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Conserved domains on  [gi|145362330|ref|NP_974018|]
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glyoxalase II 3 [Arabidopsis thaliana]

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
 51-292 0e+00

hydroxyacylglutathione hydrolase


:

Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 518.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  51 KLLFRQLFENESSTFTYLLADVSHPDKPALLIDPVDKTVDRDLKLIDELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVK 130
Cdd:PLN02962  10 KLLFRQLFEKESSTYTYLLADVSHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVK 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 131 SVISKASGSKADLFLEPGDKVSIGDIYLEVRATPGHTAGCVTYVTGEGADQPQPRMAFTGDAVLIRGCGRTDFQEGSSDQ 210
Cdd:PLN02962  90 SIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPDQPQPRMAFTGDALLIRGCGRTDFQGGSSDQ 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 211 LYESVHSQIFTLPKDTLIYPAHDYKGFEVITVGEEMQHNPRLTKDKETFKTIMSNLNLSYPKMIDVAVPANMVCGLQDVP 290
Cdd:PLN02962 170 LYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPANMVCGLQDPP 249


                 ..
gi 145362330 291 SQ 292
Cdd:PLN02962 250 AK 251
 
Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 51-292 0e+00

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 518.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  51 KLLFRQLFENESSTFTYLLADVSHPDKPALLIDPVDKTVDRDLKLIDELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVK 130
Cdd:PLN02962  10 KLLFRQLFEKESSTYTYLLADVSHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVK 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 131 SVISKASGSKADLFLEPGDKVSIGDIYLEVRATPGHTAGCVTYVTGEGADQPQPRMAFTGDAVLIRGCGRTDFQEGSSDQ 210
Cdd:PLN02962  90 SIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPDQPQPRMAFTGDALLIRGCGRTDFQGGSSDQ 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 211 LYESVHSQIFTLPKDTLIYPAHDYKGFEVITVGEEMQHNPRLTKDKETFKTIMSNLNLSYPKMIDVAVPANMVCGLQDVP 290
Cdd:PLN02962 170 LYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPANMVCGLQDPP 249


                 ..
gi 145362330 291 SQ 292
Cdd:PLN02962 250 AK 251
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 53-234 7.61e-76

ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; MBL-fold metallo-hydrolase domain; Persulfide dioxygenase (PDO, also known as sulfur dioxygenase, SDO, EC 1.13.11.18) is a non-heme iron-dependent oxygenase which catalyzes the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria. Mutations in ethe1 (the human PDO gene) are responsible for a rare autosomal recessive metabolic disorder called ethylmalonic encephalopathy. Arabidopsis thaliana ETHE1 is essential for embryo and endosperm development. Bacterial ETHE1-type PDOs are also called Type 1 PDOs. Type II PDOs (also called PDOAs), are mainly proteobacterial. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293810 [Multi-domain]  Cd Length: 177  Bit Score: 229.21  E-value: 7.61e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  53 LFRQLFENESSTFTYLLADVShpDKPALLIDPVDKTVDRDLKLIDELGLKLIYAMNTHVHADHVTGTGLLKtKLPGVKSV 132
Cdd:cd07724    1 IFRQFFDPGLGTLSYLVGDPE--TGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELA-ERTGAPIV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 133 ISK-ASGSKADLFLEPGDKVSIGDIYLEVRATPGHTAGCVTYVTGEgadqpqPRMAFTGDAVLIRGCGRTDFQ---EGSS 208
Cdd:cd07724   78 IGEgAPASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGD------PDAVFTGDTLFVGDVGRPDLPgeaEGLA 151

                        170       180
                 ....*....|....*....|....*.
gi 145362330 209 DQLYESVHSQIFTLPKDTLIYPAHDY 234
Cdd:cd07724  152 RQLYDSLQRKLLLLPDETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 53-234 4.20e-36

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: 128.65  E-value: 4.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  53 LFRQLFENESSTFTYLLADvshpDKPALLIDPV--DKTVDRDLKLIDELGLKLIYAMNTHVHADHVTGTGLLKTKLpGVK 130
Cdd:COG0491    4 LPGGTPGAGLGVNSYLIVG----GDGAVLIDTGlgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 131 SVISKA----------------SGSKADLFLEPGDKVSIGDIYLEVRATPGHTAGCVTYVTgegadqPQPRMAFTGDAVL 194
Cdd:COG0491   79 VYAHAAeaealeapaagalfgrEPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV------PDEKVLFTGDALF 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 145362330 195 IRGCGRTDFQEGSSDQLYESVHsQIFTLPkDTLIYPAHDY 234
Cdd:COG0491  153 SGGVGRPDLPDGDLAQWLASLE-RLLALP-PDLVIPGHGP 190
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 66-232 3.88e-24

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: 96.08  E-value: 3.88e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330    66 TYLLADvshpDKPALLIDPVDKTVDRDLKLIDELGL-KLIYAMNTHVHADHVTGTGLLKtKLPGVKSVISKAS------- 137
Cdd:smart00849   2 SYLVRD----DGGAILIDTGPGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELL-EAPGAPVYAPEGTaellkdl 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330   138 ------------GSKADLFLEPGDKVSIGDIYLEVRATPGHTAGCVTYVTGEGadqpqpRMAFTGDAVLIRGCGRTDFqE 205
Cdd:smart00849  77 lallgelgaeaePAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEG------KILFTGDLLFAGGDGRTLV-D 149

                          170       180
                   ....*....|....*....|....*...
gi 145362330   206 GSSDQLYESVHSQI-FTLPKDTLIYPAH 232
Cdd:smart00849 150 GGDAAASDALESLLkLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
63-232 3.10e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 69.70  E-value: 3.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330   63 STFTYLLADvshpDKPALLIDP---VDKTVDRDLKLIDELGLKLIYAMNTHVHADHVTGTGLLKTKLPGV---------- 129
Cdd:pfam00753   5 QVNSYLIEG----GGGAVLIDTggsAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPvivvaeeare 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  130 -------------KSVISKASGSKADLFLEPGDKVSIGDIYLEVRATPGHTAGCVTYVTGEGadqpqpRMAFTGDAVLIR 196
Cdd:pfam00753  81 lldeelglaasrlGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGG------KVLFTGDLLFAG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 145362330  197 GCGRTDFQEGSSDQLYESVHSQ------IFTLPKDTLIYPAH 232
Cdd:pfam00753 155 EIGRLDLPLGGLLVLHPSSAESslesllKLAKLKAAVIVPGH 196
 
Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 51-292 0e+00

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 518.58  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  51 KLLFRQLFENESSTFTYLLADVSHPDKPALLIDPVDKTVDRDLKLIDELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVK 130
Cdd:PLN02962  10 KLLFRQLFEKESSTYTYLLADVSHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVK 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 131 SVISKASGSKADLFLEPGDKVSIGDIYLEVRATPGHTAGCVTYVTGEGADQPQPRMAFTGDAVLIRGCGRTDFQEGSSDQ 210
Cdd:PLN02962  90 SIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPDQPQPRMAFTGDALLIRGCGRTDFQGGSSDQ 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 211 LYESVHSQIFTLPKDTLIYPAHDYKGFEVITVGEEMQHNPRLTKDKETFKTIMSNLNLSYPKMIDVAVPANMVCGLQDVP 290
Cdd:PLN02962 170 LYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPANMVCGLQDPP 249


                 ..
gi 145362330 291 SQ 292
Cdd:PLN02962 250 AK 251
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 53-234 7.61e-76

ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; MBL-fold metallo-hydrolase domain; Persulfide dioxygenase (PDO, also known as sulfur dioxygenase, SDO, EC 1.13.11.18) is a non-heme iron-dependent oxygenase which catalyzes the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria. Mutations in ethe1 (the human PDO gene) are responsible for a rare autosomal recessive metabolic disorder called ethylmalonic encephalopathy. Arabidopsis thaliana ETHE1 is essential for embryo and endosperm development. Bacterial ETHE1-type PDOs are also called Type 1 PDOs. Type II PDOs (also called PDOAs), are mainly proteobacterial. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293810 [Multi-domain]  Cd Length: 177  Bit Score: 229.21  E-value: 7.61e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  53 LFRQLFENESSTFTYLLADVShpDKPALLIDPVDKTVDRDLKLIDELGLKLIYAMNTHVHADHVTGTGLLKtKLPGVKSV 132
Cdd:cd07724    1 IFRQFFDPGLGTLSYLVGDPE--TGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELA-ERTGAPIV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 133 ISK-ASGSKADLFLEPGDKVSIGDIYLEVRATPGHTAGCVTYVTGEgadqpqPRMAFTGDAVLIRGCGRTDFQ---EGSS 208
Cdd:cd07724   78 IGEgAPASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGD------PDAVFTGDTLFVGDVGRPDLPgeaEGLA 151

                        170       180
                 ....*....|....*....|....*.
gi 145362330 209 DQLYESVHSQIFTLPKDTLIYPAHDY 234
Cdd:cd07724  152 RQLYDSLQRKLLLLPDETLVYPGHDY 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 63-232 5.27e-40

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 137.80  E-value: 5.27e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  63 STFTYLLADvshPDKPALLIDPVDKTVDRDLKLIDELGLKLIYAMNTHVHADHVTGTGLLKtKLPGVKSVISKA------ 136
Cdd:cd06262    9 QTNCYLVSD---EEGEAILIDPGAGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELK-EAPGAPVYIHEAdaelle 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 137 --------------SGSKADLFLEPGDKVSIGDIYLEVRATPGHTAGCVTYVTGEGadqpqpRMAFTGDAVLIRGCGRTD 202
Cdd:cd06262   85 dpelnlaffgggplPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEE------GVLFTGDTLFAGSIGRTD 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 145362330 203 FQEGSSDQLYESVHSQIFTLPKDTLIYPAH 232
Cdd:cd06262  159 LPGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 65-232 1.13e-38

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: 133.74  E-value: 1.13e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  65 FTYLLADvsHPDKPALLIDPVD-KTVdrdLKLIDELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVKsVI--SKASGSKA 141
Cdd:cd07723   10 YIYLIVD--EATGEAAVVDPGEaEPV---LAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAP-VYgpAEDRIPGL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 142 DLFLEPGDKVSIGDIYLEVRATPGHTAGCVTYVTgegadqPQPRMAFTGDAVLIRGCGRtdFQEGSSDQLYESvHSQIFT 221
Cdd:cd07723   84 DHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV------PDEPALFTGDTLFSGGCGR--FFEGTAEQMYAS-LQKLLA 154

                        170
                 ....*....|.
gi 145362330 222 LPKDTLIYPAH 232
Cdd:cd07723  155 LPDDTLVYCGH 165
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 53-234 4.20e-36

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: 128.65  E-value: 4.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  53 LFRQLFENESSTFTYLLADvshpDKPALLIDPV--DKTVDRDLKLIDELGLKLIYAMNTHVHADHVTGTGLLKTKLpGVK 130
Cdd:COG0491    4 LPGGTPGAGLGVNSYLIVG----GDGAVLIDTGlgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 131 SVISKA----------------SGSKADLFLEPGDKVSIGDIYLEVRATPGHTAGCVTYVTgegadqPQPRMAFTGDAVL 194
Cdd:COG0491   79 VYAHAAeaealeapaagalfgrEPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV------PDEKVLFTGDALF 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 145362330 195 IRGCGRTDFQEGSSDQLYESVHsQIFTLPkDTLIYPAHDY 234
Cdd:COG0491  153 SGGVGRPDLPDGDLAQWLASLE-RLLALP-PDLVIPGHGP 190
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 65-232 6.69e-29

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: 108.39  E-value: 6.69e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  65 FTYLLADVShpDKPALLIDPV-DktVDRDLKLIDELGLKLIYAMNTHVHADHVTGTGLLkTKLPGVKSVISKAsgsKADL 143
Cdd:cd16275   13 YSYIIIDKA--TREAAVVDPAwD--IEKILAKLNELGLTLTGILLTHSHFDHVNLVEPL-LAKYDAPVYMSKE---EIDY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 144 F---------LEPGDKVSIGDIYLEVRATPGHTAGCVTYVTGEgadqpqpRMaFTGDAVLIRGCGRTDFQEGSSDQLYES 214
Cdd:cd16275   85 YgfrcpnlipLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGD-------SL-FTGDTLFIEGCGRCDLPGGDPEEMYES 156

