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Conserved domains on  [gi|288895134|gb|ADC66671|]
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Zn-dependent hydrolase including glyoxylase-like protein [Ferroglobus placidus DSM 10642]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869930)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme that may have substrate towards phosphotriesters, esters, and/or lactones

CATH:  3.60.15.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  17597585|12177301|11471246|11513844
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 8-189 3.84e-52

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: 166.24  E-value: 3.84e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   8 KGCNVYLVVVDGKKYVVDTGLPGNERRIAEAVKE-------CEGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYLK 80
Cdd:cd07721    9 PPVNAYLIEDDDGLTLIDTGLPGSAKRILKALRElglspkdIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEREAPYLE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  81 GIKKHEYKGLIGSFARFYEsiKKPKYLEEVESV-------EELKDLEIIHTPGHTEGSISILVGDS--LICGDLVRckvf 151
Cdd:cd07721   89 GEKPYPPPVRLGLLGLLSP--LLPVKPVPVDRTledgdtlDLAGGLRVIHTPGHTPGHISLYLEEDgvLIAGDALV---- 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 288895134 152 SDNPTL--SSKNFNWNDEEYRRSLRKVLKFEFEKLYPGHG 189
Cdd:cd07721  163 TVGGELvpPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
 
Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 8-189 3.84e-52

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: 166.24  E-value: 3.84e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   8 KGCNVYLVVVDGKKYVVDTGLPGNERRIAEAVKE-------CEGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYLK 80
Cdd:cd07721    9 PPVNAYLIEDDDGLTLIDTGLPGSAKRILKALRElglspkdIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEREAPYLE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  81 GIKKHEYKGLIGSFARFYEsiKKPKYLEEVESV-------EELKDLEIIHTPGHTEGSISILVGDS--LICGDLVRckvf 151
Cdd:cd07721   89 GEKPYPPPVRLGLLGLLSP--LLPVKPVPVDRTledgdtlDLAGGLRVIHTPGHTPGHISLYLEEDgvLIAGDALV---- 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 288895134 152 SDNPTL--SSKNFNWNDEEYRRSLRKVLKFEFEKLYPGHG 189
Cdd:cd07721  163 TVGGELvpPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 9-202 8.42e-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: 124.80  E-value: 8.42e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   9 GCNVYLVVVDGKKYVVDTGLPGNER-RIAEAVKEC----EGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYLKGIK 83
Cdd:COG0491   14 GVNSYLIVGGDGAVLIDTGLGPADAeALLAALAALgldiKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEAPA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  84 KHEYKGLigSFARFYESIKKPkyleeVESVEELKDLEIIHTPGHTEGSISILVGDS--LICGDLVrCKVFSDNPTLSSKN 161
Cdd:COG0491   94 AGALFGR--EPVPPDRTLEDG-----DTLELGGPGLEVIHTPGHTPGHVSFYVPDEkvLFTGDAL-FSGGVGRPDLPDGD 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 288895134 162 FnwndEEYRRSLRKVLKFEFEKLYPGHGRVIRREEFEDLLK 202
Cdd:COG0491  166 L----AQWLASLERLLALPPDLVIPGHGPPTTAEAIDYLEE 202
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 11-188 5.29e-31

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 111.49  E-value: 5.29e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134    11 NVYLVVVDGKKYVVDTGLPGNERRIAEA----VKECEGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYLKGikKHE 86
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELkklgPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKD--LLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134    87 YKGLIGSFARFYESIKKPKYleEVESVEELKDLEIIHTPGHTEGSISILVGDS--LICGDLVrckVFSDNPTLSSKNFNW 164
Cdd:smart00849  79 LLGELGAEAEPAPPDRTLKD--GDELDLGGGELEVIHTPGHTPGSIVLYLPEGkiLFTGDLL---FAGGDGRTLVDGGDA 153

                          170       180
                   ....*....|....*....|....
gi 288895134   165 NDEEYRRSLRKVLKFEFEKLYPGH 188
Cdd:smart00849 154 AASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
9-188 4.31e-28

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 104.76  E-value: 4.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134    9 GCNVYLVVVDGKKYVVDTGLPGNERRIAEA------VKECEGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYLKGI 82
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTGGSAEAALLLLLaalglgPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   83 KKHEYKGLIGSFARFYESIKK-PKYLEEVESVEELKDLEIIHTPGHTEGSISILVGDS--LICGDLV--RCKVFSDNPTL 157
Cdd:pfam00753  85 ELGLAASRLGLPGPPVVPLPPdVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGkvLFTGDLLfaGEIGRLDLPLG 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 288895134  158 SSKN-FNWNDEEYRRSLRKVLKFEFEKLYPGH 188
Cdd:pfam00753 165 GLLVlHPSSAESSLESLLKLAKLKAAVIVPGH 196
ComEC_Rec2 TIGR00361
DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 ...
 14-78 1.35e-05

DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 species so far (Haemophilus influenzae, Escherichia coli, Bacillus subtilis, Neisseria gonorrhoeae, Streptococcus pneumoniae), of which all but E. coli are model systems for the study of competence for natural transformation. This protein is a predicted multiple membrane-spanning protein likely to be involved in DNA internalization. In a large number of bacterial species not known to exhibit competence, this protein is replaced by a half-length N-terminal homolog of unknown function, modelled by the related model ComEC_N-term. The role for this protein in species that are not naturally transformable is unknown. [Cellular processes, DNA transformation]


Pssm-ID: 273036 [Multi-domain]  Cd Length: 662  Bit Score: 44.89  E-value: 1.35e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 288895134   14 LVVVDGKKYVVDTGLPGNERRIAEAVK---------ECEGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEY 78
Cdd:TIGR00361 454 FIGANGKGILYDTGEPWREGSLGEKVIipfltakgiKLEALILSHADQDHIGGAEIILKHHPVKRLVIPKGFVE 527
PRK02113 PRK02113
MBL fold metallo-hydrolase;
14-89 3.60e-03

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 37.07  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  14 LVVVDGKKYVVDTGLPGNERRIAEAVKECEGIILTHSHFDHMGSARALSKILKSK---VYAHPKEFEYLKG-----IKKH 85
Cdd:PRK02113  39 LVETEGARILIDCGPDFREQMLRLPFGKIDAVLITHEHYDHVGGLDDLRPFCRFGevpIYAEQYVAERLRSrmpycFVEH 118


                 ....
gi 288895134  86 EYKG 89
Cdd:PRK02113 119 SYPG 122
 
Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 8-189 3.84e-52

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: 166.24  E-value: 3.84e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   8 KGCNVYLVVVDGKKYVVDTGLPGNERRIAEAVKE-------CEGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYLK 80
Cdd:cd07721    9 PPVNAYLIEDDDGLTLIDTGLPGSAKRILKALRElglspkdIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEREAPYLE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  81 GIKKHEYKGLIGSFARFYEsiKKPKYLEEVESV-------EELKDLEIIHTPGHTEGSISILVGDS--LICGDLVRckvf 151
Cdd:cd07721   89 GEKPYPPPVRLGLLGLLSP--LLPVKPVPVDRTledgdtlDLAGGLRVIHTPGHTPGHISLYLEEDgvLIAGDALV---- 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 288895134 152 SDNPTL--SSKNFNWNDEEYRRSLRKVLKFEFEKLYPGHG 189
Cdd:cd07721  163 TVGGELvpPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 9-202 8.42e-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: 124.80  E-value: 8.42e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   9 GCNVYLVVVDGKKYVVDTGLPGNER-RIAEAVKEC----EGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYLKGIK 83
Cdd:COG0491   14 GVNSYLIVGGDGAVLIDTGLGPADAeALLAALAALgldiKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEAPA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  84 KHEYKGLigSFARFYESIKKPkyleeVESVEELKDLEIIHTPGHTEGSISILVGDS--LICGDLVrCKVFSDNPTLSSKN 161
Cdd:COG0491   94 AGALFGR--EPVPPDRTLEDG-----DTLELGGPGLEVIHTPGHTPGHVSFYVPDEkvLFTGDAL-FSGGVGRPDLPDGD 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 288895134 162 FnwndEEYRRSLRKVLKFEFEKLYPGHGRVIRREEFEDLLK 202
Cdd:COG0491  166 L----AQWLASLERLLALPPDLVIPGHGPPTTAEAIDYLEE 202
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 11-188 5.29e-31

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 111.49  E-value: 5.29e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134    11 NVYLVVVDGKKYVVDTGLPGNERRIAEA----VKECEGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYLKGikKHE 86
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELkklgPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKD--LLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134    87 YKGLIGSFARFYESIKKPKYleEVESVEELKDLEIIHTPGHTEGSISILVGDS--LICGDLVrckVFSDNPTLSSKNFNW 164
Cdd:smart00849  79 LLGELGAEAEPAPPDRTLKD--GDELDLGGGELEVIHTPGHTPGSIVLYLPEGkiLFTGDLL---FAGGDGRTLVDGGDA 153

                          170       180
                   ....*....|....*....|....
gi 288895134   165 NDEEYRRSLRKVLKFEFEKLYPGH 188
Cdd:smart00849 154 AASDALESLLKLLKLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 9-188 1.99e-30

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: 110.45  E-value: 1.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   9 GCNVYLVVVDGKK-YVVDTGLPGNER---RIAEAVKECEGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYLKGIKK 84
Cdd:cd06262    9 QTNCYLVSDEEGEaILIDPGAGALEKileAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAELLEDPEL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  85 heykgliGSFARFYESIKKPKYLEE----VESVEELKDLEIIHTPGHTEGSISILVGDS--LICGDLVRCK--VFSDNPT 156
Cdd:cd06262   89 -------NLAFFGGGPLPPPEPDILledgDTIELGGLELEVIHTPGHTPGSVCFYIEEEgvLFTGDTLFAGsiGRTDLPG 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 288895134 157 lssknfnWNDEEYRRSLRKVLK--FEFEKLYPGH 188
Cdd:cd06262  162 -------GDPEQLIESIKKLLLllPDDTVVYPGH 188
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
9-188 4.31e-28

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 104.76  E-value: 4.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134    9 GCNVYLVVVDGKKYVVDTGLPGNERRIAEA------VKECEGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYLKGI 82
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTGGSAEAALLLLLaalglgPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   83 KKHEYKGLIGSFARFYESIKK-PKYLEEVESVEELKDLEIIHTPGHTEGSISILVGDS--LICGDLV--RCKVFSDNPTL 157
Cdd:pfam00753  85 ELGLAASRLGLPGPPVVPLPPdVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGkvLFTGDLLfaGEIGRLDLPLG 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 288895134  158 SSKN-FNWNDEEYRRSLRKVLKFEFEKLYPGH 188
Cdd:pfam00753 165 GLLVlHPSSAESSLESLLKLAKLKAAVIVPGH 196
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 11-188 1.25e-22

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: 89.52  E-value: 1.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  11 NVYLVVVDGKKY--VVDtglPGNE-----RRIAEAVKECEGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYlkgik 83
Cdd:cd16275   13 YSYIIIDKATREaaVVD---PAWDiekilAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDY----- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  84 kheYKGLIGSFARFY--ESIKkpkyleevesveeLKDLEI--IHTPGHTEGSISILVGDSLICGDLV------RCKVFSD 153
Cdd:cd16275   85 ---YGFRCPNLIPLEdgDTIK-------------IGDTEItcLLTPGHTPGSMCYLLGDSLFTGDTLfiegcgRCDLPGG 148

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 288895134 154 NPtlssknfnwndEEYRRSLRKVLKFEFE--KLYPGH 188
Cdd:cd16275  149 DP-----------EEMYESLQRLKKLPPPntRVYPGH 174
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 10-193 1.90e-20

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: 84.17  E-value: 1.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  10 CNVYLVVVDGKKYVVDTGLPGNERRIAEAVKEcEGI--------ILTHSHFDHMGSARALSKilkSKVYAHPKEFeylkg 81
Cdd:cd07711   22 STVTLIKDGGKNILVDTGTPWDRDLLLKALAE-HGLspedidyvVLTHGHPDHIGNLNLFPN---ATVIVGWDIC----- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  82 ikkHEYKGLIGSFARFYESIkkpkyleevesveeLKDLEIIHTPGHTEGSISILV-----GDSLICGDLVRCKVFSDNPT 156
Cdd:cd07711   93 ---GDSYDDHSLEEGDGYEI--------------DENVEVIPTPGHTPEDVSVLVetekkGTVAVAGDLFEREEDLEDPI 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 288895134 157 LsSKNFNWNDEEYRRSLRKVLKfEFEKLYPGHGRVIR 193
Cdd:cd07711  156 L-WDPLSEDPELQEESRKRILA-LADWIIPGHGPPFK 190
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 11-193 2.25e-20

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: 83.89  E-value: 2.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  11 NVYLVVVDGKKYVVDTGLPGNE------RRIAEA---VKECEGIILTHSHFDHMGSARALSKILKSKVYAHPkeFEYLKG 81
Cdd:cd07725   16 NVYLLRDGDETTLIDTGLATEEdaealwEGLKELglkPSDIDRVLLTHHHPDHIGLAGKLQEKSGATVYILD--VTPVKD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  82 ikkheykGLIGSFARFyesikkpkyleevesveelkDLEIIHTPGHTEGSISILVGDS--LICGDLVRCKVfSDNPTLSS 159
Cdd:cd07725   94 -------GDKIDLGGL--------------------RLKVIETPGHTPGHIVLYDEDRreLFVGDAVLPKI-TPNVSLWA 145

                        170       180       190
                 ....*....|....*....|....*....|....
gi 288895134 160 KNFNWNDEEYRRSLRKVLKFEFEKLYPGHGRVIR 193
Cdd:cd07725  146 VRVEDPLGAYLESLDKLEKLDVDLAYPGHGGPIK 179
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 9-188 4.40e-20

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: 83.06  E-value: 4.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   9 GCNVYLVVVDGKKYVVDTGLPgnERRIAEAVKECEG----IILTHSHFDHMGSARALSKilkskVYAHPKEFEYLKGIKK 84
Cdd:cd07712    8 RVNIYLLRGRDRALLIDTGLG--IGDLKEYVRTLTDlpllVVATHGHFDHIGGLHEFEE-----VYVHPADAEILAAPDN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  85 HEykgLIGSFARFYESIKKPKYLEEvesveelKD----------LEIIHTPGHTEGSISILVGDS--LICGDLVrCK--V 150
Cdd:cd07712   81 FE---TLTWDAATYSVPPAGPTLPL-------RDgdvidlgdrqLEVIHTPGHTPGSIALLDRANrlLFSGDVV-YDgpL 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 288895134 151 FSDNPTLssknfnwNDEEYRRSLRKVLKF--EFEKLYPGH 188
Cdd:cd07712  150 IMDLPHS-------DLDDYLASLEKLSKLpdEFDKVLPGH 182
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 10-188 3.12e-19

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


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 82.26  E-value: 3.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  10 CNVYLVVVDGKKYVVDTGLP------------------GNERRIAEAVKECeGI--------ILTHSHFDHMGSARALSK 63
Cdd:cd07729   32 VYAYLIEHPEGTILVDTGFHpdaaddpgglelafppgvTEEQTLEEQLARL-GLdpedidyvILSHLHFDHAGGLDLFPN 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  64 ilkSKVYAHPKEFEYLKGIKKHeYKGLIGSFARFYESIKKPKYLEEVESVEELKDLEIIHTPGHTEGSISILV----GDS 139
Cdd:cd07729  111 ---ATIIVQRAELEYATGPDPL-AAGYYEDVLALDDDLPGGRVRLVDGDYDLFPGVTLIPTPGHTPGHQSVLVrlpeGTV 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 288895134 140 LICGDLVRCKVFSDNPTLSSknFNWNDEEYRRSLRKVLKFEFE---KLYPGH 188
Cdd:cd07729  187 LLAGDAAYTYENLEEGRPPG--INYDPEAALASLERLKALAERegaRVIPGH 236
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 9-192 4.24e-18

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: 77.96  E-value: 4.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   9 GCNVYLVVVdGKKYV-VDTG--LPGNERRIAEAVKECEG-----IILTHSHFDHMGSARALSKILKS---KVYAHPKEFE 77
Cdd:cd07722   17 GTNTYLVGT-GKRRIlIDTGegRPSYIPLLKSVLDSEGNatisdILLTHWHHDHVGGLPDVLDLLRGpspRVYKFPRPEE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  78 YLKGIKKheykglIGSFARFYE--SIKKPKYLeevesveelkdLEIIHTPGHTEGSISIL--VGDSLICGDLV----RCk 149
Cdd:cd07722   96 DEDPDED------GGDIHDLQDgqVFKVEGAT-----------LRVIHTPGHTTDHVCFLleEENALFTGDCVlghgTA- 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 288895134 150 VFSDnptLSsknfnwndeEYRRSLRKVLKFEFEKLYPGHGRVI 192
Cdd:cd07722  158 VFED---LA---------AYMASLKKLLSLGPGRIYPGHGPVI 188
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 9-188 3.31e-17

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 76.03  E-value: 3.31e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   9 GCNVYLVVVDGKK-YVVDTGLPG-NERRIAEAVKECE----GIILTHSHFDHMGSARALSKILKSKVYAHPKE------- 75
Cdd:cd07743    7 PTNIGVYVFGDKEaLLIDSGLDEdAGRKIRKILEELGwklkAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEkafienp 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  76 -FE--YLKGikKHEYKGLIGSFARFyESIKKPKYLEEVESVEELKDLEIIHTPGHTEGSISILVGDS-LICGDLvrckVF 151
Cdd:cd07743   87 lLEpsYLGG--AYPPKELRNKFLMA-KPSKVDDIIEEGELELGGVGLEIIPLPGHSFGQIGILTPDGvLFAGDA----LF 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 288895134 152 SDNpTLsSK---NFNWNDEEYRRSLRKVLKFEFEKLYPGH 188
Cdd:cd07743  160 GEE-VL-EKygiPFLYDVEEQLETLEKLEELDADYYVPGH 197
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 8-192 1.51e-16

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 74.06  E-value: 1.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   8 KGCNVYLVVVDGKKYVVDTG--LPGNERRIAEAVK--ECEGIILTHSHFDHMGSARALSKILKSKVYAHPKefeylkgik 83
Cdd:cd16278   16 DGTNTYLLGAPDGVVVIDPGpdDPAHLDALLAALGggRVSAILVTHTHRDHSPGAARLAERTGAPVRAFGP--------- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  84 kHEYKGLIGSFARfyesikkpkyleevesVEELKD----------LEIIHTPGHTEGSISILVGDS--LICGDLVrckvF 151
Cdd:cd16278   87 -HRAGGQDTDFAP----------------DRPLADgevieggglrLTVLHTPGHTSDHLCFALEDEgaLFTGDHV----M 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 288895134 152 SDNPTLSSknfnWND---EEYRRSLRKVLKFEFEKLYPGHGRVI 192
Cdd:cd16278  146 GWSTTVIA----PPDgdlGDYLASLERLLALDDRLLLPGHGPPI 185
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 9-199 6.81e-15

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 69.90  E-value: 6.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   9 GCNVYLVVVDGKKYVVDTGL-PGNERRIAEAVKECEG-----IILTHSHFDHMGSARALSKiLKSKVYAHPKEFEYLKGI 82
Cdd:cd16282   14 ISNIGFIVGDDGVVVIDTGAsPRLARALLAAIRKVTDkpvryVVNTHYHGDHTLGNAAFAD-AGAPIIAHENTREELAAR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  83 KKHEYKGLIGSFARFYESIKKPK----YLEEVESVEELKDLEIIHT-PGHTEGSISILVGDS--LICGDLvrckVFSDN- 154
Cdd:cd16282   93 GEAYLELMRRLGGDAMAGTELVLpdrtFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEgvLFAGDL----VFNGRi 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 288895134 155 PTLSSKNFnwndEEYRRSLRKVLKFEFEKLYPGHGRVIRREEFED 199
Cdd:cd16282  169 PFLPDGSL----AGWIAALDRLLALDATVVVPGHGPVGDKADLRA 209
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 13-188 9.44e-14

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: 65.94  E-value: 9.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  13 YLVV--VDGKKYVVDtglPGNERRIAEAVKEC----EGIILTHSHFDHMGSARALSKILKS-KVYAHPKE-FEYLKGIKK 84
Cdd:cd07723   12 YLIVdeATGEAAVVD---PGEAEPVLAALEKNgltlTAILTTHHHWDHTGGNAELKALFPDaPVYGPAEDrIPGLDHPVK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  85 HEYKGLIGSFarfyesikkpkyleevesveelkDLEIIHTPGHTEGSISILVGDS--LICGDlvrckvfsdnpTLSS--- 159
Cdd:cd07723   89 DGDEIKLGGL-----------------------EVKVLHTPGHTLGHICYYVPDEpaLFTGD-----------TLFSggc 134

                        170       180       190
                 ....*....|....*....|....*....|.
gi 288895134 160 -KNFNWNDEEYRRSLRKVLKFEFE-KLYPGH 188
Cdd:cd07723  135 gRFFEGTAEQMYASLQKLLALPDDtLVYCGH 165
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 6-193 3.88e-13

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


Pssm-ID: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 64.91  E-value: 3.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   6 KAKGCNVYLVVVDGKKYVVDTG--LPGNERRIAEA--VKEcegIILTHShfDHMGSARALSKILKSKVYAH--------- 72
Cdd:cd07727   11 KSFGAASYLILRPEGNILVDSPrySPPLAKRIEALggIRY---IFLTHR--DDVADHAKWAERFGAKRIIHeddvnavtr 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  73 PKEFEYLKGIKKHEYkgligsfarfyesikkpkyleevesveeLKDLEIIHTPGHTEGSISILVGDS--LICGDLVRckV 150
Cdd:cd07727   86 PDEVIVLWGGDPWEL----------------------------DPDLTLIPVPGHTRGSVVLLYKEKgvLFTGDHLA--W 135

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 288895134 151 FSDNPTLS-SKNFNWND-EEYRRSLRKVLKFEFEKLYPGHGRVIR 193
Cdd:cd07727  136 SRRRGWLSaFRYVCWYSwPEQAESVERLADLDFEWVLPGHGRRVH 180
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 11-189 5.84e-13

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: 64.68  E-value: 5.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  11 NVYLVV--VDGKKYVVDTGLPGNE--RRIAEAVKECEGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYlkgikkhe 86
Cdd:cd16322   12 NTYLVAdeGGGEAVLVDPGDESEKllARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDLPL-------- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  87 YKGLIGSFARFYESIKKP-----KYLEEVESVEELKDLEIIHTPGHTEGSISILV--GDSLICGDLV------RCKVFSD 153
Cdd:cd16322   84 YEAADLGAKAFGLGIEPLpppdrLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVeeEGLLFSGDLLfqgsigRTDLPGG 163

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 288895134 154 NPtlssknfnwndEEYRRSLRKVLKFEFE-KLYPGHG 189
Cdd:cd16322  164 DP-----------KAMAASLRRLLTLPDEtRVFPGHG 189
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 6-189 1.23e-12

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: 63.19  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   6 KAKGCNVYLVVVDGKKY--VVDTGLPGNERRIAEAVKEC---EGIILTHSHFDHMGSARALSKILKSKVYAHPKefeylk 80
Cdd:cd07724    8 PGLGTLSYLVGDPETGEaaVIDPVRDSVDRYLDLAAELGlkiTYVLETHVHADHVSGARELAERTGAPIVIGEG------ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  81 GIKKHEYKGL-------IGSFArfyesikkpkyleevesveelkdLEIIHTPGHTEGSISILV--------GDSLICGDL 145
Cdd:cd07724   82 APASFFDRLLkdgdvleLGNLT-----------------------LEVLHTPGHTPESVSYLVgdpdavftGDTLFVGDV 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 288895134 146 VRCkvfsDnptLSSKNFNWNDEEYrRSLRKVLKF--EFEKLYPGHG 189
Cdd:cd07724  139 GRP----D---LPGEAEGLARQLY-DSLQRKLLLlpDETLVYPGHD 176
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 12-188 9.27e-12

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 61.74  E-value: 9.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  12 VYLVVVDGKKYVVDTG----LPGNERRIAE---AVKECEGIILTHSHFDHMGSARALSKIL-KSKVYAHPKefeylkGIK 83
Cdd:cd07726   18 SYLLDGEGRPALIDTGpsssVPRLLAALEAlgiAPEDVDYIILTHIHLDHAGGAGLLAEALpNAKVYVHPR------GAR 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  84 kHeykgLI-------GS--------FARFYESIKKPKYLEEVESVEELKD-----LEIIHTPGHTEGSISILVGDS--LI 141
Cdd:cd07726   92 -H----LIdpsklwaSAravygdeaDRLGGEILPVPEERVIVLEDGETLDlggrtLEVIDTPGHAPHHLSFLDEESdgLF 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 288895134 142 CGD----LVRCKVFSDNPTLSSKNFNWndEEYRRSLRKVLKFEFEKLYPGH 188
Cdd:cd07726  167 TGDaagvRYPELDVVGPPSTPPPDFDP--EAWLESLDRLLSLKPERIYLTH 215
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 13-56 8.57e-08

Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 50.21  E-value: 8.57e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 288895134  13 YLVVVDGKKYVVDTGlPGNERRIAEA---VKECEGIILTHSHFDHMG 56
Cdd:cd07719   21 TLVVVGGRVYLVDAG-SGVVRRLAQAglpLGDLDAVFLTHLHSDHVA 66
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 45-135 5.85e-07

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 48.35  E-value: 5.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  45 IILTHSHFDHMGSARALSKILKSKVYAHPKEFEYLkgikkHEYKGLIGSFARFyesiKKPKyleeveSVEELKD------ 118
Cdd:cd16280   65 ILITHGHGDHYGGAAYLKDLYGAKVVMSEADWDMM-----EEPPEEGDNPRWG----PPPE------RDIVIKDgdtltl 129

                         90       100
                 ....*....|....*....|.
gi 288895134 119 ----LEIIHTPGHTEGSISIL 135
Cdd:cd16280  130 gdttITVYLTPGHTPGTLSLI 150
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 18-176 9.02e-07

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


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 48.03  E-value: 9.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  18 DGKKYVVDTGL---------------------PGNERRIAEAVKEC-------EGIILTHSHFDHMGsarALSKILKSKV 69
Cdd:cd07730   32 TGGKILFDLGYrkdfeeytprvperlyrtpvpLEVEEDVAEQLAAGgidpediDAVILSHLHWDHIG---GLSDFPNARL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  70 YAHPKEFEYLK--GIKKHEYKGLIGSFARFYESIKKPKYLEEVESVEELK--D------LEIIHTPGHTEGSISILVGDS 139
Cdd:cd07730  109 IVGPGAKEALRppGYPSGFLPELLPSDFEGRLVRWEEDDFLWVPLGPFPRalDlfgdgsLYLVDLPGHAPGHLGLLARTT 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 288895134 140 -----LICGDLV--RCKVFSDNPTLSSKNFNWND--EEYRRSLRKV 176
Cdd:cd07730  189 sgtwvFLAGDAChhRIGLLRPSPLLPLPDLDDGAdrEAARETLARL 234
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 11-146 1.37e-06

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. 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: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 47.16  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  11 NVYLVVVDGKKYVVDTGLPGNER----RIAEAVKECeGI--------ILTHSHFDHMGSARALSKIL---KSKVYAHPKE 75
Cdd:cd07720   50 NAFLVRTGGRLILVDTGAGGLFGptagKLLANLAAA-GIdpediddvLLTHLHPDHIGGLVDAGGKPvfpNAEVHVSEAE 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  76 FEYLK--GIKKHEYKGLIGSFARFYESIKkpKYLEEVESVEELKDL---EIIHTPGHTEGSISILV---GDSL-ICGDLV 146
Cdd:cd07720  129 WDFWLddANAAKAPEGAKRFFDAARDRLR--PYAAAGRFEDGDEVLpgiTAVPAPGHTPGHTGYRIesgGERLlIWGDIV 206
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 13-80 1.55e-06

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 47.20  E-value: 1.55e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 288895134  13 YLVVVDGKKYVVDTGlPG---NERRIAEAVKECEGIILTHSHFDHMGSARALSKILKSK---VYAHPKEFEYLK 80
Cdd:COG1235   38 ILVEADGTRLLIDAG-PDlreQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYGPNpipVYATPGTLEALE 110
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 9-176 1.67e-06

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: 47.15  E-value: 1.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   9 GCNVYLVVVDGKKYVVDTGLPGNERRIAEAVK-------ECEGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYLK- 80
Cdd:cd07708   21 DLAAYLIVTPQGNILIDGDMEQNAPMIKANIKklgfkfsDTKLILISHAHFDHAGGSAEIKKQTGAKVMAGAEDVSLLLs 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  81 GIKKheYKGLIGSFARFYESIKKPKyleevesveELKDLEII---------H-TPGHTEGSIS-------------ILVG 137
Cdd:cd07708  101 GGSS--DFHYANDSSTYFPQSTVDR---------AVHDGERVtlggtvltaHaTPGHTPGCTTwtmtlkdhgkqyqVVFA 169

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 288895134 138 DSLICGDLVRckvFSDNPTLSSKNfnwndEEYRRSLRKV 176
Cdd:cd07708  170 DSLTVNPGYR---LVDNPTYPKIV-----EDYRHSFAVV 200
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 8-203 2.53e-06

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: 46.67  E-value: 2.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   8 KGCNVYLVVVDGKKYVVDTGLPGN----ERRIAE---AVKECEGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYLK 80
Cdd:cd16310   20 KGIGSYLITSNHGAILLDGGLEENaaliEQNIKAlgfKLSDIKIIINTHAHYDHAGGLAQLKADTGAKLWASRGDRPALE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  81 gIKKHEYKGLIGSFArfYESIKKPKyleevesveELKDLEIIH----------TPGHTEG--SISILVGDS-------LI 141
Cdd:cd16310  100 -AGKHIGDNITQPAP--FPAVKVDR---------ILGDGEKIKlgditltatlTPGHTKGctTWSTTVKENgrplrvvFP 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 288895134 142 CGDLVRCKVFSDN---PTLSsknfnwndEEYRRSLRKVLKFEFEKLYPGHgrvirrEEFEDLLKK 203
Cdd:cd16310  168 CSLSVAGNVLVGNktyPTIV--------EDYRASFARLRAMKADIVLTSH------PEVADLLAR 218
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 11-148 2.99e-06

