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Conserved domains on  [gi|446279048|ref|WP_000356903|]
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MULTISPECIES: MBL fold metallo-hydrolase [Bacillus]

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 ...
 38-249 4.52e-71

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: 217.47  E-value: 4.52e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  38 IVNICFVGNPktNDFVLVDAGMPKCANEIISIAEDRFGTNSRPKAIILTHGHFDHVGGIIELIKYWDVPVYAHQMEIPFL 117
Cdd:cd07721   10 PVNAYLIEDD--DGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEREAPYL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 118 TGQQSYPepdPTVEGGMVAKMSPLFPNEPIDlgnSVKALPTDGTVPHMPEFRWIHTSGHTPGHISLFREKDRTLIAGDAF 197
Cdd:cd07721   88 EGEKPYP---PPVRLGLLGLLSPLLPVKPVP---VDRTLEDGDTLDLAGGLRVIHTPGHTPGHISLYLEEDGVLIAGDAL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446279048 198 VTVKqeylykvitqeQEISGPPRYLTTDWKAAKESVIKLEELKPLVAITGHG 249
Cdd:cd07721  162 VTVG-----------GELVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
 
Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 38-249 4.52e-71

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: 217.47  E-value: 4.52e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  38 IVNICFVGNPktNDFVLVDAGMPKCANEIISIAEDRFGTNSRPKAIILTHGHFDHVGGIIELIKYWDVPVYAHQMEIPFL 117
Cdd:cd07721   10 PVNAYLIEDD--DGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEREAPYL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 118 TGQQSYPepdPTVEGGMVAKMSPLFPNEPIDlgnSVKALPTDGTVPHMPEFRWIHTSGHTPGHISLFREKDRTLIAGDAF 197
Cdd:cd07721   88 EGEKPYP---PPVRLGLLGLLSPLLPVKPVP---VDRTLEDGDTLDLAGGLRVIHTPGHTPGHISLYLEEDGVLIAGDAL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446279048 198 VTVKqeylykvitqeQEISGPPRYLTTDWKAAKESVIKLEELKPLVAITGHG 249
Cdd:cd07721  162 VTVG-----------GELVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 27-274 1.39e-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: 129.43  E-value: 1.39e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  27 VLPDLFCYTIQIVNICFVGNpkTNDFVLVDAGM-PKCANEIISIAEDRfgtNSRPKAIILTHGHFDHVGGIIELIKYWDV 105
Cdd:COG0491    3 VLPGGTPGAGLGVNSYLIVG--GDGAVLIDTGLgPADAEALLAALAAL---GLDIKAVLLTHLHPDHVGGLAALAEAFGA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 106 PVYAHQMEIPFLTGqqsyPEPDPTVEGGMVAKMSPLFPNEPIDLGNsvkalptdgtvphmPEFRWIHTSGHTPGHISLFR 185
Cdd:COG0491   78 PVYAHAAEAEALEA----PAAGALFGREPVPPDRTLEDGDTLELGG--------------PGLEVIHTPGHTPGHVSFYV 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 186 EKDRTLIAGDAFVTvkqeylykvitqeqEISGPPRYLTTDWKAAKESVIKLEELKPLVAITGHGIPMSGELLSTsLKTLV 265
Cdd:COG0491  140 PDEKVLFTGDALFS--------------GGVGRPDLPDGDLAQWLASLERLLALPPDLVIPGHGPPTTAEAIDY-LEELL 204


                 ....*....
gi 446279048 266 QEFDKIAVP 274
Cdd:COG0491  205 AALGERANP 213
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
38-248 3.55e-31

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 115.16  E-value: 3.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048   38 IVNICFVGNPKTNdfVLVDAGMPkCANEIISIAEDRFGTNSRPKAIILTHGHFDHVGGIIELIKYWDVPVYAHQMEIPFL 117
Cdd:pfam00753   5 QVNSYLIEGGGGA--VLIDTGGS-AEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAREL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  118 TGQqsypepdptvEGGMVAKMSPLFPNEPIDLGNSVKALPTDGTVPHMPEFRWIHTSGHTPGHISLFREKDRTLIAGDAF 197
Cdd:pfam00753  82 LDE----------ELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLL 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446279048  198 VTVKQEYLYKvitqeqEISGPPRYLTTDWKAAKESVIKLEELKPLVAITGH 248
Cdd:pfam00753 152 FAGEIGRLDL------PLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 40-248 4.77e-29

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: 108.79  E-value: 4.77e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048    40 NICFVGNPKTNdfVLVDAGMPKCANEIISIAEDRfgtNSRPKAIILTHGHFDHVGGIIELIKYWDVPVYAHQMEIPFLTG 119
Cdd:smart00849   1 NSYLVRDDGGA--ILIDTGPGEAEDLLAELKKLG---PKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKD 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048   120 QQSYPEPdPTVEGGMVAKMSPLFPNEPIDLGNsvkalptdgtvphmPEFRWIHTSGHTPGHISLFREKDRTLIAGDAFVT 199
Cdd:smart00849  76 LLALLGE-LGAEAEPAPPDRTLKDGDELDLGG--------------GELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFA 140

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 446279048   200 VKQEYLYKVitqeqeisgPPRYLTTDWkaaKESVIKLEELKPLVAITGH 248
Cdd:smart00849 141 GGDGRTLVD---------GGDAAASDA---LESLLKLLKLLPKLVVPGH 177
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 53-195 2.81e-13

hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione hydrolase, a detoxification enzyme known as glyoxalase II. It follows lactoylglutathione lyase, or glyoxalase I, and acts to remove the toxic metabolite methylglyoxal and related compounds. This protein belongs to the broader metallo-beta-lactamase family (pfam00753). [Cellular processes, Detoxification]


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 67.95  E-value: 2.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048   53 VLVDAGmpkCANEIISIAEDRfgtNSRPKAIILTHGHFDHVGGIIELIKYWDVPVYAHQME-IPFLTgqqsypepdPTVE 131
Cdd:TIGR03413  23 AVVDPG---EAEPVLDALEAR---GLTLTAILLTHHHHDHVGGVAELLEAFPAPVYGPAEErIPGIT---------HPVK 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446279048  132 GGmvakmsplfpnEPIDLGNSvkalptdgtvphmpEFRWIHTSGHTPGHISLFREKDRTLIAGD 195
Cdd:TIGR03413  88 DG-----------DTVTLGGL--------------EFEVLAVPGHTLGHIAYYLPDSPALFCGD 126
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 53-184 7.42e-06

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 46.36  E-value: 7.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  53 VLVDAGmpKCANEIISIAEDRFgtnsRPKAIILTHGHFDHVGGIIELIKYWdvpvyahqmeipfltgqqsypePDPTVEG 132
Cdd:PRK10241  25 LIVDPG--EAEPVLNAIAENNW----QPEAIFLTHHHHDHVGGVKELVEKF----------------------PQIVVYG 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446279048 133 gmvakmsplfPNEPIDLGNSVKALPTDGTVPHMPEFRWIHTSGHTPGHISLF 184
Cdd:PRK10241  77 ----------PQETQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF 118
 
Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 38-249 4.52e-71

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: 217.47  E-value: 4.52e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  38 IVNICFVGNPktNDFVLVDAGMPKCANEIISIAEDRFGTNSRPKAIILTHGHFDHVGGIIELIKYWDVPVYAHQMEIPFL 117
Cdd:cd07721   10 PVNAYLIEDD--DGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEREAPYL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 118 TGQQSYPepdPTVEGGMVAKMSPLFPNEPIDlgnSVKALPTDGTVPHMPEFRWIHTSGHTPGHISLFREKDRTLIAGDAF 197
Cdd:cd07721   88 EGEKPYP---PPVRLGLLGLLSPLLPVKPVP---VDRTLEDGDTLDLAGGLRVIHTPGHTPGHISLYLEEDGVLIAGDAL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446279048 198 VTVKqeylykvitqeQEISGPPRYLTTDWKAAKESVIKLEELKPLVAITGHG 249
Cdd:cd07721  162 VTVG-----------GELVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 27-274 1.39e-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: 129.43  E-value: 1.39e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  27 VLPDLFCYTIQIVNICFVGNpkTNDFVLVDAGM-PKCANEIISIAEDRfgtNSRPKAIILTHGHFDHVGGIIELIKYWDV 105
Cdd:COG0491    3 VLPGGTPGAGLGVNSYLIVG--GDGAVLIDTGLgPADAEALLAALAAL---GLDIKAVLLTHLHPDHVGGLAALAEAFGA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 106 PVYAHQMEIPFLTGqqsyPEPDPTVEGGMVAKMSPLFPNEPIDLGNsvkalptdgtvphmPEFRWIHTSGHTPGHISLFR 185
Cdd:COG0491   78 PVYAHAAEAEALEA----PAAGALFGREPVPPDRTLEDGDTLELGG--------------PGLEVIHTPGHTPGHVSFYV 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 186 EKDRTLIAGDAFVTvkqeylykvitqeqEISGPPRYLTTDWKAAKESVIKLEELKPLVAITGHGIPMSGELLSTsLKTLV 265
Cdd:COG0491  140 PDEKVLFTGDALFS--------------GGVGRPDLPDGDLAQWLASLERLLALPPDLVIPGHGPPTTAEAIDY-LEELL 204


                 ....*....
gi 446279048 266 QEFDKIAVP 274
Cdd:COG0491  205 AALGERANP 213
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
38-248 3.55e-31

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 115.16  E-value: 3.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048   38 IVNICFVGNPKTNdfVLVDAGMPkCANEIISIAEDRFGTNSRPKAIILTHGHFDHVGGIIELIKYWDVPVYAHQMEIPFL 117
Cdd:pfam00753   5 QVNSYLIEGGGGA--VLIDTGGS-AEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAREL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  118 TGQqsypepdptvEGGMVAKMSPLFPNEPIDLGNSVKALPTDGTVPHMPEFRWIHTSGHTPGHISLFREKDRTLIAGDAF 197
Cdd:pfam00753  82 LDE----------ELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLL 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 446279048  198 VTVKQEYLYKvitqeqEISGPPRYLTTDWKAAKESVIKLEELKPLVAITGH 248
Cdd:pfam00753 152 FAGEIGRLDL------PLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 40-248 4.77e-29

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: 108.79  E-value: 4.77e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048    40 NICFVGNPKTNdfVLVDAGMPKCANEIISIAEDRfgtNSRPKAIILTHGHFDHVGGIIELIKYWDVPVYAHQMEIPFLTG 119
Cdd:smart00849   1 NSYLVRDDGGA--ILIDTGPGEAEDLLAELKKLG---PKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKD 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048   120 QQSYPEPdPTVEGGMVAKMSPLFPNEPIDLGNsvkalptdgtvphmPEFRWIHTSGHTPGHISLFREKDRTLIAGDAFVT 199
Cdd:smart00849  76 LLALLGE-LGAEAEPAPPDRTLKDGDELDLGG--------------GELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFA 140

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 446279048   200 VKQEYLYKVitqeqeisgPPRYLTTDWkaaKESVIKLEELKPLVAITGH 248
Cdd:smart00849 141 GGDGRTLVD---------GGDAAASDA---LESLLKLLKLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 39-195 7.41e-28

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: 105.83  E-value: 7.41e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  39 VNICFVGNPKtNDFVLVDAGMPkCANEIISIAEDRfgtNSRPKAIILTHGHFDHVGGIIELIKYWDVPVYAHQMEIPFLT 118
Cdd:cd06262   10 TNCYLVSDEE-GEAILIDPGAG-ALEKILEAIEEL---GLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAELLE 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446279048 119 gqqsypEPDPTVEGGMVAKMSPLFPNEPIDLGNSVKALPTdgtvphmpEFRWIHTSGHTPGHISLFREKDRTLIAGD 195
Cdd:cd06262   85 ------DPELNLAFFGGGPLPPPEPDILLEDGDTIELGGL--------ELEVIHTPGHTPGSVCFYIEEEGVLFTGD 147
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 37-195 3.46e-21

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: 87.98  E-value: 3.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  37 QIVNIC-FVGNPKTNDFVLVDAgmpkcANEIISIAEDRFGTNSRPKAIILTHGHFDHVGGIIELIKYWDVPVYAHQMEIP 115
Cdd:cd16275    9 PMINYSyIIIDKATREAAVVDP-----AWDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEID 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 116 FltgqqsYPEPDPtveggmvaKMSPLFPNEPIDLGNSvkalptdgtvphmpEFRWIHTSGHTPGHISlFREKDRtLIAGD 195
Cdd:cd16275   84 Y------YGFRCP--------NLIPLEDGDTIKIGDT--------------EITCLLTPGHTPGSMC-YLLGDS-LFTGD 133
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 44-198 1.28e-19

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: 83.28  E-value: 1.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  44 VGNPKTNDFVLVDAGMPKcanEIISIAEDRFGTnsrPKAIILTHGHFDHVGGIIELIKYW-DVPVYAHQME-IPFLTgqq 121
Cdd:cd07723   14 IVDEATGEAAVVDPGEAE---PVLAALEKNGLT---LTAILTTHHHWDHTGGNAELKALFpDAPVYGPAEDrIPGLD--- 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446279048 122 sypepdptveggmvakmSPLFPNEPIDLGNSvkalptdgtvphmpEFRWIHTSGHTPGHISLFREKDRTLIAGDA-FV 198
Cdd:cd07723   85 -----------------HPVKDGDEIKLGGL--------------EVKVLHTPGHTLGHICYYVPDEPALFTGDTlFS 131
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 46-195 5.76e-19

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: 82.22  E-value: 5.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  46 NPKTNDFVLVDAGMPkcANEIISIAEDRfgtNSRPKAIILTHGHFDHVGGIIELIKYWDVPVYA-HQMEIPFLTG--QQS 122
Cdd:cd07737   18 CEETKEAAVIDPGGD--ADKILQAIEDL---GLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGpHKEDKFLLENlpEQS 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446279048 123 ypepdptvEGGMVAKMSPLFP------NEPIDLGNSvkalptdgtvphmpEFRWIHTSGHTPGHISLFREKDRTLIAGD 195
Cdd:cd07737   93 --------QMFGFPPAEAFTPdrwleeGDTVTVGNL--------------TLEVLHCPGHTPGHVVFFNRESKLAIVGD 149
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 53-197 4.96e-16

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: 74.20  E-value: 4.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  53 VLVDAGMPkcaneIISIAEDRFGTNSRPKAIILTHGHFDHVGGIIELIKywdvpVYAHQMEIPFL---TGQQSYPEPDPT 129
Cdd:cd07712   21 LLIDTGLG-----IGDLKEYVRTLTDLPLLVVATHGHFDHIGGLHEFEE-----VYVHPADAEILaapDNFETLTWDAAT 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446279048 130 VEGGMVAKMSPLFPNEPIDLGNSVkalptdgtvphmpeFRWIHTSGHTPGHISLFREKDRTLIAGDAF 197
Cdd:cd07712   91 YSVPPAGPTLPLRDGDVIDLGDRQ--------------LEVIHTPGHTPGSIALLDRANRLLFSGDVV 144
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 38-195 6.80e-16

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: 74.31  E-value: 6.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  38 IVNICFVGNPKTNDFVLVDAGMPKcaneiiSIAEDRFGTNS-RPKAIILTHGHFDHVGGIIELIKYWDVPVYAHQMEIP- 115
Cdd:cd16322   10 QENTYLVADEGGGEAVLVDPGDES------EKLLARFGTTGlTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDLPl 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 116 ----------FLTGQQSYPEPDPTVEGGMVakmsplfpnepIDLGNSvkalptdgtvphmpEFRWIHTSGHTPGHISLFR 185
Cdd:cd16322   84 yeaadlgakaFGLGIEPLPPPDRLLEDGQT-----------LTLGGL--------------EFKVLHTPGHSPGHVCFYV 138

                        170
                 ....*....|
gi 446279048 186 EKDRTLIAGD 195
Cdd:cd16322  139 EEEGLLFSGD 148
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 39-248 1.57e-13

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 67.56  E-value: 1.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  39 VNICFVGNpKTNDFVLVDAGMPKC----ANEIISIAEDRfgtnsrPKAIILTHGHFDHVGGIIELIKYWDVPVYAHQMEI 114
Cdd:cd07743    8 TNIGVYVF-GDKEALLIDSGLDEDagrkIRKILEELGWK------LKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 115 PFLTgqqsYPEPDPTVEGG---MVAKMSPLFPNEPIDlgnsVKALPTDGTVPHMP-EFRWIHTSGHTPGHISlFREKDRT 190
Cdd:cd07743   81 AFIE----NPLLEPSYLGGaypPKELRNKFLMAKPSK----VDDIIEEGELELGGvGLEIIPLPGHSFGQIG-ILTPDGV 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446279048 191 LIAGDAFVTvkQEYLYKVitqeqeisGPPrYLtTDWKAAKESVIKLEELKPLVAITGH 248
Cdd:cd07743  152 LFAGDALFG--EEVLEKY--------GIP-FL-YDVEEQLETLEKLEELDADYYVPGH 197
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 53-195 2.81e-13

hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione hydrolase, a detoxification enzyme known as glyoxalase II. It follows lactoylglutathione lyase, or glyoxalase I, and acts to remove the toxic metabolite methylglyoxal and related compounds. This protein belongs to the broader metallo-beta-lactamase family (pfam00753). [Cellular processes, Detoxification]


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 67.95  E-value: 2.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048   53 VLVDAGmpkCANEIISIAEDRfgtNSRPKAIILTHGHFDHVGGIIELIKYWDVPVYAHQME-IPFLTgqqsypepdPTVE 131
Cdd:TIGR03413  23 AVVDPG---EAEPVLDALEAR---GLTLTAILLTHHHHDHVGGVAELLEAFPAPVYGPAEErIPGIT---------HPVK 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446279048  132 GGmvakmsplfpnEPIDLGNSvkalptdgtvphmpEFRWIHTSGHTPGHISLFREKDRTLIAGD 195
Cdd:TIGR03413  88 DG-----------DTVTLGGL--------------EFEVLAVPGHTLGHIAYYLPDSPALFCGD 126
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 34-254 4.53e-13

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: 66.17  E-value: 4.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  34 YTIQIVNICFVGNpkTNDFV--------LVDAGMPKCAN--EIISIAEDRFGTNSRPKAIILTHGHFDHVGGIIELIKYW 103
Cdd:cd07725    2 YRLSLPLPGPLGH--VNVYLlrdgdettLIDTGLATEEDaeALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 104 DVPVYAhqmeipfltgqqsypePDPTveggmvakmsplfpnePIDLGNSVKALPTDGTVphmpefrwIHTSGHTPGHISL 183
Cdd:cd07725   80 GATVYI----------------LDVT----------------PVKDGDKIDLGGLRLKV--------IETPGHTPGHIVL 119

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446279048 184 FREKDRTLIAGDAfvtVKQEYLYKVITQEQEISGP-PRYLttdwkaakESVIKLEELKPLVAITGHGIPMSG 254
Cdd:cd07725  120 YDEDRRELFVGDA---VLPKITPNVSLWAVRVEDPlGAYL--------ESLDKLEKLDVDLAYPGHGGPIKD 180
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 38-249 1.86e-12

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: 64.89  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  38 IVNICFVgnpKTNDFVLV-DAGM-PKCANEII-SIAEDrfgTNSRPKAIILTHGHFDHVGGiielIKYW---DVPVYAH- 110
Cdd:cd16282   14 ISNIGFI---VGDDGVVViDTGAsPRLARALLaAIRKV---TDKPVRYVVNTHYHGDHTLG----NAAFadaGAPIIAHe 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 111 -------QMEIPFLTGQQSYPE----------PDPTVEGGMVakmsplfpnepIDLGNSvkalptdgtvphmpEFRWIHT 173
Cdd:cd16282   84 ntreelaARGEAYLELMRRLGGdamagtelvlPDRTFDDGLT-----------LDLGGR--------------TVELIHL 138

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446279048 174 S-GHTPGHISLFREKDRTLIAGDAFvtvkqeylykvitqeqEISGPPRYLTTDWKAAKESVIKLEELKPLVAITGHG 249
Cdd:cd16282  139 GpAHTPGDLVVWLPEEGVLFAGDLV----------------FNGRIPFLPDGSLAGWIAALDRLLALDATVVVPGHG 199
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 53-248 2.69e-12

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: 64.93  E-value: 2.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  53 VLVDAGMPKCANEIISIAEDRFGTNSRP------------------KAIILTHGHFDHVGGiIELIKywDVPVYAHQMEI 114
Cdd:cd07729   44 ILVDTGFHPDAADDPGGLELAFPPGVTEeqtleeqlarlgldpediDYVILSHLHFDHAGG-LDLFP--NATIIVQRAEL 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 115 PFLTGqqsypePDPTVEGGMVAKMSPLFPNEPIDLGnsvkalPTDGTVPHMPEFRWIHTSGHTPGHISLF--REKDRTLI 192
Cdd:cd07729  121 EYATG------PDPLAAGYYEDVLALDDDLPGGRVR------LVDGDYDLFPGVTLIPTPGHTPGHQSVLvrLPEGTVLL 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446279048 193 AGDAFvtvkqeYLYKVItqEQEISGPPRYLTTDWKAAKESVIKLEELKPLVAITGH 248
Cdd:cd07729  189 AGDAA------YTYENL--EEGRPPGINYDPEAALASLERLKALAEREGARVIPGH 236
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 34-195 2.20e-11

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: 61.40  E-value: 2.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  34 YTIQIVNICFVGNPKTndFVLVDAGMPKcaNEIISIAED--RFGTNSRPKAIILTHGHFDHVGG---IIELIKYWDVPVY 108
Cdd:cd07722   13 FTLQGTNTYLVGTGKR--RILIDTGEGR--PSYIPLLKSvlDSEGNATISDILLTHWHHDHVGGlpdVLDLLRGPSPRVY 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 109 AHQmeipfltgqqsyPEPDPTVEGGMVAKMSPLFPNEpidlgnsvkALPTDGTvphmpEFRWIHTSGHTPGHISLFREKD 188
Cdd:cd07722   89 KFP------------RPEEDEDPDEDGGDIHDLQDGQ---------VFKVEGA-----TLRVIHTPGHTTDHVCFLLEEE 142


                 ....*..
gi 446279048 189 RTLIAGD 195
Cdd:cd07722  143 NALFTGD 149
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 53-241 3.03e-11

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: 61.35  E-value: 3.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  53 VLVDAGMPKCANEIISIAEDRFGTNSRPKAIILTHGHFDHVGGIIELIKYW-DVPVYAHQMEIPFLT--------GQQSY 123
Cdd:cd07726   28 ALIDTGPSSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLAEALpNAKVYVHPRGARHLIdpsklwasARAVY 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 124 PEPDPTVEGGMV----AKMSPLFPNEPIDLGNSvkalptdgtvphmpEFRWIHTSGHTPGHISLFREKDRTLIAGDAF-V 198
Cdd:cd07726  108 GDEADRLGGEILpvpeERVIVLEDGETLDLGGR--------------TLEVIDTPGHAPHHLSFLDEESDGLFTGDAAgV 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446279048 199 TVKqeylykvitqeqEISGPPRYLTT----DWKAAKESVIKLEELKP 241
Cdd:cd07726  174 RYP------------ELDVVGPPSTPppdfDPEAWLESLDRLLSLKP 208
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 79-195 1.52e-10

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: 59.04  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  79 RPKAIILTHGHFDHVGGIIELIKYWDVPVYAHqmEIPFLTGQQSYPEPDPTVEGGMVakmsplfpnepidlgnsvkaLPT 158
Cdd:cd16278   53 RVSAILVTHTHRDHSPGAARLAERTGAPVRAF--GPHRAGGQDTDFAPDRPLADGEV--------------------IEG 110

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446279048 159 DGTvphmpEFRWIHTSGHTPGHISLFREKDRTLIAGD 195
Cdd:cd16278  111 GGL-----RLTVLHTPGHTSDHLCFALEDEGALFTGD 142
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 40-194 6.50e-10

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: 58.37  E-value: 6.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  40 NICFVGNP-------KTND-FVLVDAGMPKCANEIISIAEDRFGTN-SRPKAIILTHGHFDHVGGIIELIKYWDVPVYAH 110
Cdd:cd16280   13 NLYYVGNKwvsawaiDTGDgLILIDALNNNEAADLIVDGLEKLGLDpADIKYILITHGHGDHYGGAAYLKDLYGAKVVMS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 111 Q-----MEIPFLTGQQSY----PEPDPTVEGGmvakmsplfpnEPIDLGNSvkalptdgtvphmpEFRWIHTSGHTPGHI 181
Cdd:cd16280   93 EadwdmMEEPPEEGDNPRwgppPERDIVIKDG-----------DTLTLGDT--------------TITVYLTPGHTPGTL 147

                        170
                 ....*....|....*.
gi 446279048 182 SLF---REKDRTLIAG 194
Cdd:cd16280  148 SLIfpvKDGGKTHRAG 163
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 34-251 1.06e-09

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: 56.83  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  34 YTIQIVNICFVGNP-----KTNDF-VLVDAGMPKCANEIISIAEDRfgtNSRPKAI---ILTHGHFDHVGGiIELIKywD 104
Cdd:cd07711    9 YARRDSDGGFRASStvtliKDGGKnILVDTGTPWDRDLLLKALAEH---GLSPEDIdyvVLTHGHPDHIGN-LNLFP--N 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 105 VPVYAHQMEIpfltgqqsypepdptvegGMVAKMSPLFPNEPIDLGNSVKAlptdgtvphmpefrwIHTSGHTPGHISLF 184
Cdd:cd07711   83 ATVIVGWDIC------------------GDSYDDHSLEEGDGYEIDENVEV---------------IPTPGHTPEDVSVL 129

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 185 --REKDRT-LIAGDAFvtvKQEYLYKVITQEQEISgppryltTDWKAAKESVIKLEELKPLVaITGHGIP 251
Cdd:cd07711  130 veTEKKGTvAVAGDLF---EREEDLEDPILWDPLS-------EDPELQEESRKRILALADWI-IPGHGPP 188
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 81-239 1.18e-08

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


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 54.58  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  81 KAIILTHGHFDHVGGIIELIKywdVPVYAHQMEIPFLTGQQSYPEPDPtveggmvakmsPLFPNEPIDLGNSVKALPTDG 160
Cdd:cd07730   85 DAVILSHLHWDHIGGLSDFPN---ARLIVGPGAKEALRPPGYPSGFLP-----------ELLPSDFEGRLVRWEEDDFLW 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 161 TvPHMPEFR----------WI-HTSGHTPGHISLF-REKDRT--LIAGDAFVTVKQEylykvITQEQEISGPPRYLTTDW 226
Cdd:cd07730  151 V-PLGPFPRaldlfgdgslYLvDLPGHAPGHLGLLaRTTSGTwvFLAGDACHHRIGL-----LRPSPLLPLPDLDDGADR 224

                        170
                 ....*....|...
gi 446279048 227 KAAKESVIKLEEL 239
Cdd:cd07730  225 EAARETLARLREL 237
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
79-109 2.69e-08

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 54.30  E-value: 2.69e-08
                         10        20        30
                 ....*....|....*....|....*....|.
gi 446279048  79 RPKAIILTHGHFDHVGGIIELIKYWDVPVYA 109
Cdd:COG0595   63 KIKGIVLTHGHEDHIGALPYLLKELNVPVYG 93
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 29-198 2.81e-08

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: 52.40  E-value: 2.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  29 PDLFCYTIqivnicFVGNPKTNDFVLVDAgMPKCANEIISIAEDRfgtNSRPKAIILTHGHFDHVGGIIELIKYWDVPVY 108
Cdd:cd07724    8 PGLGTLSY------LVGDPETGEAAVIDP-VRDSVDRYLDLAAEL---GLKITYVLETHVHADHVSGARELAERTGAPIV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 109 AHqmeipfltgqqsypepdPTVEGGMVAKmsPLFPNEPIDLGN-SVKAlptdgtvphmpefrwIHTSGHTPGHISLFREK 187
Cdd:cd07724   78 IG-----------------EGAPASFFDR--LLKDGDVLELGNlTLEV---------------LHTPGHTPESVSYLVGD 123

                        170
                 ....*....|..
gi 446279048 188 DRTLIAGDA-FV 198
Cdd:cd07724  124 PDAVFTGDTlFV 135
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 ...
 53-182 4.83e-08

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


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 52.74  E-value: 4.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  53 VLVDAGMPKCANEIIS-IAedRFGTNSRP-KAIILTHGHFDHVGGIIELIKYWDVPVYAHQMEIPFLTGQQSYPEpDPTV 130
Cdd:cd16290   34 ILIDGALPQSAPQIEAnIR--ALGFRLEDvKLILNSHAHFDHAGGIAALQRDSGATVAASPAGAAALRSGGVDPD-DPQA 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446279048 131 EGGM----VAKMSPLFPNEPIDLGN-SVKAlptdgtvpHmpefrwiHTSGHTPGHIS 182
Cdd:cd16290  111 GAADpfppVAKVRVVADGEVVKLGPlAVTA--------H-------ATPGHTPGGTS 152
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 53-182 6.22e-08

Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of THIN-B2-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: 293869  Cd Length: 257  Bit Score: 52.68  E-value: 6.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  53 VLVDAGMPKCANEIIS-IAEDRFGTNSrPKAIILTHGHFDHVGGIIELIKYWDVPVYAHQMEIPFLTGQQSYPEpDPTVE 131
Cdd:cd16311   34 VLVDGGLPESAPKIIAnIEALGFRIED-VKLILNSHGHIDHAGGLAELQRRSGALVAASPSAALDLASGEVGPD-DPQYH 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446279048 132 ggmvakMSPLFPNEPidlgnSVKALPTDGTVPHMPEFRWIH-TSGHTPGHIS 182
Cdd:cd16311  112 ------ALPKYPPVK-----DMRLARDGGQFNVGPVSLTAHaTPGHTPGGLS 152
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 50-109 7.92e-08

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: 52.02  E-value: 7.92e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  50 NDFVLVDAGMpKCANEI----------ISIAEDRFgtnSRPKAIILTHGHFDHVGGIIELIKYWDVPVYA 109
Cdd:cd07714   20 DDIIIIDCGL-KFPDEDmpgvdyiipdFSYLEENK---DKIKGIFITHGHEDHIGALPYLLPELNVPIYA 85
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 53-182 9.01e-08

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


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 51.97  E-value: 9.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  53 VLVDAGMPKCANEIIS-IAedRFGTNSRPKAIILT-HGHFDHVGGIIELIKYWDVPVYAHQMEIPFLTGQQSYPEpDPtv 130
Cdd:cd16315   34 VLIDSGTEEAAPLVLAnIR--KLGFDPKDVRWLLSsHEHFDHVGGLAALQRATGARVAASAAAAPVLESGKPAPD-DP-- 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446279048 131 EGGMVAKMSP------LFPNEPIDLGNSVkalptdgtvphmpeFRWIHTSGHTPGHIS 182
Cdd:cd16315  109 QAGLHEPFPPvrvdriVEDGDTVALGSLR--------------LTAHATPGHTPGALS 152
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 82-197 1.29e-07

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: 51.40  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  82 AIILTHGHFDHVGGII-----------ElikywdvpVYAHQMEIPFLTGQ---QSYPEPDPTVEGGMVAKMSPLFPNEPI 147
Cdd:cd07720   94 DVLLTHLHPDHIGGLVdaggkpvfpnaE--------VHVSEAEWDFWLDDanaAKAPEGAKRFFDAARDRLRPYAAAGRF 165

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446279048 148 DLGNSVkalptdgtvphMPEFRWIHTSGHTPGHiSLFR---EKDRTLIAGDAF 197
Cdd:cd07720  166 EDGDEV-----------LPGITAVPAPGHTPGH-TGYRiesGGERLLIWGDIV 206
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 53-248 5.16e-07

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


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 49.85  E-value: 5.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  53 VLVDAGMPKCANEIISIAEDRFGTNSRPKAIILTHGHFDHVGGIIELIKYWDVPVYAHQMEIPFLTGQQSypePDPTVEG 132
Cdd:cd07708   34 ILIDGDMEQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAEIKKQTGAKVMAGAEDVSLLLSGGS---SDFHYAN 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 133 GMVAKMSPLFPNEPIDLGNSVKALPTDGTVPHMPefrwihtsGHTPGHIS-LFREKD-----RTLIAGDafVTVKQEYly 206
Cdd:cd07708  111 DSSTYFPQSTVDRAVHDGERVTLGGTVLTAHATP--------GHTPGCTTwTMTLKDhgkqyQVVFADS--LTVNPGY-- 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446279048 207 kvitqeqEISGPPRY--LTTDWKAakeSVIKLEELKPLVAITGH 248
Cdd:cd07708  179 -------RLVDNPTYpkIVEDYRH---SFAVVEAMRCDILLGPH 212
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 78-164 9.28e-07

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: 48.24  E-value: 9.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  78 SRPKAIILTHGHFDHVGGIIEL--IKYW---DVPVYAHQMEIPFLtgQQSYPEPDPTVEGGMVAKMSP--LFPNEPIDLG 150
Cdd:cd16279   65 RKLDAVLLTHAHADHIHGLDDLrpFNRLqqrPIPVYASEETLDDL--KRRFPYFFAATGGGGVPKLDLhiIEPDEPFTIG 142

                         90
                 ....*....|....*
gi 446279048 151 N-SVKALPtdgtVPH 164
Cdd:cd16279  143 GlEITPLP----VLH 153
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 53-164 9.88e-07

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 48.74  E-value: 9.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  53 VLVDAGmpkcaneiISIAE--DRFGTN-SRPKAIILTHGHFDHVGGIIELIKYW---DVPVYAHQMEIPFLtgQQSYPEP 126
Cdd:COG1235   47 LLIDAG--------PDLREqlLRLGLDpSKIDAILLTHEHADHIAGLDDLRPRYgpnPIPVYATPGTLEAL--ERRFPYL 116

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446279048 127 DPTVEGGMVAKmsPLFPNEPIDLGN-SVKALPtdgtVPH 164
Cdd:COG1235  117 FAPYPGKLEFH--EIEPGEPFEIGGlTVTPFP----VPH 149
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 40-179 2.50e-06

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: 47.48  E-value: 2.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  40 NICFVGN--------PKTNDFVLVDAGMPKCANEIISIAEdRFGTNSRPKAIIL-THGHFDHVGGIIELIKYWDVPVYAH 110
Cdd:cd16309   13 NIYYVGTaglgvfliTTPEGHILIDGAMPQSTPLIKDNIK-KLGFDVKDVKYLLnTHAHFDHAGGLAELKKATGAQLVAS 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446279048 111 QMEIPFLTGQQSYPEPDPTVeggmvakmspLFPNEPID--LGNSVKALPTDGTV-PHMpefrwihTSGHTPG 179
Cdd:cd16309   92 AADKPLLESGYVGSGDTKNL----------QFPPVRVDrvIGDGDKVTLGGTTLtAHL-------TPGHSPG 146
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 53-182 2.99e-06

Pseudomonas Aeruginosa AIM-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 AIM-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: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 47.58  E-value: 2.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  53 VLVDAGMPKCANEIIS-IAEDRFgtnsRP---KAIILTHGHFDHVGGIIELIKYWDVPVYAHQMEIPFLTGQQSyPEPDP 128
Cdd:cd16314   34 ILIDGGTDKAAPLIEAnIRALGF----RPedvRYIVSSHEHFDHAGGIARLQRATGAPVVAREPAATTLERGRS-DRSDP 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446279048 129 TVEggMVAKMSPLfpnepidlgNSVKALPTDGTVPHMPEFRWIH-TSGHTPGHIS 182
Cdd:cd16314  109 QFL--VVEKFPPV---------ASVQRIGDGEVLRVGPLALTAHaTPGHTPGGTS 152
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 78-110 3.10e-06

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: 47.62  E-value: 3.10e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 446279048  78 SRPKAIILTHGHFDHVGGIIELIKYW-DVPVYAH 110
Cdd:cd07713   54 SDIDAVVLSHGHYDHTGGLKALLELNpKAPVYAH 87
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
50-163 3.43e-06

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 47.11  E-value: 3.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  50 NDFVLVDAGmpkcanEIISIAEDRFGTN-SRPKAIILTHGHFDHVGGIIELIKYW-------DVPVYAHQMEIPFLTGQQ 121
Cdd:COG1234   28 GERLLIDCG------EGTQRQLLRAGLDpRDIDAIFITHLHGDHIAGLPGLLSTRslagrekPLTIYGPPGTKEFLEALL 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446279048 122 SYPEPDPTVEggmvAKMSPLFPNEPIDLGN-SVKALPTDGTVP 163
Cdd:COG1234  102 KASGTDLDFP----LEFHEIEPGEVFEIGGfTVTAFPLDHPVP 140
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 81-251 3.62e-06

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: 46.42  E-value: 3.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  81 KAIILTHGhfDHVGGIIELIKYWDVPVYAHQMEIpfltgqQSYPEPDPtveggmvakmsplfpnepidlgnsVKALPTDG 160
Cdd:cd07727   49 RYIFLTHR--DDVADHAKWAERFGAKRIIHEDDV------NAVTRPDE------------------------VIVLWGGD 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 161 TVPHMPEFRWIHTSGHTPGHISLFREKDRTLIAGD--AFVTVKqeylykvitqeQEISGPPRYLTTDWKAAKESVIKLEE 238
Cdd:cd07727   97 PWELDPDLTLIPVPGHTRGSVVLLYKEKGVLFTGDhlAWSRRR-----------GWLSAFRYVCWYSWPEQAESVERLAD 165

                        170
                 ....*....|...
gi 446279048 239 LKPLVAITGHGIP 251
Cdd:cd07727  166 LDFEWVLPGHGRR 178
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 53-109 3.75e-06

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: 46.68  E-value: 3.75e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446279048  53 VLVDAGMPKCANEIISIAEDRFGTN-SRPKAIILTHGHFDHVGGIIELIKY-WDVPVYA 109
Cdd:cd16295   24 ILLDCGLFQGGKELEELNNEPFPFDpKEIDAVILTHAHLDHSGRLPLLVKEgFRGPIYA 82
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 53-110 4.08e-06

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. 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: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 46.72  E-value: 4.08e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446279048  53 VLVDAGM-PKCANEIISIAEDRFGtnSRP-KAIILTHGHFDHVGG---IIELIKYWDVPVYAH 110
Cdd:cd07710   30 IIIDTLEsAEAAKAALELFRKHTG--DKPvKAIIYTHSHPDHFGGaggFVEEEDSGKVPIIAP 90
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 53-184 7.42e-06

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 46.36  E-value: 7.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  53 VLVDAGmpKCANEIISIAEDRFgtnsRPKAIILTHGHFDHVGGIIELIKYWdvpvyahqmeipfltgqqsypePDPTVEG 132
Cdd:PRK10241  25 LIVDPG--EAEPVLNAIAENNW----QPEAIFLTHHHHDHVGGVKELVEKF----------------------PQIVVYG 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446279048 133 gmvakmsplfPNEPIDLGNSVKALPTDGTVPHMPEFRWIHTSGHTPGHISLF 184
Cdd:PRK10241  77 ----------PQETQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF 118
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 40-111 7.88e-06

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: 44.95  E-value: 7.88e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446279048  40 NICFVGNPKTndFVLVDAGMPkcANEIISIAEDRFGTNSRPKAIILTHGHFDHVGGIIELIKYWDVPVYAHQ 111
Cdd:cd07733   10 NCTYLETEDG--KLLIDAGLS--GRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIYATA 77
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
82-110 8.17e-06

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 46.03  E-value: 8.17e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 446279048  82 AIILTHGHFDHVGGIIELIKYW-DVPVYAH 110
Cdd:COG1237   60 AVVLSHGHYDHTGGLPALLELNpKAPVYAH 89
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
42-97 9.24e-06

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 46.11  E-value: 9.24e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446279048  42 CFVGNPKTNDFVLVDAGmpkCANEIISIAEDRFGTNSRP-------KAIILTHGHFDHVGGII 97
Cdd:COG5212   31 YLLRPLGSDDYVLLDAG---TVVSGLELAEQKGAFKGRQgyvlehiKGYLISHAHLDHIAGLP 90
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 53-179 1.18e-05

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


Pssm-ID: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 45.75  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  53 VLVDAGMPKCANEIISIAEDRFGTNSRPKAIILTHGHFDHVGGIIELIKYWDVPVYAHQMEIPFL---TGQQSYPE--PD 127
Cdd:cd16312   34 VLLDGALPQSAPLIIANIEALGFRIEDVKLILNSHAHWDHAGGIAALQKASGATVAASAHGAQVLqsgTNGKDDPQyqAK 113

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446279048 128 PTVEGGMVAKMSPLFPNEPIDLGnsvkalPTDGTVpHMpefrwihTSGHTPG 179
Cdd:cd16312  114 PVVHVAKVAKVKEVGEGDTLKVG------PLRLTA-HM-------TPGHTPG 151
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 78-173 1.35e-05

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: 44.99  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048   78 SRPKAIILTHGHFDHVGGIIELIKYWDVPVYAHQMEIPFLTGQQSYPEPDPtvEGGMVAKmsPLFPNEPIDLGN---SVK 154
Cdd:pfam12706  27 DPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLRRNFPYLFLLE--HYGVRVH--EIDWGESFTVGDgglTVT 102

                          90       100
                  ....*....|....*....|
gi 446279048  155 ALPtdgtVPHM-PEFRWIHT 173
Cdd:pfam12706 103 ATP----ARHGsPRGLDPNP 118
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 53-182 1.63e-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: 45.24  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  53 VLVDAGMPKCAnEIISIAEDRFGTNSRP-KAIILTHGHFDHVGGIIELIKYWDVPVYAHQMEIPFLTGQQSyPEPDPTVE 131
Cdd:cd16313   34 ILIDGGFPKSP-EQIAASIRQLGFKLEDvKYILSSHDHWDHAGGIAALQKLTGAQVLASPATVAVLRSGSM-GKDDPQFG 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446279048 132 GgmVAKMSPLFPNEPIDLGNSVKALPTDGTVPHMPefrwihtsGHTPGHIS 182
Cdd:cd16313  112 G--LTPMPPVASVRAVRDGEVVKLGPLAVTAHATP--------GHTTGGTS 152
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 53-141 4.46e-05

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: 43.43  E-value: 4.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  53 VLVDAGM-PKCANEIISIAEDRFGtnSRPKAIILTHGHFDHVGGiIELIKYWDVPVYAHQMEIPfLTGQQSYPEPDPTVE 131
Cdd:cd16285   38 VLIDTPWtEAQTATLLDWIEKKLG--KPVTAAISTHSHDDRTGG-IKALNARGIPTYATALTNE-LAKKEGKPVPTHSLK 113

                         90
                 ....*....|
gi 446279048 132 GGMVAKMSPL 141
Cdd:cd16285  114 GALTLGFGPL 123
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 50-103 6.42e-05

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: 42.64  E-value: 6.42e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446279048  50 NDFVLVDAG---MPKCANEIISIAEdrfgtnsrPKAIILTHGHFDHVGGIIELIKYW 103
Cdd:cd16272   26 GTRILLDCGegtVYRLLKAGVDPDK--------LDAIFLSHFHLDHIGGLPTLLFAR 74
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 53-195 7.78e-05

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 43.64  E-value: 7.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  53 VLVDAGM---PKCANEiisiaeDRFGTN-SRPKAIILTHGHFDHVGGIIELIK-YWDVPVYAHQ-----MEI-----PFL 117
Cdd:COG1236   26 ILIDCGLfqgGKERNW------PPFPFRpSDVDAVVLTHAHLDHSGALPLLVKeGFRGPIYATPatadlARIllgdsAKI 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 118 TGQQSYPEPDPTVEGgmVAKMSPLF----PNEPIDLGNsVKAlptdgtvphmpEFrwiHTSGHTPG--HISLFREKDRTL 191
Cdd:COG1236  100 QEEEAEAEPLYTEED--AERALELFqtvdYGEPFEIGG-VRV-----------TF---HPAGHILGsaQVELEVGGKRIV 162


                 ....
gi 446279048 192 IAGD 195
Cdd:COG1236  163 FSGD 166
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 53-105 9.58e-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: 42.92  E-value: 9.58e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  53 VLVDAGmpkcANEIISIAED-------RFGTNsRPKAIILTHGHFDHVGGIIELIKYWDV 105
Cdd:COG2333   24 ILIDTG----PRPSFDAGERvvlpylrALGIR-RLDLLVLTHPDADHIGGLAAVLEAFPV 78
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 83-197 1.09e-04

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  83 IILTHGHFDHVGgiielikyWD--------VP------VYAHQMEIPFLTGQQSYPEPDPTVEGGMVAkmsplfpnePID 148
Cdd:cd16277   67 VLCTHLHVDHVG--------WNtrlvdgrwVPtfpnarYLFSRAEYDHWSSPDAGGPPNRGVFEDSVL---------PVI 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446279048 149 LGNSVKALPTDGTVPhmPEFRWIHTSGHTPGHIS--LFREKDRTLIAGDAF 197
Cdd:cd16277  130 EAGLADLVDDDHEIL--DGIRLEPTPGHTPGHVSveLESGGERALFTGDVM 178
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 65-138 1.49e-04

Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Bacillus cereus Beta-lactamase 2, also called BcII. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. BcII is a chromosome-encoded B1 MBL. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293862 [Multi-domain]  Cd Length: 212  Bit Score: 41.89  E-value: 1.49e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446279048  65 EIISIAEDRFgtNSRPKAIILTHGHFDHVGGIIELIKYwDVPVYAHQMEIPfLTGQQSYPEPDPTVEGGMVAKM 138
Cdd:cd16304   51 ELLDWIKKKL--KKPVTLAIVTHAHDDRIGGIKALQKR-GIPVYSTKLTAQ-LAKKQGYPSPDGILKDDTTLKF 120
PRK02113 PRK02113
MBL fold metallo-hydrolase;
82-124 1.77e-04

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 42.08  E-value: 1.77e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446279048  82 AIILTHGHFDHVGGIIEL---IKYWDVPVYAHQ-------MEIPFLTGQQSYP 124
Cdd:PRK02113  69 AVLITHEHYDHVGGLDDLrpfCRFGEVPIYAEQyvaerlrSRMPYCFVEHSYP 121
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 53-197 1.86e-04

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


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 41.70  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  53 VLVDAGMPKCANEIISIAEDRFGtNSRPKAIILTHGHFDHVGGIIELIKYW-DVPVYAHQMEIPFLTGQQSYPEPDP-TV 130
Cdd:cd07709   43 ALIDTVKEPFFDEFLENLEEVID-PRKIDYIVVNHQEPDHSGSLPELLELApNAKIVCSKKAARFLKHFYPGIDERFvVV 121

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446279048 131 EGGMVakmsplfpnepIDLGN-SVKALPTdgtvpHMPefrwihtsgHTPGHISLFREKDRTLIAGDAF 197
Cdd:cd07709  122 KDGDT-----------LDLGKhTLKFIPA-----PML---------HWPDTMVTYDPEDKILFSGDAF 164
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 53-248 2.51e-04

