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Conserved domains on  [gi|1839705774|ref|XP_034120581|]
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persulfide dioxygenase ETHE1, mitochondrial isoform X1 [Drosophila guanche]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02962 super family cl30130
hydroxyacylglutathione hydrolase
 57-288 6.13e-109

hydroxyacylglutathione hydrolase


The actual alignment was detected with superfamily member PLN02962:

Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 315.97  E-value: 6.13e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  57 PDFFFRQLFDGESSTYSYLLADLKTGE--AVIIDPVLDQAKRDAQLVKELGFKLKYAINTHMHADHITGSGWLR-ELTGC 133
Cdd:PLN02962    9 SKLLFRQLFEKESSTYTYLLADVSHPDkpALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKtKLPGV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 134 QSVIAAASGAKADRHLHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQG------CVFTGDTLLIRGCGRTDFQEGSPK 207
Cdd:PLN02962   89 KSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPdqpqprMAFTGDALLIRGCGRTDFQGGSSD 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 208 NLYENVHSKIFTLPENYRIYPAHDYKGQMESSVWEEKRYNPRLTKDLAEFIKIMDNLNLPYPKKIDASLPANRECGVYDI 287
Cdd:PLN02962  169 QLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPANMVCGLQDP 248


                  .
gi 1839705774 288 P 288
Cdd:PLN02962  249 P 249
 
Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 57-288 6.13e-109

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 315.97  E-value: 6.13e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  57 PDFFFRQLFDGESSTYSYLLADLKTGE--AVIIDPVLDQAKRDAQLVKELGFKLKYAINTHMHADHITGSGWLR-ELTGC 133
Cdd:PLN02962    9 SKLLFRQLFEKESSTYTYLLADVSHPDkpALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKtKLPGV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 134 QSVIAAASGAKADRHLHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQG------CVFTGDTLLIRGCGRTDFQEGSPK 207
Cdd:PLN02962   89 KSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPdqpqprMAFTGDALLIRGCGRTDFQGGSSD 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 208 NLYENVHSKIFTLPENYRIYPAHDYKGQMESSVWEEKRYNPRLTKDLAEFIKIMDNLNLPYPKKIDASLPANRECGVYDI 287
Cdd:PLN02962  169 QLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPANMVCGLQDP 248


                  .
gi 1839705774 288 P 288
Cdd:PLN02962  249 P 249
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 60-232 9.49e-92

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: 269.27  E-value: 9.49e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  60 FFRQLFDGESSTYSYLLADLKTGEAVIIDPVLDQAKRDAQLVKELGFKLKYAINTHMHADHITGSGWLRELTGCQSVI-A 138
Cdd:cd07724     1 IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIgE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 139 AASGAKADRHLHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQGCVFTGDTLLIRGCGRTDFQ---EGSPKNLYENVHS 215
Cdd:cd07724    81 GAPASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPgeaEGLARQLYDSLQR 160

                         170
                  ....*....|....*..
gi 1839705774 216 KIFTLPENYRIYPAHDY 232
Cdd:cd07724   161 KLLLLPDETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 60-250 7.77e-47

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: 156.39  E-value: 7.77e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  60 FFRQLFDGESSTYSYLLADlkTGEAVIIDPVLDQAKRDA--QLVKELGFKLKYAINTHMHADHITGSGWLRELTGCQSVI 137
Cdd:COG0491     4 LPGGTPGAGLGVNSYLIVG--GDGAVLIDTGLGPADAEAllAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 138 AAA----------------SGAKADRHLHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQGCVFTGDTLLIRGCGRTDF 201
Cdd:COG0491    82 HAAeaealeapaagalfgrEPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1839705774 202 QEGSPKNLYENVHsKIFTLPeNYRIYPAHDYKGQMESSVWEEK-------RYNPRL 250
Cdd:COG0491   162 PDGDLAQWLASLE-RLLALP-PDLVIPGHGPPTTAEAIDYLEEllaalgeRANPFL 215
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 72-232 2.61e-36

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: 129.96  E-value: 2.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  72 YSYLLADlKTGEAVIID-----PVLDQ-AKRDAQLVkelgfklkyAI-NTHMHADHITGSGWLRELTGCQsVIAAASGAK 144
Cdd:TIGR03413  11 YIWLLHD-PDGQAAVVDpgeaePVLDAlEARGLTLT---------AIlLTHHHHDHVGGVAELLEAFPAP-VYGPAEERI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 145 --ADRHLHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQGCVFTGDTLLIRGCGRTdFqEGSPKNLYENVhSKIFTLPE 222
Cdd:TIGR03413  80 pgITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRL-F-EGTPEQMYDSL-QRLAALPD 156

                         170
                  ....*....|
gi 1839705774 223 NYRIYPAHDY 232
Cdd:TIGR03413 157 DTLVYCAHEY 166
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 72-230 2.19e-31

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 114.96  E-value: 2.19e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774   72 YSYLLADlkTGEAVIIDPVLDQAKRDAQLVKELG-FKLKYAINTHMHADHITGSGWLRELTGCQsVIAAASGAKA----- 145
Cdd:smart00849   1 NSYLVRD--DGGAILIDTGPGEAEDLLAELKKLGpKKIDAIILTHGHPDHIGGLPELLEAPGAP-VYAPEGTAELlkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  146 ---------------DRHLHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQGCVFTGDTLLIRGCGRTDFQEGS-PKNL 209
Cdd:smart00849  78 allgelgaeaepappDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDaAASD 157

                          170       180
                   ....*....|....*....|.
gi 1839705774  210 YENVHSKIFTLPENYrIYPAH 230
Cdd:smart00849 158 ALESLLKLLKLLPKL-VVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
67-230 1.14e-20

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 87.42  E-value: 1.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  67 GESSTYSYLLADlkTGEAVIIDPVLDQAKRDAQLVKELGFKLK---YAINTHMHADHITGSGWLRELTGCQSVIAAASGA 143
Cdd:pfam00753   2 GPGQVNSYLIEG--GGGAVLIDTGGSAEAALLLLLAALGLGPKdidAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 144 KADRH------------------------LHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQGCVFTGDTLLIRGCGRT 199
Cdd:pfam00753  80 ELLDEelglaasrlglpgppvvplppdvvLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRL 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1839705774 200 DFQEGSPKNLYENVHSK------IFTLPENYRIYPAH 230
Cdd:pfam00753 160 DLPLGGLLVLHPSSAESslesllKLAKLKAAVIVPGH 196
 
Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 57-288 6.13e-109

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 315.97  E-value: 6.13e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  57 PDFFFRQLFDGESSTYSYLLADLKTGE--AVIIDPVLDQAKRDAQLVKELGFKLKYAINTHMHADHITGSGWLR-ELTGC 133
Cdd:PLN02962    9 SKLLFRQLFEKESSTYTYLLADVSHPDkpALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKtKLPGV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 134 QSVIAAASGAKADRHLHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQG------CVFTGDTLLIRGCGRTDFQEGSPK 207
Cdd:PLN02962   89 KSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPdqpqprMAFTGDALLIRGCGRTDFQGGSSD 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 208 NLYENVHSKIFTLPENYRIYPAHDYKGQMESSVWEEKRYNPRLTKDLAEFIKIMDNLNLPYPKKIDASLPANRECGVYDI 287
Cdd:PLN02962  169 QLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPANMVCGLQDP 248


                  .
gi 1839705774 288 P 288
Cdd:PLN02962  249 P 249
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 60-232 9.49e-92

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: 269.27  E-value: 9.49e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  60 FFRQLFDGESSTYSYLLADLKTGEAVIIDPVLDQAKRDAQLVKELGFKLKYAINTHMHADHITGSGWLRELTGCQSVI-A 138
Cdd:cd07724     1 IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIgE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 139 AASGAKADRHLHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQGCVFTGDTLLIRGCGRTDFQ---EGSPKNLYENVHS 215
Cdd:cd07724    81 GAPASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPgeaEGLARQLYDSLQR 160

                         170
                  ....*....|....*..
gi 1839705774 216 KIFTLPENYRIYPAHDY 232
Cdd:cd07724   161 KLLLLPDETLVYPGHDY 177
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 72-230 2.21e-51

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: 166.10  E-value: 2.21e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  72 YSYLLADLKTGEAVIIDPVldqakrDAQLV----KELGFKLKYAINTHMHADHITGSGWLRELTGCQSVIAAASG--AKA 145
Cdd:cd07723    10 YIYLIVDEATGEAAVVDPG------EAEPVlaalEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAEDriPGL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 146 DRHLHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQGCVFTGDTLLIRGCGRtdFQEGSPKNLYENvHSKIFTLPENYR 225
Cdd:cd07723    84 DHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGR--FFEGTAEQMYAS-LQKLLALPDDTL 160


                  ....*
gi 1839705774 226 IYPAH 230
Cdd:cd07723   161 VYCGH 165
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 62-230 3.75e-48

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: 158.60  E-value: 3.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  62 RQLFDGESSTYSYLLADlKTGEAVIIDPVLDQAKRDAQLVKELGFKLKYAINTHMHADHITGSGWLRELTGCQSVIAAA- 140
Cdd:cd06262     1 KRLPVGPLQTNCYLVSD-EEGEAILIDPGAGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEAd 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 141 -------------------SGAKADRHLHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQGCVFTGDTLLIRGCGRTDF 201
Cdd:cd06262    80 aelledpelnlaffgggplPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDL 159

                         170       180
                  ....*....|....*....|....*....
gi 1839705774 202 QEGSPKNLYENVHSKIFTLPENYRIYPAH 230
Cdd:cd06262   160 PGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 60-250 7.77e-47

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: 156.39  E-value: 7.77e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  60 FFRQLFDGESSTYSYLLADlkTGEAVIIDPVLDQAKRDA--QLVKELGFKLKYAINTHMHADHITGSGWLRELTGCQSVI 137
Cdd:COG0491     4 LPGGTPGAGLGVNSYLIVG--GDGAVLIDTGLGPADAEAllAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 138 AAA----------------SGAKADRHLHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQGCVFTGDTLLIRGCGRTDF 201
Cdd:COG0491    82 HAAeaealeapaagalfgrEPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1839705774 202 QEGSPKNLYENVHsKIFTLPeNYRIYPAHDYKGQMESSVWEEK-------RYNPRL 250
Cdd:COG0491   162 PDGDLAQWLASLE-RLLALP-PDLVIPGHGPPTTAEAIDYLEEllaalgeRANPFL 215
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 72-230 2.16e-39

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: 135.74  E-value: 2.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  72 YSYLLADLKTGEAVIIDPVLDqAKRDAQLVKELGFKLKYAINTHMHADHITGSGWLRELTGCQSVI----AAASGAKADR 147
Cdd:cd16275    13 YSYIIIDKATREAAVVDPAWD-IEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMskeeIDYYGFRCPN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 148 -HLHE-GDRVDFGSHVIDALATPGHTNGCMSYVIkdQGCVFTGDTLLIRGCGRTDFQEGSPKNLYENVHsKIFTL-PENY 224
Cdd:cd16275    92 lIPLEdGDTIKIGDTEITCLLTPGHTPGSMCYLL--GDSLFTGDTLFIEGCGRCDLPGGDPEEMYESLQ-RLKKLpPPNT 168


                  ....*.
gi 1839705774 225 RIYPAH 230
Cdd:cd16275   169 RVYPGH 174
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 72-232 2.61e-36

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: 129.96  E-value: 2.61e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  72 YSYLLADlKTGEAVIID-----PVLDQ-AKRDAQLVkelgfklkyAI-NTHMHADHITGSGWLRELTGCQsVIAAASGAK 144
Cdd:TIGR03413  11 YIWLLHD-PDGQAAVVDpgeaePVLDAlEARGLTLT---------AIlLTHHHHDHVGGVAELLEAFPAP-VYGPAEERI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 145 --ADRHLHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQGCVFTGDTLLIRGCGRTdFqEGSPKNLYENVhSKIFTLPE 222
Cdd:TIGR03413  80 pgITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRL-F-EGTPEQMYDSL-QRLAALPD 156

                         170
                  ....*....|
gi 1839705774 223 NYRIYPAHDY 232
Cdd:TIGR03413 157 DTLVYCAHEY 166
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 74-250 1.27e-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: 116.29  E-value: 1.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  74 YLLADLKTGEAVIIDPVlDQAKRDAQLVKELGFKLKYAINTHMHADHITGSGWLRELTGCQSVI---------AAASGAK 144
Cdd:cd16322    14 YLVADEGGGEAVLVDPG-DESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLhpddlplyeAADLGAK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 145 A-----------DRHLHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQGCVFTGDTLLIRGCGRTDFQEGSPKNLYENv 213
Cdd:cd16322    93 AfglgieplpppDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRTDLPGGDPKAMAAS- 171

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1839705774 214 HSKIFTLPENYRIYPAHdykgQMESSVWEEKRYNPRL 250
Cdd:cd16322   172 LRRLLTLPDETRVFPGH----GPPTTLGEERRTNPFL 204
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 72-230 2.19e-31

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 114.96  E-value: 2.19e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774   72 YSYLLADlkTGEAVIIDPVLDQAKRDAQLVKELG-FKLKYAINTHMHADHITGSGWLRELTGCQsVIAAASGAKA----- 145
Cdd:smart00849   1 NSYLVRD--DGGAILIDTGPGEAEDLLAELKKLGpKKIDAIILTHGHPDHIGGLPELLEAPGAP-VYAPEGTAELlkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  146 ---------------DRHLHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQGCVFTGDTLLIRGCGRTDFQEGS-PKNL 209
Cdd:smart00849  78 allgelgaeaepappDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDaAASD 157

                          170       180
                   ....*....|....*....|.
gi 1839705774  210 YENVHSKIFTLPENYrIYPAH 230
Cdd:smart00849 158 ALESLLKLLKLLPKL-VVPGH 177
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 54-230 7.15e-30

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: 111.49  E-value: 7.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  54 PFTPdffFRQlfdgesstYSYLLADLKTGEAVIIDPVLDqAKRDAQLVKELGFKLKYAINTHMHADHITGSGWLRELTGC 133
Cdd:cd07737     5 PVTP---FQQ--------NCSLIWCEETKEAAVIDPGGD-ADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 134 ------------------QSV---IAAASGAKADRHLHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQGCVFTGDTLL 192
Cdd:cd07737    73 piigphkedkfllenlpeQSQmfgFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLF 152

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1839705774 193 IRGCGRTDFQEGSPKNLYENVHSKIFTLPENYRIYPAH 230
Cdd:cd07737   153 KGSIGRTDFPGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 72-232 2.09e-26

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 104.07  E-value: 2.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  72 YSYLLADLKTGEAVIIDPVLDQAKRDAqlVKELGFKLKYAINTHMHADHITGSGWLREL-TGCQSVIAAASGAKADRH-L 149
Cdd:PLN02469   13 YAYLIIDESTKDAAVVDPVDPEKVLQA--AHEHGAKIKLVLTTHHHWDHAGGNEKIKKLvPGIKVYGGSLDNVKGCTHpV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 150 HEGDRVDFGSHV-IDALATPGHTNGCMSYVI----KDQGCVFTGDTLLIRGCGRtdFQEGSPKNLYENVHSKIFTLPENY 224
Cdd:PLN02469   91 ENGDKLSLGKDVnILALHTPCHTKGHISYYVtgkeGEDPAVFTGDTLFIAGCGK--FFEGTAEQMYQSLCVTLGSLPKPT 168


                  ....*...
gi 1839705774 225 RIYPAHDY 232
Cdd:PLN02469  169 QVYCGHEY 176
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 72-232 6.76e-26

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 104.15  E-value: 6.76e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  72 YSYLLADLKTGEAVIIDP-----VLDQAKRDAQlvkelgfKLKYAINTHMHADHITGSGWLRELTGCQsVIAaaSGAKAD 146
Cdd:PLN02398   88 YAYLLHDEDTGTVGVVDPseavpVIDALSRKNR-------NLTYILNTHHHYDHTGGNLELKARYGAK-VIG--SAVDKD 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 147 R------HLHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQGCVFTGDTLLIRGCGRtdFQEGSPKNLYENVhSKIFTL 220
Cdd:PLN02398  158 RipgidiVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGK--LFEGTPEQMLSSL-QKIISL 234

                         170
                  ....*....|..
gi 1839705774 221 PENYRIYPAHDY 232
Cdd:PLN02398  235 PDDTNIYCGHEY 246
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 54-195 4.47e-21

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 87.93  E-value: 4.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  54 PFTpdfffrqlFDGessTYSYLLADlkTGEAVIIDP-VLDQAKRDAQLVKELGFKLKYAINTHMHADHITGSGWLRELTG 132
Cdd:cd16278    12 PMT--------LDG---TNTYLLGA--PDGVVVIDPgPDDPAHLDALLAALGGGRVSAILVTHTHRDHSPGAARLAERTG 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1839705774 133 CQsVIAAASGA--------KADRHLHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQGCVFTGDTLLIRG 195
Cdd:cd16278    79 AP-VRAFGPHRaggqdtdfAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVMGWS 148
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
67-230 1.14e-20

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 87.42  E-value: 1.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  67 GESSTYSYLLADlkTGEAVIIDPVLDQAKRDAQLVKELGFKLK---YAINTHMHADHITGSGWLRELTGCQSVIAAASGA 143
Cdd:pfam00753   2 GPGQVNSYLIEG--GGGAVLIDTGGSAEAALLLLLAALGLGPKdidAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 144 KADRH------------------------LHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQGCVFTGDTLLIRGCGRT 199
Cdd:pfam00753  80 ELLDEelglaasrlglpgppvvplppdvvLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRL 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1839705774 200 DFQEGSPKNLYENVHSK------IFTLPENYRIYPAH 230
Cdd:pfam00753 160 DLPLGGLLVLHPSSAESslesllKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 79-191 1.53e-17

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 78.73  E-value: 1.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  79 LKTGEAVIIDPVLD--QAKRDAQLVKELGFKLKYAINTHMHADHITGSGWLRELTGCQsvIAAASGAKA----------- 145
Cdd:cd07743    15 FGDKEALLIDSGLDedAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCK--VYAPKIEKAfienpllepsy 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1839705774 146 ----------------------DRHLHEGDrVDFGSHVIDALATPGHTNGCMSYVIKDqGCVFTGDTL 191
Cdd:cd07743    93 lggayppkelrnkflmakpskvDDIIEEGE-LELGGVGLEIIPLPGHSFGQIGILTPD-GVLFAGDAL 158
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 73-230 1.10e-16

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: 76.18  E-value: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  73 SYLLADlkTGEAVIIDPVLDQaKRDAQLV----KELGFKL---KYAINTHMHADHITGSGWLRELTGCqsVIAAASgaka 145
Cdd:cd07725    17 VYLLRD--GDETTLIDTGLAT-EEDAEALweglKELGLKPsdiDRVLLTHHHPDHIGLAGKLQEKSGA--TVYILD---- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 146 DRHLHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQGCVFTGDTLLIR---GCGRTDFQEGSPKNLYENVHSKIFTLpE 222
Cdd:cd07725    88 VTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLPKitpNVSLWAVRVEDPLGAYLESLDKLEKL-D 166


                  ....*...
gi 1839705774 223 NYRIYPAH 230
Cdd:cd07725   167 VDLAYPGH 174
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 63-183 1.16e-16

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 77.63  E-value: 1.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  63 QLFD-----GESSTYSYLLadlKTGE-AVIIDpVLDQAKRDAQLV---KELGFK---LKYAINTHMHADHITGSGWLREL 130
Cdd:cd16280     9 QVFDnlyyvGNKWVSAWAI---DTGDgLILID-ALNNNEAADLIVdglEKLGLDpadIKYILITHGHGDHYGGAAYLKDL 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1839705774 131 TGCQsVIAAASGAKA-------------------DRHLHEGDRVDFGSHVIDALATPGHTNGCMSYVI--KDQG 183
Cdd:cd16280    85 YGAK-VVMSEADWDMmeeppeegdnprwgppperDIVIKDGDTLTLGDTTITVYLTPGHTPGTLSLIFpvKDGG 157
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 84-183 1.25e-15

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: 74.50  E-value: 1.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  84 AVIIDPVLDQ-AKRDAQLVKELGFK---LKYAINTHMHADHITGSGWLRELTGCQSVIAAAS------------------ 141
Cdd:cd07708    33 NILIDGDMEQnAPMIKANIKKLGFKfsdTKLILISHAHFDHAGGSAEIKKQTGAKVMAGAEDvslllsggssdfhyands 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1839705774 142 -----GAKADRHLHEGDRVDFGSHVIDALATPGHTNGCMSYV--IKDQG 183
Cdd:cd07708   113 styfpQSTVDRAVHDGERVTLGGTVLTAHATPGHTPGCTTWTmtLKDHG 161
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 101-180 4.03e-15

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: 73.12  E-value: 4.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 101 VKELGFK---LKYAINTHMHADHITGSGWLRELTGCQSVIAAASGA----------------------KADRHLHEGDRV 155
Cdd:cd16288    51 IRKLGFKpsdIKILLNSHAHLDHAGGLAALKKLTGAKLMASAEDAAllasggksdfhygddslafppvKVDRVLKDGDRV 130

                          90       100
                  ....*....|....*....|....*
gi 1839705774 156 DFGSHVIDALATPGHTNGCMSYVIK 180
Cdd:cd16288   131 TLGGTTLTAHLTPGHTRGCTTWTMT 155
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 72-232 8.47e-14

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 69.47  E-value: 8.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  72 YSYLLADlKTGEAVIIDPvlDQAKRDAQLVKELGFKLKYAINTHMHADHITGSGWLRELTGCQSVI--AAASGAKADRHL 149
Cdd:PRK10241   13 YIWVLND-EAGRCLIVDP--GEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYgpQETQDKGTTQVV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 150 HEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQgcVFTGDTLLIRGCGRtdFQEGSPKNLYENVHsKIFTLPENYRIYPA 229
Cdd:PRK10241   90 KDGETAFVLGHEFSVFATPGHTLGHICYFSKPY--LFCGDTLFSGGCGR--LFEGTASQMYQSLK-KINALPDDTLICCA 164


                  ...
gi 1839705774 230 HDY 232
Cdd:PRK10241  165 HEY 167
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 85-177 1.06e-12

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: 66.35  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  85 VIIDPVLDQAkrdAQLVKE----LGFK---LKYAINTHMHADHITGSGWLRELTGCQSVIAAA------SG--------- 142
Cdd:cd16309    34 ILIDGAMPQS---TPLIKDnikkLGFDvkdVKYLLNTHAHFDHAGGLAELKKATGAQLVASAAdkplleSGyvgsgdtkn 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1839705774 143 -----AKADRHLHEGDRVDFGSHVIDALATPGHTNGCMSY 177
Cdd:cd16309   111 lqfppVRVDRVIGDGDKVTLGGTTLTAHLTPGHSPGCTSW 150
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 71-197 1.62e-12

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: 65.21  E-value: 1.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  71 TYSYLLADlkTGEAVIIDP-VLDQAKRDAQLVKELGF---KLKYAINTHMHADHITGSGWL-RELTGCQSV--------- 136
Cdd:cd07726    16 IASYLLDG--EGRPALIDTgPSSSVPRLLAALEALGIapeDVDYIILTHIHLDHAGGAGLLaEALPNAKVYvhprgarhl 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 137 ------IAAAS---GAKADRH--------------LHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQGCVFTGDTLLI 193
Cdd:cd07726    94 idpsklWASARavyGDEADRLggeilpvpeervivLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDAAGV 173


                  ....
gi 1839705774 194 RGCG 197
Cdd:cd07726   174 RYPE 177
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 73-183 3.30e-12

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: 65.16  E-value: 3.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  73 SYLLAdlKTGEAVIIDPVLDQ-AKRDAQLVKELGFKL---KYAINTHMHADHITGSGWLRELTGCQSVI------AAASG 142
Cdd:cd16310    24 SYLIT--SNHGAILLDGGLEEnAALIEQNIKALGFKLsdiKIIINTHAHYDHAGGLAQLKADTGAKLWAsrgdrpALEAG 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1839705774 143 ---------------AKADRHLHEGDRVDFGSHVIDALATPGHTNGCMSYV--IKDQG 183
Cdd:cd16310   102 khigdnitqpapfpaVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTWSttVKENG 159
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 65-230 6.02e-12

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: 63.39  E-value: 6.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  65 FDGESSTYSYLLADlkTGEAVIIDP-VLDQAKRDAQLVKELGFK---LKYAINTHMHADHITGSGWLRELTGCQsVIAAA 140
Cdd:cd07721     5 LPLLPPVNAYLIED--DDGLTLIDTgLPGSAKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAALKEAPGAP-VYAHE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 141 SGA------------------------------KADRHLHEGDRVDFGsHVIDALATPGHTNGCMSYVIKDQGCVFTGDT 190
Cdd:cd07721    82 REApylegekpypppvrlgllgllspllpvkpvPVDRTLEDGDTLDLA-GGLRVIHTPGHTPGHISLYLEEDGVLIAGDA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1839705774 191 LLIRGcGRTdfqEGSPK----NLYENVHS--KIFTLPENyRIYPAH 230
Cdd:cd07721   161 LVTVG-GEL---VPPPPpftwDMEEALESlrKLAELDPE-VLAPGH 201
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 ...
 85-177 5.86e-11

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: 61.60  E-value: 5.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  85 VIIDPVLDQ-AKRDAQLVKELGFKL---KYAINTHMHADHITGSGWLRELTGCQsVIAAASGAKA--------------- 145
Cdd:cd16290    34 ILIDGALPQsAPQIEANIRALGFRLedvKLILNSHAHFDHAGGIAALQRDSGAT-VAASPAGAAAlrsggvdpddpqaga 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1839705774 146 ---------DRHLHEGDRVDFGSHVIDALATPGHTNGCMSY 177
Cdd:cd16290   113 adpfppvakVRVVADGEVVKLGPLAVTAHATPGHTPGGTSW 153
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 71-230 5.99e-11

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: 60.24  E-value: 5.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  71 TY------SYLLADlkTGE-AVIIDPVLDQAkrdaqLVKELGFKLKYAINTHMHADHITGSGWLRELTGCQSVI------ 137
Cdd:cd07722    20 TYlvgtgkRRILID--TGEgRPSYIPLLKSV-----LDSEGNATISDILLTHWHHDHVGGLPDVLDLLRGPSPRvykfpr 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 138 ----AAASGAKADRH-LHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQGCVFTGDTLLirGCGRTDFQegspkNLYEN 212
Cdd:cd07722    93 peedEDPDEDGGDIHdLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGDCVL--GHGTAVFE-----DLAAY 165

                         170       180
                  ....*....|....*....|
gi 1839705774 213 VHS--KIFTLPENyRIYPAH 230
Cdd:cd07722   166 MASlkKLLSLGPG-RIYPGH 184
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 99-230 1.15e-10

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: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  99 QLVKELGFKLKYAINTHMHADHITG-------------SGWLRELTGCQSVIAAAS-----GAKADRHLHEGDRVDFGSH 160
Cdd:cd07712    34 EYVRTLTDLPLLVVATHGHFDHIGGlhefeevyvhpadAEILAAPDNFETLTWDAAtysvpPAGPTLPLRDGDVIDLGDR 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1839705774 161 VIDALATPGHTNGCMSYVIKDQGCVFTGDTL----LIrgcgrtDFQEGSPKNLYenVHS--KIFTLPENYR-IYPAH 230
Cdd:cd07712   114 QLEVIHTPGHTPGSIALLDRANRLLFSGDVVydgpLI------MDLPHSDLDDY--LASleKLSKLPDEFDkVLPGH 182
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 101-180 1.89e-10

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: 59.77  E-value: 1.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 101 VKELGFKL---KYAINTHMHADHITGSGWLRELTGCQ------SVIAAASG-----------------AKADRHLHEGDR 154
Cdd:cd16307    51 IEKLGFKFsdtKILLISHAHFDHAAGSALIKRETHAKymvmdgDVDVVESGgksdffygndpstyfppAHVDKVLHDGEQ 130

                          90       100
                  ....*....|....*....|....*.
gi 1839705774 155 VDFGSHVIDALATPGHTNGCMSYVIK 180
Cdd:cd16307   131 VELGGTVLTAHLTAGHTKGCTTWTMK 156
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 77-177 2.47e-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: 59.67  E-value: 2.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  77 ADLKTGEA--VIIDPVLDQAkrdAQLV----KELGFKL---KYAINTHMHADHITGSGWLRELTGCQ---SVIAA---AS 141
Cdd:cd16315    24 AILITGDDghVLIDSGTEEA---APLVlaniRKLGFDPkdvRWLLSSHEHFDHVGGLAALQRATGARvaaSAAAApvlES 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1839705774 142 G-----------------AKADRHLHEGDRVDFGSHVIDALATPGHTNGCMSY 177
Cdd:cd16315   101 GkpapddpqaglhepfppVRVDRIVEDGDTVALGSLRLTAHATPGHTPGALSW 153
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 101-183 3.80e-09

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


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 55.94  E-value: 3.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 101 VKELGFK---LKYAINTHMHADHITGSGWLRELTGCQSVIAAASGA----------------------KADRHLHEGDRV 155
Cdd:cd16308    51 IQALGFKfkdIKILLTTQAHYDHVGAMAAIKQQTGAKMMVDEKDAKvladggksdyemggygstfapvKADKLLHDGDTI 130

                          90       100       110
                  ....*....|....*....|....*....|
gi 1839705774 156 DFGSHVIDALATPGHTNGCMSYVI--KDQG 183
Cdd:cd16308   131 KLGGTKLTLLHHPGHTKGSCSFLFdvKDEK 160
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 98-177 3.49e-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: 53.33  E-value: 3.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  98 AQLVKELGFKL---KYAINTHMHADHITGSGWLRELTGCQSVIAAASGA--------KAD---------------RHLHE 151
Cdd:cd16313    48 AASIRQLGFKLedvKYILSSHDHWDHAGGIAALQKLTGAQVLASPATVAvlrsgsmgKDDpqfggltpmppvasvRAVRD 127

                          90       100
                  ....*....|....*....|....*.
gi 1839705774 152 GDRVDFGSHVIDALATPGHTNGCMSY 177
Cdd:cd16313   128 GEVVKLGPLAVTAHATPGHTTGGTSW 153
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 84-208 3.86e-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) 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: 52.57  E-value: 3.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  84 AVIID--PVLDQAKRDAQLVKELGFK-LKYAINTHMHADHITGSGWLRELTGCqsVIAAASGAKA--------------- 145
Cdd:cd16282    26 VVVIDtgASPRLARALLAAIRKVTDKpVRYVVNTHYHGDHTLGNAAFADAGAP--IIAHENTREElaargeaylelmrrl 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1839705774 146 -------------DRHLHEGDRVDFGSHVIDALAT-PGHTNGCMSYVIKDQGCVFTGDTLLIrgcGRTDF-QEGSPKN 208
Cdd:cd16282   104 ggdamagtelvlpDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEGVLFAGDLVFN---GRIPFlPDGSLAG 178
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 97-189 8.65e-08

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: 51.83  E-value: 8.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  97 DAQLvKELGFK---LKYAINTHMHADHI------TGSGWL---RELTGCQSVIAAASGAKADR------------HLHEG 152
Cdd:cd07729    76 EEQL-ARLGLDpedIDYVILSHLHFDHAggldlfPNATIIvqrAELEYATGPDPLAAGYYEDVlaldddlpggrvRLVDG 154

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1839705774 153 DRVDFGShvIDALATPGHTNGCMSYVIK-DQG-CVFTGD 189
Cdd:cd07729   155 DYDLFPG--VTLIPTPGHTPGHQSVLVRlPEGtVLLAGD 191
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 84-182 3.55e-07

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


Pssm-ID: 293847  Cd Length: 239  Bit Score: 50.20  E-value: 3.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  84 AVIIDPVLDQAKrDAQL--VKELGF---KLKYAINTHMHADHITGSGWLRELTGCQ-------SVIAAASG--------- 142
Cdd:cd16289    33 AVLLDGGMPQAA-DMLLdnMRALGVapgDLKLILHSHAHADHAGPLAALKRATGARvaanaesAVLLARGGsddihfgdg 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1839705774 143 -----AKADRHLHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQ 182
Cdd:cd16289   112 itfppVQADRIVMDGEVVTLGGVTFTAHFTPGHTPGSTSWTWTDT 156
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 85-190 1.29e-06

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 48.07  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  85 VIIDPVLD---QAKRDAQLVKELGFKLKYAINTHMHADHITGSGWLRELTG-------------CQSVIAAASGAKADRH 148
Cdd:pfam12706   3 ILIDPGPDlrqQALPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPrplyaplgvlahlRRNFPYLFLLEHYGVR 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839705774 149 LHE---GDRVDFGSHVIDALATPGHTNG----------CMSYVIKDQG--CVFTGDT 190
Cdd:pfam12706  83 VHEidwGESFTVGDGGLTVTATPARHGSprgldpnpgdTLGFRIEGPGkrVYYAGDT 139
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 110-191 1.69e-06

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 47.90  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 110 YAINTHMHADHItgsGWL---------------------RELTGCQSviaaASGAKADRHLHEGDRV-----------DF 157
Cdd:cd16277    66 YVLCTHLHVDHV---GWNtrlvdgrwvptfpnarylfsrAEYDHWSS----PDAGGPPNRGVFEDSVlpvieagladlVD 138

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1839705774 158 GSHVID----ALATPGHTNGCMSYVIKDQG--CVFTGDTL 191
Cdd:cd16277   139 DDHEILdgirLEPTPGHTPGHVSVELESGGerALFTGDVM 178
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
114-215 2.22e-06

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 47.88  E-value: 2.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 114 THMHADHITG----------SGWLRELT-----GCQSVIAAASGAKADRH--------LHEGDRVDFGSHVIDALATPgH 170
Cdd:COG1234    59 THLHGDHIAGlpgllstrslAGREKPLTiygppGTKEFLEALLKASGTDLdfplefheIEPGEVFEIGGFTVTAFPLD-H 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1839705774 171 TNGCMSYVIKDQGC--VFTGDTL-------LIRGCgrtD-------FQEGSPKNLYENVHS 215
Cdd:COG1234   138 PVPAYGYRFEEPGRslVYSGDTRpcealveLAKGA---DlliheatFLDEEAELAKETGHS 195
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 101-191 2.91e-06

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


Pssm-ID: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 46.80  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 101 VKELGfKLKYAINTHMH--ADHitgSGWlRELTGCQSVIA-----AASGAKADRHLHEGDRVDFGSHViDALATPGHTNG 173
Cdd:cd07727    42 IEALG-GIRYIFLTHRDdvADH---AKW-AERFGAKRIIHeddvnAVTRPDEVIVLWGGDPWELDPDL-TLIPVPGHTRG 115

                          90
                  ....*....|....*...
gi 1839705774 174 CMSYVIKDQGCVFTGDTL 191
Cdd:cd07727   116 SVVLLYKEKGVLFTGDHL 133
NorV COG0426
Flavorubredoxin [Energy production and conversion];
62-189 8.05e-06

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 46.75  E-value: 8.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  62 RQLFDGESS-----TY-SYLLADLKTgeaVIIDPVlDQAKRD---AQLVKELGF-KLKYAINTHMHADHItGS--GWLRE 129
Cdd:COG0426    19 RRLFEGEYPtprgtTYnSYLIVDEKT---ALIDTV-GESFFEeflENLSKVIDPkKIDYIIVNHQEPDHS-GSlpELLEL 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1839705774 130 LTGCQsVIAAASGAKADRHLH-----------EGDRVDFGSHVIDALATPG-HTNGCM-SYVIKDqGCVFTGD 189
Cdd:COG0426    94 APNAK-IVCSKKAARFLPHFYgipdfrfivvkEGDTLDLGGHTLQFIPAPMlHWPDTMfTYDPED-KILFSGD 164
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 85-173 2.71e-05

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


Pssm-ID: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 44.59  E-value: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  85 VIIDPVLDQAKRDAQL-VKELGFKL---KYAINTHMHADHITGSGWLRELTGCqSVIAAASGA---------------KA 145
Cdd:cd16312    34 VLLDGALPQSAPLIIAnIEALGFRIedvKLILNSHAHWDHAGGIAALQKASGA-TVAASAHGAqvlqsgtngkddpqyQA 112

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1839705774 146 DRHLH-----------EGDRVDFGSHVIDALATPGHTNG 173
Cdd:cd16312   113 KPVVHvakvakvkevgEGDTLKVGPLRLTAHMTPGHTPG 151
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 62-189 2.76e-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: 44.40  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  62 RQLFDGES-----STY-SYLLADlktGEAVIIDPVlDQAKRD---AQLVKELGF-KLKYAINTHMHADHITG-SGWLREL 130
Cdd:cd07709    17 LRLFEGEYptprgTSYnSYLIKD---EKTALIDTV-KEPFFDeflENLEEVIDPrKIDYIVVNHQEPDHSGSlPELLELA 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1839705774 131 TGCQsVIAAASGAKADRHLH-----------EGDRVDFGSHVIDALATPG-HTNGCM-SYVIKDqGCVFTGD 189
Cdd:cd07709    93 PNAK-IVCSKKAARFLKHFYpgiderfvvvkDGDTLDLGKHTLKFIPAPMlHWPDTMvTYDPED-KILFSGD 162
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 85-177 7.68e-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: 7.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  85 VIIDPVLDQA-KRDAQLVKELGFK---LKYAINTHMHADHITGSGWLRELTGCqSVIAAASGA------KADR------- 147
Cdd:cd16314    34 ILIDGGTDKAaPLIEANIRALGFRpedVRYIVSSHEHFDHAGGIARLQRATGA-PVVAREPAAttlergRSDRsdpqflv 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1839705774 148 -----------HLHEGDRVDFGSHVIDALATPGHTNGCMSY 177
Cdd:cd16314   113 vekfppvasvqRIGDGEVLRVGPLALTAHATPGHTPGGTSW 153
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 83-129 1.82e-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: 41.72  E-value: 1.82e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1839705774  83 EAVIIDP--VLDQAKRDAQLVKELGFKLKYAINTHMHADHITGSGWLRE 129
Cdd:cd07739    26 EAVLVDAqfTRADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLE 74
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 79-195 4.40e-04

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 40.67  E-value: 4.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  79 LKTGEAVI-IDPVLDqakRDAQLVKELGFKLKYAIN------THMHADHItGSGWLREL--TGCQSVIAAASGAKADRH- 148
Cdd:COG2220    16 IETGGKRIlIDPVFS---GRASPVNPLPLDPEDLPKidavlvTHDHYDHL-DDATLRALkrTGATVVAPLGVAAWLRAWg 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1839705774 149 ------LHEGDRVDFGS---HVIDALATPGHTNGC----MSYVIKDQGCV--FTGDTLLIRG 195
Cdd:COG2220    92 fprvteLDWGESVELGGltvTAVPARHSSGRPDRNgglwVGFVIETDGKTiyHAGDTGYFPE 153
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 82-190 4.93e-04

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 40.65  E-value: 4.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774  82 GEAVIIDP---VLDQAKRDAQLVKelgfKLKYAINTHMHADHITGSGWLRE------------------LTGCQSVIAAA 140
Cdd:COG1235    44 GTRLLIDAgpdLREQLLRLGLDPS----KIDAILLTHEHADHIAGLDDLRPrygpnpipvyatpgtleaLERRFPYLFAP 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1839705774 141 SGAKADRH-LHEGDRVDFGSHVIDALATPGHTNGCMSYVIKDQG--CVFTGDT 190
Cdd:COG1235   120 YPGKLEFHeIEPGEPFEIGGLTVTPFPVPHDAGDPVGYRIEDGGkkLAYATDT 172
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 110-189 1.86e-03

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: 38.34  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705774 110 YAINTHMHADHITGSGWLRELTGCQSVIAAASGAKADRhLHEGDRVDFGSHViDALATPGHTNGCMSYVIK--DQGCVF- 186
Cdd:cd07711    63 YVVLTHGHPDHIGNLNLFPNATVIVGWDICGDSYDDHS-LEEGDGYEIDENV-EVIPTPGHTPEDVSVLVEteKKGTVAv 140


                  ...
gi 1839705774 187 TGD 189
Cdd:cd07711   141 AGD 143
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 82-129 9.61e-03

metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. Includes chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1.


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 36.49  E-value: 9.61e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1839705774  82 GEAVIIDPVLDQAKRdAQLV----KELGFKLKYAINTHMHADHITGSGWLRE 129
Cdd:cd16285    35 KGLVLIDTPWTEAQT-ATLLdwieKKLGKPVTAAISTHSHDDRTGGIKALNA 85
 
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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