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: 46.01  E-value: 2.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  11 NVYLVVVDGKKY--VVDTGlpGNERRIAEAVKE----CEGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYLkgikk 84
Cdd:cd07737   12 NCSLIWCEETKEaaVIDPG--GDADKILQAIEDlgltLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKEDKFL----- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  85 heYKGLIGSFARFY----------------ESIKKPKYLeevesveelkdLEIIHTPGHTEGSIS--------ILVGDSL 140
Cdd:cd07737   85 --LENLPEQSQMFGfppaeaftpdrwleegDTVTVGNLT-----------LEVLHCPGHTPGHVVffnresklAIVGDVL 151


                 ....*...
gi 288895134 141 ICGDLVRC 148
Cdd:cd07737  152 FKGSIGRT 159
ComEC_Rec2 TIGR00361
DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 ...
 14-78 1.35e-05

DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 species so far (Haemophilus influenzae, Escherichia coli, Bacillus subtilis, Neisseria gonorrhoeae, Streptococcus pneumoniae), of which all but E. coli are model systems for the study of competence for natural transformation. This protein is a predicted multiple membrane-spanning protein likely to be involved in DNA internalization. In a large number of bacterial species not known to exhibit competence, this protein is replaced by a half-length N-terminal homolog of unknown function, modelled by the related model ComEC_N-term. The role for this protein in species that are not naturally transformable is unknown. [Cellular processes, DNA transformation]


Pssm-ID: 273036 [Multi-domain]  Cd Length: 662  Bit Score: 44.89  E-value: 1.35e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 288895134   14 LVVVDGKKYVVDTGLPGNERRIAEAVK---------ECEGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEY 78
Cdd:TIGR00361 454 FIGANGKGILYDTGEPWREGSLGEKVIipfltakgiKLEALILSHADQDHIGGAEIILKHHPVKRLVIPKGFVE 527
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 23-204 1.80e-05

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


Pssm-ID: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 44.08  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  23 VVDTGLPGNERRIAEAVK-------ECEGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYLK----GIKKHEYKGLi 91
Cdd:cd16313   35 LIDGGFPKSPEQIAASIRqlgfkleDVKYILSSHDHWDHAGGIAALQKLTGAQVLASPATVAVLRsgsmGKDDPQFGGL- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  92 gsfarfyesikkPKYlEEVESVEELKDLEII----------HTPGHTEGSIS-------------ILVGDSL--ICGDLV 146
Cdd:cd16313  114 ------------TPM-PPVASVRAVRDGEVVklgplavtahATPGHTTGGTSwtwqsceqgrcanMVFADSLtaVSADGY 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 288895134 147 RckvFSDNPTLSSknfnwndeEYRRSLRKVLKFEFEKLYPGHgrvirrEEFEDLLKKV 204
Cdd:cd16313  181 R---FSAHPAVLA--------DVEQSIAAVEKLACDILVSAH------PEFSDMWTRV 221
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 13-100 1.80e-05

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. 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: 293799  Cd Length: 269  Bit Score: 44.15  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  13 YLVVVDGKKYVVDTGLPG----NERRIAEAVKECEGIILTHSHFDHMGS-ARALSKILKSKVYAHPKEFEYLKGIKKHEY 87
Cdd:cd07713   23 LLIETEGKKILFDTGQSGvllhNAKKLGIDLSDIDAVVLSHGHYDHTGGlKALLELNPKAPVYAHPDAFEPRYSKRGGGK 102

                         90
                 ....*....|...
gi 288895134  88 KGLIGSFARFYES 100
Cdd:cd07713  103 KGIGIGREELEKA 115
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 12-85 2.61e-05

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 43.69  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  12 VYLVVVDGKKYVVDTGLPGN----ERRIAEA-----VKECEGIILTHSHFDHMGSARAL------SKILKSKVYAHPKEF 76
Cdd:COG2333   14 ILIRTPDGKTILIDTGPRPSfdagERVVLPYlralgIRRLDLLVLTHPDADHIGGLAAVleafpvGRVLVSGPPDTSETY 93

                         90
                 ....*....|
gi 288895134  77 E-YLKGIKKH 85
Cdd:COG2333   94 ErLLEALKEK 103
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 14-88 2.89e-05

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 42.89  E-value: 2.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  14 LVVVDGKKYVVDTG--LPGNERRI-----AEAVKECEGIILTHSHFDHMGSARAL------SKILKSKVYAHPKEFE-YL 79
Cdd:cd07731   14 LIQTPGKTILIDTGprDSFGEDVVvpylkARGIKKLDYLILTHPDADHIGGLDAVlknfpvKEVYMPGVTHTTKTYEdLL 93


                 ....*....
gi 288895134  80 KGIKKHEYK 88
Cdd:cd07731   94 DAIKEKGIP 102
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 13-73 3.96e-05

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. 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: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 42.83  E-value: 3.96e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  13 YLVVVDGKKYVVDTGL-PG-------NERRIAEAVKECEGIILTHSHFDHMGSARALSKI-LKSKVYAHP 73
Cdd:cd16295   15 YLLETGGKRILLDCGLfQGgkeleelNNEPFPFDPKEIDAVILTHAHLDHSGRLPLLVKEgFRGPIYATP 84
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 ...
 8-194 4.48e-05

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: 43.11  E-value: 4.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   8 KGCNVYLVVVDGKKYVVDTGLPGNERRIAE-------AVKECEGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYLK 80
Cdd:cd16290   20 GGLSAVLITSPQGLILIDGALPQSAPQIEAniralgfRLEDVKLILNSHAHFDHAGGIAALQRDSGATVAASPAGAAALR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  81 GikkheykGLIG------SFARFYESIKKPKyleevesveELKDLEII----------HTPGHTEGSIS----------- 133
Cdd:cd16290  100 S-------GGVDpddpqaGAADPFPPVAKVR---------VVADGEVVklgplavtahATPGHTPGGTSwtwrsceggrc 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 288895134 134 --ILVGDSLicgdlvrckvfsdNPtLSSKNFNWND-------EEYRRSLRKVLKFEFEKL---YPGHGRVIRR 194
Cdd:cd16290  164 ldIVYADSL-------------TA-VSADGFRFSDdahparvAAFRRSIATVAALPCDILisaHPDASGLWEK 222
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 2-188 4.95e-05

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 42.51  E-value: 4.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   2 VELIKAkgcnvYLVVVDGKKYVVDTGLpGN--ER---------------RIAEAvkeceGI--------ILTHSHFDHMG 56
Cdd:cd16277   10 VELIHS-----WLVRTPGRTILVDTGI-GNdkPRpgppafhnlntpyleRLAAA-----GVrpedvdyvLCTHLHVDHVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  57 ---------------SARalskilkskVYAHPKEFEYLKGikkhEYKGLIGSFARFYESIKkP-----KYLEEVESVEEL 116
Cdd:cd16277   79 wntrlvdgrwvptfpNAR---------YLFSRAEYDHWSS----PDAGGPPNRGVFEDSVL-PvieagLADLVDDDHEIL 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 288895134 117 KDLEIIHTPGHTEGSISILVGDS----LICGDLVRCKVFSDNPTLSSKnFNWNDEEYRRSLRKVLKFEFEK---LYPGH 188
Cdd:cd16277  145 DGIRLEPTPGHTPGHVSVELESGgeraLFTGDVMHHPIQVARPDWSSV-FDEDPAQAAATRRRLLERAADTdtlLFPAH 222
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
13-90 5.90e-05

Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440850  Cd Length: 273  Bit Score: 42.56  E-value: 5.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  13 YLVVVDGKKYVVDTGLPG----NERRIAEAVKECEGIILTHSHFDHMGSARALSKILKS-KVYAHPKEF-EYLKGIKKHE 86
Cdd:COG1237   25 ALIETEGKRILFDTGQSDvllkNAEKLGIDLSDIDAVVLSHGHYDHTGGLPALLELNPKaPVYAHPDAFeKRYSKRPGGK 104


                 ....
gi 288895134  87 YKGL 90
Cdd:COG1237  105 YIGI 108
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 9-73 6.32e-05

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 42.21  E-value: 6.32e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 288895134   9 GCNVYLVVVDGKKYVVD-----TGLPGNERRIA-EAVKECEGIILTHSHFDHMGSArALSKILKS--KVYAHP 73
Cdd:COG2220   10 GHATFLIETGGKRILIDpvfsgRASPVNPLPLDpEDLPKIDAVLVTHDHYDHLDDA-TLRALKRTgaTVVAPL 81
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 13-136 1.10e-04

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


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 41.69  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  13 YLVVVDGKKYVVDTGLPGNERRIAEAV-------KECEGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYLKGIKKH 85
Cdd:cd16308   25 YLIVTPKGNILINTGLAESVPLIKKNIqalgfkfKDIKILLTTQAHYDHVGAMAAIKQQTGAKMMVDEKDAKVLADGGKS 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 288895134  86 EYKglIGSFARFYESIKKPKyleevesveELKDLEII----------HTPGHTEGSISILV 136
Cdd:cd16308  105 DYE--MGGYGSTFAPVKADK---------LLHDGDTIklggtkltllHHPGHTKGSCSFLF 154
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 11-74 1.39e-04

uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YycJ 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: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 40.71  E-value: 1.39e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 288895134  11 NVYLVVVDGKKYVVDTGLPGneRRIAEAVKEC-------EGIILTHSHFDHMGSARALSKILKSKVYAHPK 74
Cdd:cd07733   10 NCTYLETEDGKLLIDAGLSG--RKITGRLAEIgrdpediDAILVTHEHADHIKGLGVLARKYNVPIYATAG 78
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 13-73 1.69e-04

RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 41.71  E-value: 1.69e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  13 YLVVVDGKKYVVDTGL-PG----NERRIAEAVKECEGIILTHSHFDHmgsARALSKILKS----KVYAHP 73
Cdd:COG1236   17 YLLETGGTRILIDCGLfQGgkerNWPPFPFRPSDVDAVVLTHAHLDH---SGALPLLVKEgfrgPIYATP 83
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 9-88 4.28e-04

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. 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: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 40.08  E-value: 4.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   9 GCNVYLVVVDGKKYVVDTGL--PGNE-----------RRIAEAVKECEGIILTHSHFDHMGSARALSKILKSKVYAHP-- 73
Cdd:cd07714   10 GKNMYVVEYDDDIIIIDCGLkfPDEDmpgvdyiipdfSYLEENKDKIKGIFITHGHEDHIGALPYLLPELNVPIYATPlt 89

                         90       100
                 ....*....|....*....|...
gi 288895134  74 --------KEFEYLKGIKKHEYK 88
Cdd:cd07714   90 lalikkklEEFKLIKKVKLNEIK 112
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 14-80 5.28e-04

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; 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. Some members of this subgroup are named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 39.38  E-value: 5.28e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 288895134  14 LVVVDGKKYVVDTGlPgnERR---IAEAVKECEGIILTHSHFDH---MGSARALSKILKSK--VYAHPKEFEYLK 80
Cdd:cd16279   39 LIETGGKNILIDTG-P--DFRqqaLRAGIRKLDAVLLTHAHADHihgLDDLRPFNRLQQRPipVYASEETLDDLK 110
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
13-84 6.24e-04

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 39.41  E-value: 6.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  13 YLVVVDGKKYVVDTGlPGNERRIAEA---VKECEGIILTHSHFDHMG------SARALSKILKS-KVYAHPKEFEYLKGI 82
Cdd:COG1234   22 YLLEAGGERLLIDCG-EGTQRQLLRAgldPRDIDAIFITHLHGDHIAglpgllSTRSLAGREKPlTIYGPPGTKEFLEAL 100


                 ..
gi 288895134  83 KK 84
Cdd:COG1234  101 LK 102
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 14-80 1.37e-03

