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Conserved domains on  [gi|15596612|ref|NP_250106|]
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hypothetical protein PA1415 [Pseudomonas aeruginosa PAO1]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869773)

uncharacterized MBL fold metallo-hydrolase similar to uncharacterized human metallo-beta-lactamase domain-containing protein 2 (MBLAC2 )

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 25-220 1.81e-85

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: 251.78  E-value: 1.81e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  25 PYVRPFYRCNMWHVQGRERDVLVDSGSGLVSLCEQLPWLTERPLLAVASHTHFDHIAGHHEFAERLAHPAEAEILAAPDG 104
Cdd:cd07712   1 LFIEEDDRVNIYLLRGRDRALLIDTGLGIGDLKEYVRTLTDLPLLVVATHGHFDHIGGLHEFEEVYVHPADAEILAAPDN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 105 DNTLARayvgdemfeahpecplCYAEYRVRAAPATRLIDEGDVLDLGDRVLQVLHTPGHSPGGISLWEAATQTLFSGDIV 184
Cdd:cd07712  81 FETLTW----------------DAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVV 144

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15596612 185 YDGPLVEDAYHSNLDDYASSLARLRELP--VRTVHGGH 220
Cdd:cd07712 145 YDGPLIMDLPHSDLDDYLASLEKLSKLPdeFDKVLPGH 182
 
Name Accession Description Interval E-value
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 25-220 1.81e-85

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: 251.78  E-value: 1.81e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  25 PYVRPFYRCNMWHVQGRERDVLVDSGSGLVSLCEQLPWLTERPLLAVASHTHFDHIAGHHEFAERLAHPAEAEILAAPDG 104
Cdd:cd07712   1 LFIEEDDRVNIYLLRGRDRALLIDTGLGIGDLKEYVRTLTDLPLLVVATHGHFDHIGGLHEFEEVYVHPADAEILAAPDN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 105 DNTLARayvgdemfeahpecplCYAEYRVRAAPATRLIDEGDVLDLGDRVLQVLHTPGHSPGGISLWEAATQTLFSGDIV 184
Cdd:cd07712  81 FETLTW----------------DAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVV 144

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15596612 185 YDGPLVEDAYHSNLDDYASSLARLRELP--VRTVHGGH 220
Cdd:cd07712 145 YDGPLIMDLPHSDLDDYLASLEKLSKLPdeFDKVLPGH 182
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 22-230 4.20e-35

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: 124.42  E-value: 4.20e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  22 IHEPYVRPFYRCNMWHVQGRERDVLVDSGSGLVS---LCEQLPWLTERPLLAVASHTHFDHIAGHHEFAER-----LAHP 93
Cdd:COG0491   4 LPGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADaeaLLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAfgapvYAHA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  94 AEAEILAAPDGDntlarayvgdemfeahpecplcyAEYRVRAAPATRLIDEGDVLDLGDRVLQVLHTPGHSPGGISLWEA 173
Cdd:COG0491  84 AEAEALEAPAAG-----------------------ALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVP 140

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15596612 174 ATQTLFSGDIVY-DGPLVEDAYHSNLDDYASSLARLRELPVRTVHGGHFASFSGERLR 230
Cdd:COG0491 141 DEKVLFTGDALFsGGVGRPDLPDGDLAQWLASLERLLALPPDLVIPGHGPPTTAEAID 198
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 34-220 3.96e-28

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: 105.33  E-value: 3.96e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612     34 NMWHVQGRERDVLVDSGSGLVS-LCEQLPWLTERPLLAV-ASHTHFDHIAGHHEFAER-----LAHPAEAEILAAPDGDN 106
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEdLLAELKKLGPKKIDAIiLTHGHPDHIGGLPELLEApgapvYAPEGTAELLKDLLALL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612    107 TlarayvgdemfeahpecplcYAEYRVRAAPATRLIDEGDVLDLGDRVLQVLHTPGHSPGGISLWEAATQTLFSGDIVYD 186
Cdd:smart00849  81 G--------------------ELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFA 140

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 15596612    187 ---GPLVEDAYHSNLDDYASSLARLRELPVRTVHGGH 220
Cdd:smart00849 141 ggdGRTLVDGGDAAASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
28-220 1.05e-18

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 80.88  E-value: 1.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612    28 RPFYRCNMWHVQGRERDVLVDSGSGLVSLCEQLPWLTERPLL----AVASHTHFDHIAGHHEFAERLAHPaeaEILAAPD 103
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLGPKdidaVILTHGHFDHIGGLGELAEATDVP---VIVVAEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612   104 GDNTLARAYVGDEMFEAHPEcplcyaeYRVRAAPATRLIDEGDVLDLGDRVLQVLHTPGHSPGGISLWEAATQTLFSGDI 183
Cdd:pfam00753  78 ARELLDEELGLAASRLGLPG-------PPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 15596612   184 VYDGPLV---------EDAYHSNLDDYASSLARLRELPVRTVHGGH 220
Cdd:pfam00753 151 LFAGEIGrldlplgglLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 73-220 3.51e-04

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 40.98  E-value: 3.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612   73 SHTHFDHIAGHHEFAERLAHPAeaeILAAPDGDntlarayvgdemfeahpecplcyaeyrvRAAPATRLIDEGDVLDLGD 152
Cdd:PLN02398 128 THHHYDHTGGNLELKARYGAKV---IGSAVDKD----------------------------RIPGIDIVLKDGDKWMFAG 176

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596612  153 RVLQVLHTPGHSPGGISLWEAATQTLFSGDIVYD---GPLVEDAYHSNLddyaSSLARLRELPVRT-VHGGH 220
Cdd:PLN02398 177 HEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSlscGKLFEGTPEQML----SSLQKIISLPDDTnIYCGH 244
 
Name Accession Description Interval E-value
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 25-220 1.81e-85

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: 251.78  E-value: 1.81e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  25 PYVRPFYRCNMWHVQGRERDVLVDSGSGLVSLCEQLPWLTERPLLAVASHTHFDHIAGHHEFAERLAHPAEAEILAAPDG 104
Cdd:cd07712   1 LFIEEDDRVNIYLLRGRDRALLIDTGLGIGDLKEYVRTLTDLPLLVVATHGHFDHIGGLHEFEEVYVHPADAEILAAPDN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 105 DNTLARayvgdemfeahpecplCYAEYRVRAAPATRLIDEGDVLDLGDRVLQVLHTPGHSPGGISLWEAATQTLFSGDIV 184
Cdd:cd07712  81 FETLTW----------------DAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVV 144

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15596612 185 YDGPLVEDAYHSNLDDYASSLARLRELP--VRTVHGGH 220
Cdd:cd07712 145 YDGPLIMDLPHSDLDDYLASLEKLSKLPdeFDKVLPGH 182
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 22-230 4.20e-35

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: 124.42  E-value: 4.20e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  22 IHEPYVRPFYRCNMWHVQGRERDVLVDSGSGLVS---LCEQLPWLTERPLLAVASHTHFDHIAGHHEFAER-----LAHP 93
Cdd:COG0491   4 LPGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADaeaLLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAfgapvYAHA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  94 AEAEILAAPDGDntlarayvgdemfeahpecplcyAEYRVRAAPATRLIDEGDVLDLGDRVLQVLHTPGHSPGGISLWEA 173
Cdd:COG0491  84 AEAEALEAPAAG-----------------------ALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVP 140

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15596612 174 ATQTLFSGDIVY-DGPLVEDAYHSNLDDYASSLARLRELPVRTVHGGHFASFSGERLR 230
Cdd:COG0491 141 DEKVLFTGDALFsGGVGRPDLPDGDLAQWLASLERLLALPPDLVIPGHGPPTTAEAID 198
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 34-220 3.96e-28

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: 105.33  E-value: 3.96e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612     34 NMWHVQGRERDVLVDSGSGLVS-LCEQLPWLTERPLLAV-ASHTHFDHIAGHHEFAER-----LAHPAEAEILAAPDGDN 106
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEdLLAELKKLGPKKIDAIiLTHGHPDHIGGLPELLEApgapvYAPEGTAELLKDLLALL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612    107 TlarayvgdemfeahpecplcYAEYRVRAAPATRLIDEGDVLDLGDRVLQVLHTPGHSPGGISLWEAATQTLFSGDIVYD 186
Cdd:smart00849  81 G--------------------ELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFA 140

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 15596612    187 ---GPLVEDAYHSNLDDYASSLARLRELPVRTVHGGH 220
Cdd:smart00849 141 ggdGRTLVDGGDAAASDALESLLKLLKLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 31-220 1.16e-25

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: 98.90  E-value: 1.16e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  31 YRCNMWHVQGRERD-VLVDSGSG-LVSLCEQLPWLTERPLLAVASHTHFDHIAGHHEFAER-----LAHPAEAEILAAPD 103
Cdd:cd06262   8 LQTNCYLVSDEEGEaILIDPGAGaLEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEApgapvYIHEADAELLEDPE 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 104 GDNTLarayvgdemfeahpecplcYAEYRVRAAPATRLIDEGDVLDLGDRVLQVLHTPGHSPGGISLWEAATQTLFSGDI 183
Cdd:cd06262  88 LNLAF-------------------FGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDT 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15596612 184 V-YDGPLVEDAYHSNLDDYASSLARLRELPVR--TVHGGH 220
Cdd:cd06262 149 LfAGSIGRTDLPGGDPEQLIESIKKLLLLLPDdtVVYPGH 188
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 40-220 3.04e-23

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: 93.40  E-value: 3.04e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  40 GRERDVLVDSGSGLV---SLCEQLPWLTERPLLAVA-SHTHFDHIAGHHEFAER----LAHPAEAEILAAPDGDNTLARA 111
Cdd:cd16282  22 GDDGVVVIDTGASPRlarALLAAIRKVTDKPVRYVVnTHYHGDHTLGNAAFADAgapiIAHENTREELAARGEAYLELMR 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 112 YVGDEMFEAhpecplcyaeyrVRAAPATRLIDEGDVLDLGDRVLQVLHT-PGHSPGGISLWEAATQTLFSGDIVYDGPLV 190
Cdd:cd16282 102 RLGGDAMAG------------TELVLPDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEGVLFAGDLVFNGRIP 169

                       170       180       190
                ....*....|....*....|....*....|
gi 15596612 191 eDAYHSNLDDYASSLARLRELPVRTVHGGH 220
Cdd:cd16282 170 -FLPDGSLAGWIAALDRLLALDATVVVPGH 198
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 33-220 8.71e-23

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: 91.90  E-value: 8.71e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  33 CNMWHVQGRERDVLVDSG-----SGLVSLCEQLPWLTERPLLAVASHTHFDHIAGHHEFAER-----LAHPAEAEILAAP 102
Cdd:cd07721  11 VNAYLIEDDDGLTLIDTGlpgsaKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEApgapvYAHEREAPYLEGE 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 103 DGDNTLARAYVGDEMFEAHPECPLcyaeyrvraaPATRLIDEGDVLDLGDRvLQVLHTPGHSPGGISLWEAATQTLFSGD 182
Cdd:cd07721  91 KPYPPPVRLGLLGLLSPLLPVKPV----------PVDRTLEDGDTLDLAGG-LRVIHTPGHTPGHISLYLEEDGVLIAGD 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 15596612 183 --IVYDGPLVE--DAYHSNLDDYASSLARLRELPVRTVHGGH 220
Cdd:cd07721 160 alVTVGGELVPppPPFTWDMEEALESLRKLAELDPEVLAPGH 201
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 18-220 5.97e-21

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


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 87.16  E-value: 5.97e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  18 GISLIHEPYVRPFYRCNMWHVQGRERDVLVDSGSG-----LVSLCEQLPWLTERPLLAVASHTHFDHIAGHHEFAERL-- 90
Cdd:cd07726   1 GIYLIDLGFLGFPGRIASYLLDGEGRPALIDTGPSssvprLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLAEALpn 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  91 ----AHPAEAEILAAPDGDNTLARAYVGDEMFEAHpecplcyaeYRVRAAPATRLI--DEGDVLDLGDRVLQVLHTPGHS 164
Cdd:cd07726  81 akvyVHPRGARHLIDPSKLWASARAVYGDEADRLG---------GEILPVPEERVIvlEDGETLDLGGRTLEVIDTPGHA 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596612 165 PGGISLWEAATQTLFSGD---IVYDGPLVEDAYHS-----NLDDYASSLARLRELPVRTVHGGH 220
Cdd:cd07726 152 PHHLSFLDEESDGLFTGDaagVRYPELDVVGPPSTpppdfDPEAWLESLDRLLSLKPERIYLTH 215
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 45-220 1.37e-19

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: 83.55  E-value: 1.37e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  45 VLVDSGSGLVSLCEQLPWLTERPLLAVASHTHFDHIAG-----HHEFAERLAHPAEAEILAAPDGdntlarayvGDEMFE 119
Cdd:cd16322  25 VLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGvadlrRHPGAPVYLHPDDLPLYEAADL---------GAKAFG 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 120 AHPEcplcyaeyrvRAAPATRLIDEGDVLDLGDRVLQVLHTPGHSPGGISLWEAATQTLFSGDIVYDGPLVE-DAYHSNL 198
Cdd:cd16322  96 LGIE----------PLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRtDLPGGDP 165

                       170       180
                ....*....|....*....|...
gi 15596612 199 DDYASSLARLRELPVRT-VHGGH 220
Cdd:cd16322 166 KAMAASLRRLLTLPDETrVFPGH 188
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
28-220 1.05e-18

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 80.88  E-value: 1.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612    28 RPFYRCNMWHVQGRERDVLVDSGSGLVSLCEQLPWLTERPLL----AVASHTHFDHIAGHHEFAERLAHPaeaEILAAPD 103
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLGPKdidaVILTHGHFDHIGGLGELAEATDVP---VIVVAEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612   104 GDNTLARAYVGDEMFEAHPEcplcyaeYRVRAAPATRLIDEGDVLDLGDRVLQVLHTPGHSPGGISLWEAATQTLFSGDI 183
Cdd:pfam00753  78 ARELLDEELGLAASRLGLPG-------PPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 15596612   184 VYDGPLV---------EDAYHSNLDDYASSLARLRELPVRTVHGGH 220
Cdd:pfam00753 151 LFAGEIGrldlplgglLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 62-187 6.61e-16

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: 73.36  E-value: 6.61e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  62 WLTerpllavasHTHFDHIAGHHEFAERLA------HPAEAEILaapdgDNTLARAyvgdEMFeAHPECplcyaeyrvRA 135
Cdd:cd07737  51 LLT---------HGHLDHVGGAAELAEHYGvpiigpHKEDKFLL-----ENLPEQS----QMF-GFPPA---------EA 102

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15596612 136 APATRLIDEGDVLDLGDRVLQVLHTPGHSPGGISLWEAATQTLFSGDIVYDG 187
Cdd:cd07737 103 FTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKG 154
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 73-220 2.14e-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: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 71.75  E-value: 2.14e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  73 SHTHFDHIAGhhefAERLAHPAEAEILAAPDgdntlARAYVGDEMFeahpecplcyaeyrvraAPATRLIDeGDVLDLGD 152
Cdd:cd16278  60 THTHRDHSPG----AARLAERTGAPVRAFGP-----HRAGGQDTDF-----------------APDRPLAD-GEVIEGGG 112

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596612 153 RVLQVLHTPGHSPGGISLWEAATQTLFSGDIVYD-GPLVEDAYHSNLDDYASSLARLRELPVRTVHGGH 220
Cdd:cd16278 113 LRLTVLHTPGHTSDHLCFALEDEGALFTGDHVMGwSTTVIAPPDGDLGDYLASLERLLALDDRLLLPGH 181
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 135-230 3.99e-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: 68.09  E-value: 3.99e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 135 AAPATRLIDEGDVLDLGDRVLQVLHTPGHSPGGISLWEAATQTLFSGDIV--YDGP---LVEDAYHSNLDDYASSLARLR 209
Cdd:cd07725  84 YILDVTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVlpKITPnvsLWAVRVEDPLGAYLESLDKLE 163

                        90       100
                ....*....|....*....|.
gi 15596612 210 ELPVRTVHGGHFASFSGERLR 230
Cdd:cd07725 164 KLDVDLAYPGHGGPIKDPKAR 184
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 74-182 3.36e-12

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: 62.80  E-value: 3.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  74 HTHFDHIAGHHEFAERLahpaeaeilaapdgdntlarayvgdemfeahpECPLCYAEYrVRAAPATRLIDEGDVLDLGDR 153
Cdd:cd07724  56 HVHADHVSGARELAERT--------------------------------GAPIVIGEG-APASFFDRLLKDGDVLELGNL 102

                        90       100
                ....*....|....*....|....*....
gi 15596612 154 VLQVLHTPGHSPGGISLWEAATQTLFSGD 182
Cdd:cd07724 103 TLEVLHTPGHTPESVSYLVGDPDAVFTGD 131
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 74-220 1.40e-11

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: 60.94  E-value: 1.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  74 HTHFDHIAGHHEFAERlahpaeaeilaapdgdntlarayvgdemfeaHPECPLcYAEYRVRAAPATRLIDEGDVLDLGDR 153
Cdd:cd07723  51 HHHWDHTGGNAELKAL-------------------------------FPDAPV-YGPAEDRIPGLDHPVKDGDEIKLGGL 98

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596612 154 VLQVLHTPGHSPGGISLWEAATQTLFSGDI--------VYDGPlVEDAYHsnlddyasSLARLRELPVRT-VHGGH 220
Cdd:cd07723  99 EVKVLHTPGHTLGHICYYVPDEPALFTGDTlfsggcgrFFEGT-AEQMYA--------SLQKLLALPDDTlVYCGH 165
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 71-218 7.44e-11

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: 60.19  E-value: 7.44e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  71 VASHTHFDHIAGHHEFAERlaHPaEAEILAAPDGDNTLARAYVGDEmfeahpecplcyaeYRVRAapatrlIDEGDVLDL 150
Cdd:cd07709  73 VVNHQEPDHSGSLPELLEL--AP-NAKIVCSKKAARFLKHFYPGID--------------ERFVV------VKDGDTLDL 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 151 GDRVLQVLHTPG-HSPGGISLWEAATQTLFSGDI----VYDGPLVEDA----------YHSNLdDYASS------LARLR 209
Cdd:cd07709 130 GKHTLKFIPAPMlHWPDTMVTYDPEDKILFSGDAfgahGASGELFDDEvedyleearrYYANI-MGPFSkqvrkaLEKLE 208

                       170
                ....*....|..
gi 15596612 210 ELPVRTV---HG 218
Cdd:cd07709 209 ALDIKMIapsHG 220
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 71-169 4.64e-10

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


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 58.13  E-value: 4.64e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  71 VASHTHFDHIAGHHEFAERLAHPAEAEILAAPDGDNTLARAyvGDEMFEAHPECPlcyaeyrvrAAPATRLIDEGDVLDL 150
Cdd:cd16315  65 LSSHEHFDHVGGLAALQRATGARVAASAAAAPVLESGKPAP--DDPQAGLHEPFP---------PVRVDRIVEDGDTVAL 133

                        90
                ....*....|....*....
gi 15596612 151 GDRVLQVLHTPGHSPGGIS 169
Cdd:cd16315 134 GSLRLTAHATPGHTPGALS 152
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 40-220 7.09e-10

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 56.77  E-value: 7.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  40 GRERdVLVDSGSGLVSLCEQLPWLTERPLLA-----VASHTHFDHIAGhhefaerLAHpaeaeILAAPDGDNTlaRAYVg 114
Cdd:cd07722  26 GKRR-ILIDTGEGRPSYIPLLKSVLDSEGNAtisdiLLTHWHHDHVGG-------LPD-----VLDLLRGPSP--RVYK- 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 115 demfeaHPECPLCYAEYRVRAAPATrlIDEGDVLDLGDRVLQVLHTPGHSPGGISLWEAATQTLFSGDIVydgpL----- 189
Cdd:cd07722  90 ------FPRPEEDEDPDEDGGDIHD--LQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGDCV----Lghgta 157

                       170       180       190
                ....*....|....*....|....*....|..
gi 15596612 190 -VEDayhsnLDDYASSLARLRELPVRTVHGGH 220
Cdd:cd07722 158 vFED-----LAAYMASLKKLLSLGPGRIYPGH 184
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 73-170 1.41e-09

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 56.82  E-value: 1.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  73 SHTHFDHIAGhhefAERLAhpaeaeilaapdgDNTLARAY---VGDEMFEAHPECPlcyaEYRVRAAPATR--LIDEGDV 147
Cdd:cd16280  68 THGHGDHYGG----AAYLK-------------DLYGAKVVmseADWDMMEEPPEEG----DNPRWGPPPERdiVIKDGDT 126

                        90       100
                ....*....|....*....|...
gi 15596612 148 LDLGDRVLQVLHTPGHSPGGISL 170
Cdd:cd16280 127 LTLGDTTITVYLTPGHTPGTLSL 149
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 71-220 1.58e-09

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


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 56.59  E-value: 1.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  71 VASHTHFDHIAGhheFAErLAHPAEAEILAAPDGDNTLARAYVGDemfeAHPEcplcyAEYRVRAAPAT--RLIDEGDVL 148
Cdd:cd16290  65 LNSHAHFDHAGG---IAA-LQRDSGATVAASPAGAAALRSGGVDP----DDPQ-----AGAADPFPPVAkvRVVADGEVV 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 149 DLGDRVLQVLHTPGHSPGGISlWeaaTQTLFSG----DIVYDGPL----------VEDAYHSNLDDYASSLARLRELP-- 212
Cdd:cd16290 132 KLGPLAVTAHATPGHTPGGTS-W---TWRSCEGgrclDIVYADSLtavsadgfrfSDDAHPARVAAFRRSIATVAALPcd 207


                ....*....
gi 15596612 213 -VRTVHGGH 220
Cdd:cd16290 208 iLISAHPDA 216
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 71-211 2.73e-09

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: 55.68  E-value: 2.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  71 VASHTHFDHIAGHHEF--AERLAHPAEAEilaapdgdntlarAYVGDEMFEAHPECPLCYAEYRVRAAPaTRLIDeGDVl 148
Cdd:cd07729  93 ILSHLHFDHAGGLDLFpnATIIVQRAELE-------------YATGPDPLAAGYYEDVLALDDDLPGGR-VRLVD-GDY- 156

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596612 149 DLGDRVlQVLHTPGHSPGGISL-WEAATQT-LFSGDIVYD----GPLVEDAYHSNLDDYASSLARLREL 211
Cdd:cd07729 157 DLFPGV-TLIPTPGHTPGHQSVlVRLPEGTvLLAGDAAYTyenlEEGRPPGINYDPEAALASLERLKAL 224
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 69-220 3.30e-09

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: 55.63  E-value: 3.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  69 LAVASHTHFDHIAGHHEFAERlahpAEAEILAAPDGDNTLARAYVGDEMFEAHPEcpLCYAeyrvrAAPATRLIDEGDVL 148
Cdd:cd07708  63 LILISHAHFDHAGGSAEIKKQ----TGAKVMAGAEDVSLLLSGGSSDFHYANDSS--TYFP-----QSTVDRAVHDGERV 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 149 DLGDRVLQVLHTPGHSPGGISlWEAAT-------QTLFSGDIVYDGP--LVEDAYHSNL-DDYASSLARLRELPVRTVHG 218
Cdd:cd07708 132 TLGGTVLTAHATPGHTPGCTT-WTMTLkdhgkqyQVVFADSLTVNPGyrLVDNPTYPKIvEDYRHSFAVVEAMRCDILLG 210


                ..
gi 15596612 219 GH 220
Cdd:cd07708 211 PH 212
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 74-220 4.02e-09

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: 54.08  E-value: 4.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  74 HTHFDHIAGhhefAERLAHPAEAEIlaapdgdntlaraYVGDEmfeahpECPLcyaeYRVRAaPATRLIDEGDVLDLGDR 153
Cdd:cd16275  55 HSHFDHVNL----VEPLLAKYDAPV-------------YMSKE------EIDY----YGFRC-PNLIPLEDGDTIKIGDT 106

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596612 154 VLQVLHTPGHSPGGISLWeaATQTLFSGDIVYdgplVE-----DAYHSNLDDYASSLARLRELP---VRtVHGGH 220
Cdd:cd16275 107 EITCLLTPGHTPGSMCYL--LGDSLFTGDTLF----IEgcgrcDLPGGDPEEMYESLQRLKKLPppnTR-VYPGH 174
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 73-212 6.34e-09

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: 54.63  E-value: 6.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  73 SHTHFDHIAGHHEF-----AERLAHPAEAEILAapDGDNTlARAYVGDEMfeAHPecplcyaeyrvrAAPATRLIDEGDV 147
Cdd:cd16288  67 SHAHLDHAGGLAALkkltgAKLMASAEDAALLA--SGGKS-DFHYGDDSL--AFP------------PVKVDRVLKDGDR 129

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596612 148 LDLGDRVLQVLHTPGHSPGGISlWEAATQT-------LF--SGDIVYDGPLVEDAYHSNL-DDYASSLARLRELP 212
Cdd:cd16288 130 VTLGGTTLTAHLTPGHTRGCTT-WTMTVKDdgkvyqvVFadSLTVNPGYKLVGNPTYPGIaEDYRHSFATLRALQ 203
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 73-220 1.11e-08

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 53.30  E-value: 1.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  73 SHTHFDHIAGHHEFAERLahpaEAEILAAPdgdntLARAYVGDEMFE------AHPECPLCYAEYRVRAAPATRLIDEGD 146
Cdd:cd07743  52 THSHADHIGGNAYLQKKT----GCKVYAPK-----IEKAFIENPLLEpsylggAYPPKELRNKFLMAKPSKVDDIIEEGE 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 147 vLDLGDRVLQVLHTPGHSPG--GIslweaATQ--TLFSGDIVYDGPLVED---AYHSNLDDYASSLARLRELPVRTVHGG 219
Cdd:cd07743 123 -LELGGVGLEIIPLPGHSFGqiGI-----LTPdgVLFAGDALFGEEVLEKygiPFLYDVEEQLETLEKLEELDADYYVPG 196


                .
gi 15596612 220 H 220
Cdd:cd07743 197 H 197
NorV COG0426
Flavorubredoxin [Energy production and conversion];
71-218 1.47e-08

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 54.45  E-value: 1.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  71 VASHTHFDHIAGHHEFAERlaHPaEAEILAAPDGDNTLaRAYVGDEMFEAHPecplcyaeyrvraapatrlIDEGDVLDL 150
Cdd:COG0426  75 IVNHQEPDHSGSLPELLEL--AP-NAKIVCSKKAARFL-PHFYGIPDFRFIV-------------------VKEGDTLDL 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 151 GDRVLQVLHTPG-HSPGGISLWEAATQTLFSGDI---------VYD----GPLVEDA--YHSNLddYASS-------LAR 207
Cdd:COG0426 132 GGHTLQFIPAPMlHWPDTMFTYDPEDKILFSGDAfgshgasdeLFDdevdEHLEEEArrYYANI--MMPFskqvlkaLKK 209

                       170
                ....*....|....
gi 15596612 208 LRELPVRTV---HG 218
Cdd:COG0426 210 VRGLDIDMIapsHG 223
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 45-209 1.74e-08

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


Pssm-ID: 293869  Cd Length: 257  Bit Score: 53.45  E-value: 1.74e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  45 VLVD-----SGSGLVSLCEQLPWLTERPLLAVASHTHFDHIAGHHEFAERlahpAEAEILAAPDGDNTLARAYVG--DEM 117
Cdd:cd16311  34 VLVDgglpeSAPKIIANIEALGFRIEDVKLILNSHGHIDHAGGLAELQRR----SGALVAASPSAALDLASGEVGpdDPQ 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 118 FEAHPECPlcyaeyrvrAAPATRLIDEGDVLDLGDRVLQVLHTPGHSPGGIS-LWEA--ATQTLfsgDIVYDGPL----V 190
Cdd:cd16311 110 YHALPKYP---------PVKDMRLARDGGQFNVGPVSLTAHATPGHTPGGLSwTWQScdGPRCL---NMVYADSQnavsR 177

                       170
                ....*....|....*....
gi 15596612 191 EDAYHSNLDDYASSLARLR 209
Cdd:cd16311 178 PGFKFSASSEYPNAVADLR 196
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 71-220 7.14e-08

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


Pssm-ID: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 51.79  E-value: 7.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  71 VASHTHFDHIAGHHEFaERLAHpaeAEILAAPDGDNTLARAYVG--DEMFEAHPECPlcyaeyrvrAAPATRLIDEGDVL 148
Cdd:cd16313  65 LSSHDHWDHAGGIAAL-QKLTG---AQVLASPATVAVLRSGSMGkdDPQFGGLTPMP---------PVASVRAVRDGEVV 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 149 DLGDRVLQVLHTPGHSPGGIS-LWEAATQTLfSGDIVYD---GPLVEDAYH-----SNLDDYASSLARLRELPVRTVHGG 219
Cdd:cd16313 132 KLGPLAVTAHATPGHTTGGTSwTWQSCEQGR-CANMVFAdslTAVSADGYRfsahpAVLADVEQSIAAVEKLACDILVSA 210


                .
gi 15596612 220 H 220
Cdd:cd16313 211 H 211
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 73-209 1.18e-07

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: 50.95  E-value: 1.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  73 SHTHFDHIAGhheFAErLAHPAEAEILAAPDGDNTLARAYVGDEmfeahPECPLCYAEYRVraapaTRLIDEGDVLDLGD 152
Cdd:cd16309  67 THAHFDHAGG---LAE-LKKATGAQLVASAADKPLLESGYVGSG-----DTKNLQFPPVRV-----DRVIGDGDKVTLGG 132

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596612 153 RVLQVLHTPGHSPGGISlWEAATQ--------TLF--SGDIVYDGPLVEDAYHSNLDDYASSLARLR 209
Cdd:cd16309 133 TTLTAHLTPGHSPGCTS-WTTTVKdtagppreVLFfcSATVAGNQLVGPPTYPGIVDDYRATFAKAR 198
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 71-220 1.19e-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: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 50.28  E-value: 1.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  71 VASHTHFDHIAGHHEF----AERLAHPAEAEILAA-PDGDntlarayvgdemfeahpecplcyaeyrvRAAPaTRLIDEG 145
Cdd:cd16276  50 VYSHNHADHIGGASIFkdegATIIAHEATAELLKRnPDPK----------------------------RPVP-TVTFDDE 100

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596612 146 DVLDLGDRVLQvLHTPG--HSPGGISLWEAATQTLFSGDIVYDG--PLVEDAYHSNLDDYASSLARLRELPVRTVHGGH 220
Cdd:cd16276 101 YTLEVGGQTLE-LSYFGpnHGPGNIVIYLPKQKVLMAVDLINPGwvPFFNFAGSEDIPGYIEALDELLEYDFDTFVGGH 178
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 73-211 1.47e-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: 47.65  E-value: 1.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  73 SHTHFDHIAGHHEF--AERLAHPAEAEILAAPDGDNTLARAYVGDEmFEAHPEcplcyaEYRVRAAPATRLIDEGDVLDL 150
Cdd:cd07730  90 SHLHWDHIGGLSDFpnARLIVGPGAKEALRPPGYPSGFLPELLPSD-FEGRLV------RWEEDDFLWVPLGPFPRALDL 162

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596612 151 -GDRVLQVLHTPGHSPGGISLW---EAATQTLFSGDIVYDG----------PLVEDAYHSNLDDYASSLARLREL 211
Cdd:cd07730 163 fGDGSLYLVDLPGHAPGHLGLLartTSGTWVFLAGDACHHRigllrpspllPLPDLDDGADREAARETLARLREL 237
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 71-220 2.13e-06

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: 47.45  E-value: 2.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  71 VASHTHFDHIAGhhefAERLAHPAEAEILAAPDGDNTL-ARAYVGDEMFEAHPecplcyaeyrVRAAPATRLIDEGDVLD 149
Cdd:cd16310  65 INTHAHYDHAGG----LAQLKADTGAKLWASRGDRPALeAGKHIGDNITQPAP----------FPAVKVDRILGDGEKIK 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 150 LGDRVLQVLHTPGHSPGGISlWEAAT-------QTLFSGDIVYDGPLVED--AYHSNLDDYASSLARLRELPVRTVHGGH 220
Cdd:cd16310 131 LGDITLTATLTPGHTKGCTT-WSTTVkengrplRVVFPCSLSVAGNVLVGnkTYPTIVEDYRASFARLRAMKADIVLTSH 209
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 27-219 2.14e-06

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


Pssm-ID: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 47.29  E-value: 2.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  27 VRPF-YRCNMWHV-QGRERDVLVDSGSGLVSLCEQLPwlTERPL----------------LAVASHTHFDHIAGhhefAE 88
Cdd:cd16312   5 VKPFnVFGNTWYVgTAGLSAVLVTSPQGHVLLDGALP--QSAPLiianiealgfriedvkLILNSHAHWDHAGG----IA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  89 RLAHPAEAEILAAPDGDNTLARAYVG--DEMFEAHPECplcyaeyRVRAAPATRLIDEGDVLDLGDRVLQVLHTPGHSPG 166
Cdd:cd16312  79 ALQKASGATVAASAHGAQVLQSGTNGkdDPQYQAKPVV-------HVAKVAKVKEVGEGDTLKVGPLRLTAHMTPGHTPG 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 167 GIS-LWEAATQ-------------TLFSGDIVYDGplvEDAYHSNLDDYASSLARLRELP---VRTVHGG 219
Cdd:cd16312 152 GTTwTWTSCEGqrcldvvyadslnPYSSGDFYYTG---KGGYPDISASFRASIAKVAALPcdiIIAVHPG 218
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 75-220 4.03e-06

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


Pssm-ID: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 45.65  E-value: 4.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  75 THFDHIAGHHEFAERLAHP---AEAEILAAPDGDNTLarayvgdemfeahpecplcyaeyrvraapatrLIDEGDVLDLG 151
Cdd:cd07727  54 THRDDVADHAKWAERFGAKriiHEDDVNAVTRPDEVI--------------------------------VLWGGDPWELD 101

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596612 152 DRVlQVLHTPGHSPGGISLWEAATQTLFSGDIVYDGPLV------EDAYHSNLDDYASSLARLRELPVRTVHGGH 220
Cdd:cd07727 102 PDL-TLIPVPGHTRGSVVLLYKEKGVLFTGDHLAWSRRRgwlsafRYVCWYSWPEQAESVERLADLDFEWVLPGH 175
ODP pfam19583
ODP family beta lactamase; The ODP (Oxygen-binding Di-iron Protein) domain is a distinct ...
 143-183 1.34e-05

ODP family beta lactamase; The ODP (Oxygen-binding Di-iron Protein) domain is a distinct member of the metallo-beta-lactamase superfamily recruited to various bacterial and archaeal signal transduction pathways, including chemotaxis, to function as oxygen and iron sensors (1). ODP was shown to act as a sensor for chemotactic responses to both iron and oxygen in the human pathogen Treponema denticola (Td). The ODP di-iron site binds oxygen at high affinity to reversibly form an unusually stable peroxo adduct.


Pssm-ID: 437415  Cd Length: 194  Bit Score: 44.40  E-value: 1.34e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 15596612   143 DEGDVLDLGD-RVLQVLHTP-GHSPGGISLWEAATQTLFSGDI 183
Cdd:pfam19583  94 DEGGRITLGSgRRLEFIPAHfLHSPGNFVTYDPVSKILFSGDI 136
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 69-212 2.14e-05

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: 44.42  E-value: 2.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  69 LAVASHTHFDHIAghhEFAE-------RLAHPAEAEILAAPDGDNTLaraYVGDEMfeAHPecplcyaeyrvrAAPATRL 141
Cdd:cd16289  63 LILHSHAHADHAG---PLAAlkratgaRVAANAESAVLLARGGSDDI---HFGDGI--TFP------------PVQADRI 122

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596612 142 IDEGDVLDLGDRVLQVLHTPGHSPGGISLWEAATQTLFSGDIVY----DGP---LVEDAYHSNL-DDYASSLARLRELP 212
Cdd:cd16289 123 VMDGEVVTLGGVTFTAHFTPGHTPGSTSWTWTDTRDGKPVRIAYadslSAPgyqLLGNPRYPRIvEDYRRTFATVRALP 201
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 71-169 2.46e-05

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: 44.38  E-value: 2.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  71 VASHTHFDHIAGHHEF-----AERLAHPAEAEILAapDGDNTlarayvgDEMFEAHpecplcyaEYRVRAAPATRLIDEG 145
Cdd:cd16308  65 LTTQAHYDHVGAMAAIkqqtgAKMMVDEKDAKVLA--DGGKS-------DYEMGGY--------GSTFAPVKADKLLHDG 127

                        90       100
                ....*....|....*....|....
gi 15596612 146 DVLDLGDRVLQVLHTPGHSPGGIS 169
Cdd:cd16308 128 DTIKLGGTKLTLLHHPGHTKGSCS 151
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 71-212 4.32e-05

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


Pssm-ID: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 43.34  E-value: 4.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  71 VASHTHFDHIAGhhefaerLAHpaeaeiLAAPDGDNTLARAYVGDEMFEAHPECPLCYAEYRVRAAPAT--RLIDEGDVL 148
Cdd:cd16314  65 VSSHEHFDHAGG-------IAR------LQRATGAPVVAREPAATTLERGRSDRSDPQFLVVEKFPPVAsvQRIGDGEVL 131

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596612 149 DLGDRVLQVLHTPGHSPGGISLWEAATQTLFSGDIVYDGPL--VEDAYHSNLDD------YASSLARLRELP 212
Cdd:cd16314 132 RVGPLALTAHATPGHTPGGTSWTWRSCEGAVCRDMVYADSVtaISDDIYRYSDHpgmvaaFRNTLDTVAALP 203
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 73-220 3.51e-04

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 40.98  E-value: 3.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612   73 SHTHFDHIAGHHEFAERLAHPAeaeILAAPDGDntlarayvgdemfeahpecplcyaeyrvRAAPATRLIDEGDVLDLGD 152
Cdd:PLN02398 128 THHHYDHTGGNLELKARYGAKV---IGSAVDKD----------------------------RIPGIDIVLKDGDKWMFAG 176

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596612  153 RVLQVLHTPGHSPGGISLWEAATQTLFSGDIVYD---GPLVEDAYHSNLddyaSSLARLRELPVRT-VHGGH 220
Cdd:PLN02398 177 HEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSlscGKLFEGTPEQML----SSLQKIISLPDDTnIYCGH 244
SPM-1-like_MBL-B1-B2-like cd16286
Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; ...
 45-229 4.82e-04

Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; MBL-fold metallo-hydrolase domain; SPM-1 was first identified in a Pseudomonas aeruginosa strain from a paediatric leukaemia patient and is a major clinical problem. 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 are most closely related to each other. SPM-1 appears to be a hybrid B1/B2 MBL.


Pssm-ID: 293844 [Multi-domain]  Cd Length: 236  Bit Score: 40.21  E-value: 4.82e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  45 VLVDSGSGLVSLCEQLPWLTE----RPLLAVASHTHFDHIAGHHEFAERLAHPAEAEI---LAAPDGDNT--LARAYVGD 115
Cdd:cd16286  40 VIVDSPYTNLATQTVLDWIAKtmgpRKVVAINTHFHLDGTGGNEALKKRGIPTWGSDLtkqLLLERGKADriKAAEFLKN 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 116 EMFEAHPECplcyaeyrVRAAPATRLID--EGDVLDLGDRVLQVLHT-PGHSPGGISLWEAATQTLFSGDIVYDGPLVED 192
Cdd:cd16286 120 EDLKRRIES--------SPPVPPDNVFDlkEGKVFSFGNELVEVSFPgPAHAPDNVVVYFPERKILFGGCMIKPGKELGN 191

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15596612 193 AYHSNLDDYASSLARLRELPVRTVHGGHfasfsGERL 229
Cdd:cd16286 192 LGDANMKAWPDSVRRLKKFDAKIVIPGH-----GERG 223
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 73-221 8.26e-04

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: 39.74  E-value: 8.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  73 SHTHFDHIAGHHEFaERLAHpAEAEILaapDGDNTLARAYvGDEMFEAHPECPLCYAEYRVraapaTRLIDEGDVLDLGD 152
Cdd:cd16307  67 SHAHFDHAAGSALI-KRETH-AKYMVM---DGDVDVVESG-GKSDFFYGNDPSTYFPPAHV-----DKVLHDGEQVELGG 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 153 RVLQVLHTPGHSPgGISLWeaaTQTLFSGDIVYD-----GP-------LVEDAYHSNL-DDYASSLARLRELPVRT---V 216
Cdd:cd16307 136 TVLTAHLTAGHTK-GCTTW---TMKVKDHGKTYDvvivgSPnvnpgakLVNNITYPGIaEDYAHTFAVLRSLPCDIflgA 211


                ....*
gi 15596612 217 HGGHF 221
Cdd:cd16307 212 HGGYF 216
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 64-220 8.58e-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: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 39.41  E-value: 8.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  64 TERPLLAV-ASHTHFDHIAGHHEFAERLahPaEAEILAAPDgdnTLA--RAYVGDEMFEAHPECPlcyaeyrvRAAPATR 140
Cdd:cd07739  49 SGKTLTTIyITHGHPDHYFGLEVLLEAF--P-DAKVVATPA---VVAhiKAQLEPKLAFWGPLLG--------GNAPARL 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 141 LIDE---GDVLDLGDRVLQVLHTPGHSPGGIS-LWEAATQTLFSGDIVYDG---PLVEDAYHSNLDDYASSLARLRELPV 213
Cdd:cd07739 115 VVPEpldGDTLTLEGHPLEIVGVGGGDTDDTTyLWIPSLKTVVAGDVVYNGvhvWLADATTPELRAAWLAALDKIEALNP 194


                ....*..
gi 15596612 214 RTVHGGH 220
Cdd:cd07739 195 ETVVPGH 201
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 161-220 2.18e-03

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


Pssm-ID: 293793 [Multi-domain]  Cd Length: 219  Bit Score: 38.29  E-value: 2.18e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596612 161 PGHSPGGISLWEAATQTLFSGDIVYDGPL--VEDAyhsNLDDYASSLARL--RELPVRTVHGGH 220
Cdd:cd07707 143 PAHTPDNIVVYFPQENVLYGGCIIKETDLgnVADA---DVKEWPTSIERLkkRYRNIKAVIPGH 203
CphA_ImiS-like_MBL-B2 cd16306
Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and related metallo-beta-lactamases, ...
 145-229 2.63e-03

Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and related metallo-beta-lactamases, subclass B2; 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. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis.


Pssm-ID: 293864  Cd Length: 222  Bit Score: 38.01  E-value: 2.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 145 GDVLDLGDRVLQVLHTPGHSPGGISLWEAATQTLFSGDIVydGPLVEDAYHSNLDDYASSLARLR--ELPVRTVHGGHFA 222
Cdd:cd16306 127 GDFTLQEGKVRAFYLGPAHTPDGIFVYFPDEQVLYGNCIL--KEKLGNLSFADVKAYPQTLERLKamKLPIKTVIGGHDS 204


                ....*..
gi 15596612 223 SFSGERL 229
Cdd:cd16306 205 PLHGPEL 211
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 37-221 2.95e-03

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 37.95  E-value: 2.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612  37 HVQGRERDVLVDSGSGLVSLCEQLPwLTERPLLAVA-SHTHFDHIAGHHEFAERLaHPAEAEILAAPDGDNTLARAYvgd 115
Cdd:COG1235  39 LVEADGTRLLIDAGPDLREQLLRLG-LDPSKIDAILlTHEHADHIAGLDDLRPRY-GPNPIPVYATPGTLEALERRF--- 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596612 116 emfeahpecplCYAEYRVRAAPATRLIDEGDVLDLGD---RVLQVLHTPGHSPG--------------GISLWEAATQTL 178
Cdd:COG1235 114 -----------PYLFAPYPGKLEFHEIEPGEPFEIGGltvTPFPVPHDAGDPVGyriedggkklayatDTGYIPEEVLEL 182

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15596612 179 FSG-DI-VYDGpLVEDAY--HSNLDDyasSLARLRELPVRTVHGGHF 221
Cdd:COG1235 183 LRGaDLlILDA-TYDDPEpgHLSNEE---ALELLARLGPKRLVLTHL 225
 
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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