLLIDAGP---DLREQLLRLGldpSKIDAILLTHEHADHIAGLDDLRPRYGPNPIPV--------YATPG 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1325909070  91 NLSGLPRHDDMVDVVSKP--AEHTFVFHEEYQLEEFRFTVLPTPGHSIGGVSLVF 143
Cdd:COG1235   105 TLEALERRFPYLFAPYPGklEFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGYRI 159
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 26-193 1.67e-10

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 59.09  E-value: 1.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  26 VVDPgSHWDAIRQTIETINKPICAILLTHAHYDHIMSLDLVRETFGNPPVYIAESEaswlytpvDNLSGlprhddmVDVV 105
Cdd:PLN02398  102 VVDP-SEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVDK--------DRIPG-------IDIV 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070 106 SKPAEH-TFVFHEeyqleefrFTVLPTPGHSIGGVSLVFPDAHLVLTGDALFRETIGRtdLPTGSMEQLLHSIQtQLFTL 184
Cdd:PLN02398  166 LKDGDKwMFAGHE--------VLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGK--LFEGTPEQMLSSLQ-KIISL 234

                         170
                  ....*....|
gi 1325909070 185 PN-YDVYPGH 193
Cdd:PLN02398  235 PDdTNIYCGH 244
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 45-144 2.12e-10

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: 58.37  E-value: 2.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  45 KPICAILLTHAHYDHIMSLDLVRETFGnPPVYIAESEASWLYTPVDNLSGlPRHDDM--VDVVSKPAEhtfvfheEYQLE 122
Cdd:cd16280    60 ADIKYILITHGHGDHYGGAAYLKDLYG-AKVVMSEADWDMMEEPPEEGDN-PRWGPPpeRDIVIKDGD-------TLTLG 130

                          90       100
                  ....*....|....*....|..
gi 1325909070 123 EFRFTVLPTPGHSIGGVSLVFP 144
Cdd:cd16280   131 DTTITVYLTPGHTPGTLSLIFP 152
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 14-194 5.48e-10

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: 56.39  E-value: 5.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  14 NTYYLEGEKHLIVVDPGSHWDAIRQTIETI-----NKPICAILLTHAHYDHIMSLDLVRETFGNPPVYIaeseaswlytp 88
Cdd:cd07722    19 NTYLVGTGKRRILIDTGEGRPSYIPLLKSVldsegNATISDILLTHWHHDHVGGLPDVLDLLRGPSPRV----------- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  89 vdnlSGLPRHDDMVDVVSKPAEHTFVFH-EEYQLEEFRFTVLPTPGHSIGGVSLVFPDAHLVLTGD-------ALFreti 160
Cdd:cd07722    88 ----YKFPRPEEDEDPDEDGGDIHDLQDgQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGDcvlghgtAVF---- 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1325909070 161 grTDLPT--GSmeqlLHSIQTQLFTLpnydVYPGHG 194
Cdd:cd07722   160 --EDLAAymAS----LKKLLSLGPGR----IYPGHG 185
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 14-132 4.74e-09

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


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 53.04  E-value: 4.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  14 NTYYLEGEKHLIVVDPGSHWDAIRQTIETIN-KP--ICAILLTHAHYDHIMSLDLVRETFGNPpvyiaeseaswLYTPVD 90
Cdd:cd07733    10 NCTYLETEDGKLLIDAGLSGRKITGRLAEIGrDPedIDAILVTHEHADHIKGLGVLARKYNVP-----------IYATAG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1325909070  91 NLSGLPRHDDMVDVVSKpaeHTFVFHEEYQLEEFRFTVLPTP 132
Cdd:cd07733    79 TLRAMERKVGLIDVDQK---QIFEPGETFSIGDFDVESFGVS 117
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 9-194 9.54e-09

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: 52.69  E-value: 9.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070   9 PVAYENTYYLEGEKHLIVVDPGSH----WDAIRQTIETIN-KP--ICAILLTHAHYDHIMSLDLVRETFGnPPVYIAEse 81
Cdd:cd07725    11 PLGHVNVYLLRDGDETTLIDTGLAteedAEALWEGLKELGlKPsdIDRVLLTHHHPDHIGLAGKLQEKSG-ATVYILD-- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  82 aswlYTPVdnlsglpRHDDMVDvvskpaehtfvfheeyqLEEFRFTVLPTPGHSIGGVSLVFPDAHLVLTGDALFRE--- 158
Cdd:cd07725    88 ----VTPV-------KDGDKID-----------------LGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLPKitp 139

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1325909070 159 TIGRTDLP-TGSMEQLLHSIQtQLFTLPNYDVYPGHG 194
Cdd:cd07725   140 NVSLWAVRvEDPLGAYLESLD-KLEKLDVDLAYPGHG 175
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
16-160 2.71e-08

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 52.50  E-value: 2.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  16 YYLEGEKHLIVVDPGSH-WDAIRQTIETINKpICAILLTHAHYDHIMSLDLVRETFG----NPPVYIaeseaswlYTPVD 90
Cdd:COG1234    22 YLLEAGGERLLIDCGEGtQRQLLRAGLDPRD-IDAIFITHLHGDHIAGLPGLLSTRSlagrEKPLTI--------YGPPG 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1325909070  91 NLSGLprhDDMVDVVSKPAEHTFVFHE-----EYQLEEFRFTVLPTPgHSIG--GVSLVFPDAHLVLTGDALFRETI 160
Cdd:COG1234    93 TKEFL---EALLKASGTDLDFPLEFHEiepgeVFEIGGFTVTAFPLD-HPVPayGYRFEEPGRSLVYSGDTRPCEAL 165
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 14-79 3.30e-07

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


Pssm-ID: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 49.04  E-value: 3.30e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1325909070  14 NTYYLEGEKHLIVVDPGSH-------WDAIRQtiETINKPICAILLTHAHYDHIMSLDLVRETF--GNPPVYIAE 79
Cdd:cd07710    19 NMTFIEGDTGLIIIDTLESaeaakaaLELFRK--HTGDKPVKAIIYTHSHPDHFGGAGGFVEEEdsGKVPIIAPE 91
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 15-193 1.55e-06

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: 47.10  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  15 TYYLEGEKHLIVVDPG--SHWDAIRQTIETINKPIC---AILLTHAHYDHIMSLDLVRETFGNPPVYIAESEA------S 83
Cdd:cd07726    18 SYLLDGEGRPALIDTGpsSSVPRLLAALEALGIAPEdvdYIILTHIHLDHAGGAGLLAEALPNAKVYVHPRGArhlidpS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  84 WLYTPVDNLSGLPRHDDMVDVVSKPAEHTFVFH--EEYQLEEFRFTVLPTPGHSIGGVSLVFPDAHLVLTGDAL---FRE 158
Cdd:cd07726    98 KLWASARAVYGDEADRLGGEILPVPEERVIVLEdgETLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDAAgvrYPE 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1325909070 159 tiGRTDLPTGS------MEQLLHSIQTQLFTLPNYdVYPGH 193
Cdd:cd07726   178 --LDVVGPPSTpppdfdPEAWLESLDRLLSLKPER-IYLTH 215
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 11-186 1.97e-06

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 47.13  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  11 AYENTY---YLEGEKHLIVVDPGSHWDAIRQTIETINKPIcAILLTHAHYDHIMSLDLVRETFGNPPVY-IAESEaswly 86
Cdd:PRK10241    8 AFDDNYiwvLNDEAGRCLIVDPGEAEPVLNAIAENNWQPE-AIFLTHHHHDHVGGVKELVEKFPQIVVYgPQETQ----- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  87 tpvdnlsglprhDDMVDVVSKPAEHTFVFHEEyqleefrFTVLPTPGHSIGGVSLvFPDAHLvLTGDALFRETIGRtdLP 166
Cdd:PRK10241   82 ------------DKGTTQVVKDGETAFVLGHE-------FSVFATPGHTLGHICY-FSKPYL-FCGDTLFSGGCGR--LF 138

                         170       180
                  ....*....|....*....|
gi 1325909070 167 TGSMEQLLHSIQtQLFTLPN 186
Cdd:PRK10241  139 EGTASQMYQSLK-KINALPD 157
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 49-194 3.04e-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: 45.65  E-value: 3.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  49 AILLTHAHY--DHimslDLVRETFGnPPVYIAESEASWlYTPVDNLSGLPRHDdmvdvvskpaehTFVFHEEyqleefrF 126
Cdd:cd07727    50 YIFLTHRDDvaDH----AKWAERFG-AKRIIHEDDVNA-VTRPDEVIVLWGGD------------PWELDPD-------L 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1325909070 127 TVLPTPGHSIGGVSLVFPDAHLVLTGDALFreTIGRTDLPTGSMEQLLHSIQTQLFT---LPNYD---VYPGHG 194
Cdd:cd07727   105 TLIPVPGHTRGSVVLLYKEKGVLFTGDHLA--WSRRRGWLSAFRYVCWYSWPEQAESverLADLDfewVLPGHG 176
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 16-167 3.60e-06

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 46.72  E-value: 3.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  16 YYLEGEKHLIVVDPGshwdaIRQTIETINKP--------ICAILLTHAHYDHIMSL-DLVRETFgNPPVY---------- 76
Cdd:COG1236    17 YLLETGGTRILIDCG-----LFQGGKERNWPpfpfrpsdVDAVVLTHAHLDHSGALpLLVKEGF-RGPIYatpatadlar 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  77 --------IAESEASW--LYTPVDNLSGLPRHddmvdvvskpaeHTFVFHEEYQLEEFRFTVLPTpGHSIG--GVSLVFP 144
Cdd:COG1236    91 illgdsakIQEEEAEAepLYTEEDAERALELF------------QTVDYGEPFEIGGVRVTFHPA-GHILGsaQVELEVG 157

                         170       180
                  ....*....|....*....|...
gi 1325909070 145 DAHLVLTGDalfretIGRTDLPT 167
Cdd:COG1236   158 GKRIVFSGD------YGREDDPL 174
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 25-135 1.17e-05

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 44.22  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  25 IVVDPGshWDA------IRQTIETINKPICAILLTHAHYDHIMSLDLVRETFGNPpvyiaeseaswLYTPVDNLSGLPRH 98
Cdd:pfam12706   3 ILIDPG--PDLrqqalpALQPGRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPRP-----------LYAPLGVLAHLRRN 69

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1325909070  99 DDMVDVVSKPAE--HTFVFHEEYQLEEFRFTVLPTPGHS 135
Cdd:pfam12706  70 FPYLFLLEHYGVrvHEIDWGESFTVGDGGLTVTATPARH 108
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 12-140 3.55e-05

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: 43.11  E-value: 3.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  12 YENTYY----------LEGEKHLIVVDPGSH--WDAIRQTIETIN---KPICAILLTHAHYDHIMSLDLVRETFGNPPVY 76
Cdd:cd16315    11 FGNTYYvgtcgisailITGDDGHVLIDSGTEeaAPLVLANIRKLGfdpKDVRWLLSSHEHFDHVGGLAALQRATGARVAA 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1325909070  77 IAESE---ASWLYTPVDNLSGLprHDDM----VDVVSKPAEHTfvfheeyQLEEFRFTVLPTPGHSIGGVS 140
Cdd:cd16315    91 SAAAApvlESGKPAPDDPQAGL--HEPFppvrVDRIVEDGDTV-------ALGSLRLTAHATPGHTPGALS 152
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 17-130 4.13e-05

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


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 42.46  E-value: 4.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  17 YLEGEKHLIVVDPGSHW--DAIRQTIETINkpicAILLTHAHYDHIMSLDLVR----------ETFGNPPVyIAESEASW 84
Cdd:cd16279    39 LIETGGKNILIDTGPDFrqQALRAGIRKLD----AVLLTHAHADHIHGLDDLRpfnrlqqrpiPVYASEET-LDDLKRRF 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1325909070  85 LYTPVDNLSGLprhddmvdvVSKPAEHTFVFHEEYQLEEFRFTVLP 130
Cdd:cd16279   114 PYFFAATGGGG---------VPKLDLHIIEPDEPFTIGGLEITPLP 150
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 16-167 1.12e-04

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. 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: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 41.29  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  16 YYLEGEKHLIVVD----PGSHWDAIRQTIETINKP--ICAILLTHAHYDHIMSL-DLVRETFgNPPVY------------ 76
Cdd:cd16295    15 YLLETGGKRILLDcglfQGGKELEELNNEPFPFDPkeIDAVILTHAHLDHSGRLpLLVKEGF-RGPIYatpatkdlaell 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  77 ------IAESEASW-----LYTPVDNLSGLPRhddmvdvvSKPAEhtfvFHEEYQL-EEFRFTVLPTpGHSIGGVSLVF- 143
Cdd:cd16295    94 lldsakIQEEEAEHppaepLYTEEDVEKALKH--------FRPVE----YGEPFEIgPGVKVTFYDA-GHILGSASVELe 160

                         170       180
                  ....*....|....*....|....*.
gi 1325909070 144 --PDAHLVLTGDalfretIGRTDLPT 167
Cdd:cd16295   161 igGGKRILFSGD------LGRKNTPL 180
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 49-156 1.80e-04

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


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 40.99  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  49 AILLTHAHYDHI--MSLDLVRETFGNPPVYIAESEASWLYTPvDNLSGLPRHDDMVDVVSKPAEHTFVFHEEYQLEEfrf 126
Cdd:cd07720    94 DVLLTHLHPDHIggLVDAGGKPVFPNAEVHVSEAEWDFWLDD-ANAAKAPEGAKRFFDAARDRLRPYAAAGRFEDGD--- 169

