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Conserved domains on  [gi|1150405088|gb|AQR82495|]
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putative metallo-hydrolase [Bacillus subtilis subsp. subtilis str. 168]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10865880)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme

CATH:  3.60.15.10
Gene Ontology:  GO:0016787
PubMed:  17597585

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 4-190 1.57e-75

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: 225.63  E-value: 1.57e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   4 RRMPVGPIQANAYFLISDD-QCLIFDPGGEGH-KINQYIKEKGLTPLAILLTHAHFDHIGALDEVREKWDIPVYLHQNEK 81
Cdd:cd06262     1 KRLPVGPLQTNCYLVSDEEgEAILIDPGAGALeKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  82 NWLADASLNGSgMLRGIEVTAKPADHLIEGDGELNIGPFHLETLFTPGHSPGSVSYYVKDADLVISGDVLFQGGIGRTDL 161
Cdd:cd06262    81 ELLEDPELNLA-FFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDL 159

                         170       180
                  ....*....|....*....|....*....
gi 1150405088 162 IGGNQETLLTSIHEKLLTLPEHTLVLSGH 190
Cdd:cd06262   160 PGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 4-190 1.57e-75

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: 225.63  E-value: 1.57e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   4 RRMPVGPIQANAYFLISDD-QCLIFDPGGEGH-KINQYIKEKGLTPLAILLTHAHFDHIGALDEVREKWDIPVYLHQNEK 81
Cdd:cd06262     1 KRLPVGPLQTNCYLVSDEEgEAILIDPGAGALeKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  82 NWLADASLNGSgMLRGIEVTAKPADHLIEGDGELNIGPFHLETLFTPGHSPGSVSYYVKDADLVISGDVLFQGGIGRTDL 161
Cdd:cd06262    81 ELLEDPELNLA-FFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDL 159

                         170       180
                  ....*....|....*....|....*....
gi 1150405088 162 IGGNQETLLTSIHEKLLTLPEHTLVLSGH 190
Cdd:cd06262   160 PGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 6-195 5.56e-53

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: 169.10  E-value: 5.56e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   6 MPVGPIQANAYFLISDDQCLIFDPGGEGH---KINQYIKEKGLTPLAILLTHAHFDHIGALDEVREKWDIPVYLHQNEKN 82
Cdd:COG0491     8 TPGAGLGVNSYLIVGGDGAVLIDTGLGPAdaeALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  83 WLADAslngsGMLRGIEVTAKPADHLIEGDGELNIGPFHLETLFTPGHSPGSVSYYVKDADLVISGDVLFQGGIGRTDLI 162
Cdd:COG0491    88 ALEAP-----AAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLP 162

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1150405088 163 GGNQETLLTSIhEKLLTLPEHtLVLSGHGPETD 195
Cdd:COG0491   163 DGDLAQWLASL-ERLLALPPD-LVIPGHGPPTT 193
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 14-190 9.59e-41

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: 136.91  E-value: 9.59e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   14 NAYFLISDDQCLIFDPG-GEGHKINQYIKEKGLTPL-AILLTHAHFDHIGALDEVREKWDIPVYLHQNEKNWLADASLNG 91
Cdd:smart00849   1 NSYLVRDDGGAILIDTGpGEAEDLLAELKKLGPKKIdAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLALL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   92 SGMLRGIEvtAKPADHLIEGDGELNIGPFHLETLFTPGHSPGSVSYYVKDADLVISGDVLFQGGIGRTDLIGGNQETLLT 171
Cdd:smart00849  81 GELGAEAE--PAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAASDA 158

                          170
                   ....*....|....*....
gi 1150405088  172 SIHEKLLTLPEHTLVLSGH 190
Cdd:smart00849 159 LESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
8-190 2.89e-34

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 120.55  E-value: 2.89e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   8 VGPIQANAYFLISDDQCLIFDPGGEGHKI----NQYIKEKGLTPLAILLTHAHFDHIGALDEVREKWDIPVYLHQNEKNW 83
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAAllllLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  84 LADASLNGSGM---LRGIEVTAKPADHLIEGDGELNIGPFHLETLFTPGHSPGSVSYYVKDADLVISGDVLFQGGIGRTD 160
Cdd:pfam00753  81 LLDEELGLAASrlgLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLD 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1150405088 161 LIGGNQETLLTSIHEKLLTL------PEHTLVLSGH 190
Cdd:pfam00753 161 LPLGGLLVLHPSSAESSLESllklakLKAAVIVPGH 196
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 12-190 3.87e-20

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 85.26  E-value: 3.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  12 QANAYFLISDDQ--CLIFDPGgEGHKINQYIKEKGLTPLAILLTHAHFDHIGALDEVREKW-DIPVYLHQneknwladas 88
Cdd:PRK10241   10 DDNYIWVLNDEAgrCLIVDPG-EAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFpQIVVYGPQ---------- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  89 lngsgmlrgiEVTAKPADHLIeGDGE-LNIGPFHLETLFTPGHSPGSVSYYVKdaDLVISGDVLFQGGIGRtdLIGGNQE 167
Cdd:PRK10241   79 ----------ETQDKGTTQVV-KDGEtAFVLGHEFSVFATPGHTLGHICYFSK--PYLFCGDTLFSGGCGR--LFEGTAS 143

                         170       180
                  ....*....|....*....|...
gi 1150405088 168 TLLTSIhEKLLTLPEHTLVLSGH 190
Cdd:PRK10241  144 QMYQSL-KKINALPDDTLICCAH 165
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 4-190 1.57e-75

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: 225.63  E-value: 1.57e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   4 RRMPVGPIQANAYFLISDD-QCLIFDPGGEGH-KINQYIKEKGLTPLAILLTHAHFDHIGALDEVREKWDIPVYLHQNEK 81
Cdd:cd06262     1 KRLPVGPLQTNCYLVSDEEgEAILIDPGAGALeKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  82 NWLADASLNGSgMLRGIEVTAKPADHLIEGDGELNIGPFHLETLFTPGHSPGSVSYYVKDADLVISGDVLFQGGIGRTDL 161
Cdd:cd06262    81 ELLEDPELNLA-FFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDL 159

                         170       180
                  ....*....|....*....|....*....
gi 1150405088 162 IGGNQETLLTSIHEKLLTLPEHTLVLSGH 190
Cdd:cd06262   160 PGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 4-206 9.50e-59

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: 183.70  E-value: 9.50e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   4 RRMPVGPIQANAYFLISDD--QCLIFDPGGEGHKINQYIKEKGLTPLAILLTHAHFDHIGALDEVREKWDIPVYLHQNEK 81
Cdd:cd16322     2 RPFTLGPLQENTYLVADEGggEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  82 NWLADASLNGSGMLRGIEvTAKPADHLIEGDGELNIGPFHLETLFTPGHSPGSVSYYVKDADLVISGDVLFQGGIGRTDL 161
Cdd:cd16322    82 PLYEAADLGAKAFGLGIE-PLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRTDL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1150405088 162 IGGNQETLLTSIhEKLLTLPEHTLVLSGHGPETDVLTEQDQNPFL 206
Cdd:cd16322   161 PGGDPKAMAASL-RRLLTLPDETRVFPGHGPPTTLGEERRTNPFL 204
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 7-190 4.49e-54

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: 171.20  E-value: 4.49e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   7 PVGPIQANAYFLISDD--QCLIFDPGGEGHKINQYIKEKGLTPLAILLTHAHFDHIGALDEVREKWDIPVYLHQNEKNWL 84
Cdd:cd07737     5 PVTPFQQNCSLIWCEEtkEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKEDKFL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  85 ADASLNGSGMLRGIEVTAKPADH-LIEGDgELNIGPFHLETLFTPGHSPGSVSYYVKDADLVISGDVLFQGGIGRTDLIG 163
Cdd:cd07737    85 LENLPEQSQMFGFPPAEAFTPDRwLEEGD-TVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTDFPG 163

                         170       180
                  ....*....|....*....|....*..
gi 1150405088 164 GNQETLLTSIHEKLLTLPEHTLVLSGH 190
Cdd:cd07737   164 GNHAQLIASIKEKLLPLGDDVTFIPGH 190
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 6-195 5.56e-53

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: 169.10  E-value: 5.56e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   6 MPVGPIQANAYFLISDDQCLIFDPGGEGH---KINQYIKEKGLTPLAILLTHAHFDHIGALDEVREKWDIPVYLHQNEKN 82
Cdd:COG0491     8 TPGAGLGVNSYLIVGGDGAVLIDTGLGPAdaeALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  83 WLADAslngsGMLRGIEVTAKPADHLIEGDGELNIGPFHLETLFTPGHSPGSVSYYVKDADLVISGDVLFQGGIGRTDLI 162
Cdd:COG0491    88 ALEAP-----AAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLP 162

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1150405088 163 GGNQETLLTSIhEKLLTLPEHtLVLSGHGPETD 195
Cdd:COG0491   163 DGDLAQWLASL-ERLLALPPD-LVIPGHGPPTT 193
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 14-190 9.59e-41

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: 136.91  E-value: 9.59e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   14 NAYFLISDDQCLIFDPG-GEGHKINQYIKEKGLTPL-AILLTHAHFDHIGALDEVREKWDIPVYLHQNEKNWLADASLNG 91
Cdd:smart00849   1 NSYLVRDDGGAILIDTGpGEAEDLLAELKKLGPKKIdAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLALL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   92 SGMLRGIEvtAKPADHLIEGDGELNIGPFHLETLFTPGHSPGSVSYYVKDADLVISGDVLFQGGIGRTDLIGGNQETLLT 171
Cdd:smart00849  81 GELGAEAE--PAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAASDA 158

                          170
                   ....*....|....*....
gi 1150405088  172 SIHEKLLTLPEHTLVLSGH 190
Cdd:smart00849 159 LESLLKLLKLLPKLVVPGH 177
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 15-190 1.90e-38

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 130.27  E-value: 1.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  15 AYFLISDD--QCLIFDPGgEGHKINQYIKEKGLTPLAILLTHAHFDHIGALDEVREKW-DIPVYLHQNEKnwladaslng 91
Cdd:cd07723    11 IYLIVDEAtgEAAVVDPG-EAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFpDAPVYGPAEDR---------- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  92 sgmlrgievtAKPADHLIEGDGELNIGPFHLETLFTPGHSPGSVSYYVKDADLVISGDVLFQGGIGRtdLIGGNQETLLT 171
Cdd:cd07723    80 ----------IPGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGR--FFEGTAEQMYA 147

                         170
                  ....*....|....*....
gi 1150405088 172 SIhEKLLTLPEHTLVLSGH 190
Cdd:cd07723   148 SL-QKLLALPDDTLVYCGH 165
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 16-191 3.37e-38

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: 130.21  E-value: 3.37e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  16 YFLISDD--QCLIFDPGGEG-HKINQYIKEKGLTPLAILLTHAHFDHIGALDEVREKWDIPVYLHQNeknwladaslngs 92
Cdd:cd07724    15 YLVGDPEtgEAAVIDPVRDSvDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGEG------------- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  93 gmlrgieVTAKPADHLIEGDGELNIGPFHLETLFTPGHSPGSVSYYVKDADLVISGDVLFQGGIGRTDLIGGNQE---TL 169
Cdd:cd07724    82 -------APASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPGEAEGlarQL 154

                         170       180
                  ....*....|....*....|..
gi 1150405088 170 LTSIHEKLLTLPEHTLVLSGHG 191
Cdd:cd07724   155 YDSLQRKLLLLPDETLVYPGHD 176
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 9-190 1.50e-36

Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; Bacillus amyloliquefaciens BaeB may play a role in the synthesis of the antibiotic polyketide bacillaene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293833 [Multi-domain]  Cd Length: 174  Bit Score: 125.73  E-value: 1.50e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   9 GPIQANAYFLI--SDDQCLIFDPGGEGHKINQYIKEKGLTPLAILLTHAHFDHIGALDEVREKWDIPVYLHQNEknwlAD 86
Cdd:cd16275     8 GPMINYSYIIIdkATREAAVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEE----ID 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  87 ASLNGSGMLrgievtakpadHLIEGDGELNIGPFHLETLFTPGHSPGSVSYYVKDAdlVISGDVLFQGGIGRTDLIGGNQ 166
Cdd:cd16275    84 YYGFRCPNL-----------IPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGDS--LFTGDTLFIEGCGRCDLPGGDP 150

                         170       180
                  ....*....|....*....|....*
gi 1150405088 167 ETLLTSIHeKLLTL-PEHTLVLSGH 190
Cdd:cd16275   151 EEMYESLQ-RLKKLpPPNTRVYPGH 174
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 5-191 9.76e-36

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: 124.64  E-value: 9.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   5 RMPVGPIqANAYFLISDDQCLIFDPG--GEGHKINQYIKEKGLTPL---AILLTHAHFDHIGALDEVREKWDIPVYLHQN 79
Cdd:cd07721     4 QLPLLPP-VNAYLIEDDDGLTLIDTGlpGSAKRILKALRELGLSPKdirRILLTHGHIDHIGSLAALKEAPGAPVYAHER 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  80 EKNWLA--------DASLNGSGMLRGIEVTAKPADHLIEGDGELNIGPfHLETLFTPGHSPGSVSYYVKDADLVISGDvL 151
Cdd:cd07721    83 EAPYLEgekpypppVRLGLLGLLSPLLPVKPVPVDRTLEDGDTLDLAG-GLRVIHTPGHTPGHISLYLEEDGVLIAGD-A 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1150405088 152 FQGGIGRTDLIGG----NQETLLTSIhEKLLTLpEHTLVLSGHG 191
Cdd:cd07721   161 LVTVGGELVPPPPpftwDMEEALESL-RKLAEL-DPEVLAPGHG 202
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
8-190 2.89e-34

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 120.55  E-value: 2.89e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   8 VGPIQANAYFLISDDQCLIFDPGGEGHKI----NQYIKEKGLTPLAILLTHAHFDHIGALDEVREKWDIPVYLHQNEKNW 83
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAAllllLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  84 LADASLNGSGM---LRGIEVTAKPADHLIEGDGELNIGPFHLETLFTPGHSPGSVSYYVKDADLVISGDVLFQGGIGRTD 160
Cdd:pfam00753  81 LLDEELGLAASrlgLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLD 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1150405088 161 LIGGNQETLLTSIHEKLLTL------PEHTLVLSGH 190
Cdd:pfam00753 161 LPLGGLLVLHPSSAESSLESllklakLKAAVIVPGH 196
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 12-190 6.86e-22

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: 88.07  E-value: 6.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  12 QANAYFLISDDQCLIFDPG-GEGHkINQYIKEKGLTPLAILLTHAHFDHIGALDEVREkwdipVYLHQNEKNWLA--DAS 88
Cdd:cd07712     8 RVNIYLLRGRDRALLIDTGlGIGD-LKEYVRTLTDLPLLVVATHGHFDHIGGLHEFEE-----VYVHPADAEILAapDNF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  89 LNGSGMLRGIEVTAKPADHLI-EGDgELNIGPFHLETLFTPGHSPGSVSYYVKDADLVISGDVLFQGGIgRTDLIGGNQE 167
Cdd:cd07712    82 ETLTWDAATYSVPPAGPTLPLrDGD-VIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVYDGPL-IMDLPHSDLD 159

                         170       180
                  ....*....|....*....|....
gi 1150405088 168 TLLTSIhEKLLTLP-EHTLVLSGH 190
Cdd:cd07712   160 DYLASL-EKLSKLPdEFDKVLPGH 182
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 16-151 2.43e-20

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 84.50  E-value: 2.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  16 YFLISDDQCLIFDPGGE---GHKINQYIKEKGLTPLAILLTHAHFDHIGALDEVREKWDIPVYLHQNEKNWLADASLNGS 92
Cdd:cd07743    12 VYVFGDKEALLIDSGLDedaGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAFIENPLLEPS 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150405088  93 GM--------LRGIEVTAKP--ADHLIEgDGELNIGPFHLETLFTPGHSPGSVSYYVKD-----ADLVISGDVL 151
Cdd:cd07743    92 YLggayppkeLRNKFLMAKPskVDDIIE-EGELELGGVGLEIIPLPGHSFGQIGILTPDgvlfaGDALFGEEVL 164
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 12-190 3.87e-20

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 85.26  E-value: 3.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  12 QANAYFLISDDQ--CLIFDPGgEGHKINQYIKEKGLTPLAILLTHAHFDHIGALDEVREKW-DIPVYLHQneknwladas 88
Cdd:PRK10241   10 DDNYIWVLNDEAgrCLIVDPG-EAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFpQIVVYGPQ---------- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  89 lngsgmlrgiEVTAKPADHLIeGDGE-LNIGPFHLETLFTPGHSPGSVSYYVKdaDLVISGDVLFQGGIGRtdLIGGNQE 167
Cdd:PRK10241   79 ----------ETQDKGTTQVV-KDGEtAFVLGHEFSVFATPGHTLGHICYFSK--PYLFCGDTLFSGGCGR--LFEGTAS 143

                         170       180
                  ....*....|....*....|...
gi 1150405088 168 TLLTSIhEKLLTLPEHTLVLSGH 190
Cdd:PRK10241  144 QMYQSL-KKINALPDDTLICCAH 165
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 13-195 4.94e-20

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 83.77  E-value: 4.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  13 ANAYFLISDDQCLIFDPGG---EGHKINQYIKE-KGLTPLAILLTHAHFDHIG-------------ALDEVREkwdipvY 75
Cdd:cd16282    15 SNIGFIVGDDGVVVIDTGAsprLARALLAAIRKvTDKPVRYVVNTHYHGDHTLgnaafadagapiiAHENTRE------E 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  76 LHQNEKNWLADASLNGSGMLRGIEVTakPADHLIEGDGELNIGPFHLETL-FTPGHSPGSVSYYVKDADLVISGDVLFQG 154
Cdd:cd16282    89 LAARGEAYLELMRRLGGDAMAGTELV--LPDRTFDDGLTLDLGGRTVELIhLGPAHTPGDLVVWLPEEGVLFAGDLVFNG 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1150405088 155 GIGRTD--LIGGNQETLltsihEKLLTLPEHTLVlSGHGPETD 195
Cdd:cd16282   167 RIPFLPdgSLAGWIAAL-----DRLLALDATVVV-PGHGPVGD 203
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 40-190 4.45e-18

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 79.46  E-value: 4.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  40 IKEKGLTPLAILLTHAHFDHIGALDEVREKwdIPvylhqNEKNWLADASlngsgmlrgievTAKpADHLIEGDGELNIGP 119
Cdd:PLN02962   55 VKELGLKLIYAMNTHVHADHVTGTGLLKTK--LP-----GVKSIISKAS------------GSK-ADLFVEPGDKIYFGD 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1150405088 120 FHLETLFTPGHSPGSVSYYVKDAD------LVISGDVLFQGGIGRTDLIGGNQETLLTSIHEKLLTLPEHTLVLSGH 190
Cdd:PLN02962  115 LYLEVRATPGHTAGCVTYVTGEGPdqpqprMAFTGDALLIRGCGRTDFQGGSSDQLYKSVHSQIFTLPKDTLIYPAH 191
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-193 1.50e-17

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 76.76  E-value: 1.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  14 NAYFLISDDQCLIFDPG--GEGHkINQYIKE-KGLTPLAILLTHAHFDHIGALDEVREKWDIPVYLHqneknwladasln 90
Cdd:cd16278    19 NTYLLGAPDGVVVIDPGpdDPAH-LDALLAAlGGGRVSAILVTHTHRDHSPGAARLAERTGAPVRAF------------- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  91 GSGMLRGIEVTAKPADHLIEGDgELNIGPFHLETLFTPGHSPGSVSYYVKDADLVISGDVLFQGGigrTDLI---GGNQE 167
Cdd:cd16278    85 GPHRAGGQDTDFAPDRPLADGE-VIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVMGWS---TTVIappDGDLG 160

                         170       180
                  ....*....|....*....|....*.
gi 1150405088 168 TLLTSIhEKLLTLPEhTLVLSGHGPE 193
Cdd:cd16278   161 DYLASL-ERLLALDD-RLLLPGHGPP 184
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 6-190 9.58e-16

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 73.26  E-value: 9.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   6 MPVGPIQANAYFLISDD---QCLIFDPGgEGHKINQYIKEKGLTPLAILLTHAHFDHIGALDEVREKW-DIPVYlhqnek 81
Cdd:PLN02469    4 IPVPCLEDNYAYLIIDEstkDAAVVDPV-DPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVpGIKVY------ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  82 nwladaslngSGMLRGIEVTAKPADHlieGDgELNIGP-FHLETLFTPGHSPGSVSYYV----KDADLVISGDVLFQGGI 156
Cdd:PLN02469   77 ----------GGSLDNVKGCTHPVEN---GD-KLSLGKdVNILALHTPCHTKGHISYYVtgkeGEDPAVFTGDTLFIAGC 142

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1150405088 157 GRtdLIGGNQETLLTSIHEKLLTLPEHTLVLSGH 190
Cdd:PLN02469  143 GK--FFEGTAEQMYQSLCVTLGSLPKPTQVYCGH 174
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 50-190 3.65e-12

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 64.09  E-value: 3.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  50 ILLTHAHFDHIGALDEVREKWDipvylhqneknwladASLNGSGMLR----GIEVTAKPADHLIEGDGELNIgpfhletL 125
Cdd:PLN02398  125 ILNTHHHYDHTGGNLELKARYG---------------AKVIGSAVDKdripGIDIVLKDGDKWMFAGHEVLV-------M 182

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1150405088 126 FTPGHSPGSVSYYVKDADLVISGDVLFQGGIGRtdLIGGNQETLLTSIhEKLLTLPEHTLVLSGH 190
Cdd:PLN02398  183 ETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGK--LFEGTPEQMLSSL-QKIISLPDDTNIYCGH 244
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 31-150 6.65e-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: 62.62  E-value: 6.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  31 GEGHKINQYIKEKGLTPLAI---LLTHAHFDHIGALDEVRekwDIPVYLHQNE-KNWLADASLNGSGMLRGIEVTAKPAD 106
Cdd:cd07729    70 TEEQTLEEQLARLGLDPEDIdyvILSHLHFDHAGGLDLFP---NATIIVQRAElEYATGPDPLAAGYYEDVLALDDDLPG 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1150405088 107 ---HLIEGDGELNIGpfhLETLFTPGHSPGSVSYYVK--DADLVISGDV 150
Cdd:cd07729   147 grvRLVDGDYDLFPG---VTLIPTPGHTPGHQSVLVRlpEGTVLLAGDA 192
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 16-137 7.14e-12

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: 62.47  E-value: 7.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  16 YFLISDDQCLIFDPGGE--GHKINQYIKEKG--LTPLAILL-THAHFDHIGALDEVREKWDIPVYLHQNEKNWLADASLN 90
Cdd:cd16310    25 YLITSNHGAILLDGGLEenAALIEQNIKALGfkLSDIKIIInTHAHYDHAGGLAQLKADTGAKLWASRGDRPALEAGKHI 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1150405088  91 GSGMLRGIEVTAKPADHLIeGDGE-LNIGPFHLETLFTPGHSPGSVSY 137
Cdd:cd16310   105 GDNITQPAPFPAVKVDRIL-GDGEkIKLGDITLTATLTPGHTKGCTTW 151
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 15-150 8.23e-12

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


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 61.74  E-value: 8.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  15 AYFLISDDQCLIFDPGGEGH--KINQYIKEKGLTPL---AILLTHAHFDHIGALDEVREKW-DIPVYLHQNEKNWLADAS 88
Cdd:cd07726    18 SYLLDGEGRPALIDTGPSSSvpRLLAALEALGIAPEdvdYIILTHIHLDHAGGAGLLAEALpNAKVYVHPRGARHLIDPS 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150405088  89 --LNGS-------GMLRGIEVTAKPADHLIE-GDGE-LNIGPFHLETLFTPGHSPGSVSYYVKDADLVISGDV 150
Cdd:cd07726    98 klWASAravygdeADRLGGEILPVPEERVIVlEDGEtLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDA 170
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 14-120 3.25e-11

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: 59.20  E-value: 3.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  14 NAYFLISDDQCLIFDPGGEGHKINQYIKEKGLTPL---AILLTHAHFDHIGALDEVREKWDIPVYLhqNEKNWLADASln 90
Cdd:cd07733    10 NCTYLETEDGKLLIDAGLSGRKITGRLAEIGRDPEdidAILVTHEHADHIKGLGVLARKYNVPIYA--TAGTLRAMER-- 85

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1150405088  91 gsgMLRGIEVTAKpaDHLIEGD----GELNIGPF 120
Cdd:cd07733    86 ---KVGLIDVDQK--QIFEPGEtfsiGDFDVESF 114
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 12-151 2.43e-10

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


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 57.31  E-value: 2.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  12 QANAYFLISDDQCLIFDPG----GEGHKINQYIKEKGLTPLAI---LLTHAHFDHIGALDEVREKWDIPVYLhqneknwl 84
Cdd:cd07725    14 HVNVYLLRDGDETTLIDTGlateEDAEALWEGLKELGLKPSDIdrvLLTHHHPDHIGLAGKLQEKSGATVYI-------- 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1150405088  85 adaslngsgmlrgIEVTAkpadhLIEGDGeLNIGPFHLETLFTPGHSPGSVSYYVKDADLVISGDVL 151
Cdd:cd07725    86 -------------LDVTP-----VKDGDK-IDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAV 133
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 14-150 3.17e-10

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 57.98  E-value: 3.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  14 NAYFLISDDQCLIFDPGGEGHKINQYIKEKGLTPLAILLTHAHFDHIGALDEVREKW---DIPVYLHQNEknwLADASLN 90
Cdd:COG1235    36 SSILVEADGTRLLIDAGPDLREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYgpnPIPVYATPGT---LEALERR 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150405088  91 GSGMLRgiEVTAKPADHLIEGDGELNIGPFHLETLFTPGHSPGSVSYYVKDAD--LVISGDV 150
Cdd:COG1235   113 FPYLFA--PYPGKLEFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGYRIEDGGkkLAYATDT 172
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 50-141 4.40e-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: 57.59  E-value: 4.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  50 ILLTHAHFDHIGALDEVREKWDIPVYLHQNEKNWLADASLNGSGMLRGievTAKPADHLIEGDGELNIGPFHLETLFTPG 129
Cdd:cd16280    65 ILITHGHGDHYGGAAYLKDLYGAKVVMSEADWDMMEEPPEEGDNPRWG---PPPERDIVIKDGDTLTLGDTTITVYLTPG 141

                          90
                  ....*....|....
gi 1150405088 130 HSPGSVSYY--VKD 141
Cdd:cd16280   142 HTPGTLSLIfpVKD 155
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 49-192 7.13e-10

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: 56.00  E-value: 7.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  49 AILLTHAHFDHIGALDEVRE---KWDIPVYLHQNEKnwlADASLNGSGmlrgievtaKPADHLIEGDgELNIGPFHLETL 125
Cdd:cd07722    59 DILLTHWHHDHVGGLPDVLDllrGPSPRVYKFPRPE---EDEDPDEDG---------GDIHDLQDGQ-VFKVEGATLRVI 125

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150405088 126 FTPGHSPGSVSYYVKDADLVISGD-VLFQGGIGRTDLIggnqeTLLTSIHeKLLTLPEHTLvLSGHGP 192
Cdd:cd07722   126 HTPGHTTDHVCFLLEEENALFTGDcVLGHGTAVFEDLA-----AYMASLK-KLLSLGPGRI-YPGHGP 186
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 11-150 1.19e-09

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: 55.96  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  11 IQANAYfLISDDQCLIFDPGGEGH------KINQYIKEKGLTplAILLTHAHFDHIGALDEVREKW-DIPVYlhqneknw 83
Cdd:cd07709    30 TSYNSY-LIKDEKTALIDTVKEPFfdefleNLEEVIDPRKID--YIVVNHQEPDHSGSLPELLELApNAKIV-------- 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150405088  84 ladASLNGSGMLRGIEVTAKPADHLIEGDGELNIGPFHLETLFTPG-HSPGS-VSYYVKDAdLVISGDV 150
Cdd:cd07709    99 ---CSKKAARFLKHFYPGIDERFVVVKDGDTLDLGKHTLKFIPAPMlHWPDTmVTYDPEDK-ILFSGDA 163
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
13-149 2.49e-09