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


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 41.33  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  53 VLVDAGM-PKCANEIISIAEDrfgTNSRPKAIILTHGHFDHVGGIIELIKYW-DVPVYAHQ-----MEIPfLTGQQSYPE 125
Cdd:cd07739   28 VLVDAQFtRADAERLADWIKA---SGKTLTTIYITHGHPDHYFGLEVLLEAFpDAKVVATPavvahIKAQ-LEPKLAFWG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 126 PDPtveGGMVAKmSPLFPnEPIDL------GNSVKALPTDGTVPHMPEFRWIHTSghtpghislfrekdRTLIAGDafVT 199
Cdd:cd07739  104 PLL---GGNAPA-RLVVP-EPLDGdtltleGHPLEIVGVGGGDTDDTTYLWIPSL--------------KTVVAGD--VV 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446279048 200 VKQEYLYKVITQEQEisgppryLTTDWKAAKEsviKLEELKPLVAITGH 248
Cdd:cd07739  163 YNGVHVWLADATTPE-------LRAAWLAALD---KIEALNPETVVPGH 201
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 78-105 3.57e-04

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: 40.58  E-value: 3.57e-04
                         10        20
                 ....*....|....*....|....*...
gi 446279048  78 SRPKAIILTHGHFDHVGGIIELIKYWDV 105
Cdd:cd07731   47 KKLDYLILTHPDADHIGGLDAVLKNFPV 74
NorV COG0426
Flavorubredoxin [Energy production and conversion];
53-197 5.77e-04

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 40.97  E-value: 5.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  53 VLVDAGMPKCANEIISIAEDRFGTnSRPKAIILTHGHFDHVGGIIELIKYW-DVPVYAHQMEIPFLTGQqsYPEPDP--- 128
Cdd:COG0426   45 ALIDTVGESFFEEFLENLSKVIDP-KKIDYIIVNHQEPDHSGSLPELLELApNAKIVCSKKAARFLPHF--YGIPDFrfi 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 129 TVEGGMVakmsplfpnepIDLGN-SVKALPTdgtvpHMPefrwihtsgHTPGHISLFREKDRTLIAGDAF 197
Cdd:COG0426  122 VVKEGDT-----------LDLGGhTLQFIPA-----PML---------HWPDTMFTYDPEDKILFSGDAF 166
BDS1 COG2015
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary ...
 79-113 1.11e-03

Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441618 [Multi-domain]  Cd Length: 629  Bit Score: 40.21  E-value: 1.11e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446279048  79 RP-KAIILTHGHFDHVGGII-----ELIKYWDVPVYAHQ--ME 113
Cdd:COG2015  140 RPvKAVIYTHSHVDHFGGVRgvvdeEDVKSGKVPIIAPEgfME 182
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 53-179 1.60e-03

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: 38.97  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  53 VLVDAGMPKCANEI-ISIAEDRFGTnSRPKAIILTHGHFDHVGGIIELIKYWDVPVYAHQMEIPFLTgqQSYPEPDPTVE 131
Cdd:cd16310   34 ILLDGGLEENAALIeQNIKALGFKL-SDIKIIINTHAHYDHAGGLAQLKADTGAKLWASRGDRPALE--AGKHIGDNITQ 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446279048 132 GgmvAKMSPLFPNEPIDLGNSVKAlptdGTVPHMPEFrwihTSGHTPG 179
Cdd:cd16310  111 P---APFPAVKVDRILGDGEKIKL----GDITLTATL----TPGHTKG 147
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 53-99 1.94e-03

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


Pssm-ID: 293847  Cd Length: 239  Bit Score: 39.03  E-value: 1.94e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446279048  53 VLVDAGMPKCANEIISIAEDRFGTNSRPKAIILTHGHFDHVGGIIEL 99
Cdd:cd16289   34 VLLDGGMPQAADMLLDNMRALGVAPGDLKLILHSHAHADHAGPLAAL 80
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 30-193 3.01e-03

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: 38.22  E-value: 3.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  30 DLFCYTIQivnicfvgNPKTNdfVLVDAGMPKCANEIISIAEDRFGTNSRPKAIILTHGHFDHVGGIIELIKYWDVPVYA 109
Cdd:cd16308   21 DLACYLIV--------TPKGN--ILINTGLAESVPLIKKNIQALGFKFKDIKILLTTQAHYDHVGAMAAIKQQTGAKMMV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 110 HQMEIPFLT--GQQSYpepdptVEGGMVAKMSPLFPNEPIDLGNSVKALPTDGTVPHMPefrwihtsGHTPGHIS-LFRE 186
Cdd:cd16308   91 DEKDAKVLAdgGKSDY------EMGGYGSTFAPVKADKLLHDGDTIKLGGTKLTLLHHP--------GHTKGSCSfLFDV 156

                        170
                 ....*....|..
gi 446279048 187 KD-----RTLIA 193
Cdd:cd16308  157 KDekrtyRVLIA 168
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-179 3.40e-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: 38.07  E-value: 3.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  37 QIV-NICFVGNP-------KTND-FVLVDAGMPKCANEII-SIAEDRFGTnSRPKAIILTHGHFDHVGGiIELIKYW--- 103
Cdd:cd16288    9 RIAgNVYYVGTSglasyliTTPQgLILIDTGLESSAPMIKaNIRKLGFKP-SDIKILLNSHAHLDHAGG-LAALKKLtga 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048 104 -------DVPVYAHQMEIPFLTGQQSYPEPDPTVEGgmvakmsPLFPNEPIDLGnsvkalptdGTVphmpeFRWIHTSGH 176
Cdd:cd16288   87 klmasaeDAALLASGGKSDFHYGDDSLAFPPVKVDR-------VLKDGDRVTLG---------GTT-----LTAHLTPGH 145


                 ...
gi 446279048 177 TPG 179
Cdd:cd16288  146 TRG 148
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 79-109 4.69e-03

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 37.48  E-value: 4.69e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 446279048  79 RPKAIILTHGHFDHVGGIIELIKYWDVPVYA 109
Cdd:PRK00685  40 KVDYILLTHGHGDHLGDTVEIAKRTGATVIA 70
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 72-159 5.96e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. 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: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 37.21  E-value: 5.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446279048  72 DRFGTNSRPKAIILTHGHFDHVGgiieLIKYW--DVPVYAH-------QMEIPFLTGQQSYPEPDPTVEggmvakmsplf 142
Cdd:cd07732   68 LRSEEDPSVDAVLLSHAHLDHYG----LLNYLrpDIPVYMGeatkrilKALLPFFGEGDPVPRNIRVFE----------- 132

                         90
                 ....*....|....*...
gi 446279048 143 PNEPIDLGN-SVKALPTD 159
Cdd:cd07732  133 SGKSFTIGDfTVTPYLVD 150
PRK11539 PRK11539
ComEC family competence protein; Provisional
 79-109 6.30e-03

ComEC family competence protein; Provisional


Pssm-ID: 236924 [Multi-domain]  Cd Length: 755  Bit Score: 38.05  E-value: 6.30e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 446279048  79 RPKAIILTHGHFDHVGGIIELIKYW-DVPVYA 109
Cdd:PRK11539 551 TPEGIILSHEHLDHRGGLASLLHAWpMAWIRS 582
 
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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