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Conserved domains on  [gi|580096379|gb|EVB27796|]
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metallo-beta-lactamase [Staphylococcus aureus M0581]

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; ...
 5-190 2.64e-62

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: 191.73  E-value: 2.64e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379   5 SLTLGLVDTNTYFIEND-KAVILIDPSGES-EKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFD 82
Cdd:cd06262    2 RLPVGPLQTNCYLVSDEeGEAILIDPGAGAlEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  83 FLKDPVKNGADkfkqYGLPIITSKVTPEKLNEGST-EIEGFKFNVLHTPGHSPGSLTYVFDE--FAVVGDTLFNNGIGRT 159
Cdd:cd06262   82 LLEDPELNLAF----FGGGPLPPPEPDILLEDGDTiELGGLELEVIHTPGHTPGSVCFYIEEegVLFTGDTLFAGSIGRT 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 580096379 160 DLYKGDYETLVDSIQDKIFELEGDLPLFPGH 190
Cdd:cd06262  158 DLPGGDPEQLIESIKKLLLLLPDDTVVYPGH 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; ...
 5-190 2.64e-62

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: 191.73  E-value: 2.64e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379   5 SLTLGLVDTNTYFIEND-KAVILIDPSGES-EKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFD 82
Cdd:cd06262    2 RLPVGPLQTNCYLVSDEeGEAILIDPGAGAlEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  83 FLKDPVKNGADkfkqYGLPIITSKVTPEKLNEGST-EIEGFKFNVLHTPGHSPGSLTYVFDE--FAVVGDTLFNNGIGRT 159
Cdd:cd06262   82 LLEDPELNLAF----FGGGPLPPPEPDILLEDGDTiELGGLELEVIHTPGHTPGSVCFYIEEegVLFTGDTLFAGSIGRT 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 580096379 160 DLYKGDYETLVDSIQDKIFELEGDLPLFPGH 190
Cdd:cd06262  158 DLPGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 10-205 1.12e-51

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: 165.63  E-value: 1.12e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  10 LVDTNTYFIENDKAVILIDPSGES---EKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFDFLKD 86
Cdd:COG0491   12 GLGVNSYLIVGGDGAVLIDTGLGPadaEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  87 PvkngaDKFKQYGLPIITSKVTpekLNEGST-EIEGFKFNVLHTPGHSPGSLTYVFDE--FAVVGDTLFNNGIGRTDLYK 163
Cdd:COG0491   92 P-----AAGALFGREPVPPDRT---LEDGDTlELGGPGLEVIHTPGHTPGHVSFYVPDekVLFTGDALFSGGVGRPDLPD 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 580096379 164 GDYETLVDSIqDKIFELEGDLpLFPGHGPYTTVDD------------EQLNPFL 205
Cdd:COG0491  164 GDLAQWLASL-ERLLALPPDL-VIPGHGPPTTAEAidyleellaalgERANPFL 215
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 14-190 5.82e-38

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: 129.60  E-value: 5.82e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379    14 NTYFIENDKAVILIDP-SGESEKIIKKLNQIN-KPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFDFLKDPvkng 91
Cdd:smart00849   1 NSYLVRDDGGAILIDTgPGEAEDLLAELKKLGpKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDL---- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379    92 aDKFKQYGLPIITSKVTPEKLNEGST-EIEGFKFNVLHTPGHSPGSLTYVFDEFAVV--GDTLFNNGIGRTDLYKGDYET 168
Cdd:smart00849  77 -LALLGELGAEAEPAPPDRTLKDGDElDLGGGELEVIHTPGHTPGSIVLYLPEGKILftGDLLFAGGDGRTLVDGGDAAA 155

                          170       180
                   ....*....|....*....|..
gi 580096379   169 LVDSIQDKIFELEGDLPLFPGH 190
Cdd:smart00849 156 SDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
8-190 5.30e-34

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 119.78  E-value: 5.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379    8 LGLVDTNTYFIENDKAVILIDPSGESEKI----IKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFDF 83
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAAllllLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379   84 LKDPVKNGADKFKQYGLPIITSKVTPEKLNEGST---EIEGFKFNVLHTPGHSPGSLTYVFDEFAVVGDTLFNNGIGRTD 160
Cdd:pfam00753  81 LLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGilgGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLD 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 580096379  161 LYKGDYETLVDSIQ-------DKIFELEGDLpLFPGH 190
Cdd:pfam00753 161 LPLGGLLVLHPSSAessleslLKLAKLKAAV-IVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 4-190 2.49e-15

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 72.95  E-value: 2.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379   4 SSLTLGLV----DTNTYFI--ENDKAVILIDPSgESEKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVymh 77
Cdd:PLN02398  74 SSLQIELVpclkDNYAYLLhdEDTGTVGVVDPS-EAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKV--- 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  78 eaefdflkdpVKNGADKFKQYGLPIItskvtpekLNEGSTEI-EGFKFNVLHTPGHSPGSLTYVFDEFAVV--GDTLFNN 154
Cdd:PLN02398 150 ----------IGSAVDKDRIPGIDIV--------LKDGDKWMfAGHEVLVMETPGHTRGHISFYFPGSGAIftGDTLFSL 211

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 580096379 155 GIGRtdLYKGDYETLVDSIQdKIFELEGDLPLFPGH 190
Cdd:PLN02398 212 SCGK--LFEGTPEQMLSSLQ-KIISLPDDTNIYCGH 244
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 8-163 5.46e-07

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: 48.89  E-value: 5.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379    8 LGLVDTNTYFIENDKAVILID-----PSGE---SEKIIKK---LNQINKPLKAILLTHAHFDHIGAVDDIVDRFDV-PVY 75
Cdd:TIGR00649   9 LGEIGKNMYVVEIDDEIVIFDagilfPEDEmlgVDGVIPDftyLQENEDKVKGIFITHGHEDHIGAVPYLLHQVGFfPIY 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379   76 MHEAEFDFLKdpvkngaDKFKQYGLPIITSKVTPEKLN----EGSTEIEGFKFN---------VLHTPghsPGSLTYV-- 140
Cdd:TIGR00649  89 GTPLTIALIK-------SKIKEHGLNVRTDLLEIHEGEpvefGENTAIEFFRIThsipdsvgfALHTP---LGYIVYTgd 158

                         170       180
                  ....*....|....*....|....*
gi 580096379  141 --FDEFAVVGDtlfnngigRTDLYK 163
Cdd:TIGR00649 159 fkFDNTPVIGE--------PPDLNR 175
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 5-190 2.64e-62

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: 191.73  E-value: 2.64e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379   5 SLTLGLVDTNTYFIEND-KAVILIDPSGES-EKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFD 82
Cdd:cd06262    2 RLPVGPLQTNCYLVSDEeGEAILIDPGAGAlEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  83 FLKDPVKNGADkfkqYGLPIITSKVTPEKLNEGST-EIEGFKFNVLHTPGHSPGSLTYVFDE--FAVVGDTLFNNGIGRT 159
Cdd:cd06262   82 LLEDPELNLAF----FGGGPLPPPEPDILLEDGDTiELGGLELEVIHTPGHTPGSVCFYIEEegVLFTGDTLFAGSIGRT 157

                        170       180       190
                 ....*....|....*....|....*....|.
gi 580096379 160 DLYKGDYETLVDSIQDKIFELEGDLPLFPGH 190
Cdd:cd06262  158 DLPGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 3-205 3.40e-53

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: 169.07  E-value: 3.40e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379   3 ISSLTLGLVDTNTYFI--ENDKAVILIDPSGESEKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAE 80
Cdd:cd16322    1 VRPFTLGPLQENTYLVadEGGGEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  81 FdflkdPVKNGADKF-KQYGLPIITSKVTPEKLNEGST-EIEGFKFNVLHTPGHSPGSLTYVFDE--FAVVGDTLFNNGI 156
Cdd:cd16322   81 L-----PLYEAADLGaKAFGLGIEPLPPPDRLLEDGQTlTLGGLEFKVLHTPGHSPGHVCFYVEEegLLFSGDLLFQGSI 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 580096379 157 GRTDLYKGDYETLVDSIQdKIFELEGDLPLFPGHGPYTTVDDE-QLNPFL 205
Cdd:cd16322  156 GRTDLPGGDPKAMAASLR-RLLTLPDETRVFPGHGPPTTLGEErRTNPFL 204
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 10-205 1.12e-51

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: 165.63  E-value: 1.12e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  10 LVDTNTYFIENDKAVILIDPSGES---EKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFDFLKD 86
Cdd:COG0491   12 GLGVNSYLIVGGDGAVLIDTGLGPadaEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  87 PvkngaDKFKQYGLPIITSKVTpekLNEGST-EIEGFKFNVLHTPGHSPGSLTYVFDE--FAVVGDTLFNNGIGRTDLYK 163
Cdd:COG0491   92 P-----AAGALFGREPVPPDRT---LEDGDTlELGGPGLEVIHTPGHTPGHVSFYVPDekVLFTGDALFSGGVGRPDLPD 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 580096379 164 GDYETLVDSIqDKIFELEGDLpLFPGHGPYTTVDD------------EQLNPFL 205
Cdd:COG0491  164 GDLAQWLASL-ERLLALPPDL-VIPGHGPPTTAEAidyleellaalgERANPFL 215
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 19-190 9.43e-51

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: 162.34  E-value: 9.43e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  19 ENDKAVILIDPSGESEKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFDFLKDPVKNGAdkfKQY 98
Cdd:cd07737   19 EETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKEDKFLLENLPEQS---QMF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  99 GLPIITSKVTPEKLNEGST-EIEGFKFNVLHTPGHSPGSLTYVFDE--FAVVGDTLFNNGIGRTDLYKGDYETLVDSIQD 175
Cdd:cd07737   96 GFPPAEAFTPDRWLEEGDTvTVGNLTLEVLHCPGHTPGHVVFFNREskLAIVGDVLFKGSIGRTDFPGGNHAQLIASIKE 175

                        170
                 ....*....|....*
gi 580096379 176 KIFELEGDLPLFPGH 190
Cdd:cd07737  176 KLLPLGDDVTFIPGH 190
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 14-190 3.14e-40

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: 134.97  E-value: 3.14e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  14 NTYFIENDKA--VILIDPSGESEKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFDFLKDPVKNg 91
Cdd:cd16275   13 YSYIIIDKATreAAVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDYYGFRCPN- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  92 adkfkqygLPIITSKvtpEKLNEGSTEIEgfkfnVLHTPGHSPGSLTYVFDEFAVVGDTLFNNGIGRTDLYKGDYETLVD 171
Cdd:cd16275   92 --------LIPLEDG---DTIKIGDTEIT-----CLLTPGHTPGSMCYLLGDSLFTGDTLFIEGCGRCDLPGGDPEEMYE 155

                        170       180
                 ....*....|....*....|
gi 580096379 172 SIQdKIFEL-EGDLPLFPGH 190
Cdd:cd16275  156 SLQ-RLKKLpPPNTRVYPGH 174
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 14-190 5.82e-38

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: 129.60  E-value: 5.82e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379    14 NTYFIENDKAVILIDP-SGESEKIIKKLNQIN-KPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFDFLKDPvkng 91
Cdd:smart00849   1 NSYLVRDDGGAILIDTgPGEAEDLLAELKKLGpKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDL---- 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379    92 aDKFKQYGLPIITSKVTPEKLNEGST-EIEGFKFNVLHTPGHSPGSLTYVFDEFAVV--GDTLFNNGIGRTDLYKGDYET 168
Cdd:smart00849  77 -LALLGELGAEAEPAPPDRTLKDGDElDLGGGELEVIHTPGHTPGSIVLYLPEGKILftGDLLFAGGDGRTLVDGGDAAA 155

                          170       180
                   ....*....|....*....|..
gi 580096379   169 LVDSIQDKIFELEGDLPLFPGH 190
Cdd:smart00849 156 SDALESLLKLLKLLPKLVVPGH 177
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 14-191 1.54e-37

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: 129.26  E-value: 1.54e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  14 NTYFIENDKAVILID--PSGESEKIIKKLNQIN---KPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFDFLK--- 85
Cdd:cd07721   12 NAYLIEDDDGLTLIDtgLPGSAKRILKALRELGlspKDIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEREAPYLEgek 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  86 ---DPVKNGADKFKQYGLPIITSKVTpEKLNEGSTEIEGFKFNVLHTPGHSPGSLTYVFDEF--AVVGDtLFNNGIGRTD 160
Cdd:cd07721   92 pypPPVRLGLLGLLSPLLPVKPVPVD-RTLEDGDTLDLAGGLRVIHTPGHTPGHISLYLEEDgvLIAGD-ALVTVGGELV 169

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 580096379 161 LYKG----DYETLVDSIQdKIFELEGDLpLFPGHG 191
Cdd:cd07721  170 PPPPpftwDMEEALESLR-KLAELDPEV-LAPGHG 202
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
8-190 5.30e-34

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 119.78  E-value: 5.30e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379    8 LGLVDTNTYFIENDKAVILIDPSGESEKI----IKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFDF 83
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAAllllLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379   84 LKDPVKNGADKFKQYGLPIITSKVTPEKLNEGST---EIEGFKFNVLHTPGHSPGSLTYVFDEFAVVGDTLFNNGIGRTD 160
Cdd:pfam00753  81 LLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGilgGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLD 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 580096379  161 LYKGDYETLVDSIQ-------DKIFELEGDLpLFPGH 190
Cdd:pfam00753 161 LPLGGLLVLHPSSAessleslLKLAKLKAAV-IVPGH 196
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 16-190 8.12e-34

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: 118.33  E-value: 8.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  16 YFIEND--KAVILIDPsGESEKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRF-DVPVYMHEAE-FDFLKDPVKNG 91
Cdd:cd07723   12 YLIVDEatGEAAVVDP-GEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFpDAPVYGPAEDrIPGLDHPVKDG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  92 aDKFKqyglpiitskvtpeklnegsteIEGFKFNVLHTPGHSPGSLTYVFDEFAVV--GDTLFNNGIGRtdLYKGDYETL 169
Cdd:cd07723   91 -DEIK----------------------LGGLEVKVLHTPGHTLGHICYYVPDEPALftGDTLFSGGCGR--FFEGTAEQM 145

                        170       180
                 ....*....|....*....|.
gi 580096379 170 VDSIQdKIFELEGDLPLFPGH 190
Cdd:cd07723  146 YASLQ-KLLALPDDTLVYCGH 165
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 13-191 2.05e-33

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: 117.50  E-value: 2.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  13 TNTYFI---ENDKAVIlIDPSGES-EKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHE---AEFDFLk 85
Cdd:cd07724   12 TLSYLVgdpETGEAAV-IDPVRDSvDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGEgapASFFDR- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  86 dPVKNGadkfkqyglpiitskvtpEKLNEGSTEIEgfkfnVLHTPGHSPGSLTYVFDE--FAVVGDTLFNNGIGRTDLY- 162
Cdd:cd07724   90 -LLKDG------------------DVLELGNLTLE-----VLHTPGHTPESVSYLVGDpdAVFTGDTLFVGDVGRPDLPg 145

                        170       180       190
                 ....*....|....*....|....*....|.
gi 580096379 163 --KGDYETLVDSIQDKIFELEGDLPLFPGHG 191
Cdd:cd07724  146 eaEGLARQLYDSLQRKLLLLPDETLVYPGHD 176
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 13-152 9.68e-21

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 85.27  E-value: 9.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  13 TNT-YFIENDKAVILIDP-SGES--EKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFDFLKDPV 88
Cdd:cd07743    8 TNIgVYVFGDKEALLIDSgLDEDagRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAFIENPL 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 580096379  89 KNGADKFKQYGLPIITSKV---TPEK----LNEGSTEIEGFKFNVLHTPGHSPGSLTYVF-DEFAVVGDTLF 152
Cdd:cd07743   88 LEPSYLGGAYPPKELRNKFlmaKPSKvddiIEEGELELGGVGLEIIPLPGHSFGQIGILTpDGVLFAGDALF 159
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 13-192 8.96e-18

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: 77.15  E-value: 8.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  13 TNTYFIENDKAVILIDPSGESEK----IIKKLnqINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFDFLKDPV 88
Cdd:cd16278   18 TNTYLLGAPDGVVVIDPGPDDPAhldaLLAAL--GGGRVSAILVTHTHRDHSPGAARLAERTGAPVRAFGPHRAGGQDTD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  89 KNGAdkfkqyglpiitskvtpEKLNEGST-EIEGFKFNVLHTPGHSPGSLTYVFDEFAVV--GDTLFnnGIGRT------ 159
Cdd:cd16278   96 FAPD-----------------RPLADGEViEGGGLRLTVLHTPGHTSDHLCFALEDEGALftGDHVM--GWSTTviappd 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 580096379 160 -DLykGDY-ETLvdsiqDKIFELEGDLpLFPGHGP 192
Cdd:cd16278  157 gDL--GDYlASL-----ERLLALDDRL-LLPGHGP 183
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 9-142 1.01e-17

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: 78.40  E-value: 1.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379   9 GLVDTNTYFIENDKAVILIDP--SGESEKII----KKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFD 82
Cdd:cd16280   18 GNKWVSAWAIDTGDGLILIDAlnNNEAADLIvdglEKLGLDPADIKYILITHGHGDHYGGAAYLKDLYGAKVVMSEADWD 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 580096379  83 FLKDPVKNGADKFkqYGLPIITSKVTP--EKLNEGSTEIEgfkfnVLHTPGHSPGSLTYVFD 142
Cdd:cd16280   98 MMEEPPEEGDNPR--WGPPPERDIVIKdgDTLTLGDTTIT-----VYLTPGHTPGTLSLIFP 152
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 13-192 6.07e-17

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: 75.26  E-value: 6.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  13 TNTYFIENDKAVILIDPSGESEKIIKKLNQI-----NKPLKAILLTHAHFDHIGAVDDIVDRF---DVPVYMHeaefdfl 84
Cdd:cd07722   18 TNTYLVGTGKRRILIDTGEGRPSYIPLLKSVldsegNATISDILLTHWHHDHVGGLPDVLDLLrgpSPRVYKF------- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  85 kdpvkngadKFKQYGLPIITSKVTPEKLNEGST-EIEGFKFNVLHTPGHSPGSLTYVFDEFAVV--GDTLFNNGigrT-- 159
Cdd:cd07722   91 ---------PRPEEDEDPDEDGGDIHDLQDGQVfKVEGATLRVIHTPGHTTDHVCFLLEEENALftGDCVLGHG---Tav 158

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 580096379 160 --DLYkgdyeTLVDSIQdKIFELEGDLpLFPGHGP 192
Cdd:cd07722  159 feDLA-----AYMASLK-KLLSLGPGR-IYPGHGP 186
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 12-190 1.73e-16

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: 73.82  E-value: 1.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  12 DTNTYFIENDKAVILID---PSGESEKIIKKLNqiNKPLKAILlTHAHFDHIGAVDDivdrFDvPVYMHEAEFDFLKDPv 88
Cdd:cd07712    8 RVNIYLLRGRDRALLIDtglGIGDLKEYVRTLT--DLPLLVVA-THGHFDHIGGLHE----FE-EVYVHPADAEILAAP- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  89 KNGADKFKQYGLPIITSKVTPEKLNEGsTEIE--GFKFNVLHTPGHSPGSLTyVFDE---FAVVGDTlFNNGIGRTDLYK 163
Cdd:cd07712   79 DNFETLTWDAATYSVPPAGPTLPLRDG-DVIDlgDRQLEVIHTPGHTPGSIA-LLDRanrLLFSGDV-VYDGPLIMDLPH 155

                        170       180
                 ....*....|....*....|....*...
gi 580096379 164 GDYETLVDSIQdKIFELEGDLP-LFPGH 190
Cdd:cd07712  156 SDLDDYLASLE-KLSKLPDEFDkVLPGH 182
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 12-200 2.39e-15

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 71.44  E-value: 2.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  12 DTNTYFIENDKAVILIDPSG---ESEKIIKKLNQI-NKPLKAILLTHAHFDHIG---AVDDIvdrfDVPVYMHEAEFDFL 84
Cdd:cd16282   14 ISNIGFIVGDDGVVVIDTGAsprLARALLAAIRKVtDKPVRYVVNTHYHGDHTLgnaAFADA----GAPIIAHENTREEL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  85 KDPVKNGADKFKQYGLPII--TSKVTPEKLNEGSTEIE--GFKFNVLHT-PGHSPGSLTyVFDE-----FAvvGDTLFNN 154
Cdd:cd16282   90 AARGEAYLELMRRLGGDAMagTELVLPDRTFDDGLTLDlgGRTVELIHLgPAHTPGDLV-VWLPeegvlFA--GDLVFNG 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 580096379 155 GIGRTDlyKGDYETLVDSIqDKIFELEGDLpLFPGHGPYTTVDDEQ 200
Cdd:cd16282  167 RIPFLP--DGSLAGWIAAL-DRLLALDATV-VVPGHGPVGDKADLR 208
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 4-190 2.49e-15

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 72.95  E-value: 2.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379   4 SSLTLGLV----DTNTYFI--ENDKAVILIDPSgESEKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVymh 77
Cdd:PLN02398  74 SSLQIELVpclkDNYAYLLhdEDTGTVGVVDPS-EAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKV--- 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  78 eaefdflkdpVKNGADKFKQYGLPIItskvtpekLNEGSTEI-EGFKFNVLHTPGHSPGSLTYVFDEFAVV--GDTLFNN 154
Cdd:PLN02398 150 ----------IGSAVDKDRIPGIDIV--------LKDGDKWMfAGHEVLVMETPGHTRGHISFYFPGSGAIftGDTLFSL 211

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 580096379 155 GIGRtdLYKGDYETLVDSIQdKIFELEGDLPLFPGH 190
Cdd:PLN02398 212 SCGK--LFEGTPEQMLSSLQ-KIISLPDDTNIYCGH 244
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 10-191 1.37e-14

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 68.86  E-value: 1.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  10 LVDTNTYFIENDKAVILID---PSGESEKIIK--------KLNQINKplkaILLTHAHFDHIGAVDDIVDRFDVPVYMHE 78
Cdd:cd07725   12 LGHVNVYLLRDGDETTLIDtglATEEDAEALWeglkelglKPSDIDR----VLLTHHHPDHIGLAGKLQEKSGATVYILD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  79 AEfdflkdPVKNGadkfkqyglpiitskvtpEKLNEGSTEIEgfkfnVLHTPGHSPGSLTYVFDE--FAVVGDTLFN--- 153
Cdd:cd07725   88 VT------PVKDG------------------DKIDLGGLRLK-----VIETPGHTPGHIVLYDEDrrELFVGDAVLPkit 138

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 580096379 154 -NGIGRTDLYKGDYETLVDSIqDKIFELEGDLpLFPGHG 191
Cdd:cd07725  139 pNVSLWAVRVEDPLGAYLESL-DKLEKLDVDL-AYPGHG 175
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 11-156 2.48e-14

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: 69.11  E-value: 2.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  11 VDTNTYFIENDKAVILIDpSGESEKIIKKLNQINKPLKA----------ILLTHAHFDHIG--AVDDIVDRFdvP---VY 75
Cdd:cd07720   47 TSVNAFLVRTGGRLILVD-TGAGGLFGPTAGKLLANLAAagidpediddVLLTHLHPDHIGglVDAGGKPVF--PnaeVH 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  76 MHEAEFDF-LKDPVKNGADKFKQYGLPIITSKVTP----EKLNEGSTEIEGFKfnVLHTPGHSPGSLTYVF----DEFAV 146
Cdd:cd07720  124 VSEAEWDFwLDDANAAKAPEGAKRFFDAARDRLRPyaaaGRFEDGDEVLPGIT--AVPAPGHTPGHTGYRIesggERLLI 201

                        170
                 ....*....|
gi 580096379 147 VGDTLFNNGI 156
Cdd:cd07720  202 WGDIVHHPAL 211
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 19-183 2.87e-14

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 69.08  E-value: 2.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  19 ENDKAVILIDPsGESEKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRF-DVPVYmheaefdflkdpvkngadkfkq 97
Cdd:PRK10241  19 DEAGRCLIVDP-GEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFpQIVVY---------------------- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  98 yGLPIITSKVTPEKLNEGST-EIEGFKFNVLHTPGHSPGSLTYVFDEFAVVGDTLFNNGIGRtdLYKGDYETLVDSIQdK 176
Cdd:PRK10241  76 -GPQETQDKGTTQVVKDGETaFVLGHEFSVFATPGHTLGHICYFSKPYLFCGDTLFSGGCGR--LFEGTASQMYQSLK-K 151


                 ....*..
gi 580096379 177 IFELEGD 183
Cdd:PRK10241 152 INALPDD 158
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 11-190 5.80e-14

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: 68.01  E-value: 5.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  11 VDTNTYFIENDKAVILIDpSGESEKIIKK---------------------LNQIN-KP--LKAILLTHAHFDHIGAvddi 66
Cdd:cd07729   30 LPVYAYLIEHPEGTILVD-TGFHPDAADDpgglelafppgvteeqtleeqLARLGlDPedIDYVILSHLHFDHAGG---- 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  67 VDRF-DVPVYMHEAEFDFLKDPVknGADKFKQYGLPIITSKVTPEKLN--EGSTEIEGfKFNVLHTPGHSPGSL------ 137
Cdd:cd07729  105 LDLFpNATIIVQRAELEYATGPD--PLAAGYYEDVLALDDDLPGGRVRlvDGDYDLFP-GVTLIPTPGHTPGHQsvlvrl 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 580096379 138 ---TYVFdefavVGDTLF---NNGIGRTDLYKGDYETLVDSIqDKIFELEGDLP--LFPGH 190
Cdd:cd07729  182 pegTVLL-----AGDAAYtyeNLEEGRPPGINYDPEAALASL-ERLKALAEREGarVIPGH 236
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 15-150 1.44e-13

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: 66.75  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  15 TYFIENDKAVILIDPSGES--EKIIKKLNQINKP---LKAILLTHAHFDHIGAVDDIVDRF-DVPVYMHEAEFDFLKDPV 88
Cdd:cd07726   18 SYLLDGEGRPALIDTGPSSsvPRLLAALEALGIApedVDYIILTHIHLDHAGGAGLLAEALpNAKVYVHPRGARHLIDPS 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 580096379  89 K--NGA-----DKFKQYGLPIIT---SKVTP----EKLNEGSTEIEgfkfnVLHTPGHSPGSLTYVFDEFAVV--GDT 150
Cdd:cd07726   98 KlwASAravygDEADRLGGEILPvpeERVIVledgETLDLGGRTLE-----VIDTPGHAPHHLSFLDEESDGLftGDA 170
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 8-142 1.54e-13

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


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 67.11  E-value: 1.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379   8 LGLVDTNTYFIENDKAVILIDPS-GESEKIIKK----LNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFD 82
Cdd:cd16308   17 VGTYDLACYLIVTPKGNILINTGlAESVPLIKKniqaLGFKFKDIKILLTTQAHYDHVGAMAAIKQQTGAKMMVDEKDAK 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 580096379  83 FLKDpvkNGADKFKQYGLPIITSKVTPEKL--NEGSTEIEGFKFNVLHTPGHSPGSLTYVFD 142
Cdd:cd16308   97 VLAD---GGKSDYEMGGYGSTFAPVKADKLlhDGDTIKLGGTKLTLLHHPGHTKGSCSFLFD 155
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 13-150 3.59e-13

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 66.07  E-value: 3.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  13 TNTYFIENDKAVILIDPSGESEKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRF---DVPVYMHEAEFDFLKDPVK 89
Cdd:COG1235   35 RSSILVEADGTRLLIDAGPDLREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYgpnPIPVYATPGTLEALERRFP 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 580096379  90 ngadkfkqYGLPIITSKVTPEKLNEGST-EIEGFKFNVLHTPGHSPGSLTYVFDE----FAVVGDT 150
Cdd:COG1235  115 --------YLFAPYPGKLEFHEIEPGEPfEIGGLTVTPFPVPHDAGDPVGYRIEDggkkLAYATDT 172
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 13-205 3.23e-11

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 60.58  E-value: 3.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  13 TNTYFIEN----DKAVILIDPSGES-EKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRF-DVPVYMHEAEfdflkd 86
Cdd:PLN02962  23 TYTYLLADvshpDKPALLIDPVDKTvDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKLpGVKSIISKAS------ 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  87 pvKNGADKFKQYGlpiitskvtpEKLNEGSTEIEgfkfnVLHTPGHSPGSLTYVFDE--------FAVVGDTLFNNGIGR 158
Cdd:PLN02962  97 --GSKADLFVEPG----------DKIYFGDLYLE-----VRATPGHTAGCVTYVTGEgpdqpqprMAFTGDALLIRGCGR 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 580096379 159 TDLYKGDYETLVDSIQDKIFELEGDLPLFPGHG----PYTTVDDE-QLNPFL 205
Cdd:PLN02962 160 TDFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDykgfTVSTVGEEmLYNPRL 211
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 16-191 1.16e-10

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: 57.98  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  16 YFIENDKAVILIDPSGESEKIIKKLNQINKpLKAILLTHAHF--DHigavDDIVDRFDVPVYMHEAEFDFLKDPVKngad 93
Cdd:cd07727   18 YLILRPEGNILVDSPRYSPPLAKRIEALGG-IRYIFLTHRDDvaDH----AKWAERFGAKRIIHEDDVNAVTRPDE---- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  94 kfkqygLPIITSKVTPEkLNEGsteiegfkFNVLHTPGHSPGSLTYVFDE--FAVVGDTLF-----NNGIGRTDLYKGDY 166
Cdd:cd07727   89 ------VIVLWGGDPWE-LDPD--------LTLIPVPGHTRGSVVLLYKEkgVLFTGDHLAwsrrrGWLSAFRYVCWYSW 153

                        170       180
                 ....*....|....*....|....*...
gi 580096379 167 ETLVDSIQ---DKIFELegdlpLFPGHG 191
Cdd:cd07727  154 PEQAESVErlaDLDFEW-----VLPGHG 176
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 18-192 1.17e-10

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


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 58.37  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  18 IENDKAVILIDPSGES--EKIIKKLNQINkpLKA-----ILLTHAHFDHIGAVDDivdrF-DVPVYMHEAEFDFLKDPVk 89
Cdd:cd07711   27 IKDGGKNILVDTGTPWdrDLLLKALAEHG--LSPedidyVVLTHGHPDHIGNLNL----FpNATVIVGWDICGDSYDDH- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  90 ngadkfkqyglpiITSKVTPEKLNEGSTeiegfkfnVLHTPGHSPGSLTYVFDE-----FAVVGDtLFNNGIG-----RT 159
Cdd:cd07711  100 -------------SLEEGDGYEIDENVE--------VIPTPGHTPEDVSVLVETekkgtVAVAGD-LFEREEDledpiLW 157

                        170       180       190
                 ....*....|....*....|....*....|...
gi 580096379 160 DLYKGDYETLVDSIQdKIFELeGDLpLFPGHGP 192
Cdd:cd07711  158 DPLSEDPELQEESRK-RILAL-ADW-IIPGHGP 187
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 14-78 4.82e-10

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: 57.13  E-value: 4.82e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 580096379  14 NTYFIENDKAVILIDPsGES----EKIIKKLNQI--NKPLKAILLTHAHFDHIGAVDDIVDRFD---VPVYMHE 78
Cdd:cd07710   19 NMTFIEGDTGLIIIDT-LESaeaaKAALELFRKHtgDKPVKAIIYTHSHPDHFGGAGGFVEEEDsgkVPIIAPE 91
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 17-150 6.04e-10

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: 56.33  E-value: 6.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  17 FIENDKAVILIDPSGE-SEKIIKklNQINKpLKAILLTHAHFDHIGAVDDI-----VDRFDVPVYMHEAEFDFLKDPVKN 90
Cdd:cd16279   39 LIETGGKNILIDTGPDfRQQALR--AGIRK-LDAVLLTHAHADHIHGLDDLrpfnrLQQRPIPVYASEETLDDLKRRFPY 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 580096379  91 GADKFKQYGLPIITSKVTPEklnEGSTEIEGFK---FNVLHtpGHSPgSLTYVFDEFAVVGDT 150
Cdd:cd16279  116 FFAATGGGGVPKLDLHIIEP---DEPFTIGGLEitpLPVLH--GKLP-SLGFRFGDFAYLTDV 172
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 14-98 6.05e-10

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: 55.35  E-value: 6.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  14 NTYFIENDKAVILIDPSGESEKIIKKLNQIN-KP--LKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFDFLKDPVKN 90
Cdd:cd07733   10 NCTYLETEDGKLLIDAGLSGRKITGRLAEIGrDPedIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTLRAMERKVGL 89


                 ....*...
gi 580096379  91 GADKFKQY 98
Cdd:cd07733   90 IDVDQKQI 97
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 18-154 1.53e-09

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


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 55.20  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  18 IENDKAVILIDP---SGESEKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRF-DVPVY--------MHEAefdflK 85
Cdd:cd07739   21 IYGETEAVLVDAqftRADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAFpDAKVVatpavvahIKAQ-----L 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 580096379  86 DPVKNGADKFKQYGLPiiTSKVTPEKLNEGSTEIEGFKFNVLHTPGHSPGSLTYVF--DEFAVV-GDTLFNN 154
Cdd:cd07739   96 EPKLAFWGPLLGGNAP--ARLVVPEPLDGDTLTLEGHPLEIVGVGGGDTDDTTYLWipSLKTVVaGDVVYNG 165
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 10-194 1.85e-09

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 55.92  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  10 LVDTNTYFI--ENDKAVILIDPSgESEKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRF-DVPVYmhEAEFDFLK- 85
Cdd:PLN02469   9 LEDNYAYLIidESTKDAAVVDPV-DPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVpGIKVY--GGSLDNVKg 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  86 --DPVKNGAdkfkqyglpiitskvtpeKLNEGSTeiegFKFNVLHTPGHSPGSLTYVF-----DEFAV-VGDTLFNNGIG 157
Cdd:PLN02469  86 ctHPVENGD------------------KLSLGKD----VNILALHTPCHTKGHISYYVtgkegEDPAVfTGDTLFIAGCG 143

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 580096379 158 RtdLYKGDYETLVDSIQDKIFELEGDLPLFPGHgPYT 194
Cdd:PLN02469 144 K--FFEGTAEQMYQSLCVTLGSLPKPTQVYCGH-EYT 177
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 17-137 4.28e-09

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: 53.68  E-value: 4.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  17 FIENDKAVILID----PSGESEKIIKKLNQIN-KPLKAILLTHAHFDHIGAVDDIVDRFDV-PVYMHEAEFDflKDPVKN 90
Cdd:cd07731   14 LIQTPGKTILIDtgprDSFGEDVVVPYLKARGiKKLDYLILTHPDADHIGGLDAVLKNFPVkEVYMPGVTHT--TKTYED 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 580096379  91 GADKFKQYGLPIITSKvtpeklnEGST-EIEGFKFNVLHTPGHSPGSL 137
Cdd:cd07731   92 LLDAIKEKGIPVTPCK-------AGDRwQLGGVSFEVLSPPKDDYDDL 132
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
47-142 8.57e-09

mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 54.30  E-value: 8.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  47 LKAILLTHAHFDHIGAVDDIVDRFDVPVYMHE--AEFdflkdpVKNgadKFKQYGL----PIITskVTP-EKLNEGSTEI 119
Cdd:COG0595   64 IKGIVLTHGHEDHIGALPYLLKELNVPVYGTPltLAL------LEA---KLKEHGLlkkvKLHV--VKPgDRIKFGPFKV 132

                         90       100
                 ....*....|....*....|....
gi 580096379 120 EGFKFNvlhtpgHS-PGSLTYVFD 142
Cdd:COG0595  133 EFFRVT------HSiPDSLGLAIR 150
BDS1 COG2015
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary ...
 13-78 1.47e-08

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: 53.69  E-value: 1.47e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 580096379  13 TNTYFIENDKAVILIDP--SGESEKIIKKL-NQI--NKPLKAILLTHAHFDHIGAVDDIVDRFD-----VPVYMHE 78
Cdd:COG2015  103 ANMTFIEGDTGWIVIDPltSVETAAAALALyRKHlgDRPVKAVIYTHSHVDHFGGVRGVVDEEDvksgkVPIIAPE 178
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 11-143 1.08e-07

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


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 50.56  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  11 VDTNTYFIENDKAViLIDPSGES--EKIIKKLNQINKP--LKAILLTHAHFDHIGAVDDIVDRF-DVPVYMHEAEFDFLK 85
Cdd:cd07709   30 TSYNSYLIKDEKTA-LIDTVKEPffDEFLENLEEVIDPrkIDYIVVNHQEPDHSGSLPELLELApNAKIVCSKKAARFLK 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 580096379  86 DPVKNGADKFKqyglpIITSKvtpEKLNEGSTEiegFKFnvLHTPG-HSPGSLtYVFDE 143
Cdd:cd07709  109 HFYPGIDERFV-----VVKDG---DTLDLGKHT---LKF--IPAPMlHWPDTM-VTYDP 153
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 14-75 1.23e-07

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. 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: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 50.48  E-value: 1.23e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 580096379  14 NTYFIENDKAVILID-----PSGES---EKII---KKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVY 75
Cdd:cd07714   12 NMYVVEYDDDIIIIDcglkfPDEDMpgvDYIIpdfSYLEENKDKIKGIFITHGHEDHIGALPYLLPELNVPIY 84
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 50-151 1.45e-07

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 49.83  E-value: 1.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  50 ILLTHAHFDHIG----AVDDIVdrfdVP------VYMHEAEFDFLKDPVKNGADKFKQYG---LPIITSKVTpeKLNEGS 116
Cdd:cd16277   67 VLCTHLHVDHVGwntrLVDGRW----VPtfpnarYLFSRAEYDHWSSPDAGGPPNRGVFEdsvLPVIEAGLA--DLVDDD 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 580096379 117 TEI-EGFKFnvLHTPGHSPGSLTYVF----DEFAVVGDTL 151
Cdd:cd16277  141 HEIlDGIRL--EPTPGHTPGHVSVELesggERALFTGDVM 178
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 9-142 1.88e-07

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


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 50.01  E-value: 1.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379   9 GLVDTNTYFIENDKAVILIDPSGES-----EKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFDF 83
Cdd:cd16288   18 GTSGLASYLITTPQGLILIDTGLESsapmiKANIRKLGFKPSDIKILLNSHAHLDHAGGLAALKKLTGAKLMASAEDAAL 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 580096379  84 LKDpvknGADKFKQYGLPIIT-SKVTPEKL--NEGSTEIEGFKFNVLHTPGHSPGSLTYVFD 142
Cdd:cd16288   98 LAS----GGKSDFHYGDDSLAfPPVKVDRVlkDGDRVTLGGTTLTAHLTPGHTRGCTTWTMT 155
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 8-139 4.75e-07

metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B3 MBLs include Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Stenotrophomonas Maltophilia L1, and Bradyrhizobium diazoefficiens BJP-1, Serratia marcescens SMB-1, and Pseudomonas Aeruginosa AIM-1. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 48.70  E-value: 4.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379   8 LGLVDTNTYFIENDKAVILIDpsGESEKI-------IKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAE 80
Cdd:cd07708   17 VGTDDLAAYLIVTPQGNILID--GDMEQNapmikanIKKLGFKFSDTKLILISHAHFDHAGGSAEIKKQTGAKVMAGAED 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  81 FDFLKDPVKNGADKFKQYGLPIITSKVTpEKLNEGS-TEIEGFKFNVLHTPGHSPGSLTY 139
Cdd:cd07708   95 VSLLLSGGSSDFHYANDSSTYFPQSTVD-RAVHDGErVTLGGTVLTAHATPGHTPGCTTW 153
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
16-164 5.19e-07

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 48.65  E-value: 5.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  16 YFIENDKAVILIDPsGES-----EKIIKKLNQINkplkAILLTHAHFDHIGAVDDIVDRF-------DVPVYMHEAEFDF 83
Cdd:COG1234   22 YLLEAGGERLLIDC-GEGtqrqlLRAGLDPRDID----AIFITHLHGDHIAGLPGLLSTRslagrekPLTIYGPPGTKEF 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  84 LkDPVKNGADKFKQYGLPIITskvtpekLNEGST-EIEGFKFNVLHTPgHSPGSLTYVFDE----FAVVGDTLFNNGIgr 158
Cdd:COG1234   97 L-EALLKASGTDLDFPLEFHE-------IEPGEVfEIGGFTVTAFPLD-HPVPAYGYRFEEpgrsLVYSGDTRPCEAL-- 165


                 ....*.
gi 580096379 159 TDLYKG 164
Cdd:COG1234  166 VELAKG 171
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 8-163 5.46e-07

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: 48.89  E-value: 5.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379    8 LGLVDTNTYFIENDKAVILID-----PSGE---SEKIIKK---LNQINKPLKAILLTHAHFDHIGAVDDIVDRFDV-PVY 75
Cdd:TIGR00649   9 LGEIGKNMYVVEIDDEIVIFDagilfPEDEmlgVDGVIPDftyLQENEDKVKGIFITHGHEDHIGAVPYLLHQVGFfPIY 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379   76 MHEAEFDFLKdpvkngaDKFKQYGLPIITSKVTPEKLN----EGSTEIEGFKFN---------VLHTPghsPGSLTYV-- 140
Cdd:TIGR00649  89 GTPLTIALIK-------SKIKEHGLNVRTDLLEIHEGEpvefGENTAIEFFRIThsipdsvgfALHTP---LGYIVYTgd 158

                         170       180
                  ....*....|....*....|....*
gi 580096379  141 --FDEFAVVGDtlfnngigRTDLYK 163
Cdd:TIGR00649 159 fkFDNTPVIGE--------PPDLNR 175
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 16-85 5.52e-07

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: 47.84  E-value: 5.52e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 580096379  16 YFIENDKAVILID------PSGESEKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDR-FDVPVYMHEAEFDFLK 85
Cdd:cd16295   15 YLLETGGKRILLDcglfqgGKELEELNNEPFPFDPKEIDAVILTHAHLDHSGRLPLLVKEgFRGPIYATPATKDLAE 91
NorV COG0426
Flavorubredoxin [Energy production and conversion];
11-139 5.63e-07

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 49.06  E-value: 5.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  11 VDTNTYFIENDKaVILIDPSGES--EKIIKKLNQINKP--LKAILLTHAHFDHIGAVDDIVDRF-DVPVYMHEAEFDFLK 85
Cdd:COG0426   32 TTYNSYLIVDEK-TALIDTVGESffEEFLENLSKVIDPkkIDYIIVNHQEPDHSGSLPELLELApNAKIVCSKKAARFLP 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 580096379  86 DpvkngadkfkQYGLPIITSKVTPE--KLNEGSTEiegFKFnvLHTPG-HSPGSL-TY 139
Cdd:COG0426  111 H----------FYGIPDFRFIVVKEgdTLDLGGHT---LQF--IPAPMlHWPDTMfTY 153
PRK02113 PRK02113
MBL fold metallo-hydrolase;
18-123 7.89e-07

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 48.24  E-value: 7.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  18 IENDKAVILID--PSGESEKIIKKLnqinKPLKAILLTHAHFDHIGAVDDI--VDRF-DVPVYMHEAEFDFLKDPVKNGA 92
Cdd:PRK02113  40 VETEGARILIDcgPDFREQMLRLPF----GKIDAVLITHEHYDHVGGLDDLrpFCRFgEVPIYAEQYVAERLRSRMPYCF 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 580096379  93 DKFKQYGLPIIT--------------SKVTPEKLNEGSTEIEGFK 123
Cdd:PRK02113 116 VEHSYPGVPNIPlreiepdrpflvnhTEVTPLRVMHGKLPILGYR 160
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 14-152 9.82e-07