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


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 38.42  E-value: 1.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 288895134  14 LVVVDGKK-YVVDTglPGNERRIAEAVKECE--------GIILTHSHFDHMGSARALSKilKS-KVYAHPKEFEYLK 80
Cdd:cd16285   29 LIVIDGKGlVLIDT--PWTEAQTATLLDWIEkklgkpvtAAISTHSHDDRTGGIKALNA--RGiPTYATALTNELAK 101
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
9-88 1.50e-03

mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 38.89  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   9 GCNVYLVVVDGKKYVVDTGL--PGNE--------------RRIAEAVKeceGIILTHSHFDHMGsarALSKILKS---KV 69
Cdd:COG0595   18 GKNMYVYEYDDDIIIVDCGLkfPEDEmpgvdlvipdisylEENKDKIK---GIVLTHGHEDHIG---ALPYLLKElnvPV 91

                         90       100
                 ....*....|....*....|....*....
gi 288895134  70 YAHP----------KEFEYLKGIKKHEYK 88
Cdd:COG0595   92 YGTPltlalleaklKEHGLLKKVKLHVVK 120
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 13-94 1.80e-03

Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 37.63  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  13 YLVVVDGKKYVVDTGlPGNERRIAEA---VKECEGIILTHSHFDHMG------SARALSKILKS-KVYAHPKEFEYLKGI 82
Cdd:cd16272   20 YLLETGGTRILLDCG-EGTVYRLLKAgvdPDKLDAIFLSHFHLDHIGglptllFARRYGGRKKPlTIYGPKGIKEFLEKL 98

                         90
                 ....*....|..
gi 288895134  83 KKHEYKGLIGSF 94
Cdd:cd16272   99 LNFPVEILPLGF 110
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 7-203 2.51e-03

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: 37.69  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   7 AKGCNVYLVVVDGKKYVVDTGLP-------GNERRIAEAVKECEGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYL 79
Cdd:cd16288   19 TSGLASYLITTPQGLILIDTGLEssapmikANIRKLGFKPSDIKILLNSHAHLDHAGGLAALKKLTGAKLMASAEDAALL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  80 KGIKKHEYKglIGSFARFYESIKKPKyleevesveELKDLEII----------HTPGHTEGSISILVgdSLICGDLVRCK 149
Cdd:cd16288   99 ASGGKSDFH--YGDDSLAFPPVKVDR---------VLKDGDRVtlggttltahLTPGHTRGCTTWTM--TVKDDGKVYQV 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 288895134 150 VFSDNPT-------LSSKNFNWNDEEYRRSLRKVLKFEFEKLYPGHGRVIRREEFEDLLKK 203
Cdd:cd16288  166 VFADSLTvnpgyklVGNPTYPGIAEDYRHSFATLRALQCDIFLASHAEYFDLKEKRARLAA 226
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 14-56 2.69e-03

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. 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: 293814  Cd Length: 249  Bit Score: 37.62  E-value: 2.69e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 288895134  14 LVVVDGKKYVVDTGLpGNER---------------RIAEAVKEC-------EGIILTHSHFDHMG 56
Cdd:cd07728   47 LIQYQGKNYLIDAGI-GNGKltekqkrnfgvteesSIEESLAELgltpediDYVLMTHLHFDHAS 110
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 44-80 2.83e-03

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 37.29  E-value: 2.83e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 288895134   44 GIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYLK 80
Cdd:pfam12706  31 AVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLR 67
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 8-93 2.98e-03

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: 37.46  E-value: 2.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134   8 KGCNVYLVVVDGKKYVVDTGLPGNERRIAE-------AVKECEGIILTHSHFDHMGSARALSKILKSKVYAHPKEFEYLK 80
Cdd:cd16309   20 AGLGVFLITTPEGHILIDGAMPQSTPLIKDnikklgfDVKDVKYLLNTHAHFDHAGGLAELKKATGAQLVASAADKPLLE 99

                         90
                 ....*....|...
gi 288895134  81 GikkheykGLIGS 93
Cdd:cd16309  100 S-------GYVGS 105
PRK02113 PRK02113
MBL fold metallo-hydrolase;
14-89 3.60e-03

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 37.07  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  14 LVVVDGKKYVVDTGLPGNERRIAEAVKECEGIILTHSHFDHMGSARALSKILKSK---VYAHPKEFEYLKG-----IKKH 85
Cdd:PRK02113  39 LVETEGARILIDCGPDFREQMLRLPFGKIDAVLITHEHYDHVGGLDDLRPFCRFGevpIYAEQYVAERLRSrmpycFVEH 118


                 ....
gi 288895134  86 EYKG 89
Cdd:PRK02113 119 SYPG 122
IMP_DIM-like_MBL-B1 cd16301
IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 14-191 6.64e-03

IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the acquired MBLs IMP-1(a beta-lactamase that is active on imipenem), DIM-1 (Dutch imipenemase), GIM-1 (German imipenemase), KHM-1 (Kyorin Health Science MBL 1), SIM-1 (Seoul imipenemase), and TMB-1 (Tripoli metallo-beta-lactamase). IMP-1, DIM-1, GIM-1, SIM-1, and TMB-1 are Class 1 integron-mediated MBLs, KMH-1 is plasmid-mediated. 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 acquired 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: 293859 [Multi-domain]  Cd Length: 215  Bit Score: 36.11  E-value: 6.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  14 LVVVDGKK-YVVDTglPGNERRIAEAVK-------ECEGIILTHSHFDHMGSARALSKIlKSKVYAHPKEFEYLKGIKK- 84
Cdd:cd16301   32 LVVVDGKEaYLIDT--PWSESDTEKLVEwikaqglTLKASISTHFHEDRTGGIGYLNSH-SIPTYASELTNQLLKKNGKe 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 288895134  85 ---HEYKGliGSFarfyeSIKKPKyleevesveelkdLEIIHT-PGHTEGSISILVGDS--LICGDLVRckvfsdnpTLS 158
Cdd:cd16301  109 latHSFSG--DEF-----WLLKGK-------------IEVFYPgAGHTKDNLVVWLPKEkiLFGGCLVK--------SLE 160

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 288895134 159 SKNFNW----NDEEYRRSLRKVL-KF-EFEKLYPGHGRV 191
Cdd:cd16301  161 SKGLGNtgdaSISQWPASAQKVLsKYpNAKLVVPGHGKV 199
 
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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