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Conserved domains on  [gi|189067485|dbj|BAG37744|]
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unnamed protein product [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02962 super family cl30130
hydroxyacylglutathione hydrolase
 1-227 1.01e-122

hydroxyacylglutathione hydrolase


The actual alignment was detected with superfamily member PLN02962:

Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 348.33  E-value: 1.01e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   1 MFEPVSCTFTYLLGD--RESREAVLIDPVLETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRSLLPGCQSVISRL 78
Cdd:PLN02962  16 LFEKESSTYTYLLADvsHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVKSIISKA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  79 SGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHS------MAFTGDALLIRGCGRTDFQQGCAKTLYHSVH 152
Cdd:PLN02962  96 SGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPdqpqprMAFTGDALLIRGCGRTDFQGGSSDQLYKSVH 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189067485 153 EKIFTLPGDCLIYPAHDYHGFTVSTVEEERTLNPRLTLSCEEFVKIMGNLNLPKPQQIDFAVPANMRCGVQTPTA 227
Cdd:PLN02962 176 SQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPANMVCGLQDPPA 250
 
Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 1-227 1.01e-122

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 348.33  E-value: 1.01e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   1 MFEPVSCTFTYLLGD--RESREAVLIDPVLETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRSLLPGCQSVISRL 78
Cdd:PLN02962  16 LFEKESSTYTYLLADvsHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVKSIISKA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  79 SGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHS------MAFTGDALLIRGCGRTDFQQGCAKTLYHSVH 152
Cdd:PLN02962  96 SGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPdqpqprMAFTGDALLIRGCGRTDFQGGSSDQLYKSVH 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189067485 153 EKIFTLPGDCLIYPAHDYHGFTVSTVEEERTLNPRLTLSCEEFVKIMGNLNLPKPQQIDFAVPANMRCGVQTPTA 227
Cdd:PLN02962 176 SQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPANMVCGLQDPPA 250
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 2-170 1.59e-80

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: 238.45  E-value: 1.59e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   2 FEPVSCTFTYLLGDRESREAVLIDPVLETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRSLLpGCQSVISRLSGA 81
Cdd:cd07724    6 FDPGLGTLSYLVGDPETGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERT-GAPIVIGEGAPA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  82 -QADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQ---GCAKTLYHSVHEKIFT 157
Cdd:cd07724   85 sFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPGeaeGLARQLYDSLQRKLLL 164

                        170
                 ....*....|...
gi 189067485 158 LPGDCLIYPAHDY 170
Cdd:cd07724  165 LPDETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 8-170 1.13e-37

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 130.58  E-value: 1.13e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   8 TFTYLLGDreSREAVLIDPVLETAPRDA--QLIKELGLRLLYAVNTHCHADHITGSGLLRSLLpGCQSVISR-------- 77
Cdd:COG0491   15 VNSYLIVG--GDGAVLIDTGLGPADAEAllAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAPVYAHAaeaealea 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  78 --------LSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQGCAKTLYH 149
Cdd:COG0491   92 paagalfgREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLPDGDLAQWLA 171

                        170       180
                 ....*....|....*....|.
gi 189067485 150 SVhEKIFTLPGDcLIYPAHDY 170
Cdd:COG0491  172 SL-ERLLALPPD-LVIPGHGP 190
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 10-168 4.15e-25

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 96.85  E-value: 4.15e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485    10 TYLLGDREsrEAVLIDPVLETAPRDAQLIKELGLR-LLYAVNTHCHADHITGSG------------------LLRSLLPG 70
Cdd:smart00849   2 SYLVRDDG--GAILIDTGPGEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPelleapgapvyapegtaeLLKDLLAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485    71 CQSVISRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQG-CAKTLYH 149
Cdd:smart00849  80 LGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGdAAASDAL 159

                          170
                   ....*....|....*....
gi 189067485   150 SVHEKIFTLPGDcLIYPAH 168
Cdd:smart00849 160 ESLLKLLKLLPK-LVVPGH 177
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 11-170 4.35e-24

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: 96.07  E-value: 4.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   11 YLLGDrESREAVLID-----PVLETaprdaqlIKELGLRLLYAVNTHCHADHITG-SGLLRSLlpGCQsVI----SRLSG 80
Cdd:TIGR03413  13 WLLHD-PDGQAAVVDpgeaePVLDA-------LEARGLTLTAILLTHHHHDHVGGvAELLEAF--PAP-VYgpaeERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   81 AqaDLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTdFqQGCAKTLYHSVhEKIFTLPG 160
Cdd:TIGR03413  82 I--THPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRL-F-EGTPEQMYDSL-QRLAALPD 156

                         170
                  ....*....|
gi 189067485  161 DCLIYPAHDY 170
Cdd:TIGR03413 157 DTLVYCAHEY 166
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
8-168 8.88e-19

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 80.88  E-value: 8.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485    8 TFTYLLGDREsrEAVLIDPVLETAPRDAQLIKELGLRLL---YAVNTHCHADHITGSGLLRSLLPGCQSVISRLSGAQAD 84
Cdd:pfam00753   6 VNSYLIEGGG--GAVLIDTGGSAEAALLLLLAALGLGPKdidAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   85 LH-----------------------IEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQ 141
Cdd:pfam00753  84 EElglaasrlglpgppvvplppdvvLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPL 163

                         170       180       190
                  ....*....|....*....|....*....|....
gi 189067485  142 GCAKTLYHSVHE-------KIFTLPGDcLIYPAH 168
Cdd:pfam00753 164 GGLLVLHPSSAEsslesllKLAKLKAA-VIVPGH 196
B3_Acin_new1 NF033184
putative subclass B3 metallo-beta-lactamase; This is one of two families of putative ...
 10-115 1.11e-07

putative subclass B3 metallo-beta-lactamase; This is one of two families of putative metallo-beta-lactamases of subclass B3 that are restricted to the genus Acinetobacter, and undescribed as of January 2017.


Pssm-ID: 439394  Cd Length: 283  Bit Score: 51.26  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  10 TYLLGdrESREAVLIDPVL-ETAPRDAQLIKELGLRLL---YAVNTHCHADHI---------TGSGLL------RSLLPG 70
Cdd:NF033184  51 AYLLA--SGHQALLIDTGLpENTEQIEQNIKQLGFKLSdvkIMVTSHAHWDHVgalarikqdTGAKLIamqqdvKALEIG 128

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 189067485  71 -------CQSVisRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTF 115
Cdd:NF033184 129 kpigentFQTI--PFTPVKVDKVIHDGEVVKLGKFKLKATLTPGHTPGCTTW 178
 
Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 1-227 1.01e-122

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 348.33  E-value: 1.01e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   1 MFEPVSCTFTYLLGD--RESREAVLIDPVLETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRSLLPGCQSVISRL 78
Cdd:PLN02962  16 LFEKESSTYTYLLADvsHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVKSIISKA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  79 SGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHS------MAFTGDALLIRGCGRTDFQQGCAKTLYHSVH 152
Cdd:PLN02962  96 SGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPdqpqprMAFTGDALLIRGCGRTDFQGGSSDQLYKSVH 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 189067485 153 EKIFTLPGDCLIYPAHDYHGFTVSTVEEERTLNPRLTLSCEEFVKIMGNLNLPKPQQIDFAVPANMRCGVQTPTA 227
Cdd:PLN02962 176 SQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPANMVCGLQDPPA 250
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 2-170 1.59e-80

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: 238.45  E-value: 1.59e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   2 FEPVSCTFTYLLGDRESREAVLIDPVLETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRSLLpGCQSVISRLSGA 81
Cdd:cd07724    6 FDPGLGTLSYLVGDPETGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERT-GAPIVIGEGAPA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  82 -QADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQ---GCAKTLYHSVHEKIFT 157
Cdd:cd07724   85 sFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPGeaeGLARQLYDSLQRKLLL 164

                        170
                 ....*....|...
gi 189067485 158 LPGDCLIYPAHDY 170
Cdd:cd07724  165 LPDETLVYPGHDY 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 10-168 2.71e-42

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: 141.65  E-value: 2.71e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  10 TYLLGDrESREAVLIDPVLETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRSLlPGCQSVISR------------ 77
Cdd:cd06262   12 CYLVSD-EEGEAILIDPGAGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEA-PGAPVYIHEadaelledpeln 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  78 --------LSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQGCAKTLYH 149
Cdd:cd06262   90 laffgggpLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDLPGGDPEQLIE 169

                        170
                 ....*....|....*....
gi 189067485 150 SVHEKIFTLPGDCLIYPAH 168
Cdd:cd06262  170 SIKKLLLLLPDDTVVYPGH 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 8-170 1.13e-37

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 130.58  E-value: 1.13e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   8 TFTYLLGDreSREAVLIDPVLETAPRDA--QLIKELGLRLLYAVNTHCHADHITGSGLLRSLLpGCQSVISR-------- 77
Cdd:COG0491   15 VNSYLIVG--GDGAVLIDTGLGPADAEAllAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAPVYAHAaeaealea 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  78 --------LSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQGCAKTLYH 149
Cdd:COG0491   92 paagalfgREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLPDGDLAQWLA 171

                        170       180
                 ....*....|....*....|.
gi 189067485 150 SVhEKIFTLPGDcLIYPAHDY 170
Cdd:COG0491  172 SL-ERLLALPPD-LVIPGHGP 190
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 9-168 6.66e-37

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: 126.81  E-value: 6.66e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   9 FTYLLGDRESREAVLIDPVletaprDAQLI----KELGLRLLYAVNTHCHADHITGSGLLRSLLPGCQsVI----SRLSG 80
Cdd:cd07723   10 YIYLIVDEATGEAAVVDPG------EAEPVlaalEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAP-VYgpaeDRIPG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  81 AqaDLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRtdFQQGCAKTLYHSvHEKIFTLPG 160
Cdd:cd07723   83 L--DHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGR--FFEGTAEQMYAS-LQKLLALPD 157


                 ....*...
gi 189067485 161 DCLIYPAH 168
Cdd:cd07723  158 DTLVYCGH 165
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 9-168 4.50e-36

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: 124.96  E-value: 4.50e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   9 FTYLLGDRESREAVLIDPV--LETAprdAQLIKELGLRLLYAVNTHCHADHITGSGLLRSLlPGCQSVISR----LSGAQ 82
Cdd:cd16275   13 YSYIIIDKATREAAVVDPAwdIEKI---LAKLNELGLTLTGILLTHSHFDHVNLVEPLLAK-YDAPVYMSKeeidYYGFR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  83 A-DLH-IEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHsmAFTGDALLIRGCGRTDFQQGCAKTLYHSVHEKIFTLPG 160
Cdd:cd16275   89 CpNLIpLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGDS--LFTGDTLFIEGCGRCDLPGGDPEEMYESLQRLKKLPPP 166


                 ....*...
gi 189067485 161 DCLIYPAH 168
Cdd:cd16275  167 NTRVYPGH 174
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 10-188 3.99e-31

uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 113.21  E-value: 3.99e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  10 TYLLGDRESREAVLIDPVLEtAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRsLLPGCQSVISRL---------SG 80
Cdd:cd16322   13 TYLVADEGGGEAVLVDPGDE-SEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLR-RHPGAPVYLHPDdlplyeaadLG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  81 AQA-----------DLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFqQGCAKTLYH 149
Cdd:cd16322   91 AKAfglgieplpppDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRTDL-PGGDPKAMA 169

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 189067485 150 SVHEKIFTLPGDCLIYPAHDyhgfTVSTVEEERTLNPRL 188
Cdd:cd16322  170 ASLRRLLTLPDETRVFPGHG----PPTTLGEERRTNPFL 204
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 7-168 2.75e-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: 97.62  E-value: 2.75e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   7 CTftyLLGDRESREAVLIDPVLEtAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRSL------------------L 68
Cdd:cd07737   13 CS---LIWCEETKEAAVIDPGGD-ADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHygvpiigphkedkfllenL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  69 PGcQSVISRLSGAQA---DLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQGCAK 145
Cdd:cd07737   89 PE-QSQMFGFPPAEAftpDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTDFPGGNHA 167

                        170       180
                 ....*....|....*....|...
gi 189067485 146 TLYHSVHEKIFTLPGDCLIYPAH 168
Cdd:cd07737  168 QLIASIKEKLLPLGDDVTFIPGH 190
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 10-168 4.15e-25

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 96.85  E-value: 4.15e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485    10 TYLLGDREsrEAVLIDPVLETAPRDAQLIKELGLR-LLYAVNTHCHADHITGSG------------------LLRSLLPG 70
Cdd:smart00849   2 SYLVRDDG--GAILIDTGPGEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPelleapgapvyapegtaeLLKDLLAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485    71 CQSVISRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQG-CAKTLYH 149
Cdd:smart00849  80 LGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGdAAASDAL 159

                          170
                   ....*....|....*....
gi 189067485   150 SVHEKIFTLPGDcLIYPAH 168
Cdd:smart00849 160 ESLLKLLKLLPK-LVVPGH 177
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 11-170 4.35e-24

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: 96.07  E-value: 4.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   11 YLLGDrESREAVLID-----PVLETaprdaqlIKELGLRLLYAVNTHCHADHITG-SGLLRSLlpGCQsVI----SRLSG 80
Cdd:TIGR03413  13 WLLHD-PDGQAAVVDpgeaePVLDA-------LEARGLTLTAILLTHHHHDHVGGvAELLEAF--PAP-VYgpaeERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   81 AqaDLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTdFqQGCAKTLYHSVhEKIFTLPG 160
Cdd:TIGR03413  82 I--THPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRL-F-EGTPEQMYDSL-QRLAALPD 156

                         170
                  ....*....|
gi 189067485  161 DCLIYPAHDY 170
Cdd:TIGR03413 157 DTLVYCAHEY 166
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 4-186 3.61e-20

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 85.97  E-value: 3.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   4 PVSC---TFTYLLGDRESREAVLIDPVLETAPRDAQliKELGLRLLYAVNTHCHADHITGSGLLRSLLPGCQSVISRLSG 80
Cdd:PLN02469   5 PVPCledNYAYLIIDESTKDAAVVDPVDPEKVLQAA--HEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSLDN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  81 AQADLH-IEDGDSIRFGR----FALETrasPGHTPGCVTFVL----NDHSMAFTGDALLIRGCGRtdFQQGCAKTLYHSV 151
Cdd:PLN02469  83 VKGCTHpVENGDKLSLGKdvniLALHT---PCHTKGHISYYVtgkeGEDPAVFTGDTLFIAGCGK--FFEGTAEQMYQSL 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 189067485 152 HEKIFTLPGDCLIYPAHDYhgfTVSTVEEERTLNP 186
Cdd:PLN02469 158 CVTLGSLPKPTQVYCGHEY---TVKNLKFALTVEP 189
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
8-168 8.88e-19

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 80.88  E-value: 8.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485    8 TFTYLLGDREsrEAVLIDPVLETAPRDAQLIKELGLRLL---YAVNTHCHADHITGSGLLRSLLPGCQSVISRLSGAQAD 84
Cdd:pfam00753   6 VNSYLIEGGG--GAVLIDTGGSAEAALLLLLAALGLGPKdidAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   85 LH-----------------------IEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQ 141
Cdd:pfam00753  84 EElglaasrlglpgppvvplppdvvLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPL 163

                         170       180       190
                  ....*....|....*....|....*....|....
gi 189067485  142 GCAKTLYHSVHE-------KIFTLPGDcLIYPAH 168
Cdd:pfam00753 164 GGLLVLHPSSAEsslesllKLAKLKAA-VIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 3-170 1.05e-13

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 68.72  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   3 EPVSC---TFTYLLGDRESREAVLIDPVlETAPRDAQLIKElGLRLLYAVNTHCHADHITGSGLLRSLLpGCQSVIS--- 76
Cdd:PLN02398  79 ELVPClkdNYAYLLHDEDTGTVGVVDPS-EAVPVIDALSRK-NRNLTYILNTHHHYDHTGGNLELKARY-GAKVIGSavd 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  77 --RLSGAqaDLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRtdFQQGCAKTLYHSVhEK 154
Cdd:PLN02398 156 kdRIPGI--DIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGK--LFEGTPEQMLSSL-QK 230

                        170
                 ....*....|....*.
gi 189067485 155 IFTLPGDCLIYPAHDY 170
Cdd:PLN02398 231 IISLPDDTNIYCGHEY 246
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 9-185 2.42e-13

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 67.16  E-value: 2.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   9 FTYLLGDRESReAVLIDPVlETAPRdAQLIKELGLRLLYAVNTHCHADHITGSGLLRSLLPgcQSVISRLSGAQ---ADL 85
Cdd:PRK10241  13 YIWVLNDEAGR-CLIVDPG-EAEPV-LNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFP--QIVVYGPQETQdkgTTQ 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  86 HIEDGDSIRFGRFALETRASPGHTPGCVTFVlnDHSMAFTGDALLIRGCGRtdFQQGCAKTLYHSVhEKIFTLPGDCLIY 165
Cdd:PRK10241  88 VVKDGETAFVLGHEFSVFATPGHTLGHICYF--SKPYLFCGDTLFSGGCGR--LFEGTASQMYQSL-KKINALPDDTLIC 162

                        170       180
                 ....*....|....*....|....
gi 189067485 166 PAHDYH----GFTVSTVEEERTLN 185
Cdd:PRK10241 163 CAHEYTlsnmKFALSILPHDLSIN 186
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 17-129 8.46e-13

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: 64.47  E-value: 8.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  17 ESREAVLIDPVL--ETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRSlLPGCQSVISR---------------LS 79
Cdd:cd07743   16 GDKEALLIDSGLdeDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQK-KTGCKVYAPKiekafienpllepsyLG 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 189067485  80 GA----------------QADLHIEDGDsIRFGRFALETRASPGHTPGCVTfVLNDHSMAFTGDAL 129
Cdd:cd07743   95 GAyppkelrnkflmakpsKVDDIIEEGE-LELGGVGLEIIPLPGHSFGQIG-ILTPDGVLFAGDAL 158
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 11-168 1.89e-12

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


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 63.47  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  11 YLLGDREsrEAVLIDPVLETaPRDAQL----IKELGLRLL---YAVNTHCHADHITGSGLLRSLLpGCQSVISRLSGaqa 83
Cdd:cd07725   18 YLLRDGD--ETTLIDTGLAT-EEDAEAlwegLKELGLKPSdidRVLLTHHHPDHIGLAGKLQEKS-GATVYILDVTP--- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  84 dlhIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIR----GCGRTDFQQGCAKTLYHSVhEKIFTLP 159
Cdd:cd07725   91 ---VKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLPKitpnVSLWAVRVEDPLGAYLESL-DKLEKLD 166


                 ....*....
gi 189067485 160 GDcLIYPAH 168
Cdd:cd07725  167 VD-LAYPGH 174
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-116 2.00e-11

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: 61.45  E-value: 2.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  22 VLIDpVLETAPRDAQL---IKELGL---RLLYAVNTHCHADHITGSGLLRSLlPGCQSVISR----LSGAQA-------- 83
Cdd:cd16280   34 ILID-ALNNNEAADLIvdgLEKLGLdpaDIKYILITHGHGDHYGGAAYLKDL-YGAKVVMSEadwdMMEEPPeegdnprw 111

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 189067485  84 ------DLHIEDGDSIRFGRFALETRASPGHTPGCVTFV 116
Cdd:cd16280  112 gppperDIVIKDGDTLTLGDTTITVYLTPGHTPGTLSLI 150
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 8-133 2.01e-11

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: 60.58  E-value: 2.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   8 TFTYLLGDREsrEAVLIDPvletAPRDAQLIKEL-----GLRLLYAVNTHCHADHITGSGLLRSLL------PGCQSVIS 76
Cdd:cd16278   18 TNTYLLGAPD--GVVVIDP----GPDDPAHLDALlaalgGGRVSAILVTHTHRDHSPGAARLAERTgapvraFGPHRAGG 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 189067485  77 RLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRG 133
Cdd:cd16278   92 QDTDFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVMGWS 148
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 18-119 1.31e-10

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


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 59.48  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  18 SREAVLIDPVLE-TAPRDAQLIKELGLRLL---YAVNTHCHADHITGSGLLR-----SLLPGCQSVISRLSGAQADLH-- 86
Cdd:cd07708   30 PQGNILIDGDMEqNAPMIKANIKKLGFKFSdtkLILISHAHFDHAGGSAEIKkqtgaKVMAGAEDVSLLLSGGSSDFHya 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 189067485  87 ---------------IEDGDSIRFGRFALETRASPGHTPGCVTFVLND 119
Cdd:cd07708  110 ndsstyfpqstvdraVHDGERVTLGGTVLTAHATPGHTPGCTTWTMTL 157
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 11-168 4.19e-10

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


Pssm-ID: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 56.87  E-value: 4.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  11 YLLgdRESREAVLIDPVLETAPRDaQLIKELGLRLLYAVNTHCHADHITG-------------SGLLRSLLPGCQSVIS- 76
Cdd:cd07712   12 YLL--RGRDRALLIDTGLGIGDLK-EYVRTLTDLPLLVVATHGHFDHIGGlhefeevyvhpadAEILAAPDNFETLTWDa 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  77 ---RLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDAL----LIRGCGRTDFqqgcakTLYH 149
Cdd:cd07712   89 atySVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVydgpLIMDLPHSDL------DDYL 162

                        170       180
                 ....*....|....*....|
gi 189067485 150 SVHEKIFTLPGDC-LIYPAH 168
Cdd:cd07712  163 ASLEKLSKLPDEFdKVLPGH 182
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 10-115 1.70e-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: 56.30  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  10 TYLLGdrESREAVLIDPVL-ETAPRDAQLIKELGLRLL---YAVNTHCHADHITGSGLLRSlLPGCQSVISR-------- 77
Cdd:cd16310   24 SYLIT--SNHGAILLDGGLeENAALIEQNIKALGFKLSdikIIINTHAHYDHAGGLAQLKA-DTGAKLWASRgdrpalea 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 189067485  78 -------------LSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTF 115
Cdd:cd16310  101 gkhigdnitqpapFPAVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTW 151
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 8-168 4.56e-09

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


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 54.08  E-value: 4.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485   8 TFTYLLGDRESReaVLID---------PVLETAprdaqLIKELGLRLLYAVNTHCHADHITGSGLLRSLLPGCQSVISRL 78
Cdd:cd07722   18 TNTYLVGTGKRR--ILIDtgegrpsyiPLLKSV-----LDSEGNATISDILLTHWHHDHVGGLPDVLDLLRGPSPRVYKF 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  79 ---------SGAQADLH-IEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLirGCGRTDFQqgCAKTLY 148
Cdd:cd07722   91 prpeededpDEDGGDIHdLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGDCVL--GHGTAVFE--DLAAYM 166

                        170       180
                 ....*....|....*....|
gi 189067485 149 HSVHeKIFTLPGDcLIYPAH 168
Cdd:cd07722  167 ASLK-KLLSLGPG-RIYPGH 184
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 11-133 4.74e-09

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: 54.15  E-value: 4.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  11 YLLGDreSREAVLIDP-VLETAPRDAQLIKELGLR-------LLyavnTHCHADHItGS--------------------- 61
Cdd:cd07721   14 YLIED--DDGLTLIDTgLPGSAKRILKALRELGLSpkdirriLL----THGHIDHI-GSlaalkeapgapvyahereapy 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  62 --GLLRSLLPGCQSVISRLSG------AQADLHIEDGDSIRFGrFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRG 133
Cdd:cd07721   87 leGEKPYPPPVRLGLLGLLSPllpvkpVPVDRTLEDGDTLDLA-GGLRVIHTPGHTPGHISLYLEEDGVLIAGDALVTVG 165
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 22-118 7.61e-09

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


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 54.25  E-value: 7.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  22 VLIDPVLE-TAPRDAQLIKELGLR---LLYAVNTHCHADHITGSGLLRSLlPGCQSVISR------LSGAQADLH----- 86
Cdd:cd16288   34 ILIDTGLEsSAPMIKANIRKLGFKpsdIKILLNSHAHLDHAGGLAALKKL-TGAKLMASAedaallASGGKSDFHygdds 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 189067485  87 -----------IEDGDSIRFGRFALETRASPGHTPGCVTFVLN 118
Cdd:cd16288  113 lafppvkvdrvLKDGDRVTLGGTTLTAHLTPGHTRGCTTWTMT 155
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 ...
 22-114 1.38e-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: 53.51  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  22 VLIDPVLE-TAPRDAQLIKELGLRL---LYAVNTHCHADHITGSGLLRSLlPGCQsVISRLSGAQA-------------- 83
Cdd:cd16290   34 ILIDGALPqSAPQIEANIRALGFRLedvKLILNSHAHFDHAGGIAALQRD-SGAT-VAASPAGAAAlrsggvdpddpqag 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 189067485  84 ----------DLHIEDGDSIRFGRFALETRASPGHTPGCVT 114
Cdd:cd16290  112 aadpfppvakVRVVADGEVVKLGPLAVTAHATPGHTPGGTS 152
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 10-135 4.53e-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: 51.72  E-value: 4.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  10 TYLLgdRESREAVLIDP-VLETAPRDAQLIKELGLRLL---YAVNTHCHADHITGSGLLRSLLPGCQSVI---------- 75
Cdd:cd07726   18 SYLL--DGEGRPALIDTgPSSSVPRLLAALEALGIAPEdvdYIILTHIHLDHAGGAGLLAEALPNAKVYVhprgarhlid 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  76 -SRL-------SGAQADLH--------------IEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRG 133
Cdd:cd07726   96 pSKLwasaravYGDEADRLggeilpvpeervivLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDAAGVRY 175


                 ..
gi 189067485 134 CG 135
Cdd:cd07726  176 PE 177
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 22-117 1.08e-07

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


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 50.95  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  22 VLIDPVL-ETAPRDAQLIKELGLR---LLYAVNTHCHADHITGSGLLRSLlPGCQSVISRL-----------SGAQADLH 86
Cdd:cd16309   34 ILIDGAMpQSTPLIKDNIKKLGFDvkdVKYLLNTHAHFDHAGGLAELKKA-TGAQLVASAAdkpllesgyvgSGDTKNLQ 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 189067485  87 ---------IEDGDSIRFGRFALETRASPGHTPGCVTFVL 117
Cdd:cd16309  113 fppvrvdrvIGDGDKVTLGGTTLTAHLTPGHSPGCTSWTT 152
B3_Acin_new1 NF033184
putative subclass B3 metallo-beta-lactamase; This is one of two families of putative ...
 10-115 1.11e-07

putative subclass B3 metallo-beta-lactamase; This is one of two families of putative metallo-beta-lactamases of subclass B3 that are restricted to the genus Acinetobacter, and undescribed as of January 2017.


Pssm-ID: 439394  Cd Length: 283  Bit Score: 51.26  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  10 TYLLGdrESREAVLIDPVL-ETAPRDAQLIKELGLRLL---YAVNTHCHADHI---------TGSGLL------RSLLPG 70
Cdd:NF033184  51 AYLLA--SGHQALLIDTGLpENTEQIEQNIKQLGFKLSdvkIMVTSHAHWDHVgalarikqdTGAKLIamqqdvKALEIG 128

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 189067485  71 -------CQSVisRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTF 115
Cdd:NF033184 129 kpigentFQTI--PFTPVKVDKVIHDGEVVKLGKFKLKATLTPGHTPGCTTW 178
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 22-166 2.43e-07

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: 50.04  E-value: 2.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  22 VLIDP-VLETAPRDAQLIKELGLRLL---YAVNTHCHADHITGSGLLRSL-------LPGCQSVISR------------- 77
Cdd:cd16315   34 VLIDSgTEEAAPLVLANIRKLGFDPKdvrWLLSSHEHFDHVGGLAALQRAtgarvaaSAAAAPVLESgkpapddpqaglh 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  78 --LSGAQADLHIEDGDSIRFGRFALETRASPGHTPG-------------CVTFVLNDHSMAFTGDALliRGCGRTDFQQG 142
Cdd:cd16315  114 epFPPVRVDRIVEDGDTVALGSLRLTAHATPGHTPGalswtwrscegadCRTIVYADSLSPVSADGY--RFSDHPDYVAA 191

                        170       180
                 ....*....|....*....|....
gi 189067485 143 CAKTLyhsvhEKIFTLPGDCLIYP 166
Cdd:cd16315  192 YRAGL-----AKVAALPCDILLTP 210
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 22-133 3.95e-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: 43.59  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  22 VLIDPVLETA-PRDAQLIKELGLRLL---YAVNTHCHADHITGSGLLRSL-------LPGCQSVIsrLSGAQADLH---- 86
Cdd:cd16307   34 ILINSNLESSvPQIKASIEKLGFKFSdtkILLISHAHFDHAAGSALIKREthakymvMDGDVDVV--ESGGKSDFFygnd 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  87 -------------IEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRG 133
Cdd:cd16307  112 pstyfppahvdkvLHDGEQVELGGTVLTAHLTAGHTKGCTTWTMKVKDHGKTYDVVIVGS 171
VIM_type_MBL-B1 cd16303
VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona ...
 16-137 5.77e-05

VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona integron-encoded metallo-beta-lactamase)-type MBLs are integron-associated and are widely distributed acquired MBLs. MBLs (class B of the Ambler beta-lactamase classification) 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 VIM-type MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293861 [Multi-domain]  Cd Length: 218  Bit Score: 42.54  E-value: 5.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  16 RESREAVLIDPV---LETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRS------LLPGCQSVISRLSGAQADLH 86
Cdd:cd16303   34 RDGDELLLIDTAwgaKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAagvatyASPSTRRLAEAEGNEIPTHS 113

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 189067485  87 IED----GDSIRFGRFALeTRASPGHTPGCVTFVLNDHSMAFTGDAllIRGCGRT 137
Cdd:cd16303  114 LEGlsssGDAVRFGPVEL-FYPGAAHSTDNLVVYVPSARVLYGGCA--VRELSST 165
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 4-70 1.27e-03

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: 38.64  E-value: 1.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 189067485   4 PVSCTFTYllGDREsreAVLIDPVLETAprDAQ----LIKELGLRLLYAVNTHCHADHITGSGLLRSLLPG 70
Cdd:cd07739   15 PVTSTLIY--GETE---AVLVDAQFTRA--DAErladWIKASGKTLTTIYITHGHPDHYFGLEVLLEAFPD 78
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
51-127 2.10e-03

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 38.25  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  51 THCHADHITG-SGLLRSLL-------------PGCQSVISRLSGAQA-------DLH-IEDGDSIRFGRFALETRASPgH 108
Cdd:COG1234   59 THLHGDHIAGlPGLLSTRSlagrekpltiygpPGTKEFLEALLKASGtdldfplEFHeIEPGEVFEIGGFTVTAFPLD-H 137

                         90       100
                 ....*....|....*....|.
gi 189067485 109 TPGCV--TFVLNDHSMAFTGD 127
Cdd:COG1234  138 PVPAYgyRFEEPGRSLVYSGD 158
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 20-127 7.79e-03

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 36.41  E-value: 7.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189067485  20 EAVLIDpvletAPRDA-QLIKELGLR------LLYavnTHCHADHITGSGLLRSLLPGCQ-----------------SVI 75
Cdd:COG1235   45 TRLLID-----AGPDLrEQLLRLGLDpskidaILL---THEHADHIAGLDDLRPRYGPNPipvyatpgtlealerrfPYL 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 189067485  76 SRLSGAQADLH-IEDGDSIRFGRFALETRASPGHTPGCVTFVL--NDHSMAFTGD 127
Cdd:COG1235  117 FAPYPGKLEFHeIEPGEPFEIGGLTVTPFPVPHDAGDPVGYRIedGGKKLAYATD 171
 
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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