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Conserved domains on  [gi|566172744|ref|XP_002307560|]
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persulfide dioxygenase ETHE1 homolog, mitochondrial isoform X2 [Populus trichocarpa]

Protein Classification

PLN02962 family protein( domain architecture ID 11477331)

PLN02962 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 40-290 0e+00

hydroxyacylglutathione hydrolase


:

Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 540.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  40 ASSQAFKNKKLLFRQLFEKDSSTYTYLLADVAHPEKPALLIDPVDKTVDRDLSLVKELGLKLIYAINTHVHADHVTGTGL 119
Cdd:PLN02962   1 SSSSSSSSSKLLFRQLFEKESSTYTYLLADVSHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 120 IKTKVPSVKSIISKASKSKADLLIEAGDKIHFGDLFLEVRATPGHTLGCVTYVTGDGSDQPQPRMAFTGDALLIRGCGRT 199
Cdd:PLN02962  81 LKTKLPGVKSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPDQPQPRMAFTGDALLIRGCGRT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 200 DFQGGSAHQLYQSVHSQIFSLPKETLIYPAHDYRGFTVSTVGEEMQYNPRLTKDEEMFKSIMENLNLPYPKMIDIAVPSN 279
Cdd:PLN02962 161 DFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPAN 240

                        250
                 ....*....|.
gi 566172744 280 MVCGLQDLSVK 290
Cdd:PLN02962 241 MVCGLQDPPAK 251
 
Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 40-290 0e+00

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 540.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  40 ASSQAFKNKKLLFRQLFEKDSSTYTYLLADVAHPEKPALLIDPVDKTVDRDLSLVKELGLKLIYAINTHVHADHVTGTGL 119
Cdd:PLN02962   1 SSSSSSSSSKLLFRQLFEKESSTYTYLLADVSHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 120 IKTKVPSVKSIISKASKSKADLLIEAGDKIHFGDLFLEVRATPGHTLGCVTYVTGDGSDQPQPRMAFTGDALLIRGCGRT 199
Cdd:PLN02962  81 LKTKLPGVKSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPDQPQPRMAFTGDALLIRGCGRT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 200 DFQGGSAHQLYQSVHSQIFSLPKETLIYPAHDYRGFTVSTVGEEMQYNPRLTKDEEMFKSIMENLNLPYPKMIDIAVPSN 279
Cdd:PLN02962 161 DFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPAN 240

                        250
                 ....*....|.
gi 566172744 280 MVCGLQDLSVK 290
Cdd:PLN02962 241 MVCGLQDPPAK 251
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 51-232 7.95e-78

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: 234.22  E-value: 7.95e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  51 LFRQLFEKDSSTYTYLLADVAhpEKPALLIDPVDKTVDRDLSLVKELGLKLIYAINTHVHADHVTGTGLIKTKvPSVKSI 130
Cdd:cd07724    1 IFRQFFDPGLGTLSYLVGDPE--TGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAER-TGAPIV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 131 ISKASK-SKADLLIEAGDKIHFGDLFLEVRATPGHTLGCVTYVTGDgsdqpqPRMAFTGDALLIRGCGRTDFQG---GSA 206
Cdd:cd07724   78 IGEGAPaSFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGD------PDAVFTGDTLFVGDVGRPDLPGeaeGLA 151

                        170       180
                 ....*....|....*....|....*.
gi 566172744 207 HQLYQSVHSQIFSLPKETLIYPAHDY 232
Cdd:cd07724  152 RQLYDSLQRKLLLLPDETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 51-232 2.60e-35

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 126.73  E-value: 2.60e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  51 LFRQLFEKDSSTYTYLLADvahpEKPALLIDPV--DKTVDRDLSLVKELGLKLIYAINTHVHADHVTGTGLIKTKVpSVK 128
Cdd:COG0491    4 LPGGTPGAGLGVNSYLIVG----GDGAVLIDTGlgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 129 SIISKA----------------SKSKADLLIEAGDKIHFGDLFLEVRATPGHTLGCVTYVTgdgsdqPQPRMAFTGDALL 192
Cdd:COG0491   79 VYAHAAeaealeapaagalfgrEPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV------PDEKVLFTGDALF 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 566172744 193 IRGCGRTDFQGGSAHQLYQSVHsQIFSLPKEtLIYPAHDY 232
Cdd:COG0491  153 SGGVGRPDLPDGDLAQWLASLE-RLLALPPD-LVIPGHGP 190
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 63-230 3.05e-25

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: 99.16  E-value: 3.05e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744    63 YTYLLADvahpEKPALLIDPVDKTVDRDLSLVKELGL-KLIYAINTHVHADHVTGTGLIKtKVPSVKSIISKASK----- 136
Cdd:smart00849   1 NSYLVRD----DGGAILIDTGPGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELL-EAPGAPVYAPEGTAellkd 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744   137 --------------SKADLLIEAGDKIHFGDLFLEVRATPGHTLGCVTYVTGDGsdqpqpRMAFTGDALLIRGCGRTDFQ 202
Cdd:smart00849  76 llallgelgaeaepAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEG------KILFTGDLLFAGGDGRTLVD 149

                          170       180
                   ....*....|....*....|....*....
gi 566172744   203 GGSaHQLYQSVHSQIFSL-PKETLIYPAH 230
Cdd:smart00849 150 GGD-AAASDALESLLKLLkLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
61-230 2.70e-19

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 83.57  E-value: 2.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744   61 STYTYLLADvahpEKPALLIDP---VDKTVDRDLSLVKELGLKLIYAINTHVHADHVTGTGLIK--TKVPSV-------- 127
Cdd:pfam00753   5 QVNSYLIEG----GGGAVLIDTggsAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAeaTDVPVIvvaeeare 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  128 -------------KSIISKASKSKADLLIEAGDKIHFGDLFLEVRATPGHTLGCVTYVTGDGsdqpqpRMAFTGDALLIR 194
Cdd:pfam00753  81 lldeelglaasrlGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGG------KVLFTGDLLFAG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 566172744  195 GCGRTDFQGGSAHQLYQSVHSQIFSL------PKETLIYPAH 230
Cdd:pfam00753 155 EIGRLDLPLGGLLVLHPSSAESSLESllklakLKAAVIVPGH 196
 
Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 40-290 0e+00

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 540.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  40 ASSQAFKNKKLLFRQLFEKDSSTYTYLLADVAHPEKPALLIDPVDKTVDRDLSLVKELGLKLIYAINTHVHADHVTGTGL 119
Cdd:PLN02962   1 SSSSSSSSSKLLFRQLFEKESSTYTYLLADVSHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 120 IKTKVPSVKSIISKASKSKADLLIEAGDKIHFGDLFLEVRATPGHTLGCVTYVTGDGSDQPQPRMAFTGDALLIRGCGRT 199
Cdd:PLN02962  81 LKTKLPGVKSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPDQPQPRMAFTGDALLIRGCGRT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 200 DFQGGSAHQLYQSVHSQIFSLPKETLIYPAHDYRGFTVSTVGEEMQYNPRLTKDEEMFKSIMENLNLPYPKMIDIAVPSN 279
Cdd:PLN02962 161 DFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPAN 240

                        250
                 ....*....|.
gi 566172744 280 MVCGLQDLSVK 290
Cdd:PLN02962 241 MVCGLQDPPAK 251
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 51-232 7.95e-78

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: 234.22  E-value: 7.95e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  51 LFRQLFEKDSSTYTYLLADVAhpEKPALLIDPVDKTVDRDLSLVKELGLKLIYAINTHVHADHVTGTGLIKTKvPSVKSI 130
Cdd:cd07724    1 IFRQFFDPGLGTLSYLVGDPE--TGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAER-TGAPIV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 131 ISKASK-SKADLLIEAGDKIHFGDLFLEVRATPGHTLGCVTYVTGDgsdqpqPRMAFTGDALLIRGCGRTDFQG---GSA 206
Cdd:cd07724   78 IGEGAPaSFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGD------PDAVFTGDTLFVGDVGRPDLPGeaeGLA 151

                        170       180
                 ....*....|....*....|....*.
gi 566172744 207 HQLYQSVHSQIFSLPKETLIYPAHDY 232
Cdd:cd07724  152 RQLYDSLQRKLLLLPDETLVYPGHDY 177
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 63-230 1.21e-39

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: 1.21e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  63 YTYLLADvaHPEKPALLIDPVD-KTVdrdLSLVKELGLKLIYAINTHVHADHVTGTGLIKTKVPSVKSIISKASK-SKAD 140
Cdd:cd07723   10 YIYLIVD--EATGEAAVVDPGEaEPV---LAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAEDRiPGLD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 141 LLIEAGDKIHFGDLFLEVRATPGHTLGCVTYVTgdgsdqPQPRMAFTGDALLIRGCGRtdFQGGSAHQLYQSvHSQIFSL 220
Cdd:cd07723   85 HPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV------PDEPALFTGDTLFSGGCGR--FFEGTAEQMYAS-LQKLLAL 155

                        170
                 ....*....|
gi 566172744 221 PKETLIYPAH 230
Cdd:cd07723  156 PDDTLVYCGH 165
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 61-230 1.26e-39

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: 1.26e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  61 STYTYLLADvahPEKPALLIDPVDKTVDRDLSLVKELGLKLIYAINTHVHADHVTGTGLIKtKVPSVKSIISKA------ 134
Cdd:cd06262    9 QTNCYLVSD---EEGEAILIDPGAGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELK-EAPGAPVYIHEAdaelle 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 135 --------------SKSKADLLIEAGDKIHFGDLFLEVRATPGHTLGCVTYVTGDGsdqpqpRMAFTGDALLIRGCGRTD 200
Cdd:cd06262   85 dpelnlaffgggplPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEE------GVLFTGDTLFAGSIGRTD 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 566172744 201 FQGGSAHQLYQSVHSQIFSLPKETLIYPAH 230
Cdd:cd06262  159 LPGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 51-232 2.60e-35

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 126.73  E-value: 2.60e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  51 LFRQLFEKDSSTYTYLLADvahpEKPALLIDPV--DKTVDRDLSLVKELGLKLIYAINTHVHADHVTGTGLIKTKVpSVK 128
Cdd:COG0491    4 LPGGTPGAGLGVNSYLIVG----GDGAVLIDTGlgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 129 SIISKA----------------SKSKADLLIEAGDKIHFGDLFLEVRATPGHTLGCVTYVTgdgsdqPQPRMAFTGDALL 192
Cdd:COG0491   79 VYAHAAeaealeapaagalfgrEPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV------PDEKVLFTGDALF 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 566172744 193 IRGCGRTDFQGGSAHQLYQSVHsQIFSLPKEtLIYPAHDY 232
Cdd:COG0491  153 SGGVGRPDLPDGDLAQWLASLE-RLLALPPD-LVIPGHGP 190
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 63-230 7.84e-28

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: 105.70  E-value: 7.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  63 YTYLLADVAhpEKPALLIDPV-DktVDRDLSLVKELGLKLIYAINTHVHADHVTGT--GLIKTKVP---SVKSIISKASK 136
Cdd:cd16275   13 YSYIIIDKA--TREAAVVDPAwD--IEKILAKLNELGLTLTGILLTHSHFDHVNLVepLLAKYDAPvymSKEEIDYYGFR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 137 SKADLLIEAGDKIHFGDLFLEVRATPGHTLGCVTYVTGDgsdqpqpRMaFTGDALLIRGCGRTDFQGGSAHQLYQSVHSQ 216
Cdd:cd16275   89 CPNLIPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGD-------SL-FTGDTLFIEGCGRCDLPGGDPEEMYESLQRL 160

                        170
                 ....*....|....
gi 566172744 217 IFSLPKETLIYPAH 230
Cdd:cd16275  161 KKLPPPNTRVYPGH 174
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 64-250 1.92e-27

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: 105.51  E-value: 1.92e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  64 TYLLADVAHPEkpALLIDPVDKTVDRdLSLVKELGLKLIYAINTHVHADHVTGTGLIK--TKVP---------------- 125
Cdd:cd16322   13 TYLVADEGGGE--AVLVDPGDESEKL-LARFGTTGLTLLYILLTHAHFDHVGGVADLRrhPGAPvylhpddlplyeaadl 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 126 SVKSIISKASKS-KADLLIEAGDKIHFGDLFLEVRATPGHTLGCVTYVTgdgsdqPQPRMAFTGDALLIRGCGRTDFQGG 204
Cdd:cd16322   90 GAKAFGLGIEPLpPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYV------EEEGLLFSGDLLFQGSIGRTDLPGG 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 566172744 205 SAHQLYQSvHSQIFSLPKETLIYPAHDyrgfTVSTVGEEMQYNPRL 250
Cdd:cd16322  164 DPKAMAAS-LRRLLTLPDETRVFPGHG----PPTTLGEERRTNPFL 204
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 63-230 3.05e-25

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: 99.16  E-value: 3.05e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744    63 YTYLLADvahpEKPALLIDPVDKTVDRDLSLVKELGL-KLIYAINTHVHADHVTGTGLIKtKVPSVKSIISKASK----- 136
Cdd:smart00849   1 NSYLVRD----DGGAILIDTGPGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELL-EAPGAPVYAPEGTAellkd 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744   137 --------------SKADLLIEAGDKIHFGDLFLEVRATPGHTLGCVTYVTGDGsdqpqpRMAFTGDALLIRGCGRTDFQ 202
Cdd:smart00849  76 llallgelgaeaepAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEG------KILFTGDLLFAGGDGRTLVD 149

                          170       180
                   ....*....|....*....|....*....
gi 566172744   203 GGSaHQLYQSVHSQIFSL-PKETLIYPAH 230
Cdd:smart00849 150 GGD-AAASDALESLLKLLkLLPKLVVPGH 177
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 63-262 3.43e-25

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 100.99  E-value: 3.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  63 YTYLLADVAhpEKPALLIDPVDktVDRDLSLVKELGLKLIYAINTHVHADHVTGTGLIKTKVPSVKsiISKASKSKADLL 142
Cdd:PLN02469  13 YAYLIIDES--TKDAAVVDPVD--PEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIK--VYGGSLDNVKGC 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 143 ---IEAGDKIHFG-DLFLEVRATPGHTLGCVTY-VTGDGSDQPQprmAFTGDALLIRGCGRtdFQGGSAHQLYQSVHSQI 217
Cdd:PLN02469  87 thpVENGDKLSLGkDVNILALHTPCHTKGHISYyVTGKEGEDPA---VFTGDTLFIAGCGK--FFEGTAEQMYQSLCVTL 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 566172744 218 FSLPKETLIYPAHDYR------GFTV--------------------------STVGEEMQYNPRLTKDEemfKSIME 262
Cdd:PLN02469 162 GSLPKPTQVYCGHEYTvknlkfALTVepdneklkqklewaekqrqaglptvpSTIEEELETNPFMRVDL---PEIQE 235
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 75-230 4.42e-22

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: 91.08  E-value: 4.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  75 KPALLIDPVDKtVDRDLSLVKELGLKLIYAINTHVHADHVTGTGLIK--TKVPSVKSiiskaskSKADL-LIEA------ 145
Cdd:cd07737   22 KEAAVIDPGGD-ADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAehYGVPIIGP-------HKEDKfLLENlpeqsq 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 146 ------------------GDKIHFGDLFLEVRATPGHTLGCVTYVtgdgsdQPQPRMAFTGDALLIRGCGRTDFQGGSAH 207
Cdd:cd07737   94 mfgfppaeaftpdrwleeGDTVTVGNLTLEVLHCPGHTPGHVVFF------NRESKLAIVGDVLFKGSIGRTDFPGGNHA 167

                        170       180
                 ....*....|....*....|...
gi 566172744 208 QLYQSVHSQIFSLPKETLIYPAH 230
Cdd:cd07737  168 QLIASIKEKLLPLGDDVTFIPGH 190
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
61-230 2.70e-19

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 83.57  E-value: 2.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744   61 STYTYLLADvahpEKPALLIDP---VDKTVDRDLSLVKELGLKLIYAINTHVHADHVTGTGLIK--TKVPSV-------- 127
Cdd:pfam00753   5 QVNSYLIEG----GGGAVLIDTggsAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAeaTDVPVIvvaeeare 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  128 -------------KSIISKASKSKADLLIEAGDKIHFGDLFLEVRATPGHTLGCVTYVTGDGsdqpqpRMAFTGDALLIR 194
Cdd:pfam00753  81 lldeelglaasrlGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGG------KVLFTGDLLFAG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 566172744  195 GCGRTDFQGGSAHQLYQSVHSQIFSL------PKETLIYPAH 230
Cdd:pfam00753 155 EIGRLDLPLGGLLVLHPSSAESSLESllklakLKAAVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 63-232 5.34e-15

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 74.11  E-value: 5.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  63 YTYLLAD-------VAHPEKPALLIDPVDKTvdrdlslvkelGLKLIYAINTHVHADHVTGTGLIKTKVpSVKSIISKAS 135
Cdd:PLN02398  88 YAYLLHDedtgtvgVVDPSEAVPVIDALSRK-----------NRNLTYILNTHHHYDHTGGNLELKARY-GAKVIGSAVD 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 136 KSKA---DLLIEAGDKIHFGDLFLEVRATPGHTLGCVTYVTgdgsdqPQPRMAFTGDALLIRGCGRTdFQgGSAHQLYQS 212
Cdd:PLN02398 156 KDRIpgiDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYF------PGSGAIFTGDTLFSLSCGKL-FE-GTPEQMLSS 227

                        170       180
                 ....*....|....*....|
gi 566172744 213 VhSQIFSLPKETLIYPAHDY 232
Cdd:PLN02398 228 L-QKIISLPDDTNIYCGHEY 246
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 107-232 6.56e-15

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 72.93  E-value: 6.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 107 THVHADHVTGTGLIKTKVPSVKSIISKASKSK-ADLLIEAGDKIHFGDLFLEVRATPGHTLGCVTYVTgdgsdqpQPRMa 185
Cdd:PRK10241  52 THHHHDHVGGVKELVEKFPQIVVYGPQETQDKgTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYFS-------KPYL- 123

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 566172744 186 FTGDALLIRGCGRTdFQgGSAHQLYQSVHsQIFSLPKETLIYPAHDY 232
Cdd:PRK10241 124 FCGDTLFSGGCGRL-FE-GTASQMYQSLK-KINALPDDTLICCAHEY 167
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 74-191 3.06e-14

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: 69.87  E-value: 3.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  74 EKPALLIDP-----VDKTVDRDLslvKELGLKLIYAINTHVHADHVTGTGLIKTK------------------------- 123
Cdd:cd07743   17 DKEALLIDSgldedAGRKIRKIL---EELGWKLKAIINTHSHADHIGGNAYLQKKtgckvyapkiekafienpllepsyl 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 566172744 124 -----VPSVKSIISKASKSKADLLIEAGdKIHFGDLFLEVRATPGHTLGCVTYVTGDGsdqpqprMAFTGDAL 191
Cdd:cd07743   94 ggaypPKELRNKFLMAKPSKVDDIIEEG-ELELGGVGLEIIPLPGHSFGQIGILTPDG-------VLFAGDAL 158
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 65-194 1.06e-09

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: 56.92  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  65 YLLADvahpEKPALLIDP-VDKTVDRDL--SLVKELGLKLI---YAINTHVHADHVTGTGLIKTK-VPSVKSIISKAsks 137
Cdd:cd07725   18 YLLRD----GDETTLIDTgLATEEDAEAlwEGLKELGLKPSdidRVLLTHHHPDHIGLAGKLQEKsGATVYILDVTP--- 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 566172744 138 kadllIEAGDKIHFGDLFLEVRATPGHTLGCVTYVTGDGsdqpqpRMAFTGDALLIR 194
Cdd:cd07725   91 -----VKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDR------RELFVGDAVLPK 136
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 65-186 2.03e-09

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: 57.11  E-value: 2.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  65 YLLADVAHPEKPALLIDPVdKTVDRDLSLVKelglkliYAINTHVHADHVTGTGLIKtKVPSVKSIISKASKS------- 137
Cdd:cd16309   33 HILIDGAMPQSTPLIKDNI-KKLGFDVKDVK-------YLLNTHAHFDHAGGLAELK-KATGAQLVASAADKPllesgyv 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 566172744 138 -------------KADLLIEAGDKIHFGDLFLEVRATPGHTLGCVTYVTGDGSDQPQPRMAF 186
Cdd:cd16309  104 gsgdtknlqfppvRVDRVIGDGDKVTLGGTTLTAHLTPGHSPGCTSWTTTVKDTAGPPREVL 165
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 95-172 2.05e-09

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 56.82  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  95 KELGLK---LIYAINTHVHADHVTGTGLIKTKvPSVKSIISKA------------------SKSKADLLIEAGDKIHFGD 153
Cdd:cd16280   53 EKLGLDpadIKYILITHGHGDHYGGAAYLKDL-YGAKVVMSEAdwdmmeeppeegdnprwgPPPERDIVIKDGDTLTLGD 131

                         90
                 ....*....|....*....
gi 566172744 154 LFLEVRATPGHTLGCVTYV 172
Cdd:cd16280  132 TTITVYLTPGHTPGTLSLI 150
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 94-173 7.08e-09

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


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 55.40  E-value: 7.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  94 VKELGLK---LIYAINTHVHADHVTGTGLIKtKVPSVKSIISKASKS----------------------KADLLIEAGDK 148
Cdd:cd16288   51 IRKLGFKpsdIKILLNSHAHLDHAGGLAALK-KLTGAKLMASAEDAAllasggksdfhygddslafppvKVDRVLKDGDR 129

                         90       100
                 ....*....|....*....|....*
gi 566172744 149 IHFGDLFLEVRATPGHTLGCVTYVT 173
Cdd:cd16288  130 VTLGGTTLTAHLTPGHTRGCTTWTM 154
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 77-191 1.38e-08

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: 53.40  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  77 ALLIDPVDKTVDRDlSLVKELGLKLIYAINTHVHADHVTG-------------TGLIKTKVPSVKSIISKASKSK----A 139
Cdd:cd07712   20 ALLIDTGLGIGDLK-EYVRTLTDLPLLVVATHGHFDHIGGlhefeevyvhpadAEILAAPDNFETLTWDAATYSVppagP 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 566172744 140 DLLIEAGDKIHFGDLFLEVRATPGHTLGCVTYVtgdgsdQPQPRMAFTGDAL 191
Cdd:cd07712   99 TLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALL------DRANRLLFSGDVV 144
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 94-173 4.02e-08

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


Pssm-ID: 293868  Cd Length: 252  Bit Score: 53.22  E-value: 4.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  94 VKELGLKLI---YAINTHVHADHVTGTGLIKtKVPSVKSIISKASKS---------------------KADLLIEAGDKI 149
Cdd:cd16310   51 IKALGFKLSdikIIINTHAHYDHAGGLAQLK-ADTGAKLWASRGDRPaleagkhigdnitqpapfpavKVDRILGDGEKI 129

                         90       100
                 ....*....|....*....|....
gi 566172744 150 HFGDLFLEVRATPGHTLGCVTYVT 173
Cdd:cd16310  130 KLGDITLTATLTPGHTKGCTTWST 153
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 94-191 1.37e-07

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


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 51.39  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  94 VKELGLKLI---YAINTHVHADHVTGTGLIKTKV----------------------PSVKSIISKASKSKADLLIEAGDK 148
Cdd:cd07708   51 IKKLGFKFSdtkLILISHAHFDHAGGSAEIKKQTgakvmagaedvslllsggssdfHYANDSSTYFPQSTVDRAVHDGER 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 566172744 149 IHFGDLFLEVRATPGHTLGCVTYvTGDGSDQPQPRMAFTGDAL 191
Cdd:cd07708  131 VTLGGTVLTAHATPGHTPGCTTW-TMTLKDHGKQYQVVFADSL 172
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 62-197 2.53e-06

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: 47.49  E-value: 2.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  62 TYTYLLADvahpEKPALLIDP-VDKTVDRDLSLVKELGL---KLIYAINTHVHADHVTGTGLIKTKVPSVK--------- 128
Cdd:cd07726   16 IASYLLDG----EGRPALIDTgPSSSVPRLLAALEALGIapeDVDYIILTHIHLDHAGGAGLLAEALPNAKvyvhprgar 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 129 -----SIISKASKS----------------KADLLIEA--GDKIHFGDLFLEVRATPGHTLGCVTYVTgdgsdqPQPRMA 185
Cdd:cd07726   92 hlidpSKLWASARAvygdeadrlggeilpvPEERVIVLedGETLDLGGRTLEVIDTPGHAPHHLSFLD------EESDGL 165

                        170
                 ....*....|..
gi 566172744 186 FTGDALLIRGCG 197
Cdd:cd07726  166 FTGDAAGVRYPE 177
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 62-195 3.45e-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: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 46.72  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  62 TYTYLLADvahpEKPALLIDP-----------VDKTVDRDLSLVkelglkLIyainTHVHADHVTGTGLIK--TKVPSVK 128
Cdd:cd16278   18 TNTYLLGA----PDGVVVIDPgpddpahldalLAALGGGRVSAI------LV----THTHRDHSPGAARLAerTGAPVRA 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 566172744 129 SIISKASKS----KADLLIEAGDKIHFGDLFLEVRATPGHTLGCVTYVTGDGsdqpqpRMAFTGDALLIRG 195
Cdd:cd16278   84 FGPHRAGGQdtdfAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDE------GALFTGDHVMGWS 148
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 79-190 1.77e-05

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: 44.50  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  79 LIDPVDKtVDRD--LSLVKELGLKL--I-YAINTHVHADHVTGTGLIktkvPSVKSIISKASKS---KADLLIEAGDKIH 150
Cdd:cd07711   35 LVDTGTP-WDRDllLKALAEHGLSPedIdYVVLTHGHPDHIGNLNLF----PNATVIVGWDICGdsyDDHSLEEGDGYEI 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 566172744 151 FGDlfLEVRATPGHTLGCVTYVTGDGSDQpqpRMAFTGDA 190
Cdd:cd07711  110 DEN--VEVIPTPGHTPEDVSVLVETEKKG---TVAVAGDL 144
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 62-230 2.31e-05

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


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 44.06  E-value: 2.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  62 TYTYLLadvaHPEKPALLID---PVDKTVDRDLSLVKELGLKLI-YAINTHVHADHVTGTGLIKTKVPSVKSIISK-ASK 136
Cdd:cd07722   18 TNTYLV----GTGKRRILIDtgeGRPSYIPLLKSVLDSEGNATIsDILLTHWHHDHVGGLPDVLDLLRGPSPRVYKfPRP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 137 SKADLLIEAGDKIHF---GDLF------LEVRATPGHTlgcvtyvtgdgSDQ-----PQPRMAFTGDALLirGCGRTDFq 202
Cdd:cd07722   94 EEDEDPDEDGGDIHDlqdGQVFkvegatLRVIHTPGHT-----------TDHvcfllEEENALFTGDCVL--GHGTAVF- 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 566172744 203 ggsahqlyQSVHSQIFSLPK-----ETLIYPAH 230
Cdd:cd07722  160 --------EDLAAYMASLKKllslgPGRIYPGH 184
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 77-190 4.45e-05

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: 43.28  E-value: 4.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  77 ALLID--PVDKTVDRD-LSLVKELG-LKLIYAINTHVHADHVTGTGLIKTKVPsVKSIIS----KASKSKADLL------ 142
Cdd:cd07731   21 TILIDtgPRDSFGEDVvVPYLKARGiKKLDYLILTHPDADHIGGLDAVLKNFP-VKEVYMpgvtHTTKTYEDLLdaikek 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 566172744 143 ------IEAGDKIHFGDLFLEVRATPGHTLG------CVTYVT-GDGSdqpqprMAFTGDA 190
Cdd:cd07731  100 gipvtpCKAGDRWQLGGVSFEVLSPPKDDYDdlnnnsCVLRLTyGGTS------FLLTGDA 154
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 94-171 3.05e-04

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


Pssm-ID: 293865  Cd Length: 255  Bit Score: 41.28  E-value: 3.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  94 VKELGLKLI---YAINTHVHADHVTGTGLIKTK-----------VPSVKS-----------IISKASKSKADLLIEAGDK 148
Cdd:cd16307   51 IEKLGFKFSdtkILLISHAHFDHAAGSALIKREthakymvmdgdVDVVESggksdffygndPSTYFPPAHVDKVLHDGEQ 130

                         90       100
                 ....*....|....*....|...
gi 566172744 149 IHFGDLFLEVRATPGHTLGCVTY 171
Cdd:cd16307  131 VELGGTVLTAHLTAGHTKGCTTW 153
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 70-190 6.82e-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: 40.23  E-value: 6.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  70 VAHPEKPALLID-----PVDKTVDRDLSLVKELGLKLI-YAINTHVHADHVTGTGLIKTKVPsVKSIIS----KASKSKA 139
Cdd:COG2333   16 IRTPDGKTILIDtgprpSFDAGERVVLPYLRALGIRRLdLLVLTHPDADHIGGLAAVLEAFP-VGRVLVsgppDTSETYE 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 566172744 140 DLL------------IEAGDKIHFGDLFLEVRATPGHTLG--------CVTYVTGDGSdqpqpRMAFTGDA 190
Cdd:COG2333   95 RLLealkekgipvrpCRAGDTWQLGGVRFEVLWPPEDLLEgsdennnsLVLRLTYGGF-----SFLLTGDA 160
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 94-172 8.58e-04

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: 40.15  E-value: 8.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  94 VKELGLK---LIYAINTHVHADHVTGTGLIKTKVPSVKSIISKASKS---------------------KADLLIEAGDKI 149
Cdd:cd16308   51 IQALGFKfkdIKILLTTQAHYDHVGAMAAIKQQTGAKMMVDEKDAKVladggksdyemggygstfapvKADKLLHDGDTI 130

                         90       100
                 ....*....|....*....|...
gi 566172744 150 HFGDLFLEVRATPGHTLGCVTYV 172
Cdd:cd16308  131 KLGGTKLTLLHHPGHTKGSCSFL 153
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 63-195 1.97e-03

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: 38.74  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  63 YTYLLADvahpEKPALLID---PvdKTVDRDLSLVKELGLKL--IYAIN-THVHADHVTGTGLIKtKVPSVKSIISKA-- 134
Cdd:cd07721   12 NAYLIED----DDGLTLIDtglP--GSAKRILKALRELGLSPkdIRRILlTHGHIDHIGSLAALK-EAPGAPVYAHERea 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 135 ---------------------------SKSKADLLIEAGDKIHF-GDLflEVRATPGHTLGCVTYVtgdgsdQPQPRMAF 186
Cdd:cd07721   85 pylegekpypppvrlgllgllspllpvKPVPVDRTLEDGDTLDLaGGL--RVIHTPGHTPGHISLY------LEEDGVLI 156


                 ....*....
gi 566172744 187 TGDALLIRG 195
Cdd:cd07721  157 AGDALVTVG 165
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 82-231 4.33e-03

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: 37.96  E-value: 4.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744  82 PVDKTVDRDLslvKELGLKL--I-YAINTHVHADHVTGTGLiktkVPSVKSIISKA----------------SKSKADLL 142
Cdd:cd07729   70 TEEQTLEEQL---ARLGLDPedIdYVILSHLHFDHAGGLDL----FPNATIIVQRAeleyatgpdplaagyyEDVLALDD 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 566172744 143 IEAGDKIHF----GDLF--LEVRATPGHTLG-CVTYV-TGDGSdqpqprMAFTGDALLIR---GCGRTDFQGGSAHQLYQ 211
Cdd:cd07729  143 DLPGGRVRLvdgdYDLFpgVTLIPTPGHTPGhQSVLVrLPEGT------VLLAGDAAYTYenlEEGRPPGINYDPEAALA 216

                        170       180
                 ....*....|....*....|..
gi 566172744 212 SVHSqIFSLPKET--LIYPAHD 231
Cdd:cd07729  217 SLER-LKALAEREgaRVIPGHD 237
 
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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