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Conserved domains on  [gi|1839705778|ref|XP_034120584|]
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persulfide dioxygenase ETHE1, mitochondrial isoform X3 [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
 36-267 2.62e-113

hydroxyacylglutathione hydrolase


The actual alignment was detected with superfamily member PLN02962:

Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 325.98  E-value: 2.62e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  36 SDFFFRQLFDEESSTYSYLLADLKTGE--AVVIDPVLEQAKRDAQLVKELGFKLKYAINTHLHADHITGSGWLR-ELTGC 112
Cdd:PLN02962    9 SKLLFRQLFEKESSTYTYLLADVSHPDkpALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKtKLPGV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 113 QSMIAAASGAKADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYViKAQG-------CVFTGDTVLIRGCGRTDFQEGSS 185
Cdd:PLN02962   89 KSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYV-TGEGpdqpqprMAFTGDALLIRGCGRTDFQGGSS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 186 ESLYENVHSKIFTLPDYFRIYPAHDYKGQLESSVWEEKRYNPRLTKDLEEFIRIMDNLNLSYPNKIDVSLPANRECGVYD 265
Cdd:PLN02962  168 DQLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPANMVCGLQD 247


                  ..
gi 1839705778 266 IP 267
Cdd:PLN02962  248 PP 249
 
Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 36-267 2.62e-113

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 325.98  E-value: 2.62e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  36 SDFFFRQLFDEESSTYSYLLADLKTGE--AVVIDPVLEQAKRDAQLVKELGFKLKYAINTHLHADHITGSGWLR-ELTGC 112
Cdd:PLN02962    9 SKLLFRQLFEKESSTYTYLLADVSHPDkpALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKtKLPGV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 113 QSMIAAASGAKADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYViKAQG-------CVFTGDTVLIRGCGRTDFQEGSS 185
Cdd:PLN02962   89 KSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYV-TGEGpdqpqprMAFTGDALLIRGCGRTDFQGGSS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 186 ESLYENVHSKIFTLPDYFRIYPAHDYKGQLESSVWEEKRYNPRLTKDLEEFIRIMDNLNLSYPNKIDVSLPANRECGVYD 265
Cdd:PLN02962  168 DQLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPANMVCGLQD 247


                  ..
gi 1839705778 266 IP 267
Cdd:PLN02962  248 PP 249
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 39-211 2.29e-91

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: 267.73  E-value: 2.29e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  39 FFRQLFDEESSTYSYLLADLKTGEAVVIDPVLEQAKRDAQLVKELGFKLKYAINTHLHADHITGSGWLRELTGCQSMI-A 117
Cdd:cd07724     1 IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIgE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 118 AASGAKADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFTGDTVLIRGCGRTDFQ---EGSSESLYENVHS 194
Cdd:cd07724    81 GAPASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPgeaEGLARQLYDSLQR 160

                         170
                  ....*....|....*..
gi 1839705778 195 KIFTLPDYFRIYPAHDY 211
Cdd:cd07724   161 KLLLLPDETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 39-229 5.36e-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: 156.00  E-value: 5.36e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  39 FFRQLFDEESSTYSYLLADlkTGEAVVIDPVLEQAKRDA--QLVKELGFKLKYAINTHLHADHITGSGWLRELTGCQSMI 116
Cdd:COG0491     4 LPGGTPGAGLGVNSYLIVG--GDGAVLIDTGLGPADAEAllAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 117 AAA----------------SGAKADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFTGDTVLIRGCGRTDF 180
Cdd:COG0491    82 HAAeaealeapaagalfgrEPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1839705778 181 QEGSSESLYENVHsKIFTLPDYfRIYPAHDYKGQLESSVWEEK-------RYNPRL 229
Cdd:COG0491   162 PDGDLAQWLASLE-RLLALPPD-LVIPGHGPPTTAEAIDYLEEllaalgeRANPFL 215
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 51-211 5.67e-33

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: 120.72  E-value: 5.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  51 YSYLLADlKTGEAVVID-----PVLEQ-AKRDAQLVkelgfklkyAI-NTHLHADHITGSGWLRELTGCQSMIAAASGAK 123
Cdd:TIGR03413  11 YIWLLHD-PDGQAAVVDpgeaePVLDAlEARGLTLT---------AIlLTHHHHDHVGGVAELLEAFPAPVYGPAEERIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 124 A-DVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFTGDTVLIRGCGRTdFqEGSSESLYENVhSKIFTLPDY 202
Cdd:TIGR03413  81 GiTHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRL-F-EGTPEQMYDSL-QRLAALPDD 157


                  ....*....
gi 1839705778 203 FRIYPAHDY 211
Cdd:TIGR03413 158 TLVYCAHEY 166
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 51-209 1.20e-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: 115.34  E-value: 1.20e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778   51 YSYLLADlkTGEAVVIDPVLEQAKRDAQLVKELG-FKLKYAINTHLHADHITGSGWLRELTGC----------------- 112
Cdd:smart00849   1 NSYLVRD--DGGAILIDTGPGEAEDLLAELKKLGpKKIDAIILTHGHPDHIGGLPELLEAPGApvyapegtaellkdlla 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  113 --QSMIAAASGAKADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFTGDTVLIRGCGRTDFqEGSSESLYE 190
Cdd:smart00849  79 llGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLV-DGGDAAASD 157

                          170       180
                   ....*....|....*....|
gi 1839705778  191 NVHS-KIFTLPDYFRIYPAH 209
Cdd:smart00849 158 ALESlLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
49-209 1.86e-22

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 91.66  E-value: 1.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  49 STYSYLLADlkTGEAVVIDPVLEQAKRDAQLVKELGFKLK---YAINTHLHADHITGSGWLRELTGC------------- 112
Cdd:pfam00753   5 QVNSYLIEG--GGGAVLIDTGGSAEAALLLLLAALGLGPKdidAVILTHGHFDHIGGLGELAEATDVpvivvaeearell 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 113 -----------QSMIAAASGAKADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFTGDTVLIRGCGRTDFQ 181
Cdd:pfam00753  83 deelglaasrlGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLP 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1839705778 182 EGSSESLYENVHSK------IFTLPDYFRIYPAH 209
Cdd:pfam00753 163 LGGLLVLHPSSAESslesllKLAKLKAAVIVPGH 196
 
Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 36-267 2.62e-113

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 325.98  E-value: 2.62e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  36 SDFFFRQLFDEESSTYSYLLADLKTGE--AVVIDPVLEQAKRDAQLVKELGFKLKYAINTHLHADHITGSGWLR-ELTGC 112
Cdd:PLN02962    9 SKLLFRQLFEKESSTYTYLLADVSHPDkpALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKtKLPGV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 113 QSMIAAASGAKADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYViKAQG-------CVFTGDTVLIRGCGRTDFQEGSS 185
Cdd:PLN02962   89 KSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYV-TGEGpdqpqprMAFTGDALLIRGCGRTDFQGGSS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 186 ESLYENVHSKIFTLPDYFRIYPAHDYKGQLESSVWEEKRYNPRLTKDLEEFIRIMDNLNLSYPNKIDVSLPANRECGVYD 265
Cdd:PLN02962  168 DQLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPANMVCGLQD 247


                  ..
gi 1839705778 266 IP 267
Cdd:PLN02962  248 PP 249
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 39-211 2.29e-91

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: 267.73  E-value: 2.29e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  39 FFRQLFDEESSTYSYLLADLKTGEAVVIDPVLEQAKRDAQLVKELGFKLKYAINTHLHADHITGSGWLRELTGCQSMI-A 117
Cdd:cd07724     1 IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIgE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 118 AASGAKADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFTGDTVLIRGCGRTDFQ---EGSSESLYENVHS 194
Cdd:cd07724    81 GAPASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPgeaEGLARQLYDSLQR 160

                         170
                  ....*....|....*..
gi 1839705778 195 KIFTLPDYFRIYPAHDY 211
Cdd:cd07724   161 KLLLLPDETLVYPGHDY 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 49-209 3.76e-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: 158.22  E-value: 3.76e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  49 STYSYLLADlKTGEAVVIDPVLEQAKRDAQLVKELGFKLKYAINTHLHADHITGSGWLRELTGCQSMIAAA--------- 119
Cdd:cd06262     9 QTNCYLVSD-EEGEAILIDPGAGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEAdaelledpe 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 120 -----------SGAKADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFTGDTVLIRGCGRTDFQEGSSESL 188
Cdd:cd06262    88 lnlaffgggplPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDLPGGDPEQL 167

                         170       180
                  ....*....|....*....|.
gi 1839705778 189 YENVHSKIFTLPDYFRIYPAH 209
Cdd:cd06262   168 IESIKKLLLLLPDDTVVYPGH 188
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 51-209 1.61e-47

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: 155.70  E-value: 1.61e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  51 YSYLLADLKTGEAVVIDPVleqakrDAQLV----KELGFKLKYAINTHLHADHITGSGWLRELTGcQSMIAAASGAK--- 123
Cdd:cd07723    10 YIYLIVDEATGEAAVVDPG------EAEPVlaalEKNGLTLTAILTTHHHWDHTGGNAELKALFP-DAPVYGPAEDRipg 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 124 ADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFTGDTVLIRGCGRtdFQEGSSESLYENvHSKIFTLPDYF 203
Cdd:cd07723    83 LDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGR--FFEGTAEQMYAS-LQKLLALPDDT 159


                  ....*.
gi 1839705778 204 RIYPAH 209
Cdd:cd07723   160 LVYCGH 165
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 39-229 5.36e-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: 156.00  E-value: 5.36e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  39 FFRQLFDEESSTYSYLLADlkTGEAVVIDPVLEQAKRDA--QLVKELGFKLKYAINTHLHADHITGSGWLRELTGCQSMI 116
Cdd:COG0491     4 LPGGTPGAGLGVNSYLIVG--GDGAVLIDTGLGPADAEAllAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 117 AAA----------------SGAKADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFTGDTVLIRGCGRTDF 180
Cdd:COG0491    82 HAAeaealeapaagalfgrEPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1839705778 181 QEGSSESLYENVHsKIFTLPDYfRIYPAHDYKGQLESSVWEEK-------RYNPRL 229
Cdd:COG0491   162 PDGDLAQWLASLE-RLLALPPD-LVIPGHGPPTTAEAIDYLEEllaalgeRANPFL 215
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 51-209 1.81e-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: 135.36  E-value: 1.81e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  51 YSYLLADLKTGEAVVIDPV--LEQAKRDAQlvkELGFKLKYAINTHLHADHITGSGWLRELTGCQSMIaaaSGAKADVY- 127
Cdd:cd16275    13 YSYIIIDKATREAAVVDPAwdIEKILAKLN---ELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYM---SKEEIDYYg 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 128 --------LEEGDRIEFGSHFIDVLATPGHTNGCMSYVIkaQGCVFTGDTVLIRGCGRTDFQEGSSESLYENVHsKIFTL 199
Cdd:cd16275    87 frcpnlipLEDGDTIKIGDTEITCLLTPGHTPGSMCYLL--GDSLFTGDTLFIEGCGRCDLPGGDPEEMYESLQ-RLKKL 163

                         170
                  ....*....|.
gi 1839705778 200 -PDYFRIYPAH 209
Cdd:cd16275   164 pPPNTRVYPGH 174
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 51-211 5.67e-33

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: 120.72  E-value: 5.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  51 YSYLLADlKTGEAVVID-----PVLEQ-AKRDAQLVkelgfklkyAI-NTHLHADHITGSGWLRELTGCQSMIAAASGAK 123
Cdd:TIGR03413  11 YIWLLHD-PDGQAAVVDpgeaePVLDAlEARGLTLT---------AIlLTHHHHDHVGGVAELLEAFPAPVYGPAEERIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 124 A-DVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFTGDTVLIRGCGRTdFqEGSSESLYENVhSKIFTLPDY 202
Cdd:TIGR03413  81 GiTHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRL-F-EGTPEQMYDSL-QRLAALPDD 157


                  ....*....
gi 1839705778 203 FRIYPAHDY 211
Cdd:TIGR03413 158 TLVYCAHEY 166
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 53-229 4.31e-32

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: 117.06  E-value: 4.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  53 YLLADLKTGEAVVIDPvleqAKRDAQLVK---ELGFKLKYAINTHLHADHITGSGWLRELTGCQSMI---------AAAS 120
Cdd:cd16322    14 YLVADEGGGEAVLVDP----GDESEKLLArfgTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLhpddlplyeAADL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 121 GAKA-----------DVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFTGDTVLIRGCGRTDFqEGSSESLY 189
Cdd:cd16322    90 GAKAfglgieplpppDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRTDL-PGGDPKAM 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1839705778 190 ENVHSKIFTLPDYFRIYPAHdykgQLESSVWEEKRYNPRL 229
Cdd:cd16322   169 AASLRRLLTLPDETRVFPGH----GPPTTLGEERRTNPFL 204
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 51-209 1.20e-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: 115.34  E-value: 1.20e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778   51 YSYLLADlkTGEAVVIDPVLEQAKRDAQLVKELG-FKLKYAINTHLHADHITGSGWLRELTGC----------------- 112
Cdd:smart00849   1 NSYLVRD--DGGAILIDTGPGEAEDLLAELKKLGpKKIDAIILTHGHPDHIGGLPELLEAPGApvyapegtaellkdlla 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  113 --QSMIAAASGAKADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFTGDTVLIRGCGRTDFqEGSSESLYE 190
Cdd:smart00849  79 llGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLV-DGGDAAASD 157

                          170       180
                   ....*....|....*....|
gi 1839705778  191 NVHS-KIFTLPDYFRIYPAH 209
Cdd:smart00849 158 ALESlLKLLKLLPKLVVPGH 177
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 52-209 4.93e-31

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: 113.80  E-value: 4.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  52 SYLLADLKTGEAVVIDPVLEqAKRDAQLVKELGFKLKYAINTHLHADHITGSGWLRELTG-------------------- 111
Cdd:cd07737    13 CSLIWCEETKEAAVIDPGGD-ADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGvpiigphkedkfllenlpeq 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 112 -CQSMIAAASGAKADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFTGDtVLIRGC-GRTDFQEGSSESLY 189
Cdd:cd07737    92 sQMFGFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGD-VLFKGSiGRTDFPGGNHAQLI 170

                         170       180
                  ....*....|....*....|
gi 1839705778 190 ENVHSKIFTLPDYFRIYPAH 209
Cdd:cd07737   171 ASIKEKLLPLGDDVTFIPGH 190
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 20-211 1.01e-26

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 106.08  E-value: 1.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  20 NVQNNSSSLPVgkpftsdfffrQLFDEESSTYSYLLADLKTGEAVVIDP-----VLEQAKRDAQlvkelgfKLKYAINTH 94
Cdd:PLN02398   68 SVSNVSSSLQI-----------ELVPCLKDNYAYLLHDEDTGTVGVVDPseavpVIDALSRKNR-------NLTYILNTH 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  95 LHADHITGSGWLRELTGCQSMIAAASGAKA---DVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFTGDTVL 171
Cdd:PLN02398  130 HHYDHTGGNLELKARYGAKVIGSAVDKDRIpgiDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLF 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1839705778 172 IRGCGRtdFQEGSSESLYENVhSKIFTLPDYFRIYPAHDY 211
Cdd:PLN02398  210 SLSCGK--LFEGTPEQMLSSL-QKIISLPDDTNIYCGHEY 246
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 51-236 4.63e-26

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 102.53  E-value: 4.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  51 YSYLLADLKTGEAVVIDPVLEQAKRDAqlVKELGFKLKYAINTHLHADHITGSGWLRELTgcqSMIAAASGAKADVY--- 127
Cdd:PLN02469   13 YAYLIIDESTKDAAVVDPVDPEKVLQA--AHEHGAKIKLVLTTHHHWDHAGGNEKIKKLV---PGIKVYGGSLDNVKgct 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 128 --LEEGDRIEFGSHF-IDVLATPGHTNGCMSYVIKAQ----GCVFTGDTVLIRGCGRtdFQEGSSESLYENVHSKIFTLP 200
Cdd:PLN02469   88 hpVENGDKLSLGKDVnILALHTPCHTKGHISYYVTGKegedPAVFTGDTLFIAGCGK--FFEGTAEQMYQSLCVTLGSLP 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1839705778 201 DYFRIYPAHDY------------------KGQLE--------------SSVWEEKRYNPRLTKDLEEF 236
Cdd:PLN02469  166 KPTQVYCGHEYtvknlkfaltvepdneklKQKLEwaekqrqaglptvpSTIEEELETNPFMRVDLPEI 233
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
49-209 1.86e-22

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 91.66  E-value: 1.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  49 STYSYLLADlkTGEAVVIDPVLEQAKRDAQLVKELGFKLK---YAINTHLHADHITGSGWLRELTGC------------- 112
Cdd:pfam00753   5 QVNSYLIEG--GGGAVLIDTGGSAEAALLLLLAALGLGPKdidAVILTHGHFDHIGGLGELAEATDVpvivvaeearell 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 113 -----------QSMIAAASGAKADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFTGDTVLIRGCGRTDFQ 181
Cdd:pfam00753  83 deelglaasrlGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLP 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1839705778 182 EGSSESLYENVHSK------IFTLPDYFRIYPAH 209
Cdd:pfam00753 163 LGGLLVLHPSSAESslesllKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 50-174 2.19e-20

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: 85.62  E-value: 2.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  50 TYSYLLADlkTGEAVVIDP-VLEQAKRDAQLVKELGFKLKYAINTHLHADHITGSGWLRELTGCQSMIAAASGA------ 122
Cdd:cd16278    18 TNTYLLGA--PDGVVVIDPgPDDPAHLDALLAALGGGRVSAILVTHTHRDHSPGAARLAERTGAPVRAFGPHRAggqdtd 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1839705778 123 -KADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFTGDTVLIRG 174
Cdd:cd16278    96 fAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVMGWS 148
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 58-170 1.55e-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: 78.34  E-value: 1.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  58 LKTGEAVVIDPVL--EQAKRDAQLVKELGFKLKYAINTHLHADHITGSGWLRELTGCQsmIAAASGAKA----------- 124
Cdd:cd07743    15 FGDKEALLIDSGLdeDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCK--VYAPKIEKAfienpllepsy 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1839705778 125 ----------------------DVYLEEGDrIEFGSHFIDVLATPGHTNGCMSYVIKaQGCVFTGDTV 170
Cdd:cd07743    93 lggayppkelrnkflmakpskvDDIIEEGE-LELGGVGLEIIPLPGHSFGQIGILTP-DGVLFAGDAL 158
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 58-158 4.33e-15

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 72.62  E-value: 4.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  58 LKTGE-AVVIDpVLEQAKRDAQLV---KELGFK---LKYAINTHLHADHITGSGWLRELTGCQ--------SMIAAASGA 122
Cdd:cd16280    27 IDTGDgLILID-ALNNNEAADLIVdglEKLGLDpadIKYILITHGHGDHYGGAAYLKDLYGAKvvmseadwDMMEEPPEE 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1839705778 123 ----------KADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVI 158
Cdd:cd16280   106 gdnprwgpppERDIVIKDGDTLTLGDTTITVYLTPGHTPGTLSLIF 151
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 52-209 4.69e-14

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 68.48  E-value: 4.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  52 SYLLADlkTGEAVVIDPVLEQaKRDAQLV----KELGFKL---KYAINTHLHADHITGSGWLRELTGCqsmiaaasgaka 124
Cdd:cd07725    17 VYLLRD--GDETTLIDTGLAT-EEDAEALweglKELGLKPsdiDRVLLTHHHPDHIGLAGKLQEKSGA------------ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 125 DVY------LEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFTGDTVLIR----GCGRTDFQEGSSESLYENVhS 194
Cdd:cd07725    82 TVYildvtpVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLPKitpnVSLWAVRVEDPLGAYLESL-D 160

                         170
                  ....*....|....*
gi 1839705778 195 KIFTLpDYFRIYPAH 209
Cdd:cd07725   161 KLEKL-DVDLAYPGH 174
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 52-161 6.01e-13