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1325909070 127 TVLP----------TPGHSigGVSLVFPDAHLVLTGDALF 156
Cdd:cd07720   170 EVLPgitavpapghTPGHT--GYRIESGGERLLIWGDIVH 207
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 14-159 1.92e-04

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


Pssm-ID: 273195 [Multi-domain]  Cd Length: 422  Bit Score: 41.57  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  14 NTYYLEGEKHLIVVDPGSHWDAIR-----------QTIETINKPICAILLTHAHYDHIMSLDLVRETFGNPPVYIAESEA 82
Cdd:TIGR00649  15 NMYVVEIDDEIVIFDAGILFPEDEmlgvdgvipdfTYLQENEDKVKGIFITHGHEDHIGAVPYLLHQVGFFPIYGTPLTI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  83 SWLYTPVDNLSGLPRHDDMVDVVSKPAEhtfvFHEEYQLEEFRFTvlptpgHSIG---GVSLVFPDAHLVLTGDALFRET 159
Cdd:TIGR00649  95 ALIKSKIKEHGLNVRTDLLEIHEGEPVE----FGENTAIEFFRIT------HSIPdsvGFALHTPLGYIVYTGDFKFDNT 164
PRK02113 PRK02113
MBL fold metallo-hydrolase;
17-76 2.37e-04

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 40.92  E-value: 2.37e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1325909070  17 YLEGEKHLIVVDPGSHWDAIRQTIETINkpicAILLTHAHYDHIMSLDLVRE--TFGNPPVY 76
Cdd:PRK02113   41 ETEGARILIDCGPDFREQMLRLPFGKID----AVLITHEHYDHVGGLDDLRPfcRFGEVPIY 98
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 14-85 3.91e-04

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 39.90  E-value: 3.91e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1325909070  14 NTYYLEGEKHLIVVDP-----GSHWDAIRQTIETInKPICAILLTHAHYDHIM--SLDLVRETfgNPPVYIAESEASWL 85
Cdd:COG2220    12 ATFLIETGGKRILIDPvfsgrASPVNPLPLDPEDL-PKIDAVLVTHDHYDHLDdaTLRALKRT--GATVVAPLGVAAWL 87
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 18-154 4.07e-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: 4.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  18 LEGEKHLIVVDPGSHWDAIRQTIET------INKpICAILLTHAHYDHIMSLDLVRETFgnpPVyiaeseaSWLYTPVDN 91
Cdd:cd07731    15 IQTPGKTILIDTGPRDSFGEDVVVPylkargIKK-LDYLILTHPDADHIGGLDAVLKNF---PV-------KEVYMPGVT 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1325909070  92 LSGLPRHdDMVDVVSKPAEHTFVFH--EEYQLEEFRFTVL-PTPGHSIGG------VSLVFPDAHLVLTGDA 154
Cdd:cd07731    84 HTTKTYE-DLLDAIKEKGIPVTPCKagDRWQLGGVSFEVLsPPKDDYDDLnnnscvLRLTYGGTSFLLTGDA 154
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 17-130 4.50e-04

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. 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: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 39.53  E-value: 4.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  17 YLEGEKHLIVVDPGSHWDAIRQTIETINkpicAILLTHAHYDHIMSL-DLVRETFGNPPVYIAESEASwlytPVDnlsgL 95
Cdd:cd07736    41 LIEVDGERILLDAGLTDLAERFPPGSID----AILLTHFHMDHVQGLfHLRWGVGDPIPVYGPPDPQG----CAD----L 108

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1325909070  96 PRHDDMVDVvsKPAEHTFvfhEEYQLEEFRFTVLP 130
Cdd:cd07736   109 FKHPGILDF--QPLVAPF---QSFELGGLKITPLP 138
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 50-155 9.47e-04

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 39.04  E-value: 9.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  50 ILLTHAHYDHI-----MSLDLVRETFGNPPVYIAESEasWLYTPVDNLSGLPRHDDMVDVVSkP---AEHTFVFHEEYQL 121
Cdd:cd16277    67 VLCTHLHVDHVgwntrLVDGRWVPTFPNARYLFSRAE--YDHWSSPDAGGPPNRGVFEDSVL-PvieAGLADLVDDDHEI 143

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1325909070 122 EEfRFTVLPTPGHSIGGVSLVF--PDAHLVLTGDAL 155
Cdd:cd16277   144 LD-GIRLEPTPGHTPGHVSVELesGGERALFTGDVM 178
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 16-153 1.28e-03