                        170
                 ....*....|....*...
gi 145362330 215 VHSQIFTLPKDTLIYPAH 232
Cdd:cd16275  157 LQRLKKLPPPNTRVYPGH 174
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 66-252 1.81e-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: 1.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  66 TYLLADVShpDKPALLIDPVDKTVDRdLKLIDELGLKLIYAMNTHVHADHVTGTGLLKtKLPGVKSVI---------SKA 136
Cdd:cd16322   13 TYLVADEG--GGEAVLVDPGDESEKL-LARFGTTGLTLLYILLTHAHFDHVGGVADLR-RHPGAPVYLhpddlplyeAAD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 137 SGSKA-----------DLFLEPGDKVSIGDIYLEVRATPGHTAGCVTYVTGEGAdqpqprMAFTGDAVLIRGCGRTDFQE 205
Cdd:cd16322   89 LGAKAfglgieplpppDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEG------LLFSGDLLFQGSIGRTDLPG 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 145362330 206 GSSDQLYESvHSQIFTLPKDTLIYPAHDykgfEVITVGEEMQHNPRL 252
Cdd:cd16322  163 GDPKAMAAS-LRRLLTLPDETRVFPGHG----PPTTLGEERRTNPFL 204
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 65-234 9.93e-26

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 102.53  E-value: 9.93e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  65 FTYLLADVShpDKPALLIDPVDktVDRDLKLIDELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVK---SVISKASGSKA 141
Cdd:PLN02469  13 YAYLIIDES--TKDAAVVDPVD--PEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKvygGSLDNVKGCTH 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 142 DLflEPGDKVSIG-DIYLEVRATPGHTAGCVTY-VTGEGADQPQprmAFTGDAVLIRGCGRtdFQEGSSDQLYESVHSQI 219
Cdd:PLN02469  89 PV--ENGDKLSLGkDVNILALHTPCHTKGHISYyVTGKEGEDPA---VFTGDTLFIAGCGK--FFEGTAEQMYQSLCVTL 161

                        170
                 ....*....|....*
gi 145362330 220 FTLPKDTLIYPAHDY 234
Cdd:PLN02469 162 GSLPKPTQVYCGHEY 176
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 77-232 1.63e-25

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: 99.93  E-value: 1.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  77 KPALLIDPVDKtVDRDLKLIDELGLKLIYAMNTHVHADHVTGTGLLKTKLpGVKSV---------------------ISK 135
Cdd:cd07737   22 KEAAVIDPGGD-ADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHY-GVPIIgphkedkfllenlpeqsqmfgFPP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 136 ASGSKADLFLEPGDKVSIGDIYLEVRATPGHTAGCVTYVtgegadQPQPRMAFTGDaVLIRGC-GRTDFQEGSSDQLYES 214
Cdd:cd07737  100 AEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFF------NRESKLAIVGD-VLFKGSiGRTDFPGGNHAQLIAS 172

                        170
                 ....*....|....*...
gi 145362330 215 VHSQIFTLPKDTLIYPAH 232
Cdd:cd07737  173 IKEKLLPLGDDVTFIPGH 190
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 66-232 3.88e-24

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: 96.08  E-value: 3.88e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330    66 TYLLADvshpDKPALLIDPVDKTVDRDLKLIDELGL-KLIYAMNTHVHADHVTGTGLLKtKLPGVKSVISKAS------- 137
Cdd:smart00849   2 SYLVRD----DGGAILIDTGPGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELL-EAPGAPVYAPEGTaellkdl 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330   138 ------------GSKADLFLEPGDKVSIGDIYLEVRATPGHTAGCVTYVTGEGadqpqpRMAFTGDAVLIRGCGRTDFqE 205
Cdd:smart00849  77 lallgelgaeaePAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEG------KILFTGDLLFAGGDGRTLV-D 149

                          170       180
                   ....*....|....*....|....*...
gi 145362330   206 GSSDQLYESVHSQI-FTLPKDTLIYPAH 232
Cdd:smart00849 150 GGDAAASDALESLLkLLKLLPKLVVPGH 177
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 65-234 5.63e-15

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 74.11  E-value: 5.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  65 FTYLLADVshpDKPAL-LIDPVDKTvdrdlKLIDELGLK---LIYAMNTHVHADHVTGTGLLKTKLpGVKSVISKASGSK 140
Cdd:PLN02398  88 YAYLLHDE---DTGTVgVVDPSEAV-----PVIDALSRKnrnLTYILNTHHHYDHTGGNLELKARY-GAKVIGSAVDKDR 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 141 ---ADLFLEPGDKVSIGDIYLEVRATPGHTAGCVT-YVTGEGAdqpqprmAFTGDAVLIRGCGRtdFQEGSSDQLYESVh 216
Cdd:PLN02398 159 ipgIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISfYFPGSGA-------IFTGDTLFSLSCGK--LFEGTPEQMLSSL- 228

                        170
                 ....*....|....*...
gi 145362330 217 SQIFTLPKDTLIYPAHDY 234
Cdd:PLN02398 229 QKIISLPDDTNIYCGHEY 246
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 76-193 8.73e-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) 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: 71.41  E-value: 8.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  76 DKPALLIDP-VDKTVDRDL-KLIDELGLKLIYAMNTHVHADHVTGTGLLKtKLPGVKSVISK------------------ 135
Cdd:cd07743   17 DKEALLIDSgLDEDAGRKIrKILEELGWKLKAIINTHSHADHIGGNAYLQ-KKTGCKVYAPKiekafienpllepsylgg 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145362330 136 -------------ASGSKADLFLEPGdKVSIGDIYLEVRATPGHTAGCVTYVTGEGadqpqprMAFTGDAV 193
Cdd:cd07743   96 ayppkelrnkflmAKPSKVDDIIEEG-ELELGGVGLEIIPLPGHSFGQIGILTPDG-------VLFAGDAL 158
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
63-232 3.10e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 69.70  E-value: 3.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330   63 STFTYLLADvshpDKPALLIDP---VDKTVDRDLKLIDELGLKLIYAMNTHVHADHVTGTGLLKTKLPGV---------- 129
Cdd:pfam00753   5 QVNSYLIEG----GGGAVLIDTggsAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPvivvaeeare 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  130 -------------KSVISKASGSKADLFLEPGDKVSIGDIYLEVRATPGHTAGCVTYVTGEGadqpqpRMAFTGDAVLIR 196
Cdd:pfam00753  81 lldeelglaasrlGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGG------KVLFTGDLLFAG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 145362330  197 GCGRTDFQEGSSDQLYESVHSQ------IFTLPKDTLIYPAH 232
Cdd:pfam00753 155 EIGRLDLPLGGLLVLHPSSAESslesllKLAKLKAAVIVPGH 196
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 80-234 3.84e-14

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 70.62  E-value: 3.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  80 LLIDPVDktVDRDLKLIDELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVKSVISKASGSK-ADLFLEPGDKVSIGDIYL 158
Cdd:PRK10241  25 LIVDPGE--AEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQETQDKgTTQVVKDGETAFVLGHEF 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145362330 159 EVRATPGHTAGCVTYVTgegadqpQPRMaFTGDAVLIRGCGRtdFQEGSSDQLYESVHsQIFTLPKDTLIYPAHDY 234
Cdd:PRK10241 103 SVFATPGHTLGHICYFS-------KPYL-FCGDTLFSGGCGR--LFEGTASQMYQSLK-KINALPDDTLICCAHEY 167
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 96-175 2.21e-11

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: 62.72  E-value: 2.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  96 IDELGLK---LIYAMNTHVHADHVTGTGLLKtKLPGVKSVISKA----------------------SGSKADLFLEPGDK 150
Cdd:cd16288   51 IRKLGFKpsdIKILLNSHAHLDHAGGLAALK-KLTGAKLMASAEdaallasggksdfhygddslafPPVKVDRVLKDGDR 129

                         90       100
                 ....*....|....*....|....*
gi 145362330 151 VSIGDIYLEVRATPGHTAGCVTYVT 175
Cdd:cd16288  130 VTLGGTTLTAHLTPGHTRGCTTWTM 154
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 96-188 2.25e-10

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: 59.81  E-value: 2.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  96 IDELGLK---LIYAMNTHVHADHVTGTGLLKtKLPGVKSVISKA-----------SGSKADLFLEP---------GDKVS 152
Cdd:cd16309   51 IKKLGFDvkdVKYLLNTHAHFDHAGGLAELK-KATGAQLVASAAdkpllesgyvgSGDTKNLQFPPvrvdrvigdGDKVT 129

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 145362330 153 IGDIYLEVRATPGHTAGCVTYVTGEGADQPQPRMAF 188
Cdd:cd16309  130 LGGTTLTAHLTPGHSPGCTSWTTTVKDTAGPPREVL 165
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 67-245 2.68e-10

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: 58.46  E-value: 2.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  67 YLLADvshpDKPALLIDP-VDKTVDRDL--KLIDELGLKLI---YAMNTHVHADHVTGTGLLKTKLPGVKSVISkasgsk 140
Cdd:cd07725   18 YLLRD----GDETTLIDTgLATEEDAEAlwEGLKELGLKPSdidRVLLTHHHPDHIGLAGKLQEKSGATVYILD------ 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 141 aDLFLEPGDKVSIGDIYLEVRATPGHTAGCVTYVTGEGadqpqpRMAFTGDAVLIR----GCGRTDFQEGSSDQLYESVh 216
Cdd:cd07725   88 -VTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDR------RELFVGDAVLPKitpnVSLWAVRVEDPLGAYLESL- 159

                        170       180
                 ....*....|....*....|....*....
gi 145362330 217 SQIFTLpKDTLIYPAHdykgFEVITVGEE 245
Cdd:cd07725  160 DKLEKL-DVDLAYPGH----GGPIKDPKA 183
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 109-174 1.84e-09

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 56.82  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 109 THVHADHVTGTGLLKtKLPGVKSVISKA------------SGSKA------DLFLEPGDKVSIGDIYLEVRATPGHTAGC 170
Cdd:cd16280   68 THGHGDHYGGAAYLK-DLYGAKVVMSEAdwdmmeeppeegDNPRWgppperDIVIKDGDTLTLGDTTITVYLTPGHTPGT 146


                 ....
gi 145362330 171 VTYV 174
Cdd:cd16280  147 LSLI 150
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 91-185 5.17e-09

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


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 55.63  E-value: 5.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  91 RDLKLIdelglkliyaMNTHVHADHVTGTGLLKtKLPGVKSVISKAS-----------------------GSKADLFLEP 147
Cdd:cd07708   59 SDTKLI----------LISHAHFDHAGGSAEIK-KQTGAKVMAGAEDvslllsggssdfhyandsstyfpQSTVDRAVHD 127

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 145362330 148 GDKVSIGDIYLEVRATPGHTAGCVTYvTGEGADQPQPR 185
Cdd:cd07708  128 GERVTLGGTVLTAHATPGHTPGCTTW-TMTLKDHGKQY 164
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 66-175 9.13e-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: 55.15  E-value: 9.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  66 TYLLADvshpDKPALLIDpvdKTVDRDLKLIDE----LGLKLI---YAMNTHVHADHVTGTGLLKtKLPGVKSVISK--- 135
Cdd:cd16310   24 SYLITS----NHGAILLD---GGLEENAALIEQnikaLGFKLSdikIIINTHAHYDHAGGLAQLK-ADTGAKLWASRgdr 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 145362330 136 ---ASGS---------------KADLFLEPGDKVSIGDIYLEVRATPGHTAGCVTYVT 175
Cdd:cd16310   96 palEAGKhigdnitqpapfpavKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTWST 153
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 79-193 1.36e-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: 1.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  79 ALLIDPVDKTVDRDlKLIDELGLKLIYAMNTHVHADHVTG-------------TGLLKTKLPGVKSVISKASGSK----A 141
Cdd:cd07712   20 ALLIDTGLGIGDLK-EYVRTLTDLPLLVVATHGHFDHIGGlhefeevyvhpadAEILAAPDNFETLTWDAATYSVppagP 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 145362330 142 DLFLEPGDKVSIGDIYLEVRATPGHTAGCVTYVtgegadQPQPRMAFTGDAV 193
Cdd:cd07712   99 TLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALL------DRANRLLFSGDVV 144
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 66-199 1.68e-08

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: 53.65  E-value: 1.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  66 TYLLADvshPDKPALlIDP-VDKTVDRDLKLIDELGL---KLIYAMNTHVHADHVTGTGLLKTKLPGVKSVI-------- 133
Cdd:cd07726   18 SYLLDG---EGRPAL-IDTgPSSSVPRLLAALEALGIapeDVDYIILTHIHLDHAGGAGLLAEALPNAKVYVhprgarhl 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 134 ----------SKASGSKAD--------------LFLEPGDKVSIGDIYLEVRATPGHTAGCVTYVTgegadqPQPRMAFT 189
Cdd:cd07726   94 idpsklwasaRAVYGDEADrlggeilpvpeervIVLEDGETLDLGGRTLEVIDTPGHAPHHLSFLD------EESDGLFT 167

                        170
                 ....*....|
gi 145362330 190 GDAVLIRGCG 199
Cdd:cd07726  168 GDAAGVRYPE 177
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 64-197 9.39e-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: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 50.95  E-value: 9.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  64 TFTYLLADvshpDKPALLIDP-----------VDKTVDRDLKLIdelglkLIyamnTHVHADHVTGTGLLK--TKLP--- 127
Cdd:cd16278   18 TNTYLLGA----PDGVVVIDPgpddpahldalLAALGGGRVSAI------LV----THTHRDHSPGAARLAerTGAPvra 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145362330 128 -GVKSVISKASGSKADLFLEPGDKVSIGDIYLEVRATPGHTAGCVTYVTGEGadqpqpRMAFTGDAVLIRG 197
Cdd:cd16278   84 fGPHRAGGQDTDFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDE------GALFTGDHVMGWS 148
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 109-232 2.64e-06

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: 46.76  E-value: 2.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 109 THVHADHVTG-TGLLK---------TKLPGVKSVISKASGSKADLFLEPGDKVSIGDIYLEVRATPGHTAG-CVTYVTGE 177
Cdd:cd07722   63 THWHHDHVGGlPDVLDllrgpsprvYKFPRPEEDEDPDEDGGDIHDLQDGQVFKVEGATLRVIHTPGHTTDhVCFLLEEE 142

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145362330 178 GAdqpqprmAFTGDAVLirGCGRTDFqegssDQLYESVHS--QIFTLPKDTlIYPAH 232
Cdd:cd07722  143 NA-------LFTGDCVL--GHGTAVF-----EDLAAYMASlkKLLSLGPGR-IYPGH 184
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 96-173 1.13e-05

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


Pssm-ID: 293865  Cd Length: 255  Bit Score: 45.90  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  96 IDELGLKLI---YAMNTHVHADHVTGTGLLKTKLPGVKSVISK-----ASGSKADLF-----------------LEPGDK 150
Cdd:cd16307   51 IEKLGFKFSdtkILLISHAHFDHAAGSALIKRETHAKYMVMDGdvdvvESGGKSDFFygndpstyfppahvdkvLHDGEQ 130

                         90       100
                 ....*....|....*....|...
gi 145362330 151 VSIGDIYLEVRATPGHTAGCVTY 173
Cdd:cd16307  131 VELGGTVLTAHLTAGHTKGCTTW 153
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 81-169 6.80e-05

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: 43.49  E-value: 6.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  81 LIDP-VDKTVDRDLKLIDELGLKLI---YAMNTHVHADHVTGTGLLKtKLPGVKSVISKAS------------------- 137
Cdd:cd16315   35 LIDSgTEEAAPLVLANIRKLGFDPKdvrWLLSSHEHFDHVGGLAALQ-RATGARVAASAAAapvlesgkpapddpqaglh 113

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 145362330 138 ----GSKADLFLEPGDKVSIGDIYLEVRATPGHTAG 169
Cdd:cd16315  114 epfpPVRVDRIVEDGDTVALGSLRLTAHATPGHTPG 149
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 94-174 8.72e-05

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


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 43.23  E-value: 8.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  94 KLIDELGLK---LIYAMNTHVHADHVTGTGLLKtKLPGVKSVISKASGS----------------------KADLFLEPG 148
Cdd:cd16308   49 KNIQALGFKfkdIKILLTTQAHYDHVGAMAAIK-QQTGAKMMVDEKDAKvladggksdyemggygstfapvKADKLLHDG 127

                         90       100
                 ....*....|....*....|....*.
gi 145362330 149 DKVSIGDIYLEVRATPGHTAGCVTYV 174
Cdd:cd16308  128 DTIKLGGTKLTLLHHPGHTKGSCSFL 153
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 67-197 9.33e-05