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: 66.96  E-value: 6.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  52 SYLLadlKTGE-AVVIDPVLEQ-AKRDAQLVKELGFK---LKYAINTHLHADHITGSGWLRELTGCQSMIAAASGA---- 122
Cdd:cd16288    24 SYLI---TTPQgLILIDTGLESsAPMIKANIRKLGFKpsdIKILLNSHAHLDHAGGLAALKKLTGAKLMASAEDAAllas 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839705778 123 ------------------KADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQ 161
Cdd:cd16288   101 ggksdfhygddslafppvKVDRVLKDGDRVTLGGTTLTAHLTPGHTRGCTTWTMTVK 157
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 50-209 7.17e-13

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: 65.25  E-value: 7.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  50 TY------SYLLADlkTGEAVVI-DPVLEQAkrdaqLVKELGFKLKYAINTHLHADHITGSGWLRELTGCQSMI------ 116
Cdd:cd07722    20 TYlvgtgkRRILID--TGEGRPSyIPLLKSV-----LDSEGNATISDILLTHWHHDHVGGLPDVLDLLRGPSPRvykfpr 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 117 ----AAASGAKAD-VYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFTGDTVLirGCGRTDFqegssESLYEN 191
Cdd:cd07722    93 peedEDPDEDGGDiHDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGDCVL--GHGTAVF-----EDLAAY 165

                         170       180
                  ....*....|....*....|
gi 1839705778 192 VHS--KIFTLPdYFRIYPAH 209
Cdd:cd07722   166 MASlkKLLSLG-PGRIYPGH 184
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 50-176 9.00e-13

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: 65.59  E-value: 9.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  50 TYSYLLADlkTGEAVVID-------PVLEQAkrdaqlVKELGF---KLKYAINTHLHADHITGSGWL-RELTGCQ----- 113
Cdd:cd07726    16 IASYLLDG--EGRPALIDtgpsssvPRLLAA------LEALGIapeDVDYIILTHIHLDHAGGAGLLaEALPNAKvyvhp 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 114 ----------SMIAAAS---GAKADVY--------------LEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFT 166
Cdd:cd07726    88 rgarhlidpsKLWASARavyGDEADRLggeilpvpeervivLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFT 167

                         170
                  ....*....|
gi 1839705778 167 GDTVLIRGCG 176
Cdd:cd07726   168 GDAAGVRYPE 177
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 63-159 2.65e-12

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: 64.87  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  63 AVVIDPVLEQ-AKRDAQLVKELGFK---LKYAINTHLHADHITGSGWLRELTGCQSMIAAAS------------------ 120
Cdd:cd07708    33 NILIDGDMEQnAPMIKANIKKLGFKfsdTKLILISHAHFDHAGGSAEIKKQTGAKVMAGAEDvslllsggssdfhyands 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1839705778 121 -----GAKADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIK 159
Cdd:cd07708   113 styfpQSTVDRAVHDGERVTLGGTVLTAHATPGHTPGCTTWTMT 156
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 51-174 4.75e-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: 4.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  51 YSYLLADlkTGEAVVIDP-VLEQAKRDAQLVKELGFK---LKYAINTHLHADHITGSGWLRELTGCQSMIAAA-----SG 121
Cdd:cd07721    12 NAYLIED--DDGLTLIDTgLPGSAKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEReapylEG 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1839705778 122 AKA------------------------DVYLEEGDRIEF-GShfIDVLATPGHTNGCMSYVIKAQGCVFTGDTVLIRG 174
Cdd:cd07721    90 EKPypppvrlgllgllspllpvkpvpvDRTLEDGDTLDLaGG--LRVIHTPGHTPGHISLYLEEDGVLIAGDALVTVG 165
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 51-211 8.47e-12

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 63.30  E-value: 8.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  51 YSYLLADlKTGEAVVIDPvlEQAKRDAQLVKELGFKLKYAINTHLHADHITGSGWLREltGCQSMI----AAASGAKADV 126
Cdd:PRK10241   13 YIWVLND-EAGRCLIVDP--GEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVE--KFPQIVvygpQETQDKGTTQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 127 YLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQgcVFTGDTVLIRGCGRtdFQEGSSESLYENVHsKIFTLPDYFRIY 206
Cdd:PRK10241   88 VVKDGETAFVLGHEFSVFATPGHTLGHICYFSKPY--LFCGDTLFSGGCGR--LFEGTASQMYQSLK-KINALPDDTLIC 162


                  ....*
gi 1839705778 207 PAHDY 211
Cdd:PRK10241  163 CAHEY 167
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 46-209 1.07e-11

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


Pssm-ID: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 61.88  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  46 EESSTYSYLLadLKTGEAVVIDPVLEQAKRDaQLVKELGFKLKYAINTHLHADHITG-------------SGWLRelTGC 112
Cdd:cd07712     5 EDDRVNIYLL--RGRDRALLIDTGLGIGDLK-EYVRTLTDLPLLVVATHGHFDHIGGlhefeevyvhpadAEILA--APD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 113 QSMIAAASGAKADVY-------LEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFTGDTV----LIrgcgrtDFQ 181
Cdd:cd07712    80 NFETLTWDAATYSVPpagptlpLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVydgpLI------MDL 153

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1839705778 182 EGSSESLYenVHS--KIFTLPDYFR-IYPAH 209
Cdd:cd07712   154 PHSDLDDY--LASleKLSKLPDEFDkVLPGH 182
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 64-162 4.57e-11

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: 61.35  E-value: 4.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  64 VVIDPVLEQAkrdAQLVKE----LGFK---LKYAINTHLHADHITGSGWLRELTGCQsMIAAA-------SG-------- 121
Cdd:cd16309    34 ILIDGAMPQS---TPLIKDnikkLGFDvkdVKYLLNTHAHFDHAGGLAELKKATGAQ-LVASAadkplleSGyvgsgdtk 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1839705778 122 ------AKADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQG 162
Cdd:cd16309   110 nlqfppVRVDRVIGDGDKVTLGGTTLTAHLTPGHSPGCTSWTTTVKD 156
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 52-156 1.54e-09

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


Pssm-ID: 293868  Cd Length: 252  Bit Score: 57.08  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  52 SYLLAdlKTGEAVVIDPVLEQ-AKRDAQLVKELGFKL---KYAINTHLHADHITGSGWLRELTGCQSMI------AAASG 121
Cdd:cd16310    24 SYLIT--SNHGAILLDGGLEEnAALIEQNIKALGFKLsdiKIIINTHAHYDHAGGLAQLKADTGAKLWAsrgdrpALEAG 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1839705778 122 ---------------AKADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSY 156
Cdd:cd16310   102 khigdnitqpapfpaVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTW 151
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 43-170 1.88e-09

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 56.45  E-value: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  43 LFDeessT-YSYLLADLKTGEAVVIDPVLEQAKR-DAQLvKELGFK---LKYAINTHLHADHI------TGSGWL---RE 108
Cdd:cd07729    45 LVD----TgFHPDAADDPGGLELAFPPGVTEEQTlEEQL-ARLGLDpedIDYVILSHLHFDHAggldlfPNATIIvqrAE 119

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1839705778 109 LTGCQSMIAAASGAKADVYLE------------EGDRIEFGShfIDVLATPGHTNGCMSYVIKAQG--CVFTGDTV 170
Cdd:cd07729   120 LEYATGPDPLAAGYYEDVLALdddlpggrvrlvDGDYDLFPG--VTLIPTPGHTPGHQSVLVRLPEgtVLLAGDAA 193
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 80-158 2.89e-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: 56.32  E-value: 2.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  80 VKELGFK---LKYAINTHLHADHITGSGWLRELTGCQSMIAAASGA----------------------KADVYLEEGDRI 134
Cdd:cd16308    51 IQALGFKfkdIKILLTTQAHYDHVGAMAAIKQQTGAKMMVDEKDAKvladggksdyemggygstfapvKADKLLHDGDTI 130

                          90       100
                  ....*....|....*....|....
gi 1839705778 135 EFGSHFIDVLATPGHTNGCMSYVI 158
Cdd:cd16308   131 KLGGTKLTLLHHPGHTKGSCSFLF 154
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 63-185 1.35e-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: 53.72  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  63 AVVID--PVLEQAKRDAQLVKELGFK-LKYAINTHLHADHITGSGWLREL-------TGCQSMIAAASGAK--------- 123
Cdd:cd16282    26 VVVIDtgASPRLARALLAAIRKVTDKpVRYVVNTHYHGDHTLGNAAFADAgapiiahENTREELAARGEAYlelmrrlgg 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1839705778 124 ----------ADVYLEEGDRIEFGSHFIDVLAT-PGHTNGCMSYVIKAQGCVFTGDTVLIrgcGRTDFQEGSS 185
Cdd:cd16282   106 damagtelvlPDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEGVLFAGDLVFN---GRIPFLPDGS 175
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 ...
 64-156 1.61e-08

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: 53.89  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  64 VVIDPVLEQ-AKRDAQLVKELGFKL---KYAINTHLHADHITGSGWLRELTGCQsMIAAASGAKA--------------- 124
Cdd:cd16290    34 ILIDGALPQsAPQIEANIRALGFRLedvKLILNSHAHFDHAGGIAALQRDSGAT-VAASPAGAAAlrsggvdpddpqaga 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1839705778 125 ---------DVYLEEGDRIEFGSHFIDVLATPGHTNGCMSY 156
Cdd:cd16290   113 adpfppvakVRVVADGEVVKLGPLAVTAHATPGHTPGGTSW 153
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 80-174 2.00e-08

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: 53.60  E-value: 2.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  80 VKELGFKL---KYAINTHLHADHITGSGWLRELTGCQSMI------AAASGAKADVY-----------------LEEGDR 133
Cdd:cd16307    51 IEKLGFKFsdtKILLISHAHFDHAAGSALIKRETHAKYMVmdgdvdVVESGGKSDFFygndpstyfppahvdkvLHDGEQ 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1839705778 134 IEFGSHFIDVLATPGHTNGCMSYVIKAQGCVFTGDTVLIRG 174
Cdd:cd16307   131 VELGGTVLTAHLTAGHTKGCTTWTMKVKDHGKTYDVVIVGS 171
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 64-172 3.83e-08

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: 52.31  E-value: 3.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  64 VVIDPV---LEQAKRDAQLVKELGFKLKYAINTHLHADHITGSGWLRELTG-------------CQSMIAAASGAKADVY 127
Cdd:pfam12706   3 ILIDPGpdlRQQALPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPrplyaplgvlahlRRNFPYLFLLEHYGVR 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778 128 LEE---GDRIEFGSHFIDVLATPGHTNG----------CMSYVIKAQG--CVFTGDTVLI 172
Cdd:pfam12706  83 VHEidwGESFTVGDGGLTVTATPARHGSprgldpnpgdTLGFRIEGPGkrVYYAGDTGYF 142
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 56-160 4.31e-08

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: 52.74  E-value: 4.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  56 ADLKTGEA--VVIDPVLEQAkrdAQLV----KELGFKL---KYAINTHLHADHITGSGWLRELTGCQ------------- 113
Cdd:cd16315    24 AILITGDDghVLIDSGTEEA---APLVlaniRKLGFDPkdvRWLLSSHEHFDHVGGLAALQRATGARvaasaaaapvles 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1839705778 114 ----------SMIAAASGAKADVYLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKA 160
Cdd:cd16315   101 gkpapddpqaGLHEPFPPVRVDRIVEDGDTVALGSLRLTAHATPGHTPGALSWTWRS 157
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 89-168 5.82e-07

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 49.06  E-value: 5.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  89 YAINTHLHADHItgsGWL---------------------RELTGCQSMiAAASGAKADVY-------LEEG--DRIEFGS 138
Cdd:cd16277    66 YVLCTHLHVDHV---GWNtrlvdgrwvptfpnarylfsrAEYDHWSSP-DAGGPPNRGVFedsvlpvIEAGlaDLVDDDH 141

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1839705778 139 HFID---VLATPGHTNGCMSYVIKAQG--CVFTGD 168
Cdd:cd16277   142 EILDgirLEPTPGHTPGHVSVELESGGerALFTGD 176
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 89-210 8.56e-07

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: 48.35  E-value: 8.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  89 YAINTHLHADHITGSGWLRELTGCQSMIAAASGAKaDVYLEEGDRIEFGSHfIDVLATPGHTNGCMSYVIK--AQGCVF- 165
Cdd:cd07711    63 YVVLTHGHPDHIGNLNLFPNATVIVGWDICGDSYD-DHSLEEGDGYEIDEN-VEVIPTPGHTPEDVSVLVEteKKGTVAv 140

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1839705778 166 TGDtVLIRGCGRTDFQEGSSESLYENVH----SKIFTLPDYfrIYPAHD 210
Cdd:cd07711   141 AGD-LFEREEDLEDPILWDPLSEDPELQeesrKRILALADW--IIPGHG 186
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
93-194 3.09e-06

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 47.11  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  93 THLHADHITG----------SGWLRELT-----GCQSMIAA---ASGAKAD-----VYLEEGDRIEFGSHFIDVLATPgH 149
Cdd:COG1234    59 THLHGDHIAGlpgllstrslAGREKPLTiygppGTKEFLEAllkASGTDLDfplefHEIEPGEVFEIGGFTVTAFPLD-H 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1839705778 150 TNGCMSYVIKAQGC--VFTGDTV-------LIRGCgrtD-------FQEGSSESLYENVHS 194
Cdd:COG1234   138 PVPAYGYRFEEPGRslVYSGDTRpcealveLAKGA---DlliheatFLDEEAELAKETGHS 195
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 77-156 1.70e-05

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: 44.85  E-value: 1.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  77 AQLVKELGFKL---KYAINTHLHADHITGSGWLRELTGCQSMIAAASGA--------KADVY---------------LEE 130
Cdd:cd16313    48 AASIRQLGFKLedvKYILSSHDHWDHAGGIAALQKLTGAQVLASPATVAvlrsgsmgKDDPQfggltpmppvasvraVRD 127

                          90       100
                  ....*....|....*....|....*.
gi 1839705778 131 GDRIEFGSHFIDVLATPGHTNGCMSY 156
Cdd:cd16313   128 GEVVKLGPLAVTAHATPGHTTGGTSW 153
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 63-156 8.02e-05

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


Pssm-ID: 293847  Cd Length: 239  Bit Score: 42.88  E-value: 8.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  63 AVVIDPVLEQAKrDAQL--VKELGF---KLKYAINTHLHADHITGSGWLRELTGCQ-------SMIAAASG--------- 121
Cdd:cd16289    33 AVLLDGGMPQAA-DMLLdnMRALGVapgDLKLILHSHAHADHAGPLAALKRATGARvaanaesAVLLARGGsddihfgdg 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1839705778 122 -----AKADVYLEEGDRIEFG-----SHFidvlaTPGHTNGCMSY 156
Cdd:cd16289   112 itfppVQADRIVMDGEVVTLGgvtftAHF-----TPGHTPGSTSW 151
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 80-170 8.44e-05

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: 42.18  E-value: 8.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  80 VKELGfKLKYAINTHLH--ADHitgSGWlRELTGCQSMIA-----AASGAKADVYLEEGDRIEFGSHFiDVLATPGHTNG 152
Cdd:cd07727    42 IEALG-GIRYIFLTHRDdvADH---AKW-AERFGAKRIIHeddvnAVTRPDEVIVLWGGDPWELDPDL-TLIPVPGHTRG 115

                          90
                  ....*....|....*...
gi 1839705778 153 CMSYVIKAQGCVFTGDTV 170
Cdd:cd07727   116 SVVLLYKEKGVLFTGDHL 133
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 62-108 2.06e-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: 41.33  E-value: 2.06e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1839705778  62 EAVVIDP--VLEQAKRDAQLVKELGFKLKYAINTHLHADHITGSGWLRE 108
Cdd:cd07739    26 EAVLVDAqfTRADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLE 74
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 64-152 2.54e-04

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


Pssm-ID: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 41.51  E-value: 2.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  64 VVIDPVLEQAKRDAQL-VKELGFKL---KYAINTHLHADHITGSGWLRELTGCqSMIAAASGA----------------- 122
Cdd:cd16312    34 VLLDGALPQSAPLIIAnIEALGFRIedvKLILNSHAHWDHAGGIAALQKASGA-TVAASAHGAqvlqsgtngkddpqyqa 112

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1839705778 123 KADVYLE---------EGDRIEFGSHFIDVLATPGHTNG 152
Cdd:cd16312   113 KPVVHVAkvakvkevgEGDTLKVGPLRLTAHMTPGHTPG 151
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 58-174 5.00e-04

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 40.29  E-value: 5.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  58 LKTGEAVV-IDPVLEqakRDAQLVKELGFKLKYAIN------THLHADHItGSGWLREL----------TGCQSMIAAAS 120
Cdd:COG2220    16 IETGGKRIlIDPVFS---GRASPVNPLPLDPEDLPKidavlvTHDHYDHL-DDATLRALkrtgatvvapLGVAAWLRAWG 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1839705778 121 GAKAdVYLEEGDRIEFGshFIDVLATPG-HTNG--------CMSYVIKAQGCV--FTGDTVLIRG 174
Cdd:COG2220    92 FPRV-TELDWGESVELG--GLTVTAVPArHSSGrpdrngglWVGFVIETDGKTiyHAGDTGYFPE 153
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 61-168 6.49e-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: 6.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  61 GEAVVID----PVLEQAKRD-AQLVKELGF-KLKYAINTHLHADHITG---------------SGWLRELTGCQSMIAAA 119
Cdd:COG2333    21 GKTILIDtgprPSFDAGERVvLPYLRALGIrRLDLLVLTHPDADHIGGlaavleafpvgrvlvSGPPDTSETYERLLEAL 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1839705778 120 SGAKADVY-LEEGDRIEFGSHFIDVLATPGHTNGC-----MSYVIKAQGC----VFTGD 168
Cdd:COG2333   101 KEKGIPVRpCRAGDTWQLGGVRFEVLWPPEDLLEGsdennNSLVLRLTYGgfsfLLTGD 159
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 61-172 3.16e-03

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 37.95  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  61 GEAVVIDP---VLEQAKRDAQLVKelgfKLKYAINTHLHADHITGSGWLRELTGCQSM-IAAASGAKADV---------- 126
Cdd:COG1235    44 GTRLLIDAgpdLREQLLRLGLDPS----KIDAILLTHEHADHIAGLDDLRPRYGPNPIpVYATPGTLEALerrfpylfap 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1839705778 127 --------YLEEGDRIEFGSHFIDVLATPGHTNGCMSYVIKAQG--CVFTGDTVLI 172
Cdd:COG1235   120 ypgklefhEIEPGEPFEIGGLTVTPFPVPHDAGDPVGYRIEDGGkkLAYATDTGYI 175
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 61-168 3.54e-03

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 37.50  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  61 GEAVVID--PVLEQAKRdaQLV---KELGF-KLKYAINTHLHADHITG---------------SGWLRELTGCQSMIAAA 119
Cdd:cd07731    19 GKTILIDtgPRDSFGED--VVVpylKARGIkKLDYLILTHPDADHIGGldavlknfpvkevymPGVTHTTKTYEDLLDAI 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1839705778 120 SGAKADV-YLEEGDRIEFGSHFIDVLA----TPGHTNGcMSYVIKAQG----CVFTGD 168
Cdd:cd07731    97 KEKGIPVtPCKAGDRWQLGGVSFEVLSppkdDYDDLNN-NSCVLRLTYggtsFLLTGD 153
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 93-169 8.38e-03

Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. 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: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 36.47  E-value: 8.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839705778  93 THLHADHITG----------SGWLRELT--GCQSM-------IAAASGAKADVY------LEEGDRIEFGSHFIDVLATP 147
Cdd:cd16272    57 SHFHLDHIGGlptllfarryGGRKKPLTiyGPKGIkefleklLNFPVEILPLGFpleieeLEEGGEVLELGDLKVEAFPV 136

                          90       100
                  ....*....|....*....|....
gi 1839705778 148 GHTNGCMSYVIKAQG--CVFTGDT 169
Cdd:cd16272   137 KHSVESLGYRIEAEGksIVYSGDT 160
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 61-108 9.62e-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: 9.62e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1839705778  61 GEAVVIDPVLEQAKRdAQLV----KELGFKLKYAINTHLHADHITGSGWLRE 108
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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