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Conserved domains on  [gi|515628354|ref|WP_017060954|]
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MULTISPECIES: MBL fold metallo-hydrolase [Vibrio]

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 ...
 5-194 5.12e-120

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: 338.37  E-value: 5.12e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   5 YQVVPVTSFSQNCSIVWCDETMEGIVVDPGGDVQQLAAIIEELGVKVVNLVLTHGHLDHVGGTVPLAEILKVEIVGPHKA 84
Cdd:cd07737    1 YQIIPVTPFQQNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  85 DNFWLQGLENQSQMFGFPLCKAFEPNTWLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFSEQARLAFVGDVLFNGAIGRTD 164
Cdd:cd07737   81 DKFLLENLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTD 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 515628354 165 FPQGDFNTLIASIKTKLWPLGSDVTFVPGH 194
Cdd:cd07737  161 FPGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
 
Name Accession Description Interval E-value
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 5-194 5.12e-120

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: 338.37  E-value: 5.12e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   5 YQVVPVTSFSQNCSIVWCDETMEGIVVDPGGDVQQLAAIIEELGVKVVNLVLTHGHLDHVGGTVPLAEILKVEIVGPHKA 84
Cdd:cd07737    1 YQIIPVTPFQQNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  85 DNFWLQGLENQSQMFGFPLCKAFEPNTWLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFSEQARLAFVGDVLFNGAIGRTD 164
Cdd:cd07737   81 DKFLLENLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTD 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 515628354 165 FPQGDFNTLIASIKTKLWPLGSDVTFVPGH 194
Cdd:cd07737  161 FPGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 9-199 8.14e-55

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: 174.11  E-value: 8.14e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   9 PVTSFSQNCSIVWCDEtmEGIVVDPGGD---VQQLAAIIEELGVKVVNLVLTHGHLDHVGGTVPLAEILKVEIVGpHKAