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Conserved domains on  [gi|17538952|ref|NP_501684|]
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Metallo-beta-lactamase domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02962 super family cl30130
hydroxyacylglutathione hydrolase
 10-234 7.43e-100

hydroxyacylglutathione hydrolase


The actual alignment was detected with superfamily member PLN02962:

Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 290.55  E-value: 7.43e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952   10 IFRQLIEFKSSTYTYIIG--CHKTGKAVIIDPVVDTVSRDIQIIRDLNLDLIYGLNTHVHADHITGTNSLKTVFPTMKSV 87
Cdd:PLN02962  12 LFRQLFEKESSTYTYLLAdvSHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVKSI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952   88 LSSKSGGEADKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYV------EHSLRSAFTGDALLIRACGRTDFQQGNPASLF 161
Cdd:PLN02962  92 ISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVtgegpdQPQPRMAFTGDALLIRGCGRTDFQGGSSDQLY 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17538952  162 DSVHDKIFTLPEDYVVYVGHNYNGVLQTTVWEEKNLNPRLTKSKDQFVEIMKNLKLNYPKQIDKAVPANMVDG 234
Cdd:PLN02962 172 KSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPANMVCG 244
 
Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 10-234 7.43e-100

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 290.55  E-value: 7.43e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952   10 IFRQLIEFKSSTYTYIIG--CHKTGKAVIIDPVVDTVSRDIQIIRDLNLDLIYGLNTHVHADHITGTNSLKTVFPTMKSV 87
Cdd:PLN02962  12 LFRQLFEKESSTYTYLLAdvSHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVKSI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952   88 LSSKSGGEADKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYV------EHSLRSAFTGDALLIRACGRTDFQQGNPASLF 161
Cdd:PLN02962  92 ISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVtgegpdQPQPRMAFTGDALLIRGCGRTDFQGGSSDQLY 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17538952  162 DSVHDKIFTLPEDYVVYVGHNYNGVLQTTVWEEKNLNPRLTKSKDQFVEIMKNLKLNYPKQIDKAVPANMVDG 234
Cdd:PLN02962 172 KSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPANMVCG 244
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 10-183 4.70e-76

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: 227.67  E-value: 4.70e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  10 IFRQLIEFKSSTYTYIIGCHKTGKAVIIDPVVDTVSRDIQIIRDLNLDLIYGLNTHVHADHITGTNSLKTVfPTMKSVLS 89
Cdd:cd07724   1 IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAER-TGAPIVIG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  90 SKSGGE-ADKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYVEHSLRSAFTGDALLIRACGRTDFQQ---GNPASLFDSVH 165
Cdd:cd07724  80 EGAPASfFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPGeaeGLARQLYDSLQ 159

                       170
                ....*....|....*...
gi 17538952 166 DKIFTLPEDYVVYVGHNY 183
Cdd:cd07724 160 RKLLLLPDETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 9-183 3.49e-37

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: 129.81  E-value: 3.49e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952   9 PIFRQLIEFKSSTYTYIIGChkTGKAVIIDPVVDTVSRD--IQIIRDLNLDLIYGLNTHVHADHITGTNSLKTVF----- 81
Cdd:COG0491   3 VLPGGTPGAGLGVNSYLIVG--GDGAVLIDTGLGPADAEalLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFgapvy 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  82 --PTMKSVLSSKSGG--------EADKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYVEHSLRSAFTGDALLIRACGRTD 151
Cdd:COG0491  81 ahAAEAEALEAPAAGalfgrepvPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPD 160

                       170       180       190
                ....*....|....*....|....*....|..
gi 17538952 152 FQQGNPASLFDSVhDKIFTLPEDyVVYVGHNY 183
Cdd:COG0491 161 LPDGDLAQWLASL-ERLLALPPD-LVIPGHGP 190
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 22-183 2.02e-23

hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione hydrolase, a detoxification enzyme known as glyoxalase II. It follows lactoylglutathione lyase, or glyoxalase I, and acts to remove the toxic metabolite methylglyoxal and related compounds. This protein belongs to the broader metallo-beta-lactamase family (pfam00753). [Cellular processes, Detoxification]


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 94.53  E-value: 2.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952    22 YTYIIgCHKTGKAVIID-----PVVDTVSRdiqiiRDLNLDLIygLNTHVHADHITGTNSLKTVFPTmkSVLSSKSGG-- 94
Cdd:TIGR03413  11 YIWLL-HDPDGQAAVVDpgeaePVLDALEA-----RGLTLTAI--LLTHHHHDHVGGVAELLEAFPA--PVYGPAEERip 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952    95 EADKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYVEHSLRSAFTGDALLIRACGRTdFqQGNPASLFDSVHdKIFTLPED 174
Cdd:TIGR03413  81 GITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRL-F-EGTPEQMYDSLQ-RLAALPDD 157


                  ....*....
gi 17538952   175 YVVYVGHNY 183
Cdd:TIGR03413 158 TLVYCAHEY 166
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 22-181 9.53e-23

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: 91.08  E-value: 9.53e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952     22 YTYIIGChkTGKAVIIDPVVDTVSRDIQIIRDLNL-DLIYGLNTHVHADHITGTNSLKTVFPT----------------- 83
Cdd:smart00849   1 NSYLVRD--DGGAILIDTGPGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGApvyapegtaellkdlla 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952     84 -MKSVLSSKSGGEADKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYVEHSLRSAFTGDALLIRACGRTDFQQGN-PASLF 161
Cdd:smart00849  79 lLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDaAASDA 158

                          170       180
                   ....*....|....*....|
gi 17538952    162 DSVHDKIFTLPEDYvVYVGH 181
Cdd:smart00849 159 LESLLKLLKLLPKL-VVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
20-181 5.07e-13

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 65.47  E-value: 5.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952    20 STYTYIIGchKTGKAVIIDPVVDTVSRDIQIIRDLNL---DLIYGLNTHVHADHITGTNSLKTVFPT------------- 83
Cdd:pfam00753   5 QVNSYLIE--GGGGAVLIDTGGSAEAALLLLLAALGLgpkDIDAVILTHGHFDHIGGLGELAEATDVpvivvaeearell 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952    84 ----------MKSVLSSKSGGEADKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYVEHSLRSAFTGDALLIRACGRTDFQ 153
Cdd:pfam00753  83 deelglaasrLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLP 162

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 17538952   154 QGNPASLFDSVH-------DKIFTLPEDyVVYVGH 181
Cdd:pfam00753 163 LGGLLVLHPSSAessleslLKLAKLKAA-VIVPGH 196
 
Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 10-234 7.43e-100

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 290.55  E-value: 7.43e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952   10 IFRQLIEFKSSTYTYIIG--CHKTGKAVIIDPVVDTVSRDIQIIRDLNLDLIYGLNTHVHADHITGTNSLKTVFPTMKSV 87
Cdd:PLN02962  12 LFRQLFEKESSTYTYLLAdvSHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVKSI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952   88 LSSKSGGEADKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYV------EHSLRSAFTGDALLIRACGRTDFQQGNPASLF 161
Cdd:PLN02962  92 ISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVtgegpdQPQPRMAFTGDALLIRGCGRTDFQGGSSDQLY 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17538952  162 DSVHDKIFTLPEDYVVYVGHNYNGVLQTTVWEEKNLNPRLTKSKDQFVEIMKNLKLNYPKQIDKAVPANMVDG 234
Cdd:PLN02962 172 KSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPANMVCG 244
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 10-183 4.70e-76

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: 227.67  E-value: 4.70e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  10 IFRQLIEFKSSTYTYIIGCHKTGKAVIIDPVVDTVSRDIQIIRDLNLDLIYGLNTHVHADHITGTNSLKTVfPTMKSVLS 89
Cdd:cd07724   1 IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAER-TGAPIVIG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  90 SKSGGE-ADKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYVEHSLRSAFTGDALLIRACGRTDFQQ---GNPASLFDSVH 165
Cdd:cd07724  80 EGAPASfFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPGeaeGLARQLYDSLQ 159

                       170
                ....*....|....*...
gi 17538952 166 DKIFTLPEDYVVYVGHNY 183
Cdd:cd07724 160 RKLLLLPDETLVYPGHDY 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 20-181 1.85e-40

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: 137.03  E-value: 1.85e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  20 STYTYIIGChKTGKAVIIDPVVDTVSRDIQIIRDLNLDLIYGLNTHVHADHITGTNSLKTVF-----------PTMKSVL 88
Cdd:cd06262   9 QTNCYLVSD-EEGEAILIDPGAGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPgapvyiheadaELLEDPE 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  89 SSKSGG--------EADKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYVEHSLRSAFTGDALLIRACGRTDFQQGNPASL 160
Cdd:cd06262  88 LNLAFFgggplpppEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDLPGGDPEQL 167

                       170       180
                ....*....|....*....|.
gi 17538952 161 FDSVHDKIFTLPEDYVVYVGH 181
Cdd:cd06262 168 IESIKKLLLLLPDDTVVYPGH 188
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 22-181 2.83e-40

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: 136.05  E-value: 2.83e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  22 YTYIIGCHKTGKAVIIDPV-VDTVsrdIQIIRDLNLDLIYGLNTHVHADHITGTNSLKTVFPTMKsVLSSKSG--GEADK 98
Cdd:cd07723  10 YIYLIVDEATGEAAVVDPGeAEPV---LAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAP-VYGPAEDriPGLDH 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  99 YVSDGEIIEIGGLKLEVRETPGHTNGCLTYVEHSLRSAFTGDALLIRACGRtdFQQGNPASLFDSvHDKIFTLPEDYVVY 178
Cdd:cd07723  86 PVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGR--FFEGTAEQMYAS-LQKLLALPDDTLVY 162


                ...
gi 17538952 179 VGH 181
Cdd:cd07723 163 CGH 165
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 9-183 3.49e-37

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: 129.81  E-value: 3.49e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952   9 PIFRQLIEFKSSTYTYIIGChkTGKAVIIDPVVDTVSRD--IQIIRDLNLDLIYGLNTHVHADHITGTNSLKTVF----- 81
Cdd:COG0491   3 VLPGGTPGAGLGVNSYLIVG--GDGAVLIDTGLGPADAEalLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFgapvy 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  82 --PTMKSVLSSKSGG--------EADKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYVEHSLRSAFTGDALLIRACGRTD 151
Cdd:COG0491  81 ahAAEAEALEAPAAGalfgrepvPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPD 160

                       170       180       190
                ....*....|....*....|....*....|..
gi 17538952 152 FQQGNPASLFDSVhDKIFTLPEDyVVYVGHNY 183
Cdd:COG0491 161 LPDGDLAQWLASL-ERLLALPPD-LVIPGHGP 190
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 24-181 7.36e-32

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: 114.96  E-value: 7.36e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  24 YIIGCHKTGKAVIIDPVVDtVSRDIQIIRDLNLDLIYGLNTHVHADHITGTNSLKTVF------------PTMKSVLS-S 90
Cdd:cd07737  14 SLIWCEETKEAAVIDPGGD-ADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYgvpiigphkedkFLLENLPEqS 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  91 KSGG-------EADKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYVEHSLRSAFTGDALLIRACGRTDFQQGNPASLFDS 163
Cdd:cd07737  93 QMFGfppaeafTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTDFPGGNHAQLIAS 172

                       170
                ....*....|....*...
gi 17538952 164 VHDKIFTLPEDYVVYVGH 181
Cdd:cd07737 173 IKEKLLPLGDDVTFIPGH 190
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 23-201 6.34e-31

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: 113.21  E-value: 6.34e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  23 TYIIGCHKTGKAVIIDPVvDTVSRDIQIIRDLNLDLIYGLNTHVHADHITG------TNSLKTVFPTMKSVL------SS 90
Cdd:cd16322  13 TYLVADEGGGEAVLVDPG-DESEKLLARFGTTGLTLLYILLTHAHFDHVGGvadlrrHPGAPVYLHPDDLPLyeaadlGA 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  91 KSGG-------EADKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYVEHSLRSAFTGDALLIRACGRTDFQQGNPASLFDS 163
Cdd:cd16322  92 KAFGlgieplpPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRTDLPGGDPKAMAAS 171

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 17538952 164 vHDKIFTLPEDYVVYVGHnynGVlQTTVWEEKNLNPRL 201
Cdd:cd16322 172 -LRRLLTLPDETRVFPGH---GP-PTTLGEERRTNPFL 204
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 22-181 1.55e-30

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: 111.09  E-value: 1.55e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  22 YTYIIGCHKTGKAVIIDPVVDtVSRDIQIIRDLNLDLIYGLNTHVHADHITGTNSLKTVFPTmkSVLSSKSggEADKY-- 99
Cdd:cd16275  13 YSYIIIDKATREAAVVDPAWD-IEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDA--PVYMSKE--EIDYYgf 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952 100 -------VSDGEIIEIGGLKLEVRETPGHTNGCLTY-VEHSLrsaFTGDALLIRACGRTDFQQGNPASLFDSVHdKIFTL 171
Cdd:cd16275  88 rcpnlipLEDGDTIKIGDTEITCLLTPGHTPGSMCYlLGDSL---FTGDTLFIEGCGRCDLPGGDPEEMYESLQ-RLKKL 163

                       170
                ....*....|.
gi 17538952 172 PEDYV-VYVGH 181
Cdd:cd16275 164 PPPNTrVYPGH 174
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 22-183 2.02e-23

hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione hydrolase, a detoxification enzyme known as glyoxalase II. It follows lactoylglutathione lyase, or glyoxalase I, and acts to remove the toxic metabolite methylglyoxal and related compounds. This protein belongs to the broader metallo-beta-lactamase family (pfam00753). [Cellular processes, Detoxification]


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 94.53  E-value: 2.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952    22 YTYIIgCHKTGKAVIID-----PVVDTVSRdiqiiRDLNLDLIygLNTHVHADHITGTNSLKTVFPTmkSVLSSKSGG-- 94
Cdd:TIGR03413  11 YIWLL-HDPDGQAAVVDpgeaePVLDALEA-----RGLTLTAI--LLTHHHHDHVGGVAELLEAFPA--PVYGPAEERip 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952    95 EADKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYVEHSLRSAFTGDALLIRACGRTdFqQGNPASLFDSVHdKIFTLPED 174
Cdd:TIGR03413  81 GITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRL-F-EGTPEQMYDSLQ-RLAALPDD 157


                  ....*....
gi 17538952   175 YVVYVGHNY 183
Cdd:TIGR03413 158 TLVYCAHEY 166
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 22-181 9.53e-23

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: 91.08  E-value: 9.53e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952     22 YTYIIGChkTGKAVIIDPVVDTVSRDIQIIRDLNL-DLIYGLNTHVHADHITGTNSLKTVFPT----------------- 83
Cdd:smart00849   1 NSYLVRD--DGGAILIDTGPGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGApvyapegtaellkdlla 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952     84 -MKSVLSSKSGGEADKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYVEHSLRSAFTGDALLIRACGRTDFQQGN-PASLF 161
Cdd:smart00849  79 lLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDaAASDA 158

                          170       180
                   ....*....|....*....|
gi 17538952    162 DSVHDKIFTLPEDYvVYVGH 181
Cdd:smart00849 159 LESLLKLLKLLPKL-VVPGH 177
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 22-206 1.39e-19

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 85.66  E-value: 1.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952   22 YTYIIGCHKTGKAVIIDP-----VVDTVSRDiqiirdlNLDLIYGLNTHVHADHITGTNSLKTVFPTmKSVLSSKSGGEA 96
Cdd:PLN02398  88 YAYLLHDEDTGTVGVVDPseavpVIDALSRK-------NRNLTYILNTHHHYDHTGGNLELKARYGA-KVIGSAVDKDRI 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952   97 ---DKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYVEHSLRSAFTGDALLIRACGRtdFQQGNPASLFDSVHdKIFTLPE 173
Cdd:PLN02398 160 pgiDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGK--LFEGTPEQMLSSLQ-KIISLPD 236

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17538952  174 DYVVYVGHNY--------------NGVLQ------------------TTVWEEKNLNPRL-TKSKD 206
Cdd:PLN02398 237 DTNIYCGHEYtlsnskfalsiepnNEVLQsyaahvahlrskglptipTTVKMEKACNPFLrTSSTD 302
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 22-183 4.59e-18

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 80.19  E-value: 4.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952   22 YTYIIGCHKTGKAVIIDPV-VDTVsrdIQIIRDLNLDLIYGLNTHVHADHITGTNSLKTVFPTMKSVlssksGGEADKY- 99
Cdd:PLN02469  13 YAYLIIDESTKDAAVVDPVdPEKV---LQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVY-----GGSLDNVk 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  100 -----VSDGEIIEIGG-LKLEVRETPGHTNGCLTYV----EHSLRSAFTGDALLIRACGRtdFQQGNPASLFDSVHDKIF 169
Cdd:PLN02469  85 gcthpVENGDKLSLGKdVNILALHTPCHTKGHISYYvtgkEGEDPAVFTGDTLFIAGCGK--FFEGTAEQMYQSLCVTLG 162

                        170
                 ....*....|....
gi 17538952  170 TLPEDYVVYVGHNY 183
Cdd:PLN02469 163 SLPKPTQVYCGHEY 176
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 32-183 4.21e-13

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 66.77  E-value: 4.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952   32 GKAVIIDPvvDTVSRDIQIIRDLNLDLIYGLNTHVHADHITGTNSLKTVFP--TMKSVLSSKSGGeADKYVSDGEIIEIG 109
Cdd:PRK10241  22 GRCLIVDP--GEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPqiVVYGPQETQDKG-TTQVVKDGETAFVL 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17538952  110 GLKLEVRETPGHTNGCLTYVEHSLrsAFTGDALLIRACGRtdFQQGNPASLFDSVHdKIFTLPEDYVVYVGHNY 183
Cdd:PRK10241  99 GHEFSVFATPGHTLGHICYFSKPY--LFCGDTLFSGGCGR--LFEGTASQMYQSLK-KINALPDDTLICCAHEY 167
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
20-181 5.07e-13

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 65.47  E-value: 5.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952    20 STYTYIIGchKTGKAVIIDPVVDTVSRDIQIIRDLNL---DLIYGLNTHVHADHITGTNSLKTVFPT------------- 83
Cdd:pfam00753   5 QVNSYLIE--GGGGAVLIDTGGSAEAALLLLLAALGLgpkDIDAVILTHGHFDHIGGLGELAEATDVpvivvaeearell 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952    84 ----------MKSVLSSKSGGEADKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYVEHSLRSAFTGDALLIRACGRTDFQ 153
Cdd:pfam00753  83 deelglaasrLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLP 162

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 17538952   154 QGNPASLFDSVH-------DKIFTLPEDyVVYVGH 181
Cdd:pfam00753 163 LGGLLVLHPSSAessleslLKLAKLKAA-VIVPGH 196
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 64-181 7.37e-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: 61.93  E-value: 7.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  64 THVHADHITGTNslktvfptmksVLSSKSGGEA----DKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYVEHSLRSAFTG 139
Cdd:cd07725  62 THHHPDHIGLAG-----------KLQEKSGATVyildVTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVG 130

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 17538952 140 DALL--IRAC-GRTDFQQGNP-----ASLfdsvhDKIFTLpEDYVVYVGH 181
Cdd:cd07725 131 DAVLpkITPNvSLWAVRVEDPlgaylESL-----DKLEKL-DVDLAYPGH 174
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 13-181 3.28e-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: 60.58  E-value: 3.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  13 QLIEFKSSTYTYIIGCHktGKAVIIDP-VVDTVSRDIQIIRDLNL---DLIYGLNTHVHADHITGTNSLKTVFPTMKSVL 88
Cdd:cd07726   8 GFLGFPGRIASYLLDGE--GRPALIDTgPSSSVPRLLAALEALGIapeDVDYIILTHIHLDHAGGAGLLAEALPNAKVYV 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  89 ----------------SSKS--GGEADKY--------------VSDGEIIEIGGLKLEVRETPGHTNGCLTYVEHSLRSA 136
Cdd:cd07726  86 hprgarhlidpsklwaSARAvyGDEADRLggeilpvpeervivLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESDGL 165

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17538952 137 FTGDALLIRACGR----------TDFqqgNPASLFDSVhDKIFTLPEDYvVYVGH 181
Cdd:cd07726 166 FTGDAAGVRYPELdvvgppstppPDF---DPEAWLESL-DRLLSLKPER-IYLTH 215
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 33-181 6.35e-11

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: 59.18  E-value: 6.35e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  33 KAVIID---PVVDTvsrdIQIIRDLNLDLIYGLNTHVHADHITGTNS-------------LKTVFPTMKSVLSSKS---- 92
Cdd:cd07712  19 RALLIDtglGIGDL----KEYVRTLTDLPLLVVATHGHFDHIGGLHEfeevyvhpadaeiLAAPDNFETLTWDAATysvp 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  93 GGEADKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYVEHSLRSAFTGDAL----LIRACGRTDFQQGNpASLfdsvhDKI 168
Cdd:cd07712  95 PAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVydgpLIMDLPHSDLDDYL-ASL-----EKL 168

                       170
                ....*....|....
gi 17538952 169 FTLPEDY-VVYVGH 181
Cdd:cd07712 169 SKLPDEFdKVLPGH 182
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-129 2.16e-10

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 58.75  E-value: 2.16e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  35 VIIDPVVDTVSRDIQI--IRDLNL---DLIYGLNTHVHADHITGTNSLKTVFPTmKSVLS-----------SKSGGEA-- 96
Cdd:cd16280  34 ILIDALNNNEAADLIVdgLEKLGLdpaDIKYILITHGHGDHYGGAAYLKDLYGA-KVVMSeadwdmmeeppEEGDNPRwg 112

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 17538952  97 -----DKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYV 129
Cdd:cd16280 113 ppperDIVIKDGDTLTLGDTTITVYLTPGHTPGTLSLI 150
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 57-128 5.96e-10

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: 57.56  E-value: 5.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  57 DLIYGLNTHVHADHITGTNSLK----------------------TVFPTMKSVLSSKSGGEADKYVSDGEIIEIGGLKLE 114
Cdd:cd07708  60 DTKLILISHAHFDHAGGSAEIKkqtgakvmagaedvslllsggsSDFHYANDSSTYFPQSTVDRAVHDGERVTLGGTVLT 139

                        90
                ....*....|....
gi 17538952 115 VRETPGHTNGCLTY 128
Cdd:cd07708 140 AHATPGHTPGCTTW 153
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 21-143 4.16e-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: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 54.42  E-value: 4.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  21 TYTYIIGCHKTgkAVIIDPVVDTVS--RDIQ-IIRDLNLDLIygLNTHVHADHITGTNSLK--TVFPTM----KSVLSSK 91
Cdd:cd16278  18 TNTYLLGAPDG--VVVIDPGPDDPAhlDALLaALGGGRVSAI--LVTHTHRDHSPGAARLAerTGAPVRafgpHRAGGQD 93

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 17538952  92 SGGEADKYVSDGEIIEIGGLKLEVRETPGHTNGCLTYVEHSLRSAFTGDALL 143
Cdd:cd16278  94 TDFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVM 145
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 21-143 7.24e-09

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: 53.69  E-value: 7.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  21 TYTYIIGCHK------TG----------KAVIIDPVVDTVSrDIqIIrdlnldliyglnTHVHADHITGTNSLKTV---- 80
Cdd:cd07722  18 TNTYLVGTGKrrilidTGegrpsyipllKSVLDSEGNATIS-DI-LL------------THWHHDHVGGLPDVLDLlrgp 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17538952  81 ------FPTMKSVLSSKSGGEADKYVSDGEIIEIGGLKLEVRETPGHTNG--CLTYVEhsLRSAFTGDALL 143
Cdd:cd07722  84 sprvykFPRPEEDEDPDEDGGDIHDLQDGQVFKVEGATLRVIHTPGHTTDhvCFLLEE--ENALFTGDCVL 152
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 57-199 1.89e-07

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: 50.37  E-value: 1.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  57 DLIYGLNTHVHADHITGTNSLK-----TVF--PTMKSVLSSKSGGEAD-----------------KYVSDGEIIEIGGLK 112
Cdd:cd16312  60 DVKLILNSHAHWDHAGGIAALQkasgaTVAasAHGAQVLQSGTNGKDDpqyqakpvvhvakvakvKEVGEGDTLKVGPLR 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952 113 LEVRETPGHTNG-------------CLTYV-EHSLRSAFTGDallIRACGRTDFQqgNPASLFDSVHDKIFTLPEDYVVY 178
Cdd:cd16312 140 LTAHMTPGHTPGgttwtwtscegqrCLDVVyADSLNPYSSGD---FYYTGKGGYP--DISASFRASIAKVAALPCDIIIA 214

                       170       180
                ....*....|....*....|.
gi 17538952 179 VGHNYNGVLQTTVWEEKNLNP 199
Cdd:cd16312 215 VHPGFTDVLDKAKRRSGDTNP 235
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 29-142 1.90e-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) 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: 49.84  E-value: 1.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  29 HKTGKAVIIDPVVD--TVSRDIQIIRDLNLDLIYGLNTHVHADHITGTNSLK--------------------TVFPTM-- 84
Cdd:cd07743  15 FGDKEALLIDSGLDedAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQkktgckvyapkiekafienpLLEPSYlg 94

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17538952  85 ----------KSVLSSKSggEADKYVSDGEiIEIGGLKLEVRETPGHTNGCLTYVeHSLRSAFTGDAL 142
Cdd:cd07743  95 gayppkelrnKFLMAKPS--KVDDIIEEGE-LELGGVGLEIIPLPGHSFGQIGIL-TPDGVLFAGDAL 158
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 57-129 2.94e-07

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


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 50.01  E-value: 2.94e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  57 DLIYGLNTHVHADHITGTNSLKTVfpTMKSVLSSK-------SGG----------------EADKYVSDGEIIEIGGLKL 113
Cdd:cd16288  60 DIKILLNSHAHLDHAGGLAALKKL--TGAKLMASAedaallaSGGksdfhygddslafppvKVDRVLKDGDRVTLGGTTL 137

                        90
                ....*....|....*.
gi 17538952 114 EVRETPGHTNGCLTYV 129
Cdd:cd16288 138 TAHLTPGHTRGCTTWT 153
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 57-128 4.53e-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: 49.40  E-value: 4.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  57 DLIYGLNTHVHADHITGTNSLKTVfpTMKSVLSSK------------SGGEA---------DKYVSDGEIIEIGGLKLEV 115
Cdd:cd16309  60 DVKYLLNTHAHFDHAGGLAELKKA--TGAQLVASAadkpllesgyvgSGDTKnlqfppvrvDRVIGDGDKVTLGGTTLTA 137

                        90
                ....*....|...
gi 17538952 116 RETPGHTNGCLTY 128
Cdd:cd16309 138 HLTPGHSPGCTSW 150
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 33-128 6.69e-07

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: 48.99  E-value: 6.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  33 KAVIIDPVVD----TVSRDIQIIrDLNL-DLIYGLNTHVHADHITGTNSLKT-----VFPTMKSVLSSKSGG-------- 94
Cdd:cd16310  32 GAILLDGGLEenaaLIEQNIKAL-GFKLsDIKIIINTHAHYDHAGGLAQLKAdtgakLWASRGDRPALEAGKhigdnitq 110

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17538952  95 -------EADKYVSDGEIIEIGGLKLEVRETPGHTNGCLTY 128
Cdd:cd16310 111 papfpavKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTW 151
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 57-128 1.44e-06

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: 47.89  E-value: 1.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  57 DLIYGLNTHVHADHITGTNSLK------TVFPTMKSVLSSKSGGE--------------ADKYVSDGEIIEIGGLKLEVR 116
Cdd:cd16289  60 DLKLILHSHAHADHAGPLAALKratgarVAANAESAVLLARGGSDdihfgdgitfppvqADRIVMDGEVVTLGGVTFTAH 139

                        90
                ....*....|..
gi 17538952 117 ETPGHTNGCLTY 128
Cdd:cd16289 140 FTPGHTPGSTSW 151
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 ...
 57-128 2.02e-06

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: 47.34  E-value: 2.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  57 DLIYGLNTHVHADHITGTNSLK-----TVFPTMKSVLSSKSG---------GEADKY--------VSDGEIIEIGGLKLE 114
Cdd:cd16290  60 DVKLILNSHAHFDHAGGIAALQrdsgaTVAASPAGAAALRSGgvdpddpqaGAADPFppvakvrvVADGEVVKLGPLAVT 139

                        90
                ....*....|....
gi 17538952 115 VRETPGHTNGCLTY 128
Cdd:cd16290 140 AHATPGHTPGGTSW 153
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 62-129 4.73e-06

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: 46.31  E-value: 4.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  62 LNTHVHADHITGTNSLKT-----VFPTMKSVLSSKSGG----------------EADKYVSDGEIIEIGGLKLEVRETPG 120
Cdd:cd16308  65 LTTQAHYDHVGAMAAIKQqtgakMMVDEKDAKVLADGGksdyemggygstfapvKADKLLHDGDTIKLGGTKLTLLHHPG 144


                ....*....
gi 17538952 121 HTNGCLTYV 129
Cdd:cd16308 145 HTKGSCSFL 153
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 64-142 5.33e-06

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: 45.68  E-value: 5.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  64 THVHADHI------------------------TGTNSLKTVFPTMKSVLSSKS----GGEADKYVSDGEIIEIGGlKLEV 115
Cdd:cd07721  56 THGHIDHIgslaalkeapgapvyahereapylEGEKPYPPPVRLGLLGLLSPLlpvkPVPVDRTLEDGDTLDLAG-GLRV 134

                        90       100
                ....*....|....*....|....*..
gi 17538952 116 RETPGHTNGCLTYVEHSLRSAFTGDAL 142
Cdd:cd07721 135 IHTPGHTPGHISLYLEEDGVLIAGDAL 161
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 23-177 7.58e-06

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: 45.62  E-value: 7.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  23 TYIIGCHKTGKAVIIDP----VVDTVSRDI--QI---IRDLNL---DLIYGLNTHVHADHITGTNSLK-----TVF--PT 83
Cdd:cd16313  14 TYYVGTGGISAVLITSPqghiLIDGGFPKSpeQIaasIRQLGFkleDVKYILSSHDHWDHAGGIAALQkltgaQVLasPA 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  84 MKSVLSSKSGGEAD---------------KYVSDGEIIEIGGLKLEVRETPGHTNGCLTYVEHS-----LRSAFTGDALL 143
Cdd:cd16313  94 TVAVLRSGSMGKDDpqfggltpmppvasvRAVRDGEVVKLGPLAVTAHATPGHTTGGTSWTWQSceqgrCANMVFADSLT 173

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 17538952 144 IRACGRTDFqQGNPASLFDSVHD--KIFTLPEDYVV 177
Cdd:cd16313 174 AVSADGYRF-SAHPAVLADVEQSiaAVEKLACDILV 208
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 62-128 1.24e-05

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: 45.13  E-value: 1.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  62 LNTHVHADHITGTNSLK-----TVFPTMKSVLSSKSGGEA-----------------DKYVSDGEIIEIGGLKLEVRETP 119
Cdd:cd16307  65 LISHAHFDHAAGSALIKrethaKYMVMDGDVDVVESGGKSdffygndpstyfppahvDKVLHDGEQVELGGTVLTAHLTA 144


                ....*....
gi 17538952 120 GHTNGCLTY 128
Cdd:cd16307 145 GHTKGCTTW 153
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 20-141 6.13e-05

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: 42.86  E-value: 6.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  20 STY-TYIIgchKTGKAVIIDPVVDTVSRDI-----QIIRDLNLDLIYgLNtHVHADHITGTNSLKTVFPTMKSVLSSKS- 92
Cdd:cd07709  30 TSYnSYLI---KDEKTALIDTVKEPFFDEFlenleEVIDPRKIDYIV-VN-HQEPDHSGSLPELLELAPNAKIVCSKKAa 104

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  93 -------GGEADKY--VSDGEIIEIGGLKLEVRETPG-HTNGCL-TYVEHSlRSAFTGDA 141
Cdd:cd07709 105 rflkhfyPGIDERFvvVKDGDTLDLGKHTLKFIPAPMlHWPDTMvTYDPED-KILFSGDA 163
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 19-127 2.16e-04

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: 41.03  E-value: 2.16e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  19 SSTYTYIigchKTGKAVIIdpvVDT---VSRD--IQIIRDLNL---DLIYGLNTHVHADHITGTNslktVFPTMKSVLSS 90
Cdd:cd07711  21 SSTVTLI----KDGGKNIL---VDTgtpWDRDllLKALAEHGLspeDIDYVVLTHGHPDHIGNLN----LFPNATVIVGW 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 17538952  91 KsggEADKYVSDGEIIEIGGLKL----EVRETPGHTNGCLT 127
Cdd:cd07711  90 D---ICGDSYDDHSLEEGDGYEIdenvEVIPTPGHTPEDVS 127
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 62-128 2.51e-04

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: 41.18  E-value: 2.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  62 LNTHVHADHITGTNSLK-------TVFPTMKSVLSSKSGGEAD---------------KYVSDGEIIEIGGLKLEVRETP 119
Cdd:cd16315  65 LSSHEHFDHVGGLAALQratgarvAASAAAAPVLESGKPAPDDpqaglhepfppvrvdRIVEDGDTVALGSLRLTAHATP 144


                ....*....
gi 17538952 120 GHTNGCLTY 128
Cdd:cd16315 145 GHTPGALSW 153
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 32-141 9.37e-04

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 39.46  E-value: 9.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  32 GKAVIID----PVVDTVSRDI-QIIRDLN---LDLIygLNTHVHADHITGTNSLKTVFPTmKSVLSSKSGGEADKY---- 99
Cdd:COG2333  21 GKTILIDtgprPSFDAGERVVlPYLRALGirrLDLL--VLTHPDADHIGGLAAVLEAFPV-GRVLVSGPPDTSETYerll 97

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17538952 100 ------------VSDGEIIEIGGLKLEV--------RETPGHTNGCLTYVEHSLRSA-FTGDA 141
Cdd:COG2333  98 ealkekgipvrpCRAGDTWQLGGVRFEVlwppedllEGSDENNNSLVLRLTYGGFSFlLTGDA 160
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 32-141 1.36e-03

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 38.27  E-value: 1.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538952  32 GKAVIID--PVVDTVSRDI------QIIRDLnlDLIygLNTHVHADHITGTNSLKTVFPTmKSVLSS------------- 90
Cdd:cd07731  19 GKTILIDtgPRDSFGEDVVvpylkaRGIKKL--DYL--ILTHPDADHIGGLDAVLKNFPV-KEVYMPgvthttktyedll 93

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17538952  91 ---KSGGEADKYVSDGEIIEIGGLKLEV----RETPGHTNG--CLTYVEHSLRSA-FTGDA 141
Cdd:cd07731  94 daiKEKGIPVTPCKAGDRWQLGGVSFEVlsppKDDYDDLNNnsCVLRLTYGGTSFlLTGDA 154
 
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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