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


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 38.01  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  16 YYLEGEKHLIVVDPGSH-WDAIRQTIETINKPIcAILLTHAHYDHIMslDLV------RETFGNPPVYIaeseaswlYTP 88
Cdd:cd16272    20 YLLETGGTRILLDCGEGtVYRLLKAGVDPDKLD-AIFLSHFHLDHIG--GLPtllfarRYGGRKKPLTI--------YGP 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1325909070  89 VDNLSGLPRHDDmVDVVSKPAEHTFVFHE------EYQLEEFRFTVLPTPgHSIG--GVSLVFPDAHLVLTGD 153
Cdd:cd16272    89 KGIKEFLEKLLN-FPVEILPLGFPLEIEEleeggeVLELGDLKVEAFPVK-HSVEslGYRIEAEGKSIVYSGD 159
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 49-154 3.57e-03

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: 37.14  E-value: 3.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  49 AILLTHAHYDHIMSLDLVRETFgnpPVyiaeseaSWLYTPVDNLSGLPRHDDMVDVVSKPAEHTFVFH-EEYQLEEFRFT 127
Cdd:COG2333    55 LLVLTHPDADHIGGLAAVLEAF---PV-------GRVLVSGPPDTSETYERLLEALKEKGIPVRPCRAgDTWQLGGVRFE 124

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1325909070 128 VL-PTPGHSIGGV----SLV----FPDAHLVLTGDA 154
Cdd:COG2333   125 VLwPPEDLLEGSDennnSLVlrltYGGFSFLLTGDA 160
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 13-137 4.31e-03

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: 37.04  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  13 ENTYYL-----------EGEKHlIVVDPGSHWDA--IRQTIETIN---KPICAILLTHAHYDHIMSLDLVRETFGnPPVY 76
Cdd:cd16310    12 DNIYYVgtkgigsylitSNHGA-ILLDGGLEENAalIEQNIKALGfklSDIKIIINTHAHYDHAGGLAQLKADTG-AKLW 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1325909070  77 IAESEASWLYTpvdnlsGLPRHDDMVDVVSKPA---EHTFVFHEEYQLEEFRFTVLPTPGHSIG 137
Cdd:cd16310    90 ASRGDRPALEA------GKHIGDNITQPAPFPAvkvDRILGDGEKIKLGDITLTATLTPGHTKG 147
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-60 5.11e-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: 36.41  E-value: 5.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1325909070  14 NTYYLEGEKHLIVVD-PGSHWDAIRQTIETI-NKPICAILLTHAHYDHI 60
Cdd:cd16276    11 QSMFLVTDKGVIVVDaPPSLGENLLAAIRKVtDKPVTHVVYSHNHADHI 59
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 13-194 6.24e-03

metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B1 MBls include chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1. B2 MBLs have a narrow substrate profile that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis. B2 MBLs include Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I.


Pssm-ID: 293793 [Multi-domain]  Cd Length: 219  Bit Score: 36.37  E-value: 6.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  13 ENTYYLEGEKHLIVVDpgSHWDA------IRQTIETINKPICAILLTHAHYDHIMSLDLVR----ETFGNPPVY-IAESE 81
Cdd:cd07707    21 SNGLVYNGSKGLVLVD--STWTPkttkelIKEIEKVSQKPVTEVINTHFHTDRAGGNAYLKergaKTVSTALTRdLAKSE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325909070  82 asWLYTPVDNLSGLPRHDDMVDVvskPAEHTFVFHEEYQLEEFRfTVLPTPGHSIGGVSLVFPDAHLVLTGDALFRETIG 161
Cdd:cd07707    99 --WAEIVAFTRKGLPEYPDLGYE---LPDGVLDGDFNLQFGKVE-AFYPGPAHTPDNIVVYFPQENVLYGGCIIKETDLG 172

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1325909070 162 ------RTDLPTgSMEQLlhsiqtQLFTLPNYDVYPGHG 194
Cdd:cd07707   173 nvadadVKEWPT-SIERL------KKRYRNIKAVIPGHG 204
BDS1 COG2015
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary ...
 19-76 6.85e-03

Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441618 [Multi-domain]  Cd Length: 629  Bit Score: 36.74  E-value: 6.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1325909070  19 EGEKHLIVVDPGSH-------WDAIRQTIEtiNKPICAILLTHAHYDH------IMSLDLVREtfGNPPVY 76
Cdd:COG2015   109 EGDTGWIVIDPLTSvetaaaaLALYRKHLG--DRPVKAVIYTHSHVDHfggvrgVVDEEDVKS--GKVPII 175
 
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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