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 55.20  E-value: 2.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  13 ANAYFLISDDQCLIFDPGgEGhkINQYIKEKGLTPL---AILLTHAHFDHIGALDEV--------REKwDIPVYLHQNEK 81
Cdd:COG1234    19 TSSYLLEAGGERLLIDCG-EG--TQRQLLRAGLDPRdidAIFITHLHGDHIAGLPGLlstrslagREK-PLTIYGPPGTK 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  82 NWLaDASLNGSGMLRGIEVTAkpadHLIEGDGELNIGPFHLETLFTPgHSPGSVSYYVKDAD--LVISGD 149
Cdd:COG1234    95 EFL-EALLKASGTDLDFPLEF----HEIEPGEVFEIGGFTVTAFPLD-HPVPAYGYRFEEPGrsLVYSGD 158
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 50-137 2.69e-09

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: 55.38  E-value: 2.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  50 ILLTHAHFDHIGALDEVREKWDIPVYLHQNEKNWLADASLNGS----GMLRGIevtAKPADHLIEGDGE-LNIGPFHLET 124
Cdd:cd16311    64 ILNSHGHIDHAGGLAELQRRSGALVAASPSAALDLASGEVGPDdpqyHALPKY---PPVKDMRLARDGGqFNVGPVSLTA 140

                          90
                  ....*....|...
gi 1150405088 125 LFTPGHSPGSVSY 137
Cdd:cd16311   141 HATPGHTPGGLSW 153
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-154 3.60e-09

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: 54.16  E-value: 3.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  48 LAILLTHAHFDHIGALDEVREkwDIPVYLHQNEKNwLADASLNGSGMLRGIEVTAKPadhlIEGDGELNIGPFHLeTLFT 127
Cdd:cd07732    77 DAVLLSHAHLDHYGLLNYLRP--DIPVYMGEATKR-ILKALLPFFGEGDPVPRNIRV----FESGKSFTIGDFTV-TPYL 148

                          90       100       110
                  ....*....|....*....|....*....|
gi 1150405088 128 PGHS-PGSVSYYVKDADLVI--SGDVLFQG 154
Cdd:cd07732   149 VDHSaPGAYAFLIEAPGKRIfyTGDFRFHG 178
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
39-149 3.93e-09

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 55.45  E-value: 3.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  39 YIKEKGLTPLAILLTHAHFDHIGALDEVREKWDIPVY-----LHqneknwLADASLNGSGMLRGIEVtakpadHLIEGDG 113
Cdd:COG0595    56 YLEENKDKIKGIVLTHGHEDHIGALPYLLKELNVPVYgtpltLA------LLEAKLKEHGLLKKVKL------HVVKPGD 123

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1150405088 114 ELNIGPFHLEtLFTPGHS-PGSVSYYVKDAD--LVISGD 149
Cdd:COG0595   124 RIKFGPFKVE-FFRVTHSiPDSLGLAIRTPAgtIVHTGD 161
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 50-142 1.12e-08

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: 53.63  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  50 ILLTHAHFDHIGALDEVREKWDIPVYLHQNEKNWLADASlNGSGMLRGIEVTAKP--ADHLIEGDGELNIGPFHLETLFT 127
Cdd:cd16308    64 LLTTQAHYDHVGAMAAIKQQTGAKMMVDEKDAKVLADGG-KSDYEMGGYGSTFAPvkADKLLHDGDTIKLGGTKLTLLHH 142

                          90
                  ....*....|....*..
gi 1150405088 128 PGHSPGSVSYY--VKDA 142
Cdd:cd16308   143 PGHTKGSCSFLfdVKDE 159
NorV COG0426
Flavorubredoxin [Energy production and conversion];
11-150 1.99e-08

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 53.30  E-value: 1.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  11 IQANAYfLISDDQCLIFDPGGEGH------KINQYIKEKGLTplAILLTHAHFDHIGALDEVREKW-DIPVYlhqneknw 83
Cdd:COG0426    32 TTYNSY-LIVDEKTALIDTVGESFfeefleNLSKVIDPKKID--YIIVNHQEPDHSGSLPELLELApNAKIV-------- 100

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150405088  84 ladASLNGSGMLRGIevTAKPADHLI---EGDgELNIGPFHLETLFTPG-HSPGSVSYYVKDADLVISGDV 150
Cdd:COG0426   101 ---CSKKAARFLPHF--YGIPDFRFIvvkEGD-TLDLGGHTLQFIPAPMlHWPDTMFTYDPEDKILFSGDA 165
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 8-157 3.55e-08

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: 52.16  E-value: 3.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   8 VGPIQANAYFLISDDQCLIFD---PGGEGHkINQYIKEKGLTPL---AILLTHAHFDHIGALDEVREKWDIPVYLHQNEK 81
Cdd:cd07708    17 VGTDDLAAYLIVTPQGNILIDgdmEQNAPM-IKANIKKLGFKFSdtkLILISHAHFDHAGGSAEIKKQTGAKVMAGAEDV 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1150405088  82 NWLADASLNGSGMLRGIEVTAKPA--DHLIEgDGEL-NIGPFHLETLFTPGHSPGSVSYYVKDADLVISGDVLFQGGIG 157
Cdd:cd07708    96 SLLLSGGSSDFHYANDSSTYFPQStvDRAVH-DGERvTLGGTVLTAHATPGHTPGCTTWTMTLKDHGKQYQVVFADSLT 173
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 18-150 9.12e-08

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: 50.28  E-value: 9.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  18 LISDDQCLI-FDPGGEGHK--INQYIKEKGLTPLAI---LLTHAHFDHIGALDEVREKwdiPVYLHQNEKNWLADaslng 91
Cdd:cd07711    26 LIKDGGKNIlVDTGTPWDRdlLLKALAEHGLSPEDIdyvVLTHGHPDHIGNLNLFPNA---TVIVGWDICGDSYD----- 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150405088  92 sgmlrgievtakpaDHLIEGDGELNIGPfHLETLFTPGHSPGSVSYYVKDADL---VISGDV 150
Cdd:cd07711    98 --------------DHSLEEGDGYEIDE-NVEVIPTPGHTPEDVSVLVETEKKgtvAVAGDL 144
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 50-207 1.02e-07

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: 50.76  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  50 ILLTHAHFDHIGALDEVrekwdipvylhQNEKNWLADASLNGSGMLRG-------IEVTAKPADHLIE-------GDGE- 114
Cdd:cd16312    64 ILNSHAHWDHAGGIAAL-----------QKASGATVAASAHGAQVLQSgtngkddPQYQAKPVVHVAKvakvkevGEGDt 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088 115 LNIGPFHLETLFTPGHSPGSVSY--------------YVKDADLVISGDVLFQGGIGRTDLIGGNQETLltsihEKLLTL 180
Cdd:cd16312   133 LKVGPLRLTAHMTPGHTPGGTTWtwtscegqrcldvvYADSLNPYSSGDFYYTGKGGYPDISASFRASI-----AKVAAL 207

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1150405088 181 PeHTLVLSGHGPETDVLTEQ-----DQNPFLN 207
Cdd:cd16312   208 P-CDIIIAVHPGFTDVLDKAkrrsgDTNPFID 238
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 50-137 1.84e-07

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


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 50.18  E-value: 1.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  50 ILLTHAHFDHIGALDEVREKWDIPVYLHQNEKnWLADASLNGSGMLRGIEVTAKPADHLIeGDGE-LNIGPFHLETLFTP 128
Cdd:cd16309    64 LLNTHAHFDHAGGLAELKKATGAQLVASAADK-PLLESGYVGSGDTKNLQFPPVRVDRVI-GDGDkVTLGGTTLTAHLTP 141


                  ....*....
gi 1150405088 129 GHSPGSVSY 137
Cdd:cd16309   142 GHSPGCTSW 150
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 49-152 2.43e-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: 49.47  E-value: 2.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  49 AILLTHAHFDHIGALdeVREKwDIP------VYLHQNEKN-WLADASLNGS-----GMLRGIEVTAKPADHLIEGDGELN 116
Cdd:cd07720    94 DVLLTHLHPDHIGGL--VDAG-GKPvfpnaeVHVSEAEWDfWLDDANAAKApegakRFFDAARDRLRPYAAAGRFEDGDE 170

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1150405088 117 IGPfHLETLFTPGHSPGSVSYYV--KDADLVISGDVLF 152
Cdd:cd07720   171 VLP-GITAVPAPGHTPGHTGYRIesGGERLLIWGDIVH 207
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 ...
 50-137 3.18e-07

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: 49.27  E-value: 3.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  50 ILLTHAHFDHIGALDEVREKWDIPVYlhqneknwladASLNGSGMLRGIEVTAK-PADHLIE-----------GDGE-LN 116
Cdd:cd16290    64 ILNSHAHFDHAGGIAALQRDSGATVA-----------ASPAGAAALRSGGVDPDdPQAGAADpfppvakvrvvADGEvVK 132

                          90       100
                  ....*....|....*....|.
gi 1150405088 117 IGPFHLETLFTPGHSPGSVSY 137
Cdd:cd16290   133 LGPLAVTAHATPGHTPGGTSW 153
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 49-131 5.34e-07

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: 48.07  E-value: 5.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  49 AILLTHAHFDHIGALDEVREKWDIPVYLHQNeknwlADASLNGSGMLRGIEVTAKPADHLIEGDGELNIGPFHLETLFTP 128
Cdd:pfam12706  31 AVLLTHDHYDHLAGLLDLREGRPRPLYAPLG-----VLAHLRRNFPYLFLLEHYGVRVHEIDWGESFTVGDGGLTVTATP 105


                  ...
gi 1150405088 129 GHS 131
Cdd:pfam12706 106 ARH 108
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 8-125 5.47e-07

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: 47.90  E-value: 5.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   8 VGpiQANAYFLISDDQCLIFDPGGEGHKINQ----YIKEKGLTPL-AILLTHAHFDHIGALDEVREKWDI-PVYLHQNEK 81
Cdd:cd07731     7 VG--QGDAILIQTPGKTILIDTGPRDSFGEDvvvpYLKARGIKKLdYLILTHPDADHIGGLDAVLKNFPVkEVYMPGVTH 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1150405088  82 NWLADASLNGSGMLRGIEVTAkpadhLIEGDgELNIGPFHLETL 125
Cdd:cd07731    85 TTKTYEDLLDAIKEKGIPVTP-----CKAGD-RWQLGGVSFEVL 122
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 15-149 1.22e-06

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: 46.87  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  15 AYFLISDDQCLIFDPG-GEGHKINQYIKeKGLTPLAILLTHAHFDHIGaldevrekwDIPVYLHQNeKNWLADASLN--- 90
Cdd:cd16272    19 SYLLETGGTRILLDCGeGTVYRLLKAGV-DPDKLDAIFLSHFHLDHIG---------GLPTLLFAR-RYGGRKKPLTiyg 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150405088  91 GSGMLRGIE------VTAKPADH------LIEGDGELNIGPFHLETLFTPgHSPGSVSYYVKDAD--LVISGD 149
Cdd:cd16272    88 PKGIKEFLEkllnfpVEILPLGFpleieeLEEGGEVLELGDLKVEAFPVK-HSVESLGYRIEAEGksIVYSGD 159
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 39-149 1.28e-06

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: 47.40  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  39 YIKEKGLTPLAILLTHAHFDHIGALDEVREKWDIPVY----------LHQNEKNWLADASLngsgmlrgievtakpadHL 108
Cdd:cd07714    48 YLEENKDKIKGIFITHGHEDHIGALPYLLPELNVPIYatpltlalikKKLEEFKLIKKVKL-----------------NE 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1150405088 109 IEGDGELNIGPFHLEtLFTPGHS-PGSVSYYVK--DADLVISGD 149
Cdd:cd07714   111 IKPGERIKLGDFEVE-FFRVTHSiPDSVGLAIKtpEGTIVHTGD 153
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 44-151 1.62e-06

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: 47.13  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  44 GLTPLAI---LLTHAHFDHIG---ALDEvrEKWdIPV-----YL-HQNEKNWLADASLNGSGMLRGIE------VTAKPA 105
Cdd:cd16277    58 GVRPEDVdyvLCTHLHVDHVGwntRLVD--GRW-VPTfpnarYLfSRAEYDHWSSPDAGGPPNRGVFEdsvlpvIEAGLA 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1150405088 106 DhLIEGDGElnIGPfHLETLFTPGHSPGSVSYYVKDAD--LVISGDVL 151
Cdd:cd16277   135 D-LVDDDHE--ILD-GIRLEPTPGHTPGHVSVELESGGerALFTGDVM 178
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 49-191 1.89e-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: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  49 AILLTHAHF--DHigalDEVREKWDIPVYLHQNEKNWLADASlngsgmlrGIEVtakpadhlIEGDGELNIGPfHLETLF 126
Cdd:cd07727    50 YIFLTHRDDvaDH----AKWAERFGAKRIIHEDDVNAVTRPD--------EVIV--------LWGGDPWELDP-DLTLIP 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1150405088 127 TPGHSPGSVSYYVKDADLVISGDVLFQGGiGRTDLIGGNQ------ETLLTSIhEKLLTLP-EHtlVLSGHG 191
Cdd:cd07727   109 VPGHTRGSVVLLYKEKGVLFTGDHLAWSR-RRGWLSAFRYvcwyswPEQAESV-ERLADLDfEW--VLPGHG 176
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 49-79 2.14e-06

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: 46.31  E-value: 2.14e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1150405088  49 AILLTHAHFDHIGALDEVRE-----KWDIPVYLHQN 79
Cdd:cd16279    69 AVLLTHAHADHIHGLDDLRPfnrlqQRPIPVYASEE 104
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 8-137 2.61e-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: 46.81  E-value: 2.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   8 VGPIQANAYFLISDDQCLIFDPGGE--GHKINQYIKEKGLTP---LAILLTHAHFDHIGALDEVREKWDIPVYLHQNEKN 82
Cdd:cd16314    17 VGTCGISALLVTSDAGHILIDGGTDkaAPLIEANIRALGFRPedvRYIVSSHEHFDHAGGIARLQRATGAPVVAREPAAT 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1150405088  83 WLADASLNGSG-MLRGIEVTAKPADHLIEGDGE-LNIGPFHLETLFTPGHSPGSVSY 137
Cdd:cd16314    97 TLERGRSDRSDpQFLVVEKFPPVASVQRIGDGEvLRVGPLALTAHATPGHTPGGTSW 153
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 13-160 3.03e-06

