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Conserved domains on  [gi|492142700|ref|WP_005761057|]
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MBL fold metallo-hydrolase [Pasteurella bettyae]

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 1.17e-108

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: 309.48  E-value: 1.17e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700   3 IDIIPVTTFQQNCSLIWDDD-KNAAIIDPGGEAQKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHFNVDIIGPHED 81
Cdd:cd07737    1 YQIIPVTPFQQNCSLIWCEEtKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  82 DVFWFESLLTQSEQFGLFGSESFLPDRWLNqEHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGDVLFRNSIGRT 161
Cdd:cd07737   81 DKFLLENLPEQSQMFGFPPAEAFTPDRWLE-EGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRT 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 492142700 162 DFPGGSHEDLMSSIKEKLLPLGDDWIIIAGH 192
Cdd:cd07737  160 DFPGGNHAQLIASIKEKLLPLGDDVTFIPGH 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 1.17e-108

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: 309.48  E-value: 1.17e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700   3 IDIIPVTTFQQNCSLIWDDD-KNAAIIDPGGEAQKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHFNVDIIGPHED 81
Cdd:cd07737    1 YQIIPVTPFQQNCSLIWCEEtKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  82 DVFWFESLLTQSEQFGLFGSESFLPDRWLNqEHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGDVLFRNSIGRT 161
Cdd:cd07737   81 DKFLLENLPEQSQMFGFPPAEAFTPDRWLE-EGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRT 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 492142700 162 DFPGGSHEDLMSSIKEKLLPLGDDWIIIAGH 192
Cdd:cd07737  160 DFPGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 7-208 8.97e-56

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: 176.42  E-value: 8.97e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700   7 PVTTFQQNCSLIWDDDKnAAIIDPGGE---AQKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHFNVDIIGpHEDDV 83
Cdd:COG0491    9 PGAGLGVNSYLIVGGDG-AVLIDTGLGpadAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYA-HAAEA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  84 FWfeslLTQSEQFGLFGSESFLPDRWLnQEHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGDVLFRNSIGRTDF 163
Cdd:COG0491   87 EA----LEAPAAGALFGREPVPPDRTL-EDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 492142700 164 PGGSHEDLMSSIkEKLLPLGDDWiIIAGHGPYTTIGA-----------ERKSNPFL 208
Cdd:COG0491  162 PDGDLAQWLASL-ERLLALPPDL-VIPGHGPPTTAEAidyleellaalGERANPFL 215
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 14-192 5.81e-39

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: 131.91  E-value: 5.81e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700    14 NCSLIWDDDKNAaIIDPG-GEAQKLIKKIEDDGL-KLQKILLTHGHLDHVGAALSLKKHFNVDIIGPHEDDVFWFESLLT 91
Cdd:smart00849   1 NSYLVRDDGGAI-LIDTGpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700    92 QSEQFGLFgsESFLPDRWLNqEHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGDVLFRNSIGRTDFPGGSHEDL 171
Cdd:smart00849  80 LGELGAEA--EPAPPDRTLK-DGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAAS 156

                          170       180
                   ....*....|....*....|.
gi 492142700   172 MSSIKEKLLPLGDDWIIIAGH 192
Cdd:smart00849 157 DALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
8-192 3.29e-33

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 117.85  E-value: 3.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700    8 VTTFQQNCSLIWDDDKNAaIIDPGGEA----QKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHFNVDIIGPHEDDV 83
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAV-LIDTGGSAeaalLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700   84 FWFESLLTQSEQFGLFGSESFLPDRWLNQ--EHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGDVLFRNSIGRT 161
Cdd:pfam00753  80 ELLDEELGLAASRLGLPGPPVVPLPPDVVleEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRL 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 492142700  162 DFPGGSHEDLMSSIKEKLLPL------GDDWIIIAGH 192
Cdd:pfam00753 160 DLPLGGLLVLHPSSAESSLESllklakLKAAVIVPGH 196
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 5-208 6.08e-31

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


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 113.40  E-value: 6.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700    5 IIPVTTFQQNcsLIW---DDDKNAAIIDPGgEAQKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHFNVDIIGPHED 81
Cdd:TIGR03413   1 IIPIPALSDN--YIWllhDPDGQAAVVDPG-EAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAFPAPVYGPAEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700   82 DvfwfeslltqseqfglfgsesfLP--DRWLnQEHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGDVLFRNSIG 159
Cdd:TIGR03413  78 R----------------------IPgiTHPV-KDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCG 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  160 RTdFpGGSHEDLMSSIKeKLLPLGDDWIIIAGHgPYT-------------------------------------TIGAER 202
Cdd:TIGR03413 135 RL-F-EGTPEQMYDSLQ-RLAALPDDTLVYCAH-EYTlsnlrfaltvepdnpalqerlkevealraqgqptlpsTLGLER 210


                  ....*.
gi 492142700  203 KSNPFL 208
Cdd:TIGR03413 211 ATNPFL 216
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 1-196 3.86e-17

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 77.17  E-value: 3.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700   1 MNIDIIPvtTFQQNcsLIW---DDDKNAAIIDPGgEAQKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHF-NVDII 76
Cdd:PRK10241   1 MNLNSIP--AFDDN--YIWvlnDEAGRCLIVDPG-EAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFpQIVVY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  77 GPHEddvfwfesllTQSEQFGLFGSESflpDRWLNQEHEiievgslqLEVIHLPGHTPGHIGFLEHSntVAFTGDVLFRN 156
Cdd:PRK10241  76 GPQE----------TQDKGTTQVVKDG---ETAFVLGHE--------FSVFATPGHTLGHICYFSKP--YLFCGDTLFSG 132

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 492142700 157 SIGRTdFPGGSHEDLMSSIKEKLLPlgDDWIIIAGHgPYT 196
Cdd:PRK10241 133 GCGRL-FEGTASQMYQSLKKINALP--DDTLICCAH-EYT 168
 
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 1.17e-108

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: 309.48  E-value: 1.17e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700   3 IDIIPVTTFQQNCSLIWDDD-KNAAIIDPGGEAQKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHFNVDIIGPHED 81
Cdd:cd07737    1 YQIIPVTPFQQNCSLIWCEEtKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  82 DVFWFESLLTQSEQFGLFGSESFLPDRWLNqEHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGDVLFRNSIGRT 161
Cdd:cd07737   81 DKFLLENLPEQSQMFGFPPAEAFTPDRWLE-EGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRT 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 492142700 162 DFPGGSHEDLMSSIKEKLLPLGDDWIIIAGH 192
Cdd:cd07737  160 DFPGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 5-192 3.66e-70

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: 211.76  E-value: 3.66e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700   5 IIPVTTFQQNCSLIWDDDKNAAIIDPGGEAQ-KLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHFNVDIIGpHEDDV 83
Cdd:cd06262    2 RLPVGPLQTNCYLVSDEEGEAILIDPGAGALeKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYI-HEADA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  84 FWFESLLTQSEQFGLFGSESFLPDRWLNqEHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGDVLFRNSIGRTDF 163
Cdd:cd06262   81 ELLEDPELNLAFFGGGPLPPPEPDILLE-DGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDL 159

                        170       180
                 ....*....|....*....|....*....
gi 492142700 164 PGGSHEDLMSSIKEKLLPLGDDWIIIAGH 192
Cdd:cd06262  160 PGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 3-208 3.93e-70

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: 212.21  E-value: 3.93e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700   3 IDIIPVTTFQQNCSLIWDDD-KNAAIIDPGGEAQKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHFNVDIIgPHED 81
Cdd:cd16322    1 VRPFTLGPLQENTYLVADEGgGEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVY-LHPD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  82 DVFWFESLLTQSEQFGLFGSESFLPDRWLNqEHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGDVLFRNSIGRT 161
Cdd:cd16322   80 DLPLYEAADLGAKAFGLGIEPLPPPDRLLE-DGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRT 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 492142700 162 DFPGGSHEDLMSSIKEkLLPLGDDWIIIAGHGPYTTIGAERKSNPFL 208
Cdd:cd16322  159 DLPGGDPKAMAASLRR-LLTLPDETRVFPGHGPPTTLGEERRTNPFL 204
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 7-208 8.97e-56

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: 176.42  E-value: 8.97e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700   7 PVTTFQQNCSLIWDDDKnAAIIDPGGE---AQKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHFNVDIIGpHEDDV 83
Cdd:COG0491    9 PGAGLGVNSYLIVGGDG-AVLIDTGLGpadAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYA-HAAEA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  84 FWfeslLTQSEQFGLFGSESFLPDRWLnQEHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGDVLFRNSIGRTDF 163
Cdd:COG0491   87 EA----LEAPAAGALFGREPVPPDRTL-EDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 492142700 164 PGGSHEDLMSSIkEKLLPLGDDWiIIAGHGPYTTIGA-----------ERKSNPFL 208
Cdd:COG0491  162 PDGDLAQWLASL-ERLLALPPDL-VIPGHGPPTTAEAidyleellaalGERANPFL 215
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 17-193 3.24e-42

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: 140.23  E-value: 3.24e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  17 LIWDDD-KNAAIIDPGGE-AQKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHFNVDI-IGPHEDDVFWFESLltqs 93
Cdd:cd07724   16 LVGDPEtGEAAVIDPVRDsVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIvIGEGAPASFFDRLL---- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  94 eqfglfgsesflpdrwlnQEHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGDVLFRNSIGRTDFPGGSHED--- 170
Cdd:cd07724   92 ------------------KDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPGEAEGLarq 153

                        170       180
                 ....*....|....*....|...
gi 492142700 171 LMSSIKEKLLPLGDDWIIIAGHG 193
Cdd:cd07724  154 LYDSLQRKLLLLPDETLVYPGHD 176
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 14-192 5.81e-39

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: 131.91  E-value: 5.81e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700    14 NCSLIWDDDKNAaIIDPG-GEAQKLIKKIEDDGL-KLQKILLTHGHLDHVGAALSLKKHFNVDIIGPHEDDVFWFESLLT 91
Cdd:smart00849   1 NSYLVRDDGGAI-LIDTGpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700    92 QSEQFGLFgsESFLPDRWLNqEHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGDVLFRNSIGRTDFPGGSHEDL 171
Cdd:smart00849  80 LGELGAEA--EPAPPDRTLK-DGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAAS 156

                          170       180
                   ....*....|....*....|.
gi 492142700   172 MSSIKEKLLPLGDDWIIIAGH 192
Cdd:smart00849 157 DALESLLKLLKLLPKLVVPGH 177
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 6-192 5.31e-38

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


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 129.12  E-value: 5.31e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700   6 IPVTTFQQN-CSLIWDDD-KNAAIIDPGgEAQKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHF-NVDIIGPHEDD 82
Cdd:cd07723    1 VPIPALSDNyIYLIVDEAtGEAAVVDPG-EAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFpDAPVYGPAEDR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  83 VFwfeslltqseqfglfgsesfLPDRWLnQEHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGDVLFRNSIGRTD 162
Cdd:cd07723   80 IP--------------------GLDHPV-KDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGRFF 138

                        170       180       190
                 ....*....|....*....|....*....|
gi 492142700 163 fpGGSHEDLMSSIkEKLLPLGDDWIIIAGH 192
Cdd:cd07723  139 --EGTAEQMYASL-QKLLALPDDTLVYCGH 165
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
8-192 3.29e-33

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 117.85  E-value: 3.29e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700    8 VTTFQQNCSLIWDDDKNAaIIDPGGEA----QKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHFNVDIIGPHEDDV 83
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAV-LIDTGGSAeaalLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700   84 FWFESLLTQSEQFGLFGSESFLPDRWLNQ--EHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGDVLFRNSIGRT 161
Cdd:pfam00753  80 ELLDEELGLAASRLGLPGPPVVPLPPDVVleEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRL 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 492142700  162 DFPGGSHEDLMSSIKEKLLPL------GDDWIIIAGH 192
Cdd:pfam00753 160 DLPLGGLLVLHPSSAESSLESllklakLKAAVIVPGH 196
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 5-208 6.08e-31

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


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 113.40  E-value: 6.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700    5 IIPVTTFQQNcsLIW---DDDKNAAIIDPGgEAQKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHFNVDIIGPHED 81
Cdd:TIGR03413   1 IIPIPALSDN--YIWllhDPDGQAAVVDPG-EAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAFPAPVYGPAEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700   82 DvfwfeslltqseqfglfgsesfLP--DRWLnQEHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGDVLFRNSIG 159
Cdd:TIGR03413  78 R----------------------IPgiTHPV-KDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCG 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  160 RTdFpGGSHEDLMSSIKeKLLPLGDDWIIIAGHgPYT-------------------------------------TIGAER 202
Cdd:TIGR03413 135 RL-F-EGTPEQMYDSLQ-RLAALPDDTLVYCAH-EYTlsnlrfaltvepdnpalqerlkevealraqgqptlpsTLGLER 210


                  ....*.
gi 492142700  203 KSNPFL 208
Cdd:TIGR03413 211 ATNPFL 216
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 11-192 2.74e-29

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: 106.85  E-value: 2.74e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  11 FQQNCSLIWDDDKN-AAIIDPGGEAQKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHFNVDI-IGPHEDDVFWFes 88
Cdd:cd16275   10 MINYSYIIIDKATReAAVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVyMSKEEIDYYGF-- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  89 lltQSEQFGLFgsesflpdrwlnQEHEIIEVGSLQLEVIHLPGHTPGHIGFL-EHSntvAFTGDVLFRNSIGRTDFPGGS 167
Cdd:cd16275   88 ---RCPNLIPL------------EDGDTIKIGDTEITCLLTPGHTPGSMCYLlGDS---LFTGDTLFIEGCGRCDLPGGD 149

                        170       180
                 ....*....|....*....|....*.
gi 492142700 168 HEDLMSSIkEKLLPLGDDWIII-AGH 192
Cdd:cd16275  150 PEEMYESL-QRLKKLPPPNTRVyPGH 174
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 14-193 2.98e-27

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: 102.68  E-value: 2.98e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  14 NCSLIWDDDKnAAIIDPG--GEAQKLIKKIEDDGLKLQK---ILLTHGHLDHVGAALSLKKHFNVDIIGpHEDDVFWFE- 87
Cdd:cd07721   12 NAYLIEDDDG-LTLIDTGlpGSAKRILKALRELGLSPKDirrILLTHGHIDHIGSLAALKEAPGAPVYA-HEREAPYLEg 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  88 --SLLTQSEQFGLFGSESFLPDRWLNQEHEIIEVGSL----QLEVIHLPGHTPGHIGFLEHSNTVAFTGDvLFRNSIGRT 161
Cdd:cd07721   90 ekPYPPPVRLGLLGLLSPLLPVKPVPVDRTLEDGDTLdlagGLRVIHTPGHTPGHISLYLEEDGVLIAGD-ALVTVGGEL 168

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 492142700 162 DFPGG----SHEDLMSSIKeKLLPLGDDWIIIaGHG 193
Cdd:cd07721  169 VPPPPpftwDMEEALESLR-KLAELDPEVLAP-GHG 202
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-154 1.36e-22

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: 90.28  E-value: 1.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  14 NCSLIWDDDKNAAIIDPGGE---AQKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHFNVDIIGPheddvfWFESLL 90
Cdd:cd07743    9 NIGVYVFGDKEALLIDSGLDedaGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAP------KIEKAF 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492142700  91 TQS---EQFGLFGSESF--LPDRWLNQ---------EHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNtVAFTGDVLF 154
Cdd:cd07743   83 IENpllEPSYLGGAYPPkeLRNKFLMAkpskvddiiEEGELELGGVGLEIIPLPGHSFGQIGILTPDG-VLFAGDALF 159
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 21-194 2.07e-22

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: 89.47  E-value: 2.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  21 DDKNAAIIDPGGEAQKLIKKIED--DGLKLQKILLTHGHLDHVGAALSLKKHFNVDIIGPHEDDvfwfeslltqseqfGL 98
Cdd:cd16278   25 APDGVVVIDPGPDDPAHLDALLAalGGGRVSAILVTHTHRDHSPGAARLAERTGAPVRAFGPHR--------------AG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  99 FGSESFLPDRWLnQEHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGD-VLFRNSigrT--DFPGGSHEDLMSSI 175
Cdd:cd16278   91 GQDTDFAPDRPL-ADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDhVMGWST---TviAPPDGDLGDYLASL 166

