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Conserved domains on  [gi|655192880|ref|WP_028618886|]
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MULTISPECIES: MBL fold metallo-hydrolase [Pseudomonas]

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; ...
 11-196 2.17e-68

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: 207.52  E-value: 2.17e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  11 ETFPVGPLQCNCTIIGDPiSKKAIVVDPG-GNHELILARLDALGLKVVSIIHTHAHLDHFLASGQLKEKTGATLHLHKED 89
Cdd:cd06262    1 KRLPVGPLQTNCYLVSDE-EGEAILIDPGaGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEAD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  90 QFLWDNLEMQCQMFRVPYIPVPSPDRWLEHDEELACGCG--VALHTPGHTPGSMSFWFADAKLLIAGDTLFRRGIGRTDL 167
Cdd:cd06262   80 AELLEDPELNLAFFGGGPLPPPEPDILLEDGDTIELGGLelEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDL 159

                        170       180
                 ....*....|....*....|....*....
gi 655192880 168 WGGDQATIVRSIKQRLYTLDEGATVVTGH 196
Cdd:cd06262  160 PGGDPEQLIESIKKLLLLLPDDTVVYPGH 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; ...
 11-196 2.17e-68

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: 207.52  E-value: 2.17e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  11 ETFPVGPLQCNCTIIGDPiSKKAIVVDPG-GNHELILARLDALGLKVVSIIHTHAHLDHFLASGQLKEKTGATLHLHKED 89
Cdd:cd06262    1 KRLPVGPLQTNCYLVSDE-EGEAILIDPGaGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEAD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  90 QFLWDNLEMQCQMFRVPYIPVPSPDRWLEHDEELACGCG--VALHTPGHTPGSMSFWFADAKLLIAGDTLFRRGIGRTDL 167
Cdd:cd06262   80 AELLEDPELNLAFFGGGPLPPPEPDILLEDGDTIELGGLelEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDL 159

                        170       180
                 ....*....|....*....|....*....
gi 655192880 168 WGGDQATIVRSIKQRLYTLDEGATVVTGH 196
Cdd:cd06262  160 PGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 9-212 2.47e-50

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: 162.55  E-value: 2.47e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880   9 IRETFPVGPLQCNCTIIGDPisKKAIVVDPGGN---HELILARLDALGLKVVSIIHTHAHLDHFLASGQLKEKTGATLHL 85
Cdd:COG0491    4 LPGGTPGAGLGVNSYLIVGG--DGAVLIDTGLGpadAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  86 HKEDQFLWDNLEMQcQMFRVPYIPvpsPDRWLEHDEELACGCG--VALHTPGHTPGSMSFWFADAKLLIAGDTLFRRGIG 163
Cdd:COG0491   82 HAAEAEALEAPAAG-ALFGREPVP---PDRTLEDGDTLELGGPglEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVG 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880 164 RTDLWGGDQATIVRSIkQRLYTLDEgATVVTGHGPDT---------RLGDEMRE--NPFV 212
Cdd:COG0491  158 RPDLPDGDLAQWLASL-ERLLALPP-DLVIPGHGPPTtaeaidyleELLAALGEraNPFL 215
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 21-196 5.81e-35

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: 121.89  E-value: 5.81e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880    21 NCTIIGDPisKKAIVVDPG-GNHELILARLDALGL-KVVSIIHTHAHLDHFLASGQLKEKTGATLHLHKEDQFLWDNLEM 98
Cdd:smart00849   1 NSYLVRDD--GGAILIDTGpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880    99 QCQMFRvPYIPVPSPDRWLEHDEELACGCG--VALHTPGHTPGSMSFWFADAKLLIAGDTLFRRGIGRTDLWGGDQATIV 176
Cdd:smart00849  79 LLGELG-AEAEPAPPDRTLKDGDELDLGGGelEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAASD 157

                          170       180
                   ....*....|....*....|
gi 655192880   177 RSIKQRLYTLDEGATVVTGH 196
Cdd:smart00849 158 ALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
15-196 3.75e-31

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 112.85  E-value: 3.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880   15 VGPLQCNCTIIGDPisKKAIVVDPGG----NHELILARLDALGLKVVSIIHTHAHLDHFLASGQLKEKTGATLHLHKEDQ 90
Cdd:pfam00753   1 LGPGQVNSYLIEGG--GGAVLIDTGGsaeaALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880   91 FLWDNLEMQCQMFRV------PYIPVPSPDRWLEHDEELACGCGVALHTPGHTPGSMSFWFADAKLLIAGDTLFRRGIGR 164
Cdd:pfam00753  79 RELLDEELGLAASRLglpgppVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGR 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 655192880  165 TDLWGGDQATIVRSIKQ------RLYTLDEGATVVTGH 196
Cdd:pfam00753 159 LDLPLGGLLVLHPSSAEssleslLKLAKLKAAVIVPGH 196
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 25-210 6.57e-13