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: 42.59  E-value: 9.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  67 YLLADvshpDKPALLID---PvdKTVDRDLKLIDELGLK-------LIyamnTHVHADHVtgtGLLKT--KLPGVKSVIS 134
Cdd:cd07721   14 YLIED----DDGLTLIDtglP--GSAKRILKALRELGLSpkdirriLL----THGHIDHI---GSLAAlkEAPGAPVYAH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 135 KA-----SGSKA------------------------DLFLEPGDKVSI-GDiyLEVRATPGHTAGCVTYVtgegadQPQP 184
Cdd:cd07721   81 EReapylEGEKPypppvrlgllgllspllpvkpvpvDRTLEDGDTLDLaGG--LRVIHTPGHTPGHISLY------LEED 152

                        170
                 ....*....|...
gi 145362330 185 RMAFTGDAVLIRG 197
Cdd:cd07721  153 GVLIAGDALVTVG 165
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 81-192 2.33e-04

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 41.03  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  81 LIDPVDKtVDRD--LKLIDELGLKL--I-YAMNTHVHADHVTGTGLLktklPGVKSVISKA-SGSKADLF-LEPGDKVSI 153
Cdd:cd07711   35 LVDTGTP-WDRDllLKALAEHGLSPedIdYVVLTHGHPDHIGNLNLF----PNATVIVGWDiCGDSYDDHsLEEGDGYEI 109

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 145362330 154 GDiYLEVRATPGHTAGCVTYVTGEGADQpqpRMAFTGDA 192
Cdd:cd07711  110 DE-NVEVIPTPGHTPEDVSVLVETEKKG---TVAVAGDL 144
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
109-217 2.42e-04

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 41.72  E-value: 2.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 109 THVHADHVTG-TGLLKT--------KL-----PGVKSVIS---KASGSKADLFL-----EPGDKVSIGDIYLEVRATPgH 166
Cdd:COG1234   59 THLHGDHIAGlPGLLSTrslagrekPLtiygpPGTKEFLEallKASGTDLDFPLefheiEPGEVFEIGGFTVTAFPLD-H 137

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145362330 167 TAGCVTY-VTGEGAdqpqpRMAFTGD-------AVLIRGCgrtD-------FQEGSSDQLYESVHS 217
Cdd:COG1234  138 PVPAYGYrFEEPGR-----SLVYSGDtrpcealVELAKGA---DlliheatFLDEEAELAKETGHS 195
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 55-192 4.09e-03

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 37.85  E-value: 4.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  55 RQLFENESST---FT---YLLADvshpDKPALlIDPVDKTVDRDL--KLIDELGL-KLIYAMNTHVHADHVTGTGLLKTK 125
Cdd:cd07709   17 LRLFEGEYPTprgTSynsYLIKD----EKTAL-IDTVKEPFFDEFleNLEEVIDPrKIDYIVVNHQEPDHSGSLPELLEL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330 126 LPGVKSVISKasgsKADLFLE--------------PGDKVSIGDIYLEVRATPG-HTAGC-VTYVTGEGadqpqprMAFT 189
Cdd:cd07709   92 APNAKIVCSK----KAARFLKhfypgiderfvvvkDGDTLDLGKHTLKFIPAPMlHWPDTmVTYDPEDK-------ILFS 160


                 ...
gi 145362330 190 GDA 192
Cdd:cd07709  161 GDA 163
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 72-192 7.01e-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: 36.73  E-value: 7.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145362330  72 VSHPDKpALLID--PVDKTVDRD-LKLIDELG-LKLIYAMNTHVHADHVTGTGLLKTKLPgVKSVIS------------- 134
Cdd:cd07731   15 IQTPGK-TILIDtgPRDSFGEDVvVPYLKARGiKKLDYLILTHPDADHIGGLDAVLKNFP-VKEVYMpgvthttktyedl 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145362330 135 ----KASGSKAdLFLEPGDKVSIGDIYLEVRATPGHTAG------CVTYVTGEGAdqpqpRMAFTGDA 192
Cdd:cd07731   93 ldaiKEKGIPV-TPCKAGDRWQLGGVSFEVLSPPKDDYDdlnnnsCVLRLTYGGT-----SFLLTGDA 154
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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