                        170
                 ....*....|....*....
gi 492142700 176 kEKLLPLGDDWiIIAGHGP 194
Cdd:cd16278  167 -ERLLALDDRL-LLPGHGP 183
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-203 4.61e-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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 78.76  E-value: 4.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  14 NCSLIwDDDKNAAIIDPGG---EAQKLIKKI-EDDGLKLQKILLTHGHLDHVGAALSLKKHfNVDIIGPH--------ED 81
Cdd:cd16282   16 NIGFI-VGDDGVVVIDTGAsprLARALLAAIrKVTDKPVRYVVNTHYHGDHTLGNAAFADA-GAPIIAHEntreelaaRG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  82 DVFWFESLLTQSEQFGlfGSESFLPDRWLNQEHEiIEVGSLQLEVIHL-PGHTPGHIG-FLEHSNTVaFTGDVLFrnsIG 159
Cdd:cd16282   94 EAYLELMRRLGGDAMA--GTELVLPDRTFDDGLT-LDLGGRTVELIHLgPAHTPGDLVvWLPEEGVL-FAGDLVF---NG 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 492142700 160 RTDF-PGGSHEDLMSSIkEKLLPLGDDwIIIAGHGPYTTIGAERK 203
Cdd:cd16282  167 RIPFlPDGSLAGWIAAL-DRLLALDAT-VVVPGHGPVGDKADLRA 209
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 14-192 5.28e-18

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: 77.67  E-value: 5.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  14 NCSLIWDDDKnAAIIDPG---GEAQKLIKKIEDDGLKLqkiLLTHGHLDHVGAAlslkKHFnvDIIGPHEDDVFWFESLL 90
Cdd:cd07712   10 NIYLLRGRDR-ALLIDTGlgiGDLKEYVRTLTDLPLLV---VATHGHFDHIGGL----HEF--EEVYVHPADAEILAAPD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  91 TQSEQFGLFGSESFLPD---RWLnQEHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGDVLFRNSIgrTDFPGGS 167
Cdd:cd07712   80 NFETLTWDAATYSVPPAgptLPL-RDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVYDGPL--IMDLPHS 156

                        170       180
                 ....*....|....*....|....*.
gi 492142700 168 HEDLMSSIKEKLLPLGDDW-IIIAGH 192
Cdd:cd07712  157 DLDDYLASLEKLSKLPDEFdKVLPGH 182
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 1-196 3.86e-17

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 77.17  E-value: 3.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700   1 MNIDIIPvtTFQQNcsLIW---DDDKNAAIIDPGgEAQKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHF-NVDII 76
Cdd:PRK10241   1 MNLNSIP--AFDDN--YIWvlnDEAGRCLIVDPG-EAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFpQIVVY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  77 GPHEddvfwfesllTQSEQFGLFGSESflpDRWLNQEHEiievgslqLEVIHLPGHTPGHIGFLEHSntVAFTGDVLFRN 156
Cdd:PRK10241  76 GPQE----------TQDKGTTQVVKDG---ETAFVLGHE--------FSVFATPGHTLGHICYFSKP--YLFCGDTLFSG 132

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 492142700 157 SIGRTdFPGGSHEDLMSSIKEKLLPlgDDWIIIAGHgPYT 196
Cdd:PRK10241 133 GCGRL-FEGTASQMYQSLKKINALP--DDTLICCAH-EYT 168
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 14-153 1.72e-16

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: 73.87  E-value: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  14 NCSLIWDDDKNAaIIDPG----GEAQKLIKKIEDDGLKLQ---KILLTHGHLDHVGAALSLKKHFNVDIIGPheddvfwf 86
Cdd:cd07725   16 NVYLLRDGDETT-LIDTGlateEDAEALWEGLKELGLKPSdidRVLLTHHHPDHIGLAGKLQEKSGATVYIL-------- 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492142700  87 eslltqseqfglfgSESFLPDRwlnqehEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGDVL 153
Cdd:cd07725   87 --------------DVTPVKDG------DKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAV 133
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 14-194 2.32e-16

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: 73.77  E-value: 2.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  14 NCSLIWDDDKNAaIIDPGGEA--QKLIKKIEDDGLKLQKI---LLTHGHLDHVGaalslkkhfNVD-------IIGPHED 81
Cdd:cd07711   23 TVTLIKDGGKNI-LVDTGTPWdrDLLLKALAEHGLSPEDIdyvVLTHGHPDHIG---------NLNlfpnatvIVGWDIC 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  82 DVFWFESLLTQSEQFGLFGSesflpdrwlnqeheiievgslqLEVIHLPGHTPGHIGFL---EHSNTVAFTGDVLFR--N 156
Cdd:cd07711   93 GDSYDDHSLEEGDGYEIDEN----------------------VEVIPTPGHTPEDVSVLvetEKKGTVAVAGDLFEReeD 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 492142700 157 SIGRTDFPGGSH--EDLMSSIKeKLLPLGDdwIIIAGHGP 194
Cdd:cd07711  151 LEDPILWDPLSEdpELQEESRK-RILALAD--WIIPGHGP 187
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 21-192 3.99e-16

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 75.26  E-value: 3.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  21 DDKNAAIIDPGgEAQKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHFNVDIIGP--HEDDVFWFESLLTQSeqfgl 98
Cdd:PLN02398  96 DTGTVGVVDPS-EAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSavDKDRIPGIDIVLKDG----- 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  99 fgsesflpDRWLNQEHEIIevgslqleVIHLPGHTPGHIGFLEHSNTVAFTGDVLFRNSIGRtdFPGGSHEDLMSSIKeK 178
Cdd:PLN02398 170 --------DKWMFAGHEVL--------VMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGK--LFEGTPEQMLSSLQ-K 230

                        170
                 ....*....|....
gi 492142700 179 LLPLGDDWIIIAGH 192
Cdd:PLN02398 231 IISLPDDTNIYCGH 244
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 5-196 1.82e-15

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 72.49  E-value: 1.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700   5 IIPVTTFQQNCS-LIWDDD-KNAAIIDPGgEAQKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHF-NVDIIGPHED 81
Cdd:PLN02469   3 IIPVPCLEDNYAyLIIDEStKDAAVVDPV-DPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVpGIKVYGGSLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  82 DVFWFESLLTQSEQFGLfGSesflpdrwlnqeheiievgSLQLEVIHLPGHTPGHIGFL----EHSNTVAFTGDVLFRNS 157
Cdd:PLN02469  82 NVKGCTHPVENGDKLSL-GK-------------------DVNILALHTPCHTKGHISYYvtgkEGEDPAVFTGDTLFIAG 141

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 492142700 158 IGRtdFPGGSHEDLMSSIKEKLLPLGDDWIIIAGHgPYT 196
Cdd:PLN02469 142 CGK--FFEGTAEQMYQSLCVTLGSLPKPTQVYCGH-EYT 177
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 20-208 5.43e-15

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 70.98  E-value: 5.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  20 DDDKNAAIIDP-GGEAQKLIKKIEDDGLKLQKILLTHGHLDHV-GAALSLKKHFNVdiigpheddvfwfESLLTQSEqfg 97
Cdd:PLN02962  33 HPDKPALLIDPvDKTVDRDLSLVKELGLKLIYAMNTHVHADHVtGTGLLKTKLPGV-------------KSIISKAS--- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  98 lfGSESFLpdrwLNQEHEIIEVGSLQLEVIHLPGHTPGHIGFL------EHSNTVAFTGDVLFRNSIGRTDFPGGSHEDL 171
Cdd:PLN02962  97 --GSKADL----FVEPGDKIYFGDLYLEVRATPGHTAGCVTYVtgegpdQPQPRMAFTGDALLIRGCGRTDFQGGSSDQL 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 492142700 172 MSSIKEKLLPLGDDWIIIAGHG----PYTTIGAERKSNPFL 208
Cdd:PLN02962 171 YKSVHSQIFTLPKDTLIYPAHDykgfTVSTVGEEMLYNPRL 211
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 20-152 9.03e-14

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: 67.13  E-value: 9.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  20 DDDKNAAIIDPGGE--AQKLIKKIEDDGLKLQK---ILLTHGHLDHVGAALSLKKHF-NVDII----G-PHEDDvfwfES 88
Cdd:cd07726   22 DGEGRPALIDTGPSssVPRLLAALEALGIAPEDvdyIILTHIHLDHAGGAGLLAEALpNAKVYvhprGaRHLID----PS 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492142700  89 LLTQS------EQFGLFGSEsFLP---DRWLNQEH-EIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGDV 152
Cdd:cd07726   98 KLWASaravygDEADRLGGE-ILPvpeERVIVLEDgETLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDA 170
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 48-194 8.03e-12

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


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 61.40  E-value: 8.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  48 LQKILLTHGHLDHVGAALSLKKHFNvdiigPHEDDVFWFesLLTQSEQFGLFGSESFLPdrwLnQEHEIIEVGSLQLEVI 127
Cdd:cd07722   57 ISDILLTHWHHDHVGGLPDVLDLLR-----GPSPRVYKF--PRPEEDEDPDEDGGDIHD---L-QDGQVFKVEGATLRVI 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492142700 128 HLPGHTPGHIGFLEHSNTVAFTGD-VLfrnSIGRTDFpggshEDL---MSSIKeKLLPLGDDwIIIAGHGP 194
Cdd:cd07722  126 HTPGHTTDHVCFLLEEENALFTGDcVL---GHGTAVF-----EDLaayMASLK-KLLSLGPG-RIYPGHGP 186
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 34-193 9.51e-12

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: 61.06  E-value: 9.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  34 AQKLIKKIEDDGlKLQKILLTHghLDHVGAALSLKKHFNVDIIgPHEDDVFWfeslLTQSEQFGLFGSESFLPdrwlnqe 113
Cdd:cd07727   35 SPPLAKRIEALG-GIRYIFLTH--RDDVADHAKWAERFGAKRI-IHEDDVNA----VTRPDEVIVLWGGDPWE------- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700 114 heiievGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGDVLF----RNS-IGRTDFPGGSHEDLMSSIkEKLLPLGDDWiI 188
Cdd:cd07727  100 ------LDPDLTLIPVPGHTRGSVVLLYKEKGVLFTGDHLAwsrrRGWlSAFRYVCWYSWPEQAESV-ERLADLDFEW-V 171


                 ....*
gi 492142700 189 IAGHG 193
Cdd:cd07727  172 LPGHG 176
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 8-140 3.31e-10

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: 57.86  E-value: 3.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700   8 VTTFQQNCSLIWDDDKNAAIIDPGGEAQKLIKK-IEDDGLKLQKI---LLTHGHLDHVGAALSLKKH----FNVDiigph 79
Cdd:cd16308   17 VGTYDLACYLIVTPKGNILINTGLAESVPLIKKnIQALGFKFKDIkilLTTQAHYDHVGAMAAIKQQtgakMMVD----- 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492142700  80 EDDVFWFESLLTQSEQFGLFGSeSFLP---DRWLnQEHEIIEVGSLQLEVIHLPGHTPGHIGFL 140
Cdd:cd16308   92 EKDAKVLADGGKSDYEMGGYGS-TFAPvkaDKLL-HDGDTIKLGGTKLTLLHHPGHTKGSCSFL 153
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 27-140 6.41e-10

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 56.82  E-value: 6.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  27 IIDPG--GEAQK-LIKKIEDDGLKLQKI---LLTHGHLDHVGAALSLKKHFNVDIIGPHEDdvfwFESLLTQSEQFGLFG 100
Cdd:cd16280   35 LIDALnnNEAADlIVDGLEKLGLDPADIkyiLITHGHGDHYGGAAYLKDLYGAKVVMSEAD----WDMMEEPPEEGDNPR 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 492142700 101 -SESFLPDRWLNQEHEiIEVGSLQLEVIHLPGHTPGHIGFL 140
Cdd:cd16280  111 wGPPPERDIVIKDGDT-LTLGDTTITVYLTPGHTPGTLSLI 150
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 51-192 3.06e-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: 54.91  E-value: 3.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  51 ILLTHGHLDHVGAAlslkKHF-NVDIIgPHEDDV-FWFESLLTQSEQFGLFGSESFLPD----RWLNQEHEIieVGSLql 124
Cdd:cd07729   92 VILSHLHFDHAGGL----DLFpNATII-VQRAELeYATGPDPLAAGYYEDVLALDDDLPggrvRLVDGDYDL--FPGV-- 162

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492142700 125 EVIHLPGHTPGHIGFLEH--SNTVAFTGDVL-FRNSIGRTDFPG--GSHEDLMSSIkEKLLPL--GDDWIIIAGH 192
Cdd:cd07729  163 TLIPTPGHTPGHQSVLVRlpEGTVLLAGDAAyTYENLEEGRPPGinYDPEAALASL-ERLKALaeREGARVIPGH 236
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 13-151 3.47e-07

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


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 48.41  E-value: 3.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  13 QNCSLIWDDDKNAAIIDPG-GEAQKLIKKIEDDgLKLQKILLTHGHLDHVGAALSLKKHF-------NVDIIGPHEddvf 84
Cdd:cd16272   16 NTSSYLLETGGTRILLDCGeGTVYRLLKAGVDP-DKLDAIFLSHFHLDHIGGLPTLLFARryggrkkPLTIYGPKG---- 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492142700  85 wFESLLTQSEQFGLFGSESFLPDRW--LNQEHEIIEVGSLQLEVIHLPgHTPGHIG--FLEHSNTVAFTGD 151
Cdd:cd16272   91 -IKEFLEKLLNFPVEILPLGFPLEIeeLEEGGEVLELGDLKVEAFPVK-HSVESLGyrIEAEGKSIVYSGD 159
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 41-139 7.54e-07

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: 48.27  E-value: 7.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  41 IEDDGLKLqkILLTHGHLDHVGAALSLKKHFNVDIIGPHEDDVfwfesLLTQSEQFGL-FGSESFLP----DRWLnQEHE 115
Cdd:cd16289   56 VAPGDLKL--ILHSHAHADHAGPLAALKRATGARVAANAESAV-----LLARGGSDDIhFGDGITFPpvqaDRIV-MDGE 127

                         90       100
                 ....*....|....*....|....
gi 492142700 116 IIEVGSLQLEVIHLPGHTPGHIGF 139
Cdd:cd16289  128 VVTLGGVTFTAHFTPGHTPGSTSW 151
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
13-151 7.96e-07

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 48.27  E-value: 7.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  13 QNCSLIWDDDKNAaIIDPGGEAQKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHFN-------VDIIGPHEDDVFW 85
Cdd:COG1234   19 TSSYLLEAGGERL-LIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSlagrekpLTIYGPPGTKEFL 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492142700  86 feslltqSEQFGLFGSESFLPDRWLN-QEHEIIEVGSLQLEVIHLPgHTPGHIGFL--EHSNTVAFTGD 151
Cdd:COG1234   98 -------EALLKASGTDLDFPLEFHEiEPGEVFEIGGFTVTAFPLD-HPVPAYGYRfeEPGRSLVYSGD 158
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 51-154 2.64e-06

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 46.39  E-value: 2.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  51 ILLTHGHLDHVGAALS--LKKHF-NVDIIgPHEDDV-FW----FESLLTQSEQFGLFGSES----FLPDRWLNQEHEIIE 118
Cdd:cd07720   95 VLLTHLHPDHIGGLVDagGKPVFpNAEVH-VSEAEWdFWlddaNAAKAPEGAKRFFDAARDrlrpYAAAGRFEDGDEVLP 173

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 492142700 119 vgslQLEVIHLPGHTPGHIGFLEHSN--TVAFTGDVLF 154
Cdd:cd07720  174 ----GITAVPAPGHTPGHTGYRIESGgeRLLIWGDIVH 207
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 47-128 2.71e-06

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 46.39  E-value: 2.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  47 KLQKILLTHGHLDHVGAALSLKKHFNVD--IIGPHEDDVFWFESLLTQSEQFGlfgsesfLPDRWLnQEHEIIEVGSLQL 124
Cdd:COG2333   52 RLDLLVLTHPDADHIGGLAAVLEAFPVGrvLVSGPPDTSETYERLLEALKEKG-------IPVRPC-RAGDTWQLGGVRF 123


                 ....
gi 492142700 125 EVIH 128
Cdd:COG2333  124 EVLW 127
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 14-78 3.74e-06

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


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 44.95  E-value: 3.74e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492142700  14 NCSLIWDDDKnAAIIDPGGEAQKLIKKIEDDGLK---LQKILLTHGHLDHVGAALSLKKHFNVDIIGP 78
Cdd:cd07733   10 NCTYLETEDG-KLLIDAGLSGRKITGRLAEIGRDpedIDAILVTHEHADHIKGLGVLARKYNVPIYAT 76
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 34-135 1.14e-05

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: 44.98  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  34 AQKLIKKIEDDGLKLQK---ILLTHGHLDHVGAALSLKKHFNVdIIGPHEDDVFWFESLLTQSE--QFGLFGSESFLPDR 108
Cdd:cd16311   44 APKIIANIEALGFRIEDvklILNSHGHIDHAGGLAELQRRSGA-LVAASPSAALDLASGEVGPDdpQYHALPKYPPVKDM 122

                         90       100
                 ....*....|....*....|....*..
gi 492142700 109 WLNQEHEIIEVGSLQLEVIHLPGHTPG 135
Cdd:cd16311  123 RLARDGGQFNVGPVSLTAHATPGHTPG 149
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 22-135 1.42e-05

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: 44.36  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  22 DKNAAIIDPG-GEAQKLIKK-IEDDGLKLQ--KILL-THGHLDHVGAALSLKKHFNVDIIGpHEDDVFWFESllTQSEQF 96
Cdd:cd16310   30 NHGAILLDGGlEENAALIEQnIKALGFKLSdiKIIInTHAHYDHAGGLAQLKADTGAKLWA-SRGDRPALEA--GKHIGD 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 492142700  97 GLFGSESFLP---DRWLNqEHEIIEVGSLQLEVIHLPGHTPG 135
Cdd:cd16310  107 NITQPAPFPAvkvDRILG-DGEKIKLGDITLTATLTPGHTKG 147
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 34-135 1.95e-05

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: 44.07  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  34 AQKLIKKIEDDGLKLQK---ILLTHGHLDHVGAALSLKKHFNVDIIGPHEDDVFwfesLLT-QSEQFGLFGSES--FLP- 106
Cdd:cd07708   44 APMIKANIKKLGFKFSDtklILISHAHFDHAGGSAEIKKQTGAKVMAGAEDVSL----LLSgGSSDFHYANDSStyFPQs 119

                         90       100       110
                 ....*....|....*....|....*....|.
gi 492142700 107 --DRWLnQEHEIIEVGSLQLEVIHLPGHTPG 135
Cdd:cd07708  120 tvDRAV-HDGERVTLGGTVLTAHATPGHTPG 149
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 13-152 4.41e-05

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 42.96  E-value: 4.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  13 QNCSLIWDDDKNAaIIDPGGEAQKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHFN---VDIIGPHEDdvfwFESL 89
Cdd:COG1235   35 RSSILVEADGTRL-LIDAGPDLREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYGpnpIPVYATPGT----LEAL 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  90 LTQSEQFGLFGSESFlpdrwlnQEHEI-----IEVGSLQLEVIHLPGHTPGHIGF-LEHSN-TVAFTGDV 152
Cdd:COG1235  110 ERRFPYLFAPYPGKL-------EFHEIepgepFEIGGLTVTPFPVPHDAGDPVGYrIEDGGkKLAYATDT 172
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 51-153 4.55e-05

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 42.89  E-value: 4.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  51 ILLTHGHLDHVGAALSL------------KKHFnvdiigPHEDDVFWFESLLTQSEQFGLFGsESFLPD------RWLNQ 112
Cdd:cd16277   67 VLCTHLHVDHVGWNTRLvdgrwvptfpnaRYLF------SRAEYDHWSSPDAGGPPNRGVFE-DSVLPVieaglaDLVDD 139

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 492142700 113 EHEIIEVgslqLEVIHLPGHTPGHIGFLEHSN--TVAFTGDVL 153
Cdd:cd16277  140 DHEILDG----IRLEPTPGHTPGHVSVELESGgeRALFTGDVM 178
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 15-128 6.86e-05

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 41.74  E-value: 6.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  15 CSLIWDDDKNAaIIDPGGEAQKLIKKIED-----DGLKLQKILLTHGHLDHVGAALSLKKHFNVD--IIGPHEDDVFWFE 87
Cdd:cd07731   12 AILIQTPGKTI-LIDTGPRDSFGEDVVVPylkarGIKKLDYLILTHPDADHIGGLDAVLKNFPVKevYMPGVTHTTKTYE 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 492142700  88 SLLTQSEQFGLFGSESFLPDRWlnqeheiiEVGSLQLEVIH 128
Cdd:cd07731   91 DLLDAIKEKGIPVTPCKAGDRW--------QLGGVSFEVLS 123
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 27-158 9.93e-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: 42.16  E-value: 9.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  27 IID--PGGEAQKLIKKIEDDGLKLQK---ILLTHGHLDHVGAALSLKKHFNVDII-GPHEDDVFWFESLLTQSEQFGLFG 100
Cdd:cd16313   35 LIDggFPKSPEQIAASIRQLGFKLEDvkyILSSHDHWDHAGGIAALQKLTGAQVLaSPATVAVLRSGSMGKDDPQFGGLT 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492142700 101 SESFLPDRWLNQEHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFTGDVLFRNSI 158
Cdd:cd16313  115 PMPPVASVRAVRDGEVVKLGPLAVTAHATPGHTTGGTSWTWQSCEQGRCANMVFADSL 172
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 27-80 1.74e-04

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 40.95  E-value: 1.74e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492142700  27 IIDP---GGEAQKLikKIEDdgLKLQKILLTHGHLDHVGAALSLKKHFNVDIIGPHE 80
Cdd:PRK00685  21 LIDPfitGNPLADL--KPED--VKVDYILLTHGHGDHLGDTVEIAKRTGATVIANAE 73
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 38-151 1.95e-04

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 40.85  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  38 IKKIEDdglKLQKILLTHGHLDHVGAALSLKKHFNVDIIGPHeddvFWFESLLTQSEQFGLFGSESF--LPDRwlnqehE 115
Cdd:cd07714   49 LEENKD---KIKGIFITHGHEDHIGALPYLLPELNVPIYATP----LTLALIKKKLEEFKLIKKVKLneIKPG------E 115

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 492142700 116 IIEVGSLQLEVIHLPGHTPGHIGFLEHSN--TVAFTGD 151
Cdd:cd07714  116 RIKLGDFEVEFFRVTHSIPDSVGLAIKTPegTIVHTGD 153
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 51-151 6.45e-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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 39.56  E-value: 6.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  51 ILLTHGHLDHVGAalsLKKHFNVDII-GPheddvfWFESLLTQSEQFGLFGSEsFLPDRWLNQEHEIIEVGSLQ------ 123
Cdd:cd07730   87 VILSHLHWDHIGG---LSDFPNARLIvGP------GAKEALRPPGYPSGFLPE-LLPSDFEGRLVRWEEDDFLWvplgpf 156

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 492142700 124 -----------LEVIHLPGHTPGHIGFL---EHSNTVAFTGD 151
Cdd:cd07730  157 praldlfgdgsLYLVDLPGHAPGHLGLLartTSGTWVFLAGD 198
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 27-155 6.71e-04

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 39.41  E-value: 6.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  27 IIDPG------GEAQKLIKKIEDDgLKLQKILLTHGHLDHVGAALSLKK---HFNVDIIGPHE-DDVFWFESLLTQ---- 92
Cdd:cd07710   31 IIDTLesaeaaKAALELFRKHTGD-KPVKAIIYTHSHPDHFGGAGGFVEeedSGKVPIIAPEGfMEEAVSENVLAGnams 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  93 ---SEQFGLF-------------------GSESFL-PDRWLNQEHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSNTVAFT 149
Cdd:cd07710  110 rraAYQFGALlpkgekgqvgaglgpglstGTVGFIpPTITITETGETLTIDGVELEFQHAPGEAPDEMMVWLPDYKVLFC 189


                 ....*.
gi 492142700 150 GDVLFR 155
Cdd:cd07710  190 ADNVYH 195
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-71 8.21e-04

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


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 39.02  E-value: 8.21e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 492142700  22 DKNAAIIDPG---GEAQKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHF 71
Cdd:cd07739   24 ETEAVLVDAQftrADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAF 76
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 28-194 8.43e-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: 38.72  E-value: 8.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  28 IDP---GGEA-QKLIKKIEDdgLKLQKILLTHGHLDHVGAALSLKKHfNVDIIGpHEDDVFWFESLLtqseqfglfGSES 103
Cdd:cd16276   24 VDAppsLGENlLAAIRKVTD--KPVTHVVYSHNHADHIGGASIFKDE-GATIIA-HEATAELLKRNP---------DPKR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700 104 FLPDRWLNQEHEiIEVGSLQLEVI-HLPGHTPGHIGFLEHSNTVAFTGDVL------FRNSIGRTDFPGgsHEDLMSSIK 176
Cdd:cd16276   91 PVPTVTFDDEYT-LEVGGQTLELSyFGPNHGPGNIVIYLPKQKVLMAVDLInpgwvpFFNFAGSEDIPG--YIEALDELL 167

                        170
                 ....*....|....*....
gi 492142700 177 EKllplgdDW-IIIAGHGP 194
Cdd:cd16276  168 EY------DFdTFVGGHGN 180
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 27-135 1.77e-03

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


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 38.23  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  27 IIDPG--GEAQKLIKKIEDDGLKLQ--KILL-THGHLDHVGAALSLKKHFNVDIIGPhEDDVFWFESlltqseqfGLFGS 101
Cdd:cd16309   35 LIDGAmpQSTPLIKDNIKKLGFDVKdvKYLLnTHAHFDHAGGLAELKKATGAQLVAS-AADKPLLES--------GYVGS 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 492142700 102 E-----SFLP---DRWLNQEHEIIeVGSLQLEVIHLPGHTPG 135
Cdd:cd16309  106 GdtknlQFPPvrvDRVIGDGDKVT-LGGTTLTAHLTPGHSPG 146
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 17-158 2.65e-03

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


Pssm-ID: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 37.55  E-value: 2.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492142700  17 LIWDDDKNAAIIDPGGEAQKLIKKIEDDGLKLQKILLTHGHLDHVGAALSL--------KKHFNVdIIGPheddvfwfES 88
Cdd:cd07741   23 IWIELNGKNIHIDPGPGALVRMCRPKLDPTKLDAIILSHRHLDHSNDANVLieamteggFKKRGT-LLAP--------ED 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492142700  89 LLTQSEQFGLFGSESFLPDRWLNQEHEIIEVGSLQLEVIHLPGHTPGHIGFLEHSN--TVAFTGDVLFRNSI 158
Cdd:cd07741   94 ALNGEPVVLLYYHRRKLEEIEILEEGDEYELGGIKIEATRHKHSDPTTYGFIFRTSdkKIGYISDTRYFEEL 165
ComEC_Rec2 TIGR00361
DNA internalization-related competence protein ComEC/Rec2; Apparant orthologs are found in 5 ...
 35-78 2.81e-03

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


Pssm-ID: 273036 [Multi-domain]  Cd Length: 662  Bit Score: 37.96  E-value: 2.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 492142700   35 QKLIKKIEDDGLKLQKILLTHGHLDHVGAALSLKKHF-NVDIIGP 78
Cdd:TIGR00361 478 KVIIPFLTAKGIKLEALILSHADQDHIGGAEIILKHHpVKRLVIP 522
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
38-78 3.44e-03

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 37.73  E-value: 3.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 492142700  38 IKKIEDdglKLQKILLTHGHLDHVGAALSLKKHFNVDIIGP 78
Cdd:COG0595   57 LEENKD---KIKGIVLTHGHEDHIGALPYLLKELNVPVYGT 94
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 14-76 5.67e-03

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 37.09  E-value: 5.67e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492142700  14 NCSLIWDDDKNAaIIDPG---GEAQKLIKKIEDDGLKLQKILLTHGHLDHVGAA-LSLKKHFNVDII 76
Cdd:COG1236   15 SCYLLETGGTRI-LIDCGlfqGGKERNWPPFPFRPSDVDAVVLTHAHLDHSGALpLLVKEGFRGPIY 80
 
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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