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 65.59  E-value: 6.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  25 IGDPiSKKAIVVDP-GGNHELILARLDALGLKVVSIIHTHAHLDHFLASGQLKEK-------------TGATLHLHKEDQ 90
Cdd:PLN02962  31 VSHP-DKPALLIDPvDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKlpgvksiiskasgSKADLFVEPGDK 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  91 FLWDNLemqcqmfrvpYIPVPSpdrwlehdeelacgcgvalhTPGHTPGSMSFWFADA------KLLIAGDTLFRRGIGR 164
Cdd:PLN02962 110 IYFGDL----------YLEVRA--------------------TPGHTAGCVTYVTGEGpdqpqpRMAFTGDALLIRGCGR 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 655192880 165 TDLWGGDQATIVRSIKQRLYTLDEGATVVTGHgpDTR------LGDEMRENP 210
Cdd:PLN02962 160 TDFQGGSSDQLYKSVHSQIFTLPKDTLIYPAH--DYKgftvstVGEEMLYNP 209
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 11-196 2.17e-68

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: 207.52  E-value: 2.17e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  11 ETFPVGPLQCNCTIIGDPiSKKAIVVDPG-GNHELILARLDALGLKVVSIIHTHAHLDHFLASGQLKEKTGATLHLHKED 89
Cdd:cd06262    1 KRLPVGPLQTNCYLVSDE-EGEAILIDPGaGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEAD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  90 QFLWDNLEMQCQMFRVPYIPVPSPDRWLEHDEELACGCG--VALHTPGHTPGSMSFWFADAKLLIAGDTLFRRGIGRTDL 167
Cdd:cd06262   80 AELLEDPELNLAFFGGGPLPPPEPDILLEDGDTIELGGLelEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDL 159

                        170       180
                 ....*....|....*....|....*....
gi 655192880 168 WGGDQATIVRSIKQRLYTLDEGATVVTGH 196
Cdd:cd06262  160 PGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 11-196 4.07e-66

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: 202.01  E-value: 4.07e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  11 ETFPVGPLQCNCTIIGDPISKKAIVVDPGGNHELILARLDALGLKVVSIIHTHAHLDHFLASGQLKEKTGA-TLHLHKED 89
Cdd:cd07737    2 QIIPVTPFQQNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVpIIGPHKED 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  90 QFLWDNLEMQCQMFRVPYIPVPSPDRWLEHDEELACGCGV--ALHTPGHTPGSMSFWFADAKLLIAGDTLFRRGIGRTDL 167
Cdd:cd07737   82 KFLLENLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTleVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTDF 161

                        170       180
                 ....*....|....*....|....*....
gi 655192880 168 WGGDQATIVRSIKQRLYTLDEGATVVTGH 196
Cdd:cd07737  162 PGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 11-212 5.37e-61

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: 189.48  E-value: 5.37e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  11 ETFPVGPLQCNCTIIGDPISKKAIVVDPGGNHELILARLDALGLKVVSIIHTHAHLDHFLASGQLKEKTGATLHLHKEDQ 90
Cdd:cd16322    2 RPFTLGPLQENTYLVADEGGGEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  91 FLWDNLEMQCQMFRVPYIPVPSPDRWLEHDEELACGcGV---ALHTPGHTPGSMSFWFADAKLLIAGDTLFRRGIGRTDL 167
Cdd:cd16322   82 PLYEAADLGAKAFGLGIEPLPPPDRLLEDGQTLTLG-GLefkVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRTDL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 655192880 168 WGGDQATIVRSIKqRLYTLDEGATVVTGHGPDTRLGDEMRENPFV 212
Cdd:cd16322  161 PGGDPKAMAASLR-RLLTLPDETRVFPGHGPPTTLGEERRTNPFL 204
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 9-212 2.47e-50

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: 162.55  E-value: 2.47e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880   9 IRETFPVGPLQCNCTIIGDPisKKAIVVDPGGN---HELILARLDALGLKVVSIIHTHAHLDHFLASGQLKEKTGATLHL 85
Cdd:COG0491    4 LPGGTPGAGLGVNSYLIVGG--DGAVLIDTGLGpadAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  86 HKEDQFLWDNLEMQcQMFRVPYIPvpsPDRWLEHDEELACGCG--VALHTPGHTPGSMSFWFADAKLLIAGDTLFRRGIG 163
Cdd:COG0491   82 HAAEAEALEAPAAG-ALFGREPVP---PDRTLEDGDTLELGGPglEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVG 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880 164 RTDLWGGDQATIVRSIkQRLYTLDEgATVVTGHGPDT---------RLGDEMRE--NPFV 212
Cdd:COG0491  158 RPDLPDGDLAQWLASL-ERLLALPP-DLVIPGHGPPTtaeaidyleELLAALGEraNPFL 215
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 24-197 7.12e-41

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: 137.15  E-value: 7.12e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  24 IIGDPISKKAIVVDPGGNH-ELILARLDALGLKVVSIIHTHAHLDHFLASGQLKEKTGATLHLHKedqflwdnlemqcqm 102
Cdd:cd07724   16 LVGDPETGEAAVIDPVRDSvDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGE--------------- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880 103 frvpYIPVPSPDRWLEHDEELACGC--GVALHTPGHTPGSMSFWFADAKLLIAGDTLFRRGIGRTDLWGGDQ---ATIVR 177
Cdd:cd07724   81 ----GAPASFFDRLLKDGDVLELGNltLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPGEAEglaRQLYD 156

                        170       180
                 ....*....|....*....|
gi 655192880 178 SIKQRLYTLDEGATVVTGHG 197
Cdd:cd07724  157 SLQRKLLLLPDETLVYPGHD 176
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 7-196 4.92e-37

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: 127.27  E-value: 4.92e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880   7 TLIRETFpvGPLQCNCTIIGDPISKKAIVVDPGGNHELILARLDALGLKVVSIIHTHAHLDHFLASGQLKEKTGATLHLH 86
Cdd:cd16275    1 FVIRVKA--GPMINYSYIIIDKATREAAVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  87 KEDqflwdnlemqcqmfrVPYIPVPSPD-RWLEHDEELACG-----CgvaLHTPGHTPGSMSFWFADAklLIAGDTLFRR 160
Cdd:cd16275   79 KEE---------------IDYYGFRCPNlIPLEDGDTIKIGdteitC---LLTPGHTPGSMCYLLGDS--LFTGDTLFIE 138

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 655192880 161 GIGRTDLWGGDQATIVRSIkQRLYTLDEGATVV-TGH 196
Cdd:cd16275  139 GCGRCDLPGGDPEEMYESL-QRLKKLPPPNTRVyPGH 174
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 21-196 5.81e-35

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: 121.89  E-value: 5.81e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880    21 NCTIIGDPisKKAIVVDPG-GNHELILARLDALGL-KVVSIIHTHAHLDHFLASGQLKEKTGATLHLHKEDQFLWDNLEM 98
Cdd:smart00849   1 NSYLVRDD--GGAILIDTGpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880    99 QCQMFRvPYIPVPSPDRWLEHDEELACGCG--VALHTPGHTPGSMSFWFADAKLLIAGDTLFRRGIGRTDLWGGDQATIV 176
Cdd:smart00849  79 LLGELG-AEAEPAPPDRTLKDGDELDLGGGelEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAASD 157

                          170       180
                   ....*....|....*....|
gi 655192880   177 RSIKQRLYTLDEGATVVTGH 196
Cdd:smart00849 158 ALESLLKLLKLLPKLVVPGH 177
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 20-197 8.08e-32

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: 114.63  E-value: 8.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  20 CNCTIIGDPisKKAIVVDPG--GNHELILARLDALGLK---VVSIIHTHAHLDHFLASGQLKEKTGATLHLHKED----- 89
Cdd:cd07721   11 VNAYLIEDD--DGLTLIDTGlpGSAKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEREapyle 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  90 ---QFLWDNLEMQCQMFRVPY-IPVPSPDRWLEHDEELACGCGV-ALHTPGHTPGSMSFWFADAKLLIAGDTLFRRGiGR 164
Cdd:cd07721   89 gekPYPPPVRLGLLGLLSPLLpVKPVPVDRTLEDGDTLDLAGGLrVIHTPGHTPGHISLYLEEDGVLIAGDALVTVG-GE 167

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 655192880 165 TDLWGG----DQATIVRSIKqRLYTLDEgATVVTGHG 197
Cdd:cd07721  168 LVPPPPpftwDMEEALESLR-KLAELDP-EVLAPGHG 202
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
15-196 3.75e-31

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 112.85  E-value: 3.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880   15 VGPLQCNCTIIGDPisKKAIVVDPGG----NHELILARLDALGLKVVSIIHTHAHLDHFLASGQLKEKTGATLHLHKEDQ 90
Cdd:pfam00753   1 LGPGQVNSYLIEGG--GGAVLIDTGGsaeaALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880   91 FLWDNLEMQCQMFRV------PYIPVPSPDRWLEHDEELACGCGVALHTPGHTPGSMSFWFADAKLLIAGDTLFRRGIGR 164
Cdd:pfam00753  79 RELLDEELGLAASRLglpgppVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGR 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 655192880  165 TDLWGGDQATIVRSIKQ------RLYTLDEGATVVTGH 196
Cdd:pfam00753 159 LDLPLGGLLVLHPSSAEssleslLKLAKLKAAVIVPGH 196
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 24-196 1.76e-28

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: 104.85  E-value: 1.76e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  24 IIGDPISKKAIVVDPGgNHELILARLDALGLKVVSIIHTHAHLDHFLASGQLKEKTG-ATLHLHKEDQflwdnlemqcqm 102
Cdd:cd07723   13 LIVDEATGEAAVVDPG-EAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPdAPVYGPAEDR------------ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880 103 frvpyipVPSPDRWLEHDEELACGCGV--ALHTPGHTPGSMSFWFADAKLLIAGDTLFRRGIGRtdLWGGDQATIVRSIk 180
Cdd:cd07723   80 -------IPGLDHPVKDGDEIKLGGLEvkVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGR--FFEGTAEQMYASL- 149

                        170
                 ....*....|....*.
gi 655192880 181 QRLYTLDEGATVVTGH 196
Cdd:cd07723  150 QKLLALPDDTLVYCGH 165
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 21-198 1.50e-19

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 82.15  E-value: 1.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  21 NCTIIGDPISkkAIVVDPGGNHELILARL-DAL-GLKVVSIIHTHAHLDHFLASGQLKEKTGATLHLHKEDQFLWDNLEm 98
Cdd:cd16278   19 NTYLLGAPDG--VVVIDPGPDDPAHLDALlAALgGGRVSAILVTHTHRDHSPGAARLAERTGAPVRAFGPHRAGGQDTD- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  99 qcqmfrvpyipvPSPDRWLEHDEELACGCG--VALHTPGHTPGSMSFWFADAKLLIAGDTLFRRG---IGRTDlwgGDQA 173
Cdd:cd16278   96 ------------FAPDRPLADGEVIEGGGLrlTVLHTPGHTSDHLCFALEDEGALFTGDHVMGWSttvIAPPD---GDLG 160

                        170       180
                 ....*....|....*....|....*
gi 655192880 174 TIVRSIkQRLYTLDEgATVVTGHGP 198
Cdd:cd16278  161 DYLASL-ERLLALDD-RLLLPGHGP 183
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 20-198 1.46e-16

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 74.91  E-value: 1.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  20 CNCT-IIGDpisKKAIVVDPGGNHEL---ILARLDAL-GLKVVSIIHTHAHLDHFLASGQLKEKtGATLHLH-------K 87
Cdd:cd16282   15 SNIGfIVGD---DGVVVIDTGASPRLaraLLAAIRKVtDKPVRYVVNTHYHGDHTLGNAAFADA-GAPIIAHentreelA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  88 EDQFLWDNLEMQCQMFRVPYIPVPSPDRWLEHDEELACGcGVALH----TPGHTPGSMSFWFADAKLLIAGDTLFRRGIg 163
Cdd:cd16282   91 ARGEAYLELMRRLGGDAMAGTELVLPDRTFDDGLTLDLG-GRTVElihlGPAHTPGDLVVWLPEEGVLFAGDLVFNGRI- 168

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 655192880 164 rTDLWGGDqatIVRSIK--QRLYTLDEgATVVTGHGP 198
Cdd:cd16282  169 -PFLPDGS---LAGWIAalDRLLALDA-TVVVPGHGP 200
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 34-145 7.93e-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: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 70.69  E-value: 7.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  34 IVVDPGGNHE---LILARLDALGLK---VVSIIHTHAHLDHFLASGQLKEKTGATLHLHKEDqflWDNLEMQCQMFRVP- 106
Cdd:cd16280   34 ILIDALNNNEaadLIVDGLEKLGLDpadIKYILITHGHGDHYGGAAYLKDLYGAKVVMSEAD---WDMMEEPPEEGDNPr 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 655192880 107 YIPVPSPDRWLEHDEELACGcGVALH---TPGHTPGSMSFWF 145
Cdd:cd16280  111 WGPPPERDIVIKDGDTLTLG-DTTITvylTPGHTPGTLSLIF 151
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 20-196 8.17e-15

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: 70.71  E-value: 8.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  20 CNCTIIGDPISKKAIVVDPGGNHELILARLDALGLK---VVSIIHTHAHLDHflaSGQLKEKTGATLHLHKE--DQFLWD 94
Cdd:cd07729   50 FHPDAADDPGGLELAFPPGVTEEQTLEEQLARLGLDpedIDYVILSHLHFDH---AGGLDLFPNATIIVQRAelEYATGP 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  95 NLEMQCQMFRVPYIPVPSPD---RWLEHDEELACGCgVALHTPGHTPGSMSFWF--ADAKLLIAGDTL-FRRGI--GRTD 166
Cdd:cd07729  127 DPLAAGYYEDVLALDDDLPGgrvRLVDGDYDLFPGV-TLIPTPGHTPGHQSVLVrlPEGTVLLAGDAAyTYENLeeGRPP 205

                        170       180       190
                 ....*....|....*....|....*....|..
gi 655192880 167 LWGGDQATIVRSIkQRLYTL--DEGATVVTGH 196
Cdd:cd07729  206 GINYDPEAALASL-ERLKALaeREGARVIPGH 236
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 30-196 4.16e-13

uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 64.96  E-value: 4.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  30 SKKAIVVDPGGNHELILARLDALGLKVVSIIHTHAHLDHflaSGQLKEKTGATLHLHKEDQF-LWDNLEMQCQMFRVPYI 108
Cdd:cd07712   17 RDRALLIDTGLGIGDLKEYVRTLTDLPLLVVATHGHFDH---IGGLHEFEEVYVHPADAEILaAPDNFETLTWDAATYSV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880 109 PVPSPDRWLEHDEELACG--CGVALHTPGHTPGSMSFWFADAKLLIAGDTlFRRGIGRTDLWGGDQATIVRSIKQRLYTL 186
Cdd:cd07712   94 PPAGPTLPLRDGDVIDLGdrQLEVIHTPGHTPGSIALLDRANRLLFSGDV-VYDGPLIMDLPHSDLDDYLASLEKLSKLP 172

                        170
                 ....*....|
gi 655192880 187 DEGATVVTGH 196
Cdd:cd07712  173 DEFDKVLPGH 182
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 25-210 6.57e-13

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 65.59  E-value: 6.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  25 IGDPiSKKAIVVDP-GGNHELILARLDALGLKVVSIIHTHAHLDHFLASGQLKEK-------------TGATLHLHKEDQ 90
Cdd:PLN02962  31 VSHP-DKPALLIDPvDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKlpgvksiiskasgSKADLFVEPGDK 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  91 FLWDNLemqcqmfrvpYIPVPSpdrwlehdeelacgcgvalhTPGHTPGSMSFWFADA------KLLIAGDTLFRRGIGR 164
Cdd:PLN02962 110 IYFGDL----------YLEVRA--------------------TPGHTAGCVTYVTGEGpdqpqpRMAFTGDALLIRGCGR 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 655192880 165 TDLWGGDQATIVRSIKQRLYTLDEGATVVTGHgpDTR------LGDEMRENP 210
Cdd:PLN02962 160 TDFQGGSSDQLYKSVHSQIFTLPKDTLIYPAH--DYKgftvstVGEEMLYNP 209
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 30-158 1.83e-12

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 63.32  E-value: 1.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  30 SKKAIVVDPGGNHEL---ILARLDALGLKVVSIIHTHAHLDHFLASGQLKEKTGATLHLHKEDQ-----------FLWD- 94
Cdd:cd07743   17 DKEALLIDSGLDEDAgrkIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKafienpllepsYLGGa 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 655192880  95 --NLEMQCQMFRVPYIPVpspDRWLEHDEELACGCGV-ALHTPGHTPGSMSFwFADAKLLIAGDTLF 158
Cdd:cd07743   97 ypPKELRNKFLMAKPSKV---DDIIEEGELELGGVGLeIIPLPGHSFGQIGI-LTPDGVLFAGDALF 159
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 12-157 8.05e-12

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: 61.55  E-value: 8.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  12 TFPVGPLqcNCTIIGDPISkkAIVVDPGGNH----ELILARLDALGLKVVSI---IHTHAHLDHFLASGQLKEKTGATLH 84
Cdd:cd07725    9 PGPLGHV--NVYLLRDGDE--TTLIDTGLATeedaEALWEGLKELGLKPSDIdrvLLTHHHPDHIGLAGKLQEKSGATVY 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655192880  85 LhkedqflwdnlemqcqmfrVPYIPVPSPDRWLEHDEELacgcgVALHTPGHTPGSMSFWFADAKLLIAGDTL 157
Cdd:cd07725   85 I-------------------LDVTPVKDGDKIDLGGLRL-----KVIETPGHTPGHIVLYDEDRRELFVGDAV 133
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 31-156 3.95e-11

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


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 60.20  E-value: 3.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  31 KKAIVVDPGGNH--ELILARLDALGLKVVSIIH---THAHLDHFLASGQL-KEKTGATLHLH-----------KedqfLW 93
Cdd:cd07726   25 GRPALIDTGPSSsvPRLLAALEALGIAPEDVDYiilTHIHLDHAGGAGLLaEALPNAKVYVHprgarhlidpsK----LW 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655192880  94 DNLE--MQCQMFR--VPYIPVPsPDRWLEHDEELACGCG----VALHTPGHTPGSMSFWFADAKLLIAGDT 156
Cdd:cd07726  101 ASARavYGDEADRlgGEILPVP-EERVIVLEDGETLDLGgrtlEVIDTPGHAPHHLSFLDEESDGLFTGDA 170
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 44-142 3.99e-10

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: 57.72  E-value: 3.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  44 LILARLDALGLKVVSI---IHTHAHLDHFLASGQLKEKTGATLHLHKED----------QFLWDNLEMqcqmfrvPYIPV 110
Cdd:cd16288   46 MIKANIRKLGFKPSDIkilLNSHAHLDHAGGLAALKKLTGAKLMASAEDaallasggksDFHYGDDSL-------AFPPV 118

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 655192880 111 pSPDRWLEHDEELACGcGV---ALHTPGHTPGSMS 142
Cdd:cd16288  119 -KVDRVLKDGDRVTLG-GTtltAHLTPGHTRGCTT 151
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 20-198 1.00e-09

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: 55.67  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  20 CNCTIIGDPisKKAIVVDPGG--NHELILARLDALGLK---VVSIIHTHAHLDHFLASGqLKEKtgATLHLHK-EDQFLW 93
Cdd:cd07711   22 STVTLIKDG--GKNILVDTGTpwDRDLLLKALAEHGLSpedIDYVVLTHGHPDHIGNLN-LFPN--ATVIVGWdICGDSY 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  94 DnlemqcqmfrvpyipvpsPDRWLEHDEELACGCGVALHTPGHTPGSMSFWFADAKL---LIAGDTLFRRG-IGRTDLWG 169
Cdd:cd07711   97 D------------------DHSLEEGDGYEIDENVEVIPTPGHTPEDVSVLVETEKKgtvAVAGDLFEREEdLEDPILWD 158

                        170       180
                 ....*....|....*....|....*....
gi 655192880 170 GDQATIVRSIKQRLYTLDEGATVVTGHGP 198
Cdd:cd07711  159 PLSEDPELQEESRKRILALADWIIPGHGP 187
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 15-145 1.97e-09

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: 55.94  E-value: 1.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  15 VGPLQCNCTIIGDPisKKAIVVDPG--GNHELILARLDALGLKVVSI---IHTHAHLDHFLASGQLKEKTGATLHLHKED 89
Cdd:cd16308   17 VGTYDLACYLIVTP--KGNILINTGlaESVPLIKKNIQALGFKFKDIkilLTTQAHYDHVGAMAAIKQQTGAKMMVDEKD 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 655192880  90 -QFLWDNLEMQCQM--FRVPYIPVpSPDRWLEHDEELACGCG--VALHTPGHTPGSMSFWF 145
Cdd:cd16308   95 aKVLADGGKSDYEMggYGSTFAPV-KADKLLHDGDTIKLGGTklTLLHHPGHTKGSCSFLF 154
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 35-196 2.44e-09

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 56.00  E-value: 2.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  35 VVDPGGNHELIlarlDALGLK---VVSIIHTHAHLDHFLASGQLKEKTGATLHLHKEDQflwDnlemqcqmfRVPYIPV- 110
Cdd:PLN02398 102 VVDPSEAVPVI----DALSRKnrnLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVDK---D---------RIPGIDIv 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880 111 -PSPDRWLEHDEELacgcgVALHTPGHTPGSMSFWFADAKLLIAGDTLFRRGIGRtdLWGGDQATIVRSIkQRLYTLDEG 189
Cdd:PLN02398 166 lKDGDKWMFAGHEV-----LVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGK--LFEGTPEQMLSSL-QKIISLPDD 237


                 ....*..
gi 655192880 190 ATVVTGH 196
Cdd:PLN02398 238 TNIYCGH 244
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 30-143 9.44e-09

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: 53.99  E-value: 9.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  30 SKKAIVVDPG--GNHELILARLDALGLK---VVSIIHTHAHLDHFLASGQLKEKTGATLHLHKEDQF-LWDNLEMQCQMF 103
Cdd:cd16310   30 NHGAILLDGGleENAALIEQNIKALGFKlsdIKIIINTHAHYDHAGGLAQLKADTGAKLWASRGDRPaLEAGKHIGDNIT 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 655192880 104 RVPYIPVPSPDRWLEHDEELACGcGVALH---TPGHTPGSMSF 143
Cdd:cd16310  110 QPAPFPAVKVDRILGDGEKIKLG-DITLTatlTPGHTKGCTTW 151
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 45-158 3.08e-08

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: 52.17  E-value: 3.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  45 ILARLDALGLKVVSIIH---THAHLDHflaSGQLKEKTG------ATLHLHKEDQFLWDN-------LEMQCQMFRV--- 105
Cdd:cd07720   78 LLANLAAAGIDPEDIDDvllTHLHPDH---IGGLVDAGGkpvfpnAEVHVSEAEWDFWLDdanaakaPEGAKRFFDAard 154

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 655192880 106 ---PYIPVpspdRWLEHDEELACGCgVALHTPGHTPGSMSFWFA--DAKLLIAGDTLF 158
Cdd:cd07720  155 rlrPYAAA----GRFEDGDEVLPGI-TAVPAPGHTPGHTGYRIEsgGERLLIWGDIVH 207
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 11-164 8.69e-08

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 50.92  E-value: 8.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  11 ETFPVGPLQCNCT-IIGDPISKKAIVVDPGgNHELILARLDALGLKVVSIIHTHAHLDHflASGQLKEKTgatlhlhked 89
Cdd:PLN02469   2 KIIPVPCLEDNYAyLIIDESTKDAAVVDPV-DPEKVLQAAHEHGAKIKLVLTTHHHWDH--AGGNEKIKK---------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  90 qflwdnlemqcqmfRVPYIP--------VPSPDRWLEHDEELACGCGV---ALHTPGHTPGSMSFWF----ADAKLLIAG 154
Cdd:PLN02469  69 --------------LVPGIKvyggsldnVKGCTHPVENGDKLSLGKDVnilALHTPCHTKGHISYYVtgkeGEDPAVFTG 134

                        170
                 ....*....|
gi 655192880 155 DTLFRRGIGR 164
Cdd:PLN02469 135 DTLFIAGCGK 144
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 33-149 7.05e-07

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: 48.27  E-value: 7.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  33 AIVVDPGGNH--ELILARLDALG-----LKVvsIIHTHAHLDHFLASGQLKEKTGATLHLHKEDQFLW-----DNLEMQC 100
Cdd:cd16289   33 AVLLDGGMPQaaDMLLDNMRALGvapgdLKL--ILHSHAHADHAGPLAALKRATGARVAANAESAVLLarggsDDIHFGD 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 655192880 101 QMFrvpYIPVpSPDRWLEHDEELACGcGVAL--H-TPGHTPGSMSFWFADAK 149
Cdd:cd16289  111 GIT---FPPV-QADRIVMDGEVVTLG-GVTFtaHfTPGHTPGSTSWTWTDTR 157
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 30-144 1.53e-06

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: 47.54  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  30 SKKAIVVDPG--GNHELILARLDALGLKVVS---IIHTHAHLDHFLASGQLKEKTGATLHLHKEDQFL-----------W 93
Cdd:cd07708   30 PQGNILIDGDmeQNAPMIKANIKKLGFKFSDtklILISHAHFDHAGGSAEIKKQTGAKVMAGAEDVSLllsggssdfhyA 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 655192880  94 DNLEMqcqmfrvpYIPVPSPDRWLeHDEELACGCGVAL--H-TPGHTPGSMSfW 144
Cdd:cd07708  110 NDSST--------YFPQSTVDRAV-HDGERVTLGGTVLtaHaTPGHTPGCTT-W 153
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 34-149 1.69e-06

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


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 47.09  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  34 IVVDPG--GNHELILARLDALGLKVVSI---IHTHAHLDHFLASGQLKEKTGATLHLHKEDQFLWDNLEMQCQMFRVPYI 108
Cdd:cd16309   34 ILIDGAmpQSTPLIKDNIKKLGFDVKDVkylLNTHAHFDHAGGLAELKKATGAQLVASAADKPLLESGYVGSGDTKNLQF 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 655192880 109 PVPSPDRWLEHDEELACGcGVAL--H-TPGHTPGSMSfWFADAK 149
Cdd:cd16309  114 PPVRVDRVIGDGDKVTLG-GTTLtaHlTPGHSPGCTS-WTTTVK 155
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 34-158 2.81e-06

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


Pssm-ID: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 46.03  E-value: 2.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  34 IVVDPGGN--------HELILARLDALGlKVVSIIHTHAHldhFLASGQ-LKEKTGATLHLHKEDqflwdnleMQCQMFR 104
Cdd:cd07727   19 LILRPEGNilvdsprySPPLAKRIEALG-GIRYIFLTHRD---DVADHAkWAERFGAKRIIHEDD--------VNAVTRP 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 655192880 105 VPYIPVPSPDRWlehdeELACGCgVALHTPGHTPGSMSFWFADAKLLIAGDTLF 158
Cdd:cd07727   87 DEVIVLWGGDPW-----ELDPDL-TLIPVPGHTRGSVVLLYKEKGVLFTGDHLA 134
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 43-145 5.60e-06

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


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 45.80  E-value: 5.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  43 ELILARLDALGLK---VVSIIHTHAHLDHFLASGQLKEKTGATL-------------HLHKEDQflwdnlemQCQMFRvP 106
Cdd:cd16315   45 PLVLANIRKLGFDpkdVRWLLSSHEHFDHVGGLAALQRATGARVaasaaaapvlesgKPAPDDP--------QAGLHE-P 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 655192880 107 YIPVPSpDRWLEHDEELACGCGV--ALHTPGHTPGSMSfWF 145
Cdd:cd16315  116 FPPVRV-DRIVEDGDTVALGSLRltAHATPGHTPGALS-WT 154
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 21-156 1.22e-05

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: 44.06  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  21 NCTIIGDPISKkaIVVDPG-GNHELILAR---LDALGLKVVS-IIHTHAHLDHFLASGQ-LKEKTGATLHLHKedqFLWD 94
Cdd:cd07722   19 NTYLVGTGKRR--ILIDTGeGRPSYIPLLksvLDSEGNATISdILLTHWHHDHVGGLPDvLDLLRGPSPRVYK---FPRP 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 655192880  95 NLEMQCQMFRVPYIPvpspdrwLEHDEELACGcGV---ALHTPGHTPGSMSFWFADAKLLIAGDT 156
Cdd:cd07722   94 EEDEDPDEDGGDIHD-------LQDGQVFKVE-GAtlrVIHTPGHTTDHVCFLLEEENALFTGDC 150
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 13-196 2.08e-05

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


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 43.64  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  13 FPVgplqcNCTII-GDpisKKAIVVDPG---GNHELILARLDALGLKVVSIIHTHAHLDHFLASGQLKEK--------TG 80
Cdd:cd07739   14 FPV-----TSTLIyGE---TEAVLVDAQftrADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAfpdakvvaTP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  81 ATLHL---HKEDQFLWDNLEMQCQMFRVPYIPVPSPDRWLEHDeelacGCGVALHTPGH--TPGSMSFWFADAKLLIAGD 155
Cdd:cd07739   86 AVVAHikaQLEPKLAFWGPLLGGNAPARLVVPEPLDGDTLTLE-----GHPLEIVGVGGgdTDDTTYLWIPSLKTVVAGD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 655192880 156 TLFrrgiGRTDLWGGDQATiVRSIKQRLYTLDEGA-----TVVTGH 196
Cdd:cd07739  161 VVY----NGVHVWLADATT-PELRAAWLAALDKIEalnpeTVVPGH 201
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 37-198 2.72e-04

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


Pssm-ID: 293793 [Multi-domain]  Cd Length: 219  Bit Score: 40.61  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  37 DPGGNHELILARLDALGLKVVSIIHTHAHLDHFLASGQLKE------KTGATLHLHKEDQFLWDNLEMQCQMfRVPYIPV 110
Cdd:cd07707   40 TPKTTKELIKEIEKVSQKPVTEVINTHFHTDRAGGNAYLKErgaktvSTALTRDLAKSEWAEIVAFTRKGLP-EYPDLGY 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880 111 PSPDRWLEHDEELACGCGVALHT-PGHTPGSMSFWFADAKLLIAGDTLFRRGIGrtDLWGGDQATIVRSIkQRLYTLDEG 189
Cdd:cd07707  119 ELPDGVLDGDFNLQFGKVEAFYPgPAHTPDNIVVYFPQENVLYGGCIIKETDLG--NVADADVKEWPTSI-ERLKKRYRN 195

                        170
                 ....*....|
gi 655192880 190 A-TVVTGHGP 198
Cdd:cd07707  196 IkAVIPGHGE 205
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 44-143 5.55e-04

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: 39.97  E-value: 5.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  44 LILARLDALGLK---VVSIIHTHAHLDHFLASGQLKEKTGATL-HLHKEDQFLWDNL----EMQCQMFRVPYIPVPSPDR 115
Cdd:cd16312   46 LIIANIEALGFRiedVKLILNSHAHWDHAGGIAALQKASGATVaASAHGAQVLQSGTngkdDPQYQAKPVVHVAKVAKVK 125

                         90       100       110
                 ....*....|....*....|....*....|
gi 655192880 116 WLEHDEELACG-CGVALH-TPGHTPGSMSF 143
Cdd:cd16312  126 EVGEGDTLKVGpLRLTAHmTPGHTPGGTTW 155
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 34-203 1.68e-03

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 37.95  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  34 IVVD-PGGNHELILARLDAL-GLKVVSIIHTHAHLDHFLASGQLKEKtGATLHLHKEdqflwdNLEMqcqMFRVPYIPVP 111
Cdd:cd16276   22 IVVDaPPSLGENLLAAIRKVtDKPVTHVVYSHNHADHIGGASIFKDE-GATIIAHEA------TAEL---LKRNPDPKRP 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880 112 SPDRWLEHDEELACGcGVAL----HTPGHTPGSMSFWFADAKLLIAGDTL------FRRGIGRTDL--WGGDQATIVRsi 179
Cdd:cd16276   92 VPTVTFDDEYTLEVG-GQTLelsyFGPNHGPGNIVIYLPKQKVLMAVDLInpgwvpFFNFAGSEDIpgYIEALDELLE-- 168

                        170       180
                 ....*....|....*....|....
gi 655192880 180 kqrlYTLDegaTVVTGHGPdtRLG 203
Cdd:cd16276  169 ----YDFD---TFVGGHGN--RLG 183
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 34-157 1.79e-03

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 38.27  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  34 IVVDPG-GNH-------------ELILARLDALGLKVVSI---IHTHAHLDHflasgqlkekTG---------------- 80
Cdd:cd16277   25 ILVDTGiGNDkprpgppafhnlnTPYLERLAAAGVRPEDVdyvLCTHLHVDH----------VGwntrlvdgrwvptfpn 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  81 ATLHLHKEDQFLWDNLEMQCQMFRVPY----IPVPSPDR--WLEHDEELAcGCGVALHTPGHTPGSMSFWF--ADAKLLI 152
Cdd:cd16277   95 ARYLFSRAEYDHWSSPDAGGPPNRGVFedsvLPVIEAGLadLVDDDHEIL-DGIRLEPTPGHTPGHVSVELesGGERALF 173


                 ....*
gi 655192880 153 AGDTL 157
Cdd:cd16277  174 TGDVM 178
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 21-155 4.78e-03

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: 37.09  E-value: 4.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  21 NCTII-GDpisKKAIVVDPGGNHE-----LILARLDALGLKVVSIIHTHAHLDHF-----LASGQLKEKT------GATL 83
Cdd:cd07710   19 NMTFIeGD---TGLIIIDTLESAEaakaaLELFRKHTGDKPVKAIIYTHSHPDHFggaggFVEEEDSGKVpiiapeGFME 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  84 HLHKEDQFLWDNLEMQCQ-MF-----------------------RVPYIPvpsPDRWLEHDEE---LAcgcGVAL---HT 133
Cdd:cd07710   96 EAVSENVLAGNAMSRRAAyQFgallpkgekgqvgaglgpglstgTVGFIP---PTITITETGEtltID---GVELefqHA 169

                        170       180
                 ....*....|....*....|..
gi 655192880 134 PGHTPGSMSFWFADAKLLIAGD 155
Cdd:cd07710  170 PGEAPDEMMVWLPDYKVLFCAD 191
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 45-156 5.92e-03

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


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 36.86  E-value: 5.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655192880  45 ILARLDALGLK---VVSIIHTHAHLDHflaSGQLKEKTGATLHLHKE--DQFLWDNLemqCQMFRVPYIPV--PSPDRWL 117
Cdd:cd07730   70 VAEQLAAGGIDpedIDAVILSHLHWDH---IGGLSDFPNARLIVGPGakEALRPPGY---PSGFLPELLPSdfEGRLVRW 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 655192880 118 EHDEELACGCG--------------VALHTPGHTPGSMSFWF---ADAKLLIAGDT 156
Cdd:cd07730  144 EEDDFLWVPLGpfpraldlfgdgslYLVDLPGHAPGHLGLLArttSGTWVFLAGDA 199
 
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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