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 47.60  E-value: 9.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  14 NTYFIENDKAVILIDP--SGESEKIIKKLNQINK--PLKAILLTHAHFDHIG-AVDDIVDRFDVPVYMHEAefdflkdpv 88
Cdd:COG2220   12 ATFLIETGGKRILIDPvfSGRASPVNPLPLDPEDlpKIDAVLVTHDHYDHLDdATLRALKRTGATVVAPLG--------- 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 580096379  89 knGADKFKQYGLPIITSkvtpekLNEG-STEIEGFKFNVL---HTPGHSPGSLT----YVFDE----FAVVGDTLF 152
Cdd:COG2220   83 --VAAWLRAWGFPRVTE------LDWGeSVELGGLTVTAVparHSSGRPDRNGGlwvgFVIETdgktIYHAGDTGY 150
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-133 1.22e-06

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 46.81  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  14 NTYFIENDKAVILID-PSGESEKIIKKLNQI-NKPLKAILLTHAHFDHIGAVDDIVDRfDVPVYMHEAEFDFLKdpvkng 91
Cdd:cd16276   11 QSMFLVTDKGVIVVDaPPSLGENLLAAIRKVtDKPVTHVVYSHNHADHIGGASIFKDE-GATIIAHEATAELLK------ 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 580096379  92 adKFKQYGLPIITSKVTPEK-LNEGSTEIE--GFKFNvlHTPGHS 133
Cdd:cd16276   84 --RNPDPKRPVPTVTFDDEYtLEVGGQTLElsYFGPN--HGPGNI 124
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 12-153 1.80e-06

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: 46.49  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  12 DTNTYFIENDKAVILID-PSGESEKIIKKLNQINKpLKAILLTHAHFDHIgavddivdrFDVPVYMHEAEFDFLKDPV-- 88
Cdd:cd16272   16 NTSSYLLETGGTRILLDcGEGTVYRLLKAGVDPDK-LDAIFLSHFHLDHI---------GGLPTLLFARRYGGRKKPLti 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 580096379  89 ------KNGADKFKQYGLPI--ITSKVTPEKLNEGSTEIEGFKFNVLHTPG-HSPGSLTYVFDE----FAVVGDTLFN 153
Cdd:cd16272   86 ygpkgiKEFLEKLLNFPVEIlpLGFPLEIEELEEGGEVLELGDLKVEAFPVkHSVESLGYRIEAegksIVYSGDTGPC 163
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 16-120 2.00e-06

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. 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: 293799  Cd Length: 269  Bit Score: 46.85  E-value: 2.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  16 YFIENDKAVILIDpSGESEKIIKKLNQINKPLK---AILLTHAHFDHIGAVDDIVDRF-DVPVYMHEAEF-------DFL 84
Cdd:cd07713   23 LLIETEGKKILFD-TGQSGVLLHNAKKLGIDLSdidAVVLSHGHYDHTGGLKALLELNpKAPVYAHPDAFepryskrGGG 101

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 580096379  85 KDPVKNGADKFKQYGLPIITSKvTPEKLNEG---STEIE 120
Cdd:cd07713  102 KKGIGIGREELEKAGARLVLVE-EPTEIAPGvylTGEIP 139
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-85 2.00e-06

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 47.49  E-value: 2.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379   1 MRISSLtlGLVDTNT---YFIENDKAVILIDP---SGESEKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDR-FDVP 73
Cdd:COG1236    1 MKLTFL--GAAGEVTgscYLLETGGTRILIDCglfQGGKERNWPPFPFRPSDVDAVVLTHAHLDHSGALPLLVKEgFRGP 78

                         90
                 ....*....|..
gi 580096379  74 VYMHEAEFDFLK 85
Cdd:COG1236   79 IYATPATADLAR 90
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
16-120 2.80e-06

Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440850  Cd Length: 273  Bit Score: 46.41  E-value: 2.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  16 YFIENDKAVILIDpSGESEKIIKKLNQINKPLK---AILLTHAHFDHIGAVDDIVDRF-DVPVYMHEAEFD--FLKDPVK 89
Cdd:COG1237   25 ALIETEGKRILFD-TGQSDVLLKNAEKLGIDLSdidAVVLSHGHYDHTGGLPALLELNpKAPVYAHPDAFEkrYSKRPGG 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 580096379  90 NGA------DKFKQYGLPIITSKvTPEKLNEG---STEIE 120
Cdd:COG1237  104 KYIgipfsrEELEKLGARLILVK-EPTEIAPGvylTGEIP 142
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 44-85 4.13e-06

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. 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: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 45.68  E-value: 4.13e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 580096379  44 NKPLKAILLTHAHFDHIGAVDDIvdRFDVPVYMHEAEFDFLK 85
Cdd:cd07732   73 DPSVDAVLLSHAHLDHYGLLNYL--RPDIPVYMGEATKRILK 112
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-137 4.27e-06

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


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 46.11  E-value: 4.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  48 KAILLTHAHFDHIGAVDDIvdrFDVPVYMHEAEFDFLKDP-VKNGADKfkqyglPIITS-----KVTPEKLNEGSTEIEG 121
Cdd:cd07730   85 DAVILSHLHWDHIGGLSDF---PNARLIVGPGAKEALRPPgYPSGFLP------ELLPSdfegrLVRWEEDDFLWVPLGP 155

                         90       100
                 ....*....|....*....|....*.
gi 580096379 122 FK-----FN-----VLHTPGHSPGSL 137
Cdd:cd07730  156 FPraldlFGdgslyLVDLPGHAPGHL 181
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 21-136 1.60e-05

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 44.08  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  21 DKAVILID-----PSGESEKIIK---KLNQINKpLKAILLTHAHFDHIGAVDDIVDRFDV-PVYMHEAEFDflKDPVKNG 91
Cdd:COG2333   20 DGKTILIDtgprpSFDAGERVVLpylRALGIRR-LDLLVLTHPDADHIGGLAAVLEAFPVgRVLVSGPPDT--SETYERL 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 580096379  92 ADKFKQYGLPIITskvtpekLNEGST-EIEGFKFNVLHTPGHSPGS 136
Cdd:COG2333   97 LEALKEKGIPVRP-------CRAGDTwQLGGVRFEVLWPPEDLLEG 135
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 9-134 2.05e-05

metallo-beta-lactamases, subclass B1; 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. Includes 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.


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 43.81  E-value: 2.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379   9 GLVDTNTYFIENDKAVILIDPSGESEKIIKKLN----QINKPLKAILLTHAHFDHIGAVDDIVDRfDVPVYMHEAEFDFL 84
Cdd:cd16285   22 GAVPSNGLIVIDGKGLVLIDTPWTEAQTATLLDwiekKLGKPVTAAISTHSHDDRTGGIKALNAR-GIPTYATALTNELA 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 580096379  85 KdpvKNGadkfkqyglpiitsKVTPEKLNEGSTEIEGFKFNVLHT-PGHSP 134
Cdd:cd16285  101 K---KEG--------------KPVPTHSLKGALTLGFGPLEVFYPgPGHTP 134
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 25-79 3.55e-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: 42.68  E-value: 3.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 580096379   25 ILIDPS----GESEKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEA 79
Cdd:pfam12706   3 ILIDPGpdlrQQALPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLG 61
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 14-205 4.04e-05

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


Pssm-ID: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 43.05  E-value: 4.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  14 NTYFIEND--KAVILIDPSGE----------SEKIIKKLNQIN---KPLKAILLTHAHFDHIGAVDDIvDRFDVPVYMHE 78
Cdd:cd16312   13 NTWYVGTAglSAVLVTSPQGHvlldgalpqsAPLIIANIEALGfriEDVKLILNSHAHWDHAGGIAAL-QKASGATVAAS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  79 AEFDFLKDPVKNGADKFKQYGLPII-TSKVTPEKL-NEGST-EIEGFKFNVLHTPGHSPGSLTYVFDEF-------AVVG 148
Cdd:cd16312   92 AHGAQVLQSGTNGKDDPQYQAKPVVhVAKVAKVKEvGEGDTlKVGPLRLTAHMTPGHTPGGTTWTWTSCegqrcldVVYA 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 580096379 149 DTLfnNGIGRTDLY---KGDYETLVDSIQ---DKIFELEGDLpLFPGHGPYTTVDDE------QLNPFL 205
Cdd:cd16312  172 DSL--NPYSSGDFYytgKGGYPDISASFRasiAKVAALPCDI-IIAVHPGFTDVLDKakrrsgDTNPFI 237
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 11-122 1.69e-04

Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Bacillus cereus Beta-lactamase 2, also called BcII. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. BcII is a chromosome-encoded B1 MBL. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293862 [Multi-domain]  Cd Length: 212  Bit Score: 41.12  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  11 VDTNTYFIENDKAVILID-PSGES--EKIIKKL-NQINKPLKAILLTHAHFDHIGAVDDIVDRfDVPVYmheaefdflkd 86
Cdd:cd16304   24 VPSNGLIVETSKGVVLIDtPWDDEqtEELLDWIkKKLKKPVTLAIVTHAHDDRIGGIKALQKR-GIPVY----------- 91

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 580096379  87 PVKNGADKFKQYGLP---IITSKVTpeKLNEGSTEIEGF 122
Cdd:cd16304   92 STKLTAQLAKKQGYPspdGILKDDT--TLKFGNTKIETF 128
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 15-139 2.27e-04

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


Pssm-ID: 293868  Cd Length: 252  Bit Score: 40.90  E-value: 2.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  15 TYFIENDKAVILIDPSGES-----EKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFDFLKDPVK 89
Cdd:cd16310   24 SYLITSNHGAILLDGGLEEnaaliEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQLKADTGAKLWASRGDRPALEAGKH 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 580096379  90 NGADKFkqYGLPIITSKVTpEKLNEGST-EIEGFKFNVLHTPGHSPGSLTY 139
Cdd:cd16310  104 IGDNIT--QPAPFPAVKVD-RILGDGEKiKLGDITLTATLTPGHTKGCTTW 151
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 47-139 4.39e-04

Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of L1- and Pom-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293847  Cd Length: 239  Bit Score: 39.80  E-value: 4.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  47 LKAILLTHAHFDHIGAVDDIVDRFDVPVyMHEAEFDFLKdpVKNGADKFkQYGLPIITSKVTPEK-LNEGST-EIEGFKF 124
Cdd:cd16289   61 LKLILHSHAHADHAGPLAALKRATGARV-AANAESAVLL--ARGGSDDI-HFGDGITFPPVQADRiVMDGEVvTLGGVTF 136

                         90
                 ....*....|....*
gi 580096379 125 NVLHTPGHSPGSLTY 139
Cdd:cd16289  137 TAHFTPGHTPGSTSW 151
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 50-82 4.94e-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) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 39.92  E-value: 4.94e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 580096379  50 ILLTHAHFDHIGAVDDivdrF-DVPVYMHEAEFD 82
Cdd:cd07742   84 IVLTHLDLDHAGGLAD----FpHATVHVHAAELD 113
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 50-135 1.34e-03

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. 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: 293814  Cd Length: 249  Bit Score: 38.39  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  50 ILLTHAHFDHIGAVDDIVDRFDVPV------YMHEAEFDFLKDPVKNGADKFKQYGLPIITSKVTPeklNEGSTEI-EGF 122
Cdd:cd07728   99 VLMTHLHFDHASGLTKVKGEQLVSVfpnatiYVSEIEWEEMRNPNIRSKNTYWKENWEPIEDQVKT---FSDEIEIvPGI 175

                         90
                 ....*....|...
gi 580096379 123 KFnvLHTPGHSPG 135
Cdd:cd07728  176 TM--IHTGGHSDG 186
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 25-136 2.27e-03

Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; CPSF3 (cleavage and polyadenylation specificity factor subunit 3; also known as cleavage and polyadenylation specificity factor 73 kDa subunit, CPSF-73) and CPSF2 (also known as cleavage and polyadenylation specificity factor 100 kDa subunit /CPSF-100) are components of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. CPSF3 functions as a 3' endonuclease. Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)), and Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74) are subunits of Integrator, a metazoan-specific multifunctional protein complex composed of 14 subunits. Integrator has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. 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: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 37.70  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  25 ILIDP-----SGESEKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIV--DRFDVPVYMHEAEFDF----LKDPVKNGAD 93
Cdd:cd07734   23 VLLDCgmnpgKEDPEACLPQFELLPPEIDAILISHFHLDHCGALPYLFrgFIFRGPIYATHPTVALgrllLEDYVKSAER 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 580096379  94 KFKQyglpiiTSKVTPEKLNEGSTEIEGFKFN-----------VLHTPGHSPGS 136
Cdd:cd07734  103 IGQD------QSLYTPEDIEEALKHIVPLGYGqsidlfpalslTAYNAGHVLGA 150
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 18-74 2.52e-03

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 37.48  E-value: 2.52e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 580096379  18 IENDKAVILIDP--SGeSEKIIKKLNQINkpLKAILLTHAHFDHIGAVDDIVDRFDVPV 74
Cdd:PRK00685  13 IETGGKKILIDPfiTG-NPLADLKPEDVK--VDYILLTHGHGDHLGDTVEIAKRTGATV 68
NDM_FIM-like_MBL-B1 cd16300
NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase ...
 9-64 2.60e-03

NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the ISCR-mediated MBLs NDM-1 (NDM (New Delhi metallo-beta-lactamase) and FIM-1 (Florence imipenemase). 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 MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293858  Cd Length: 214  Bit Score: 37.49  E-value: 2.60e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379   9 GLVDTNTYFIENDKAVILIDPS---GESEKIIKKLNQ-INKPLKAILLTHAHFDHIGAVD 64
Cdd:cd16300   23 GAVPSNGLIVRDGDRVLLVDTAwtdDQTAQILNWAKQeLNLPVRLAVVTHAHQDKMGGMD 82
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 37-76 5.53e-03

Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a metazoan-specific multisubunit, multifunctional protein complex composed of 14 subunits named Int1-Int14 (Integrator subunits). This subgroup includes Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)). Integrator complex has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. 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: 293849  Cd Length: 199  Bit Score: 36.47  E-value: 5.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 580096379  37 IKKLNQINKPLKAILLTHAHFDHIGAVDDIVDR--FDVPVYM 76
Cdd:cd16291   46 ISQNGPFTEHIDCVIISHFHLDHCGALPYFTEVvgYDGPIYM 87
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 12-141 7.16e-03

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


Pssm-ID: 293865  Cd Length: 255  Bit Score: 36.27  E-value: 7.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  12 DTNTYFIENDKAVILIDPSGES-----EKIIKKLNQINKPLKAILLTHAHFDHIGAVDDIVDRFDVPVYMHEAEFdflkD 86
Cdd:cd16307   21 DLASYLITTPRGNILINSNLESsvpqiKASIEKLGFKFSDTKILLISHAHFDHAAGSALIKRETHAKYMVMDGDV----D 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 580096379  87 PVKNGADKFKQYGLPIITsKVTPEK----LNEGST-EIEGFKFNVLHTPGHSPGSLTYVF 141
Cdd:cd16307   97 VVESGGKSDFFYGNDPST-YFPPAHvdkvLHDGEQvELGGTVLTAHLTAGHTKGCTTWTM 155
 
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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