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Conserved domains on  [gi|16128894|ref|NP_415447|]
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hydroxyacylglutathione hydrolase GloC [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10870212)

MBL fold metallo-hydrolase similar to Salmonella enterica YcbL: a type II glyoxalase

Gene Ontology:  GO:0016787
PubMed:  17597585

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 3-192 1.26e-130

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: 365.34  E-value: 1.26e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894   3 YRIIPVTAFSQNCSLIWCEQTRLAALVDPGGDAEKIKQEVDDSGLTLMQILLTHGHLDHVGAAAELAQHYGVPVFGPEKE 82
Cdd:cd07737   1 YQIIPVTPFQQNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  83 DEFWLQGLPAQSRMFGLEECQPLTPDRWLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDRAKLLISGDVIFKGGVGRSD 162
Cdd:cd07737  81 DKFLLENLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTD 160

                       170       180       190
                ....*....|....*....|....*....|
gi 16128894 163 FPRGDHNQLISSIKDKLLPLGDDVIFIPGH 192
Cdd:cd07737 161 FPGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
 
Name Accession Description Interval E-value
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 3-192 1.26e-130

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: 365.34  E-value: 1.26e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894   3 YRIIPVTAFSQNCSLIWCEQTRLAALVDPGGDAEKIKQEVDDSGLTLMQILLTHGHLDHVGAAAELAQHYGVPVFGPEKE 82
Cdd:cd07737   1 YQIIPVTPFQQNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  83 DEFWLQGLPAQSRMFGLEECQPLTPDRWLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDRAKLLISGDVIFKGGVGRSD 162
Cdd:cd07737  81 DKFLLENLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTD 160

                       170       180       190
                ....*....|....*....|....*....|
gi 16128894 163 FPRGDHNQLISSIKDKLLPLGDDVIFIPGH 192
Cdd:cd07737 161 FPGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 7-208 1.17e-61

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: 191.44  E-value: 1.17e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894   7 PVTAFSQNCSLIWCeqTRLAALVDPGGD---AEKIKQEVDDSGLTLMQILLTHGHLDHVGAAAELAQHYGVPVFGPEKED 83
Cdd:COG0491   9 PGAGLGVNSYLIVG--GDGAVLIDTGLGpadAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEA 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  84 EFWLQglPAQSRMFGLEecqPLTPDRWLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDRAKLLISGDVIFKGGVGRSDF 163
Cdd:COG0491  87 EALEA--PAAGALFGRE---PVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDL 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16128894 164 PRGDHNQLISSIkDKLLPLGDDVIfIPGHGPLSTLG-----------YERLHNPFL 208
Cdd:COG0491 162 PDGDLAQWLASL-ERLLALPPDLV-IPGHGPPTTAEaidyleellaaLGERANPFL 215
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 14-192 1.83e-43

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: 143.85  E-value: 1.83e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894     14 NCSLIWCEQTrlAALVDPG-GDAEKIKQEVDDSGL-TLMQILLTHGHLDHVGAAAELAQHYGVPVFGPEKEDEFWLQGLP 91
Cdd:smart00849   1 NSYLVRDDGG--AILIDTGpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894     92 AQSRMFGLEEcqPLTPDRWLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDRAKLLISGDVIFKGGVGRSDFPRGDHNQL 171
Cdd:smart00849  79 LLGELGAEAE--PAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAAS 156

                          170       180
                   ....*....|....*....|.
gi 16128894    172 ISSIKDKLLPLGDDVIFIPGH 192
Cdd:smart00849 157 DALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
8-192 1.97e-34

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 121.32  E-value: 1.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894     8 VTAFSQNCSLIwcEQTRLAALVDPGGDAEKIKQE----VDDSGLTLMQILLTHGHLDHVGAAAELAQHYGVPVFGPEKED 83
Cdd:pfam00753   1 LGPGQVNSYLI--EGGGGAVLIDTGGSAEAALLLllaaLGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894    84 EFWLQGLPAQSRMFG---LEECQPLTPDRWLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDRAKLLISGDVIFKGGVGR 160
Cdd:pfam00753  79 RELLDEELGLAASRLglpGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGR 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 16128894   161 SDFPRGDHNQLISSIKDKLLPLGDDV------IFIPGH 192
Cdd:pfam00753 159 LDLPLGGLLVLHPSSAESSLESLLKLaklkaaVIVPGH 196
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 1-192 6.46e-19

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 81.79  E-value: 6.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894    1 MNYRIIPvtAFSQNCSLIWCEQTRLAALVDPGgDAEKIKQEVDDSGLTLMQILLTHGHLDHVGAAAELAQHY-GVPVFGP 79
Cdd:PRK10241   1 MNLNSIP--AFDDNYIWVLNDEAGRCLIVDPG-EAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFpQIVVYGP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894   80 ekedefwlqglpaqsrmfglEECQPLTPDRWLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDraKLLISGDVIFKGGVG 159
Cdd:PRK10241  78 --------------------QETQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYFSK--PYLFCGDTLFSGGCG 135

                        170       180       190
                 ....*....|....*....|....*....|...
gi 16128894  160 RsdFPRGDHNQLISSIKdKLLPLGDDVIFIPGH 192
Cdd:PRK10241 136 R--LFEGTASQMYQSLK-KINALPDDTLICCAH 165
 
Name Accession Description Interval E-value
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 3-192 1.26e-130

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: 365.34  E-value: 1.26e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894   3 YRIIPVTAFSQNCSLIWCEQTRLAALVDPGGDAEKIKQEVDDSGLTLMQILLTHGHLDHVGAAAELAQHYGVPVFGPEKE 82
Cdd:cd07737   1 YQIIPVTPFQQNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  83 DEFWLQGLPAQSRMFGLEECQPLTPDRWLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDRAKLLISGDVIFKGGVGRSD 162
Cdd:cd07737  81 DKFLLENLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTD 160

                       170       180       190
                ....*....|....*....|....*....|
gi 16128894 163 FPRGDHNQLISSIKDKLLPLGDDVIFIPGH 192
Cdd:cd07737 161 FPGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 4-192 2.81e-73

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: 219.85  E-value: 2.81e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894   4 RIIPVTAFSQNCSLIWCEQTRlAALVDPGGDA-EKIKQEVDDSGLTLMQILLTHGHLDHVGAAAELAQHYGVPVFGPEKe 82
Cdd:cd06262   1 KRLPVGPLQTNCYLVSDEEGE-AILIDPGAGAlEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEA- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  83 DEFWLQGLPAQSRMFGLEECQPLTPDRWLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDRAKLLISGDVIFKGGVGRSD 162
Cdd:cd06262  79 DAELLEDPELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTD 158

                       170       180       190
                ....*....|....*....|....*....|
gi 16128894 163 FPRGDHNQLISSIKDKLLPLGDDVIFIPGH 192
Cdd:cd06262 159 LPGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 4-208 5.11e-73

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: 219.91  E-value: 5.11e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894   4 RIIPVTAFSQNCSLIWCEQTRLAALVDPGGDAEKIKQEVDDSGLTLMQILLTHGHLDHVGAAAELAQHYGVPVFGPEKED 83
Cdd:cd16322   2 RPFTLGPLQENTYLVADEGGGEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  84 EFWlQGLPAQSRMFGLEECQPLTPDRWLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDRAKLLISGDVIFKGGVGRSDF 163
Cdd:cd16322  82 PLY-EAADLGAKAFGLGIEPLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRTDL 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 16128894 164 PRGDHNQLISSIKdKLLPLGDDVIFIPGHGPLSTLGYERLHNPFL 208
Cdd:cd16322 161 PGGDPKAMAASLR-RLLTLPDETRVFPGHGPPTTLGEERRTNPFL 204
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 7-208 1.17e-61

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: 191.44  E-value: 1.17e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894   7 PVTAFSQNCSLIWCeqTRLAALVDPGGD---AEKIKQEVDDSGLTLMQILLTHGHLDHVGAAAELAQHYGVPVFGPEKED 83
Cdd:COG0491   9 PGAGLGVNSYLIVG--GDGAVLIDTGLGpadAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEA 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  84 EFWLQglPAQSRMFGLEecqPLTPDRWLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDRAKLLISGDVIFKGGVGRSDF 163
Cdd:COG0491  87 EALEA--PAAGALFGRE---PVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDL 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16128894 164 PRGDHNQLISSIkDKLLPLGDDVIfIPGHGPLSTLG-----------YERLHNPFL 208
Cdd:COG0491 162 PDGDLAQWLASL-ERLLALPPDLV-IPGHGPPTTAEaidyleellaaLGERANPFL 215
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 6-192 3.86e-46

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: 150.30  E-value: 3.86e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894   6 IPVTAFSQN-CSLIWCEQTRLAALVDPGgDAEKIKQEVDDSGLTLMQILLTHGHLDHVGAAAELAQHYG-VPVFGPEKEd 83
Cdd:cd07723   1 VPIPALSDNyIYLIVDEATGEAAVVDPG-EAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPdAPVYGPAED- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  84 efwlqglpaqsRMFGLeecqpltpDRWLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDRAKLLISGDVIFKGGVGRsdF 163
Cdd:cd07723  79 -----------RIPGL--------DHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGR--F 137

                       170       180
                ....*....|....*....|....*....
gi 16128894 164 PRGDHNQLISSIkDKLLPLGDDVIFIPGH 192
Cdd:cd07723 138 FEGTAEQMYASL-QKLLALPDDTLVYCGH 165
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 17-193 1.15e-43

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: 144.08  E-value: 1.15e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  17 LIWCEQTRLAALVDPGGD-AEKIKQEVDDSGLTLMQILLTHGHLDHVGAAAELAQHYGVPVFGPEKEDEFwlqglpaqsr 95
Cdd:cd07724  16 LVGDPETGEAAVIDPVRDsVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGEGAPAS---------- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  96 mfgleecqplTPDRWLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDRAKLLISGDVIFKGGVGRSDFP---RGDHNQLI 172
Cdd:cd07724  86 ----------FFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPgeaEGLARQLY 155

                       170       180
                ....*....|....*....|.
gi 16128894 173 SSIKDKLLPLGDDVIFIPGHG 193
Cdd:cd07724 156 DSLQRKLLLLPDETLVYPGHD 176
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 14-192 1.83e-43

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: 143.85  E-value: 1.83e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894     14 NCSLIWCEQTrlAALVDPG-GDAEKIKQEVDDSGL-TLMQILLTHGHLDHVGAAAELAQHYGVPVFGPEKEDEFWLQGLP 91
Cdd:smart00849   1 NSYLVRDDGG--AILIDTGpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894     92 AQSRMFGLEEcqPLTPDRWLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDRAKLLISGDVIFKGGVGRSDFPRGDHNQL 171
Cdd:smart00849  79 LLGELGAEAE--PAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAAS 156

                          170       180
                   ....*....|....*....|.
gi 16128894    172 ISSIKDKLLPLGDDVIFIPGH 192
Cdd:smart00849 157 DALESLLKLLKLLPKLVVPGH 177
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 23-192 3.82e-40

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: 134.97  E-value: 3.82e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  23 TRLAALVDPGGDAEKIKQEVDDSGLTLMQILLTHGHLDHVGAAAELAQHYGVPVFGPEKEDEFWlqGLPaqsrmfgleeC 102
Cdd:cd16275  22 TREAAVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDYY--GFR----------C 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894 103 QPLTPdrwLNEGDTISIGNVTLQVLHCPGHTPGHVVFF-DDRaklLISGDVIFKGGVGRSDFPRGDHNQLISSIK--DKL 179
Cdd:cd16275  90 PNLIP---LEDGDTIKIGDTEITCLLTPGHTPGSMCYLlGDS---LFTGDTLFIEGCGRCDLPGGDPEEMYESLQrlKKL 163

                       170
                ....*....|...
gi 16128894 180 LPlgDDVIFIPGH 192
Cdd:cd16275 164 PP--PNTRVYPGH 174
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 14-193 3.10e-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: 126.18  E-value: 3.10e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  14 NCSLIWCEQTrlAALVDPG--GDAEKIKQEVDDSGLTLMQ---ILLTHGHLDHVGAAAELAQHYGVPVFGPEKE------ 82
Cdd:cd07721  12 NAYLIEDDDG--LTLIDTGlpGSAKRILKALRELGLSPKDirrILLTHGHIDHIGSLAALKEAPGAPVYAHEREapyleg 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  83 --DEFWLQGLPAQSRMFGLEECQPLTPDRWLNEGDTISIGnVTLQVLHCPGHTPGHVVFFDDRAKLLISGDVIFKGGvGR 160
Cdd:cd07721  90 ekPYPPPVRLGLLGLLSPLLPVKPVPVDRTLEDGDTLDLA-GGLRVIHTPGHTPGHISLYLEEDGVLIAGDALVTVG-GE 167

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 16128894 161 SDFPRG----DHNQLISSIKdKLLPLGDDVIfIPGHG 193
Cdd:cd07721 168 LVPPPPpftwDMEEALESLR-KLAELDPEVL-APGHG 202
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
8-192 1.97e-34

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 121.32  E-value: 1.97e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894     8 VTAFSQNCSLIwcEQTRLAALVDPGGDAEKIKQE----VDDSGLTLMQILLTHGHLDHVGAAAELAQHYGVPVFGPEKED 83
Cdd:pfam00753   1 LGPGQVNSYLI--EGGGGAVLIDTGGSAEAALLLllaaLGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894    84 EFWLQGLPAQSRMFG---LEECQPLTPDRWLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDRAKLLISGDVIFKGGVGR 160
Cdd:pfam00753  79 RELLDEELGLAASRLglpGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGR 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 16128894   161 SDFPRGDHNQLISSIKDKLLPLGDDV------IFIPGH 192
Cdd:pfam00753 159 LDLPLGGLLVLHPSSAESSLESLLKLaklkaaVIVPGH 196
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 26-194 1.15e-28

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: 106.04  E-value: 1.15e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  26 AALVDPGGDAEKIKQEVDD--SGLTLMQILLTHGHLDHVGAAAELAQHYGVPVFGPEKEDEFWLQGLPAqsrmfgleecq 103
Cdd:cd16278  29 VVVIDPGPDDPAHLDALLAalGGGRVSAILVTHTHRDHSPGAARLAERTGAPVRAFGPHRAGGQDTDFA----------- 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894 104 pltPDRWLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDRAKLLISGDVIFkggvGRS----DFPRGDHNQLISSIkDKL 179
Cdd:cd16278  98 ---PDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVM----GWSttviAPPDGDLGDYLASL-ERL 169

                       170
                ....*....|....*
gi 16128894 180 LPLGDDVIFiPGHGP 194
Cdd:cd16278 170 LALDDRLLL-PGHGP 183
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 26-192 1.69e-24

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: 95.00  E-value: 1.69e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  26 AALVDPGGDAEKIKQEVDDSGLTLMQILLTHGHLDHVGAAAELAQHYGVPVFGPEKEDEFWLQGLPAQSRMFgleECQPL 105
Cdd:cd07712  20 ALLIDTGLGIGDLKEYVRTLTDLPLLVVATHGHFDHIGGLHEFEEVYVHPADAEILAAPDNFETLTWDAATY---SVPPA 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894 106 TPDRWLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDRAKLLISGDVIFKGGVgRSDFPRGDHNQLISSIKdKLLPLGDD 185
Cdd:cd07712  97 GPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVYDGPL-IMDLPHSDLDDYLASLE-KLSKLPDE 174


                ....*...
gi 16128894 186 V-IFIPGH 192
Cdd:cd07712 175 FdKVLPGH 182
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 26-197 9.28e-24

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: 93.78  E-value: 9.28e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  26 AALVDPGGD---AEKIKQEVDD-SGLTLMQILLTHGHLDHVGAAAELAQHyGVPVFGPEK-------EDEFWLQGLPAQS 94
Cdd:cd16282  26 VVVIDTGASprlARALLAAIRKvTDKPVRYVVNTHYHGDHTLGNAAFADA-GAPIIAHENtreelaaRGEAYLELMRRLG 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  95 RmFGLEECQPLTPDRWLNEGDTISIGNVTLQVLH-CPGHTPGHVVFFDDRAKLLISGDVIFKGGVGrsDFPRGDHNQLIS 173
Cdd:cd16282 105 G-DAMAGTELVLPDRTFDDGLTLDLGGRTVELIHlGPAHTPGDLVVWLPEEGVLFAGDLVFNGRIP--FLPDGSLAGWIA 181

                       170       180
                ....*....|....*....|....
gi 16128894 174 SIkDKLLPLGDDVIfIPGHGPLST 197
Cdd:cd16282 182 AL-DRLLALDATVV-VPGHGPVGD 203
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 27-193 4.30e-19

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: 80.81  E-value: 4.30e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  27 ALVDPG----GDAEKIKQEVDDSGLTLMQI---LLTHGHLDHVGAAAELAQHYGVPVFGPekedefwlqglpaqsrmfgl 99
Cdd:cd07725  27 TLIDTGlateEDAEALWEGLKELGLKPSDIdrvLLTHHHPDHIGLAGKLQEKSGATVYIL-------------------- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894 100 eecqpltPDRWLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDRAKLLISGDVI---FKGGVGRSDFPRGDH-NQLISSI 175
Cdd:cd07725  87 -------DVTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVlpkITPNVSLWAVRVEDPlGAYLESL 159

                       170
                ....*....|....*...
gi 16128894 176 kDKLLPLGDDVIFiPGHG 193
Cdd:cd07725 160 -DKLEKLDVDLAY-PGHG 175
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 1-192 6.46e-19

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 81.79  E-value: 6.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894    1 MNYRIIPvtAFSQNCSLIWCEQTRLAALVDPGgDAEKIKQEVDDSGLTLMQILLTHGHLDHVGAAAELAQHY-GVPVFGP 79
Cdd:PRK10241   1 MNLNSIP--AFDDNYIWVLNDEAGRCLIVDPG-EAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFpQIVVYGP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894   80 ekedefwlqglpaqsrmfglEECQPLTPDRWLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDraKLLISGDVIFKGGVG 159
Cdd:PRK10241  78 --------------------QETQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYFSK--PYLFCGDTLFSGGCG 135

                        170       180       190
                 ....*....|....*....|....*....|...
gi 16128894  160 RsdFPRGDHNQLISSIKdKLLPLGDDVIFIPGH 192
Cdd:PRK10241 136 R--LFEGTASQMYQSLK-KINALPDDTLICCAH 165
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 26-192 8.85e-19

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: 80.61  E-value: 8.85e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  26 AALVDPGGD--AEKIKQEVDDSGLTLMQ---ILLTHGHLDHVGAAAELAQHY----------GVP--------------V 76
Cdd:cd07726  27 PALIDTGPSssVPRLLAALEALGIAPEDvdyIILTHIHLDHAGGAGLLAEALpnakvyvhprGARhlidpsklwasaraV 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  77 FGpEKEDEFWLQGLP-AQSRMFGLEEcqpltpdrwlneGDTISIGNVTLQVLHCPGHTPGHVVFFDDRAKLLISGD---V 152
Cdd:cd07726 107 YG-DEADRLGGEILPvPEERVIVLED------------GETLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDaagV 173

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 16128894 153 IFKGGVGRSDF----PRGDHNQLISSIkDKLLPLGDDVIFiPGH 192
Cdd:cd07726 174 RYPELDVVGPPstppPDFDPEAWLESL-DRLLSLKPERIY-LTH 215
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 4-192 1.75e-18

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 80.96  E-value: 1.75e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894    4 RIIPVTAFSQNCS-LIWCEQTRLAALVDPGgDAEKIKQEVDDSGLTLMQILLTHGHLDHVGAAAELAQHY-GVPVFGPEK 81
Cdd:PLN02469   2 KIIPVPCLEDNYAyLIIDESTKDAAVVDPV-DPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVpGIKVYGGSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894   82 EdefwlqglpaqsrmfGLEECQpltpdRWLNEGDTISIGN-VTLQVLHCPGHTPGHVVFF------DDRAklLISGDVIF 154
Cdd:PLN02469  81 D---------------NVKGCT-----HPVENGDKLSLGKdVNILALHTPCHTKGHISYYvtgkegEDPA--VFTGDTLF 138

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 16128894  155 KGGVGRsdFPRGDHNQLISSIKDKLLPLGDDVIFIPGH 192
Cdd:PLN02469 139 IAGCGK--FFEGTAEQMYQSLCVTLGSLPKPTQVYCGH 174
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 14-194 2.09e-18

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


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 79.11  E-value: 2.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  14 NCSLIWCEQTRLaaLVDPG----GDAEKIKQEVDDSGL-TLMQILLTHGHLDHVGAAAELAQHYGVPvfgpekEDEFWLQ 88
Cdd:cd07722  19 NTYLVGTGKRRI--LIDTGegrpSYIPLLKSVLDSEGNaTISDILLTHWHHDHVGGLPDVLDLLRGP------SPRVYKF 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  89 GLPAQSRMFGLEEcQPLTPdrwLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDRAKLLISGDVIFkgGVGRSDFprGDH 168
Cdd:cd07722  91 PRPEEDEDPDEDG-GDIHD---LQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGDCVL--GHGTAVF--EDL 162

                       170       180
                ....*....|....*....|....*.
gi 16128894 169 NQLISSIKdKLLPLGDDVIFiPGHGP 194
Cdd:cd07722 163 AAYMASLK-KLLSLGPGRIY-PGHGP 186
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 52-140 4.35e-18

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: 79.55  E-value: 4.35e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  52 ILLTHGHLDHVGAAAELAQHYGVPVFGPEKEDEFWLQ--GLPAQSRMFgleecQPLTPDRWLNEGDTISIGNVTLQVLHC 129
Cdd:cd16280  65 ILITHGHGDHYGGAAYLKDLYGAKVVMSEADWDMMEEppEEGDNPRWG-----PPPERDIVIKDGDTLTLGDTTITVYLT 139

                        90
                ....*....|.
gi 16128894 130 PGHTPGHVVFF 140
Cdd:cd16280 140 PGHTPGTLSLI 150
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 21-192 1.11e-15

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 74.11  E-value: 1.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894   21 EQTRLAALVDPGgDAEKIKQEVDDSGLTLMQILLTHGHLDHVGAAAELAQHYGVPVFGPEKEdefwlqglpaQSRMFGLe 100
Cdd:PLN02398  95 EDTGTVGVVDPS-EAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVD----------KDRIPGI- 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  101 ecqpltpDRWLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDRAKLLISGDVIFKGGVGRsdFPRGDHNQLISSIKdKLL 180
Cdd:PLN02398 163 -------DIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGK--LFEGTPEQMLSSLQ-KII 232

                        170
                 ....*....|..
gi 16128894  181 PLGDDVIFIPGH 192
Cdd:PLN02398 233 SLPDDTNIYCGH 244
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 38-139 2.57e-15

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: 72.12  E-value: 2.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  38 IKQEVDDSGLTLMQI---LLTHGHLDHVGAAAELAQHYGVPVFGPEKEDEFWLQGLPAQSRMFGLEEC-QPLTPDRWLNE 113
Cdd:cd16308  47 IKKNIQALGFKFKDIkilLTTQAHYDHVGAMAAIKQQTGAKMMVDEKDAKVLADGGKSDYEMGGYGSTfAPVKADKLLHD 126

                        90       100
                ....*....|....*....|....*.
gi 16128894 114 GDTISIGNVTLQVLHCPGHTPGHVVF 139
Cdd:cd16308 127 GDTIKLGGTKLTLLHHPGHTKGSCSF 152
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 26-154 4.33e-15

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 70.64  E-value: 4.33e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  26 AALVDPGGD---AEKIKQEVDDSGLTLMQILLTHGHLDHVGAAAELAQHYGVPVFGPEKEDEF-----------WLQGLP 91
Cdd:cd07743  20 ALLIDSGLDedaGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAFienpllepsylGGAYPP 99

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128894  92 AQSRMFGLEEcQPLTPDRWLNEGDtISIGNVTLQVLHCPGHTPGHV-VFFDDraKLLISGDVIF 154
Cdd:cd07743 100 KELRNKFLMA-KPSKVDDIIEEGE-LELGGVGLEIIPLPGHSFGQIgILTPD--GVLFAGDALF 159
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 26-211 7.95e-15

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 70.98  E-value: 7.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894   26 AALVDP-GGDAEKIKQEVDDSGLTLMQILLTHGHLDHVGAAAELAQHygvpvfgpekedefwlqgLPAQ----SRMFGLE 100
Cdd:PLN02962  38 ALLIDPvDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTK------------------LPGVksiiSKASGSK 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  101 ecqpltPDRWLNEGDTISIGNVTLQVLHCPGHTPGHVVFFDDRA------KLLISGDVIFKGGVGRSDFPRGDHNQLISS 174
Cdd:PLN02962 100 ------ADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGpdqpqpRMAFTGDALLIRGCGRTDFQGGSSDQLYKS 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 16128894  175 IKDKLLPLGDDVIFIPGHG----PLSTLGYERLHNPFL-QDE 211
Cdd:PLN02962 174 VHSQIFTLPKDTLIYPAHDykgfTVSTVGEEMLYNPRLtKDE 215
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 26-135 1.44e-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: 64.78  E-value: 1.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  26 AALVDPGGD--AEKIKQEVDDSGLTLMQ---ILLTHGHLDHVGAAAELAQHYGVPVFGPEKEDEFWLQGLPAQSRMFGLE 100
Cdd:cd16310  33 AILLDGGLEenAALIEQNIKALGFKLSDikiIINTHAHYDHAGGLAQLKADTGAKLWASRGDRPALEAGKHIGDNITQPA 112

                        90       100       110
                ....*....|....*....|....*....|....*
gi 16128894 101 ECQPLTPDRWLNEGDTISIGNVTLQVLHCPGHTPG 135
Cdd:cd16310 113 PFPAVKVDRILGDGEKIKLGDITLTATLTPGHTKG 147
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 7-194 4.08e-12

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: 62.22  E-value: 4.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894   7 PVTAFSqNCSLIWCEQTRLaaLVDPGG--DAEKIKQEVDDSGLTLMQI---LLTHGHLDHVGAAA--ELAQHYgvpvFGP 79
Cdd:cd07711  17 GFRASS-TVTLIKDGGKNI--LVDTGTpwDRDLLLKALAEHGLSPEDIdyvVLTHGHPDHIGNLNlfPNATVI----VGW 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  80 EKEDEFWLqglpaqsrMFGLEECQPLTPDrwlnegdtisiGNVtlQVLHCPGHTPGHVVFF---DDRAKLLISGDVIFKG 156
Cdd:cd07711  90 DICGDSYD--------DHSLEEGDGYEID-----------ENV--EVIPTPGHTPEDVSVLvetEKKGTVAVAGDLFERE 148

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 16128894 157 G--VGRSDFPRGDHN--QLISSIKdKLLPLGdDVIfIPGHGP 194
Cdd:cd07711 149 EdlEDPILWDPLSEDpeLQEESRK-RILALA-DWI-IPGHGP 187
NorV COG0426
Flavorubredoxin [Energy production and conversion];
26-152 6.11e-11

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 60.62  E-value: 6.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  26 AALVDPGGDA------EKIKQEVDDSGLTLmqILLTHGHLDHVGAAAELAQHY-GVPVFGPEKedefWLQGLPAqsrMFG 98
Cdd:COG0426  44 TALIDTVGESffeeflENLSKVIDPKKIDY--IIVNHQEPDHSGSLPELLELApNAKIVCSKK----AARFLPH---FYG 114

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16128894  99 LEEcqpltpDRWL--NEGDTISIGNVTLQVLHCPG-HTPGHVVFFDDRAKLLISGDV 152
Cdd:COG0426 115 IPD------FRFIvvKEGDTLDLGGHTLQFIPAPMlHWPDTMFTYDPEDKILFSGDA 165
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 52-154 1.20e-10

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: 59.10  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  52 ILLTHGHLDHVGAaaeLAQHYGVPVFG------PEKEDEFWL-----QGLPAQSRMFgLEECQ----PLTPDRWLNEGDT 116
Cdd:cd07720  95 VLLTHLHPDHIGG---LVDAGGKPVFPnaevhvSEAEWDFWLddanaAKAPEGAKRF-FDAARdrlrPYAAAGRFEDGDE 170

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 16128894 117 IsIGNVTlqVLHCPGHTPGHVVFF--DDRAKLLISGDVIF 154
Cdd:cd07720 171 V-LPGIT--AVPAPGHTPGHTGYRieSGGERLLIWGDIVH 207
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 52-135 1.47e-10

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


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 59.03  E-value: 1.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  52 ILLTHGHLDHVGAAAELAQHYGVPVFGPEKeDEFWLQGLPAQSRMFGLEECQPLTPDRWLNEGDTISIGNVTLQVLHCPG 131
Cdd:cd16309  64 LLNTHAHFDHAGGLAELKKATGAQLVASAA-DKPLLESGYVGSGDTKNLQFPPVRVDRVIGDGDKVTLGGTTLTAHLTPG 142


                ....
gi 16128894 132 HTPG 135
Cdd:cd16309 143 HSPG 146
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 52-141 5.39e-10

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: 57.33  E-value: 5.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  52 ILLTHGHLDHVGAAAELAQHYGVPVFGPEKEDEFWLQG------LPAQSRMFgleecQPLTPDRWLNEGDTISIGNVTLQ 125
Cdd:cd16288  64 LLNSHAHLDHAGGLAALKKLTGAKLMASAEDAALLASGgksdfhYGDDSLAF-----PPVKVDRVLKDGDRVTLGGTTLT 138

                        90       100       110
                ....*....|....*....|....*....|.
gi 16128894 126 VLHCPGHTPG---------------HVVFFD 141
Cdd:cd16288 139 AHLTPGHTRGcttwtmtvkddgkvyQVVFAD 169
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 ...
 52-135 6.40e-10

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: 57.36  E-value: 6.40e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  52 ILLTHGHLDHVGAAAELAQHYGVPVF-GPEKEDEFWLQGLPAQSRMFG-LEECQPLTPDRWLNEGDTISIGNVTLQVLHC 129
Cdd:cd16290  64 ILNSHAHFDHAGGIAALQRDSGATVAaSPAGAAALRSGGVDPDDPQAGaADPFPPVAKVRVVADGEVVKLGPLAVTAHAT 143


                ....*.
gi 16128894 130 PGHTPG 135
Cdd:cd16290 144 PGHTPG 149
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 52-192 2.05e-09

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: 55.68  E-value: 2.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  52 ILLTHGHLDHVGAAAELAqhyGVPVFGPEKEDEFWLQGLPAQsRMFGLEECQPLTPDRWLN----EGDTISIGNVTLqvL 127
Cdd:cd07729  92 VILSHLHFDHAGGLDLFP---NATIIVQRAELEYATGPDPLA-AGYYEDVLALDDDLPGGRvrlvDGDYDLFPGVTL--I 165

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128894 128 HCPGHTPGH-VVFFD-DRAKLLISGDVI-----FKGGVGrsDFPRGDHNQLISSIK--DKLLPLGDDVIfIPGH 192
Cdd:cd07729 166 PTPGHTPGHqSVLVRlPEGTVLLAGDAAytyenLEEGRP--PGINYDPEAALASLErlKALAEREGARV-IPGH 236
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 26-195 2.11e-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: 55.57  E-value: 2.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  26 AALVDPGGDA------EKIKQEVDDSGLTlmQILLTHGHLDHVGAAAELAQHY-GVPVFGPEKedefWLQGLPAqsrMFG 98
Cdd:cd07709  42 TALIDTVKEPffdeflENLEEVIDPRKID--YIVVNHQEPDHSGSLPELLELApNAKIVCSKK----AARFLKH---FYP 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  99 LEEcqplTPDRWLNEGDTISIGNVTLQVLHCPG-HTPGHVVFFDDRAKLLISGDvIFkGGVGRS----DFPRGDH----- 168
Cdd:cd07709 113 GID----ERFVVVKDGDTLDLGKHTLKFIPAPMlHWPDTMVTYDPEDKILFSGD-AF-GAHGASgelfDDEVEDYleear 186

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 16128894 169 ----------NQLISSIKDKLLPLGDDVIFiPGHGPL 195
Cdd:cd07709 187 ryyanimgpfSKQVRKALEKLEALDIKMIA-PSHGPI 222
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 13-152 5.90e-09

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 54.52  E-value: 5.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  13 QNCSLIWCEQTRLaaLVDPGGDAEKIKQEVDDSGLTLMQILLTHGHLDHVGAAAELAQHYG---VPVFGPEKEDEFWLQG 89
Cdd:COG1235  35 RSSILVEADGTRL--LIDAGPDLREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYGpnpIPVYATPGTLEALERR 112

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128894  90 LP-AQSRMFGLEECQPLTPdrwlneGDTISIGNVTLQ---VLHcPGHTPGHVVFFDDRAKLLISGDV 152
Cdd:COG1235 113 FPyLFAPYPGKLEFHEIEP------GEPFEIGGLTVTpfpVPH-DAGDPVGYRIEDGGKKLAYATDT 172
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 14-125 1.55e-08

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: 51.88  E-value: 1.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  14 NCSLIWCEQTRLaaLVDPGGDAEKIKQEVDDSGLTLMQ---ILLTHGHLDHVGAAAELAQHYGVPVFGPEKEdefwLQGL 90
Cdd:cd07733  10 NCTYLETEDGKL--LIDAGLSGRKITGRLAEIGRDPEDidaILVTHEHADHIKGLGVLARKYNVPIYATAGT----LRAM 83

                        90       100       110
                ....*....|....*....|....*....|....*
gi 16128894  91 PAQSRMFGLEECQPLTPdrwlneGDTISIGNVTLQ 125
Cdd:cd07733  84 ERKVGLIDVDQKQIFEP------GETFSIGDFDVE 112
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 52-135 1.56e-08

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


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 53.12  E-value: 1.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  52 ILLTHGHLDHVGAAAELAQHYGVPVFGPEKEDEFWLQGLPA----QSRMfgLEECQPLTPDRWLNEGDTISIGNVTLQVL 127
Cdd:cd16315  64 LLSSHEHFDHVGGLAALQRATGARVAASAAAAPVLESGKPApddpQAGL--HEPFPPVRVDRIVEDGDTVALGSLRLTAH 141


                ....*...
gi 16128894 128 HCPGHTPG 135
Cdd:cd16315 142 ATPGHTPG 149
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 26-135 1.70e-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: 52.93  E-value: 1.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  26 AALVDpgGDAEKIKQEVDDS----GLTLMQ---ILLTHGHLDHVGAAAELAQHYGVPVFGPEKEDEFWLQGLPAQSRMFG 98
Cdd:cd07708  33 NILID--GDMEQNAPMIKANikklGFKFSDtklILISHAHFDHAGGSAEIKKQTGAKVMAGAEDVSLLLSGGSSDFHYAN 110

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16128894  99 LEECQ--PLTPDRWLNEGDTISIGNVTLQVLHCPGHTPG 135
Cdd:cd07708 111 DSSTYfpQSTVDRAVHDGERVTLGGTVLTAHATPGHTPG 149
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 49-135 3.00e-08

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: 52.13  E-value: 3.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  49 LMQILLTHGHLDHVGAAAELAQHYGVPVFGpEKEDEFWLQGLPAQSRMFGLEEC-QPLTPDRWLNEGDTISIGNVTLQVL 127
Cdd:cd16289  61 LKLILHSHAHADHAGPLAALKRATGARVAA-NAESAVLLARGGSDDIHFGDGITfPPVQADRIVMDGEVVTLGGVTFTAH 139


                ....*...
gi 16128894 128 HCPGHTPG 135
Cdd:cd16289 140 FTPGHTPG 147
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 7-156 3.42e-08

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 51.73  E-value: 3.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894   7 PVTAFSQNCSLIWCEQTrlAALVDPG---GDAEKIKQEVDDSGLTLMQILLTHGHLDHVGAAAELAQHY-GVPVFGP--- 79
Cdd:cd07739  10 EISSFPVTSTLIYGETE--AVLVDAQftrADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAFpDAKVVATpav 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  80 --------EKEDEFWLQGLPAQSrmfgleECQPLTPDRWlnEGDTISIGNVTLQVLHCP-GHTPGHVVFFDDRAKLLISG 150
Cdd:cd07739  88 vahikaqlEPKLAFWGPLLGGNA------PARLVVPEPL--DGDTLTLEGHPLEIVGVGgGDTDDTTYLWIPSLKTVVAG 159


                ....*.
gi 16128894 151 DVIFKG 156
Cdd:cd07739 160 DVVYNG 165
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 52-151 8.17e-08

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: 51.01  E-value: 8.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  52 ILLTHGHLDHVGAAAELAQHYGVpvfgpekeDEFWLQGLPAQSRMFG--LEECQPL-TPDRWLNEGDTISIGNVTLQVLH 128
Cdd:COG2333  56 LVLTHPDADHIGGLAAVLEAFPV--------GRVLVSGPPDTSETYErlLEALKEKgIPVRPCRAGDTWQLGGVRFEVLW 127

                        90       100       110
                ....*....|....*....|....*....|..
gi 16128894 129 CPGHTPGH--------VVFFDDRAK-LLISGD 151
Cdd:COG2333 128 PPEDLLEGsdennnslVLRLTYGGFsFLLTGD 159
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 52-154 9.10e-08

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: 50.27  E-value: 9.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  52 ILLTHghLDHVGAAAELAQHYGVPVFgpEKEDEFWLQGLPAQSRMFGLEECQPLTPDrwlnegdtisignvtLQVLHCPG 131
Cdd:cd07727  51 IFLTH--RDDVADHAKWAERFGAKRI--IHEDDVNAVTRPDEVIVLWGGDPWELDPD---------------LTLIPVPG 111

                        90       100
                ....*....|....*....|...
gi 16128894 132 HTPGHVVFFDDRAKLLISGDVIF 154
Cdd:cd07727 112 HTRGSVVLLYKEKGVLFTGDHLA 134
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 52-193 1.18e-07

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: 50.58  E-value: 1.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  52 ILLTHGHLDHVGAA---AELAQHYGVPVFGPEK-----EDEFWLQGlPAQSR----MFG--LEECQP------------- 104
Cdd:cd07710  60 IIYTHSHPDHFGGAggfVEEEDSGKVPIIAPEGfmeeaVSENVLAG-NAMSRraayQFGalLPKGEKgqvgaglgpglst 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894 105 -----LTPDRWLNE-GDTISIGNVTLQVLHCPGHTPGHVVFFDDRAKLLISGDVIFKGgvgrsdFP-----RG----DHN 169
Cdd:cd07710 139 gtvgfIPPTITITEtGETLTIDGVELEFQHAPGEAPDEMMVWLPDYKVLFCADNVYHT------FPnlytlRGakyrDAL 212

                       170       180
                ....*....|....*....|....
gi 16128894 170 QLISSIkDKLLPLGDDVIFiPGHG 193
Cdd:cd07710 213 AWAKSL-DEAISLKAEVLF-PSHT 234
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 52-135 1.43e-07

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: 50.28  E-value: 1.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  52 ILLTHGHLDHVGAAAELAQHYGVPVFGPEKEDEFWLQGLPAQS--RMFGLEECQPLTPDRWLNEGDTISIGNVTLQVLHC 129
Cdd:cd16314  64 IVSSHEHFDHAGGIARLQRATGAPVVAREPAATTLERGRSDRSdpQFLVVEKFPPVASVQRIGDGEVLRVGPLALTAHAT 143


                ....*.
gi 16128894 130 PGHTPG 135
Cdd:cd16314 144 PGHTPG 149
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 24-153 3.54e-07

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 49.06  E-value: 3.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  24 RLAAL-VDPGgdaekikqEVDDsgltlmqILLTHGHLDHVGAAAELAQHYGVPVFG------PEKEDEFWLQGLPAQSRM 96
Cdd:cd16277  53 RLAAAgVRPE--------DVDY-------VLCTHLHVDHVGWNTRLVDGRWVPTFPnarylfSRAEYDHWSSPDAGGPPN 117

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16128894  97 FGLEE--CQPLtPD----RWLNEGDTISIGnvtLQVLHCPGHTPGH--VVFFDDRAKLLISGDVI 153
Cdd:cd16277 118 RGVFEdsVLPV-IEaglaDLVDDDHEILDG---IRLEPTPGHTPGHvsVELESGGERALFTGDVM 178
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 52-151 1.63e-06

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 47.22  E-value: 1.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  52 ILLTHGHLDHVGAAAELA-QHYGVPVFGPEkEDEFWLQGLpaqsrmfGLEECQPltpdrwLNEGDTISIGNVTLQVL--- 127
Cdd:COG2220  52 VLVTHDHYDHLDDATLRAlKRTGATVVAPL-GVAAWLRAW-------GFPRVTE------LDWGESVELGGLTVTAVpar 117

                        90       100       110
                ....*....|....*....|....*....|
gi 16128894 128 HCPGHTPGHV------VFFDDRAKLLISGD 151
Cdd:COG2220 118 HSSGRPDRNGglwvgfVIETDGKTIYHAGD 147
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 52-128 2.37e-06

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: 45.97  E-value: 2.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  52 ILLTHGHLDHVGAAAELAQHYGVpvfgpekeDEFWLQGLPAQSRMFG---LEECQPLTPDRWLNEGDTISIGNVTLQVLH 128
Cdd:cd07731  52 LILTHPDADHIGGLDAVLKNFPV--------KEVYMPGVTHTTKTYEdllDAIKEKGIPVTPCKAGDRWQLGGVSFEVLS 123
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 28-79 2.79e-06

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 46.34  E-value: 2.79e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16128894   28 LVDP---GGDAEKIKqeVDDSGLTLmqILLTHGHLDHVGAAAELAQHYGVPVFGP 79
Cdd:PRK00685  21 LIDPfitGNPLADLK--PEDVKVDY--ILLTHGHGDHLGDTVEIAKRTGATVIAN 71
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 52-80 2.79e-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: 46.63  E-value: 2.79e-06
                        10        20
                ....*....|....*....|....*....
gi 16128894  52 ILLTHGHLDHVGAAAELAQHYGVPVFGPE 80
Cdd:cd07714  59 IFITHGHEDHIGALPYLLPELNVPIYATP 87
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 52-135 3.71e-06

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: 46.52  E-value: 3.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  52 ILLTHGHLDHVGAAAELAQHYGVPVfGPEKEDEFWL---QGLPAQSRMFGLEECQPLTPDRWLNEGDTISIGNVTLQVLH 128
Cdd:cd16311  64 ILNSHGHIDHAGGLAELQRRSGALV-AASPSAALDLasgEVGPDDPQYHALPKYPPVKDMRLARDGGQFNVGPVSLTAHA 142


                ....*..
gi 16128894 129 CPGHTPG 135
Cdd:cd16311 143 TPGHTPG 149
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
52-155 1.29e-05

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 45.05  E-value: 1.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  52 ILLTHGHLDHVGAAAELAQHYGVPVFGPekedEFWLqGLpAQSRM--FGLEECQPLTPdrwLNEGDTISIGNVTLQVLH- 128
Cdd:COG0595  67 IVLTHGHEDHIGALPYLLKELNVPVYGT----PLTL-AL-LEAKLkeHGLLKKVKLHV---VKPGDRIKFGPFKVEFFRv 137

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 16128894 129 ---CPG------HTPGHVVFFddraklliSGDviFK 155
Cdd:COG0595 138 thsIPDslglaiRTPAGTIVH--------TGD--FK 163
SPM-1-like_MBL-B1-B2-like cd16286
Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; ...
 55-193 4.86e-05

Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; MBL-fold metallo-hydrolase domain; SPM-1 was first identified in a Pseudomonas aeruginosa strain from a paediatric leukaemia patient and is a major clinical problem. 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 are most closely related to each other. SPM-1 appears to be a hybrid B1/B2 MBL.


Pssm-ID: 293844 [Multi-domain]  Cd Length: 236  Bit Score: 42.90  E-value: 4.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  55 THGHLDHVGAAaELAQHYGVPVFGPE----------KEDEFWLQGLPAQSRMFGLEECQP-LTPDRW--LNEGDTISIGN 121
Cdd:cd16286  72 THFHLDGTGGN-EALKKRGIPTWGSDltkqlllergKADRIKAAEFLKNEDLKRRIESSPpVPPDNVfdLKEGKVFSFGN 150

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16128894 122 VTLQVLH-CPGHTPGHVVFFDDRAKLLISGDVIFKG-GVGRsdfpRGDHNqlISSIKDKLLPLG--DDVIFIPGHG 193
Cdd:cd16286 151 ELVEVSFpGPAHAPDNVVVYFPERKILFGGCMIKPGkELGN----LGDAN--MKAWPDSVRRLKkfDAKIVIPGHG 220
Lactamase_B_5 pfam14597
Metallo-beta-lactamase superfamily; This is a small family of putative metal-dependent ...
 52-153 6.10e-05

Metallo-beta-lactamase superfamily; This is a small family of putative metal-dependent hydrolases.


Pssm-ID: 373150  Cd Length: 199  Bit Score: 42.14  E-value: 6.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894    52 ILLTHGhlDHVGAAAELAQHYGVPVFGPEKEdefwlqglpaqsrmfglEECQPLTPDRWLNEGDTISIGnvtLQVLHCPG 131
Cdd:pfam14597  59 IVLTNS--DHIRAAKEIAHQTYAKIAGPAGE-----------------KETFPIACDRWLSDGDELVPG---LQVLELQG 116

                          90       100
                  ....*....|....*....|...
gi 16128894   132 -HTPGHVVFFDDRaKLLISGDVI 153
Cdd:pfam14597 117 sKTPGELALLLEE-TTLITGDLV 138
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 38-135 6.53e-05

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


Pssm-ID: 293865  Cd Length: 255  Bit Score: 42.43  E-value: 6.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  38 IKQEVDDSGLTL--MQILL-THGHLDHVGAAAELAQ--HYGVPVFGPE--------KEDEFWlqGLPAQSRMfgleecQP 104
Cdd:cd16307  47 IKASIEKLGFKFsdTKILLiSHAHFDHAAGSALIKRetHAKYMVMDGDvdvvesggKSDFFY--GNDPSTYF------PP 118

                        90       100       110
                ....*....|....*....|....*....|.
gi 16128894 105 LTPDRWLNEGDTISIGNVTLQVLHCPGHTPG 135
Cdd:cd16307 119 AHVDKVLHDGEQVELGGTVLTAHLTAGHTKG 149
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 28-135 7.97e-05

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


Pssm-ID: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 42.54  E-value: 7.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  28 LVD--PGGDAEKIKQEVDDSGLTLMQ---ILLTHGHLDHVGAAAELAQHYGVPVFGPEKEDEFWLQGLPAQS--RMFGLE 100
Cdd:cd16313  35 LIDggFPKSPEQIAASIRQLGFKLEDvkyILSSHDHWDHAGGIAALQKLTGAQVLASPATVAVLRSGSMGKDdpQFGGLT 114

                        90       100       110
                ....*....|....*....|....*....|....*
gi 16128894 101 ECQPLTPDRWLNEGDTISIGNVTLQVLHCPGHTPG 135
Cdd:cd16313 115 PMPPVASVRAVRDGEVVKLGPLAVTAHATPGHTTG 149
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 52-152 2.83e-04

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 40.94  E-value: 2.83e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  52 ILLTHGHLDHVGAAAEL-AQHYGVPVFGPE--------------KEDEFWLQGLPAQSR---MFGLEECQPLTPDRWlne 113
Cdd:COG1236  54 VVLTHAHLDHSGALPLLvKEGFRGPIYATPatadlarillgdsaKIQEEEAEAEPLYTEedaERALELFQTVDYGEP--- 130

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 16128894 114 gdtISIGNVTLQvLHCPGHTPG--HVVFFDDRAKLLISGDV 152
Cdd:COG1236 131 ---FEIGGVRVT-FHPAGHILGsaQVELEVGGKRIVFSGDY 167
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 28-194 3.67e-04

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 39.88  E-value: 3.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  28 LVD-PGGDAEKIKQEVDDsgLTLMQI---LLTHGHLDHVGAAAELAQHYgvPVFGPEKEDEFWLQGLPaqsrmfgleECQ 103
Cdd:cd16276  23 VVDaPPSLGENLLAAIRK--VTDKPVthvVYSHNHADHIGGASIFKDEG--ATIIAHEATAELLKRNP---------DPK 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894 104 PLTPDRWLNEGDTISIGNVTLQ-VLHCPGHTPGHVVFFDDRAKLLISGDVI------FKGGVGRSDFPrGDHNQLissik 176
Cdd:cd16276  90 RPVPTVTFDDEYTLEVGGQTLElSYFGPNHGPGNIVIYLPKQKVLMAVDLInpgwvpFFNFAGSEDIP-GYIEAL----- 163

                       170
                ....*....|....*...
gi 16128894 177 DKLLPLgDDVIFIPGHGP 194
Cdd:cd16276 164 DELLEY-DFDTFVGGHGN 180
UlaG-like_MBL-fold cd16284
UlaG a putative l-ascorbate-6-P lactonase and related proteins; MBL-fold metallo hydrolase ...
 52-127 4.11e-04

UlaG a putative l-ascorbate-6-P lactonase and related proteins; MBL-fold metallo hydrolase domain; UlaG is essential for L-ascorbate utilization under anaerobic conditions; it is a putative l-ascorbate-6-P lactonase thought to catalyze the hydrolysis of L-ascorbate-6-phosphate to 3-keto-L-gulonate-6-phosphate. 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: 293842  Cd Length: 178  Bit Score: 39.76  E-value: 4.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  52 ILLTHGHLDHVG---AAAELAQ-HYGVPVFGPEKEDEFWLQ-GLPAqsrmfglEECQPLTPdrwlneGDTISIGNVTLQV 126
Cdd:cd16284  42 VLATHDHNDHIDvnvAAAVLQNcAPDVPFIGPQACVDLWIGwGVPK-------ERCIVVKP------GDVVKIKDIEIHV 108


                .
gi 16128894 127 L 127
Cdd:cd16284 109 L 109
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 21-156 1.32e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 38.36  E-value: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  21 EQTRLAALVDPGGDAEKIKQEVDDSGLTLMQILLTHGHLDHVGAAAELAQhyGVPVF-GPEKEDEfwlqgLPAQSRMFGL 99
Cdd:cd07732  48 ELGLLPDIVGLYRDPLLLGGLRSEEDPSVDAVLLSHAHLDHYGLLNYLRP--DIPVYmGEATKRI-----LKALLPFFGE 120

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16128894 100 EECQPLTPdRWLNEGDTISIGNVTLQVLH----CPG------HTPGHVVFFddraklliSGDVIFKG 156
Cdd:cd07732 121 GDPVPRNI-RVFESGKSFTIGDFTVTPYLvdhsAPGayafliEAPGKRIFY--------TGDFRFHG 178
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
13-151 1.39e-03

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 38.64  E-value: 1.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894  13 QNCSLIWCEQTRLaaLVDPGGDA-EKIKQevddSGLTLMQ---ILLTHGHLDHVGAAAELAQHYG-------VPVFGPEK 81
Cdd:COG1234  19 TSSYLLEAGGERL--LIDCGEGTqRQLLR----AGLDPRDidaIFITHLHGDHIAGLPGLLSTRSlagrekpLTIYGPPG 92

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16128894  82 EDEFW--LQGLPAQSRMFGLEEcqpltpdRWLNEGDTISIGNVTLQVLHCPgHTPGHV--VFFDDRAKLLISGD 151
Cdd:COG1234  93 TKEFLeaLLKASGTDLDFPLEF-------HEIEPGEVFEIGGFTVTAFPLD-HPVPAYgyRFEEPGRSLVYSGD 158
PRK09331 PRK09331
Sep-tRNA:Cys-tRNA synthetase; Provisional
 1-76 3.55e-03

Sep-tRNA:Cys-tRNA synthetase; Provisional


Pssm-ID: 236469  Cd Length: 387  Bit Score: 37.60  E-value: 3.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16128894    1 MNYRIIPVTAFSQNcsliwceqtrlaaLVDPGGDAEKIKQEVDDSGLTLMQILLTH-----GHLDHVGAAAELAQHYGVP 75
Cdd:PRK09331 124 LNVREVPKTGYPEY-------------KITPEAYAEKIEEVKEETGKPPALALLTHvdgnyGNLADAKKVAKVAHEYGIP 190


                 .
gi 16128894   76 V 76
Cdd:PRK09331 191 F 191
PRK11539 PRK11539
ComEC family competence protein; Provisional
 46-79 6.87e-03

ComEC family competence protein; Provisional


Pssm-ID: 236924 [Multi-domain]  Cd Length: 755  Bit Score: 36.89  E-value: 6.87e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 16128894   46 GLTLMQILLTHGHLDHVGAAAELAQHY-GVPVFGP 79
Cdd:PRK11539 549 GLTPEGIILSHEHLDHRGGLASLLHAWpMAWIRSP 583
 
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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