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 46.72  E-value: 3.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  13 ANAYFLISDDQCLIFDPGgeghkINQYIKEKGLTPL--------AILLTHAHFDHIGAL-DEVREKWDIPVYLHQNEKNw 83
Cdd:COG1236    14 GSCYLLETGGTRILIDCG-----LFQGGKERNWPPFpfrpsdvdAVVLTHAHLDHSGALpLLVKEGFRGPIYATPATAD- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  84 LADASLNGSGMLRGIEVTAKP---------ADHLIEG---DGELNIGPFHLEtlFTP-GHSPGSVSYYVKDAD--LVISG 148
Cdd:COG1236    88 LARILLGDSAKIQEEEAEAEPlyteedaerALELFQTvdyGEPFEIGGVRVT--FHPaGHILGSAQVELEVGGkrIVFSG 165

                         170
                  ....*....|..
gi 1150405088 149 DvlfqggIGRTD 160
Cdd:COG1236   166 D------YGRED 171
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 8-125 5.28e-06

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: 45.62  E-value: 5.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   8 VGpiQANAYFLIS-DDQCLIFDPGGE------GHKINQYIKEKGLTPL-AILLTHAHFDHIGALDEVREKWDIPVYLHqn 79
Cdd:COG2333     8 VG--QGDAILIRTpDGKTILIDTGPRpsfdagERVVLPYLRALGIRRLdLLVLTHPDADHIGGLAAVLEAFPVGRVLV-- 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1150405088  80 ekNWLADASLNGSGMLRGIEVTAKPADHLIEGDgELNIGPFHLETL 125
Cdd:COG2333    84 --SGPPDTSETYERLLEALKEKGIPVRPCRAGD-TWQLGGVRFEVL 126
PRK11539 PRK11539
ComEC family competence protein; Provisional
 25-84 1.13e-05

ComEC family competence protein; Provisional


Pssm-ID: 236924 [Multi-domain]  Cd Length: 755  Bit Score: 45.37  E-value: 1.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150405088  25 LIFD-----PGGE--GHKINQYIKEKGLTPLAILLTHAHFDHIGALDEVREKW-DIPVYLHQNEKNWL 84
Cdd:PRK11539  523 ILYDtgnawPTGDsaQQVIIPWLRWHGLTPEGIILSHEHLDHRGGLASLLHAWpMAWIRSPLNWANHL 590
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 15-157 1.97e-05

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: 44.23  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  15 AYFLISDDQCLIF-DPGGE--GHKINQYIKEKGLTP--LAILL-THAHFDHIGALDEVREKWDIPVYLHQNEKNWLA--- 85
Cdd:cd16288    23 ASYLITTPQGLILiDTGLEssAPMIKANIRKLGFKPsdIKILLnSHAHLDHAGGLAALKKLTGAKLMASAEDAALLAsgg 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150405088  86 --DASLNGSGMLrgieVTAKPADHLIEGDGELNIGPFHLETLFTPGHSPGSVSYYVKDADLVISGDVLFQGGIG 157
Cdd:cd16288   103 ksDFHYGDDSLA----FPPVKVDRVLKDGDRVTLGGTTLTAHLTPGHTRGCTTWTMTVKDDGKVYQVVFADSLT 172
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 50-137 2.07e-05

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


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 43.88  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  50 ILLTHAHFDHIGALDEVREKWDIPVYLHQNEKNWLADASLNG----SGMLRGIEvtAKPADHLIEgDGE-LNIGPFHLET 124
Cdd:cd16315    64 LLSSHEHFDHVGGLAALQRATGARVAASAAAAPVLESGKPAPddpqAGLHEPFP--PVRVDRIVE-DGDtVALGSLRLTA 140

                          90
                  ....*....|...
gi 1150405088 125 LFTPGHSPGSVSY 137
Cdd:cd16315   141 HATPGHTPGALSW 153
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-192 2.21e-05

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 43.34  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  14 NAYFLISDDQCLIFD-PGGEGHKINQYIKEkgLTPLAI---LLTHAHFDHIGALDEVREkwDIPVYL-HQNEKNWLadas 88
Cdd:cd16276    11 QSMFLVTDKGVIVVDaPPSLGENLLAAIRK--VTDKPVthvVYSHNHADHIGGASIFKD--EGATIIaHEATAELL---- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  89 lngsgmlrgiEVTAKPA----DHLIEGDGELNIGPFHLE-TLFTPGHSPGSVSYYVKD------ADLVISGDVLFQGGIG 157
Cdd:cd16276    83 ----------KRNPDPKrpvpTVTFDDEYTLEVGGQTLElSYFGPNHGPGNIVIYLPKqkvlmaVDLINPGWVPFFNFAG 152

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1150405088 158 RTDlIGGNQETlltsiHEKLLTLPEHTLVlSGHGP 192
Cdd:cd16276   153 SED-IPGYIEA-----LDELLEYDFDTFV-GGHGN 180
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 17-124 3.78e-05

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 42.98  E-value: 3.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  17 FLI-SDDQCLIFDP--GGEGHKINQY-IKEKGLTPL-AILLTHAHFDHIG--ALDEVREKwDIPVYLHQNEKNWLADASL 89
Cdd:COG2220    14 FLIeTGGKRILIDPvfSGRASPVNPLpLDPEDLPKIdAVLVTHDHYDHLDdaTLRALKRT-GATVVAPLGVAAWLRAWGF 92

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1150405088  90 N--------GSGMLRGIEVTAKPADH---LIEGDGELNIGpFHLET 124
Cdd:COG2220    93 PrvteldwgESVELGGLTVTAVPARHssgRPDRNGGLWVG-FVIET 137
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 40-137 3.78e-05

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


Pssm-ID: 293847  Cd Length: 239  Bit Score: 43.27  E-value: 3.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  40 IKEKGLTPLA---ILLTHAHFDHIGALDEVREKWDIPVYLHQNEKNWLADAslnGSGMLR-GIEVTAKP--ADHLIEgDG 113
Cdd:cd16289    51 MRALGVAPGDlklILHSHAHADHAGPLAALKRATGARVAANAESAVLLARG---GSDDIHfGDGITFPPvqADRIVM-DG 126

                          90       100
                  ....*....|....*....|....*
gi 1150405088 114 E-LNIGPFHLETLFTPGHSPGSVSY 137
Cdd:cd16289   127 EvVTLGGVTFTAHFTPGHTPGSTSW 151
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 41-196 5.70e-05

metallo-beta-lactamases; subclasses B1 and B2 and related proteins; 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. B1 MBls include 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. B2 MBLs have a narrow substrate profile that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis. B2 MBLs include Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I.


Pssm-ID: 293793 [Multi-domain]  Cd Length: 219  Bit Score: 42.53  E-value: 5.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  41 KEKGLTPLAILLTHAHFDHIGALDEVREK----WDIPVYLHQNEKNWLADASLNGSGMLRGIEVTAKPADHLIEGDGELN 116
Cdd:cd07707    53 KVSQKPVTEVINTHFHTDRAGGNAYLKERgaktVSTALTRDLAKSEWAEIVAFTRKGLPEYPDLGYELPDGVLDGDFNLQ 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088 117 IGPfhLETLFT-PGHSPGSVSYYVKDADLVISGDVLFQGGIGrtDLIGGNQETLLTSIhEKLLTL-PEHTLVLSGHGPET 194
Cdd:cd07707   133 FGK--VEAFYPgPAHTPDNIVVYFPQENVLYGGCIIKETDLG--NVADADVKEWPTSI-ERLKKRyRNIKAVIPGHGEVG 207


                  ..
gi 1150405088 195 DV 196
Cdd:cd07707   208 GP 209
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 3-191 1.23e-04

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: 41.50  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088   3 WRRMPVGPIQANAYFLISDDQCLIFDPG-GEGH--KINQYIKEK-GLTPLAILLTHAHFDHIGALDEVREKwDIPVYLHQ 78
Cdd:cd16285    16 LAEFNGGAVPSNGLIVIDGKGLVLIDTPwTEAQtaTLLDWIEKKlGKPVTAAISTHSHDDRTGGIKALNAR-GIPTYATA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  79 neknwLADASLNGSGMlrgievtaKPADHLIEGDGELNIGPFhlETLFT-PGHSPGS-VSYYVKDadlvisgDVLFQG-- 154
Cdd:cd16285    95 -----LTNELAKKEGK--------PVPTHSLKGALTLGFGPL--EVFYPgPGHTPDNiVVWLPKS-------KILFGGcl 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1150405088 155 --GIGRTDL--IGG-NQETLLTSIHEKLLTLPEHTLVLSGHG 191
Cdd:cd16285   153 vkSASATSLgnVGDaDVEAWPKSIENLKAKYPEARMVVPGHG 194
PRK02113 PRK02113
MBL fold metallo-hydrolase;
49-79 3.42e-04

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 40.54  E-value: 3.42e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1150405088  49 AILLTHAHFDHIGALDEVR---EKWDIPVYLHQN 79
Cdd:PRK02113   69 AVLITHEHYDHVGGLDDLRpfcRFGEVPIYAEQY 102
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 13-151 8.50e-04

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: 39.02  E-value: 8.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  13 ANAYFLISDDQCLIFDPG---GEGHK----INQYIKEKGLTplAILLTHAHFDHIG---ALDEVREKWDIPVYLHQN-EK 81
Cdd:cd07710    18 SNMTFIEGDTGLIIIDTLesaEAAKAalelFRKHTGDKPVK--AIIYTHSHPDHFGgagGFVEEEDSGKVPIIAPEGfME 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  82 NWLADASLNGSGMLR--------------------GI-------EVTAKPADHLIEGDGE-LNIGPFHLETLFTPGHSPG 133
Cdd:cd07710    96 EAVSENVLAGNAMSRraayqfgallpkgekgqvgaGLgpglstgTVGFIPPTITITETGEtLTIDGVELEFQHAPGEAPD 175

                         170
                  ....*....|....*...
gi 1150405088 134 SVSYYVKDADLVISGDVL 151
Cdd:cd07710   176 EMMVWLPDYKVLFCADNV 193
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 49-77 8.81e-04

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: 39.14  E-value: 8.81e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1150405088  49 AILLTHAHFDHIGALDEVREKW-DIPVYLH 77
Cdd:cd07713    58 AVVLSHGHYDHTGGLKALLELNpKAPVYAH 87
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 49-75 8.82e-04

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: 38.98  E-value: 8.82e-04
                          10        20
                  ....*....|....*....|....*...
gi 1150405088  49 AILLTHAHFDHIGALDE-VREKWDIPVY 75
Cdd:cd16295    54 AVILTHAHLDHSGRLPLlVKEGFRGPIY 81
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 20-60 9.83e-04

MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain; Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. 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: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 38.63  E-value: 9.83e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1150405088  20 SDDQCLIFDpGGEGhkI----NQYIKEKGLTPLAILLTHAHFDHI 60
Cdd:cd07715    30 AGGELLILD-AGTG--IrelgNELMKEGPPGEAHLLLSHTHWDHI 71
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
49-151 1.14e-03

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 38.71  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  49 AILLTHAHFDHIGALDEV-REKWDIPVYLHQN--EKNWLADASLNGSGMLRGIEVTAKPADHLIEGDGELNI-------G 118
Cdd:COG1237    60 AVVLSHGHYDHTGGLPALlELNPKAPVYAHPDafEKRYSKRPGGKYIGIPFSREELEKLGARLILVKEPTEIapgvyltG 139

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1150405088 119 PFHLETLFtpghSPGSVSYYVKDADLVISGDVL 151
Cdd:COG1237   140 EIPRVTDF----EKGDPGLYVKEDGGLVPDPFL 168
VIM_type_MBL-B1 cd16303
VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona ...
 36-192 1.83e-03

VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona integron-encoded metallo-beta-lactamase)-type MBLs are integron-associated and are widely distributed acquired MBLs. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of VIM-type MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293861 [Multi-domain]  Cd Length: 218  Bit Score: 37.92  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  36 INQYIKEKGLTPLAILLTHAHFDHIGALDeVREKWDIPVYLHQNEKNwLADAslngsgmlRGIEVtakpADHLIEG---- 111
Cdd:cd16303    55 LAEIEKQIGLPVTRAVSTHFHDDRVGGVD-VLRAAGVATYASPSTRR-LAEA--------EGNEI----PTHSLEGlsss 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088 112 DGELNIGPfhLETLFT-PGHSPGSVSYYVKDADLVISGDVLFqgGIGRTDLIG---GNQETLLTSIHEKLLTLPEHTLVL 187
Cdd:cd16303   121 GDAVRFGP--VELFYPgAAHSTDNLVVYVPSARVLYGGCAVR--ELSSTSAGNvadADLAEWPTSIERIQKHYPEAEFVI 196


                  ....*
gi 1150405088 188 SGHGP 192
Cdd:cd16303   197 PGHGL 201
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 40-83 2.92e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 293839  Cd Length: 252  Bit Score: 37.47  E-value: 2.92e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1150405088  40 IKEKGLTP---LAILLTHAHFDHI-GALDEVREKWDIPVY----LHQNEKNW 83
Cdd:cd16281    85 LARLGLSPediTDVILTHLHFDHCgGATRADDDGLVELLFpnatYWVQKRHW 136
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 40-154 5.47e-03

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


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 36.33  E-value: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  40 IKEKGLTPLAILLTHAHFDHIGALDEVREKW-DIPVYLHQN----------EKNWLADASLNGSGMLRGIEVTAKPADHL 108
Cdd:cd07739    46 IKASGKTLTTIYITHGHPDHYFGLEVLLEAFpDAKVVATPAvvahikaqlePKLAFWGPLLGGNAPARLVVPEPLDGDTL 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1150405088 109 iEGDGELnigpfhLETLFTPGHSPGSVSY-YVKDADLVISGDVLFQG 154
Cdd:cd07739   126 -TLEGHP------LEIVGVGGGDTDDTTYlWIPSLKTVVAGDVVYNG 165
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 27-150 6.36e-03

class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. 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: 293821  Cd Length: 259  Bit Score: 36.42  E-value: 6.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150405088  27 FDPGGEGHKINQYIKekgltplAILLTHAHFDHIGAL----DEVREKWD--IPVY--------LHQNEKNWLA--DASLN 90
Cdd:cd07735    53 FPSQKAAYELYQRIR-------HYLITHAHLDHIAGLpllsPNDGGQRGspKTIYglpetidaLKKHIFNWVIwpDFTSI 125

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150405088  91 GSGMLRGIEVTAKPADHLIEGDGeLNIGPFHLEtlftpgHS-PGSVSYYVKDAD--LVISGDV 150
Cdd:cd07735   126 PSGKYPYLRLEPIEPEYPIALTG-LSVTAFPVS------HGvPVSTAFLIRDGGdsFLFFGDT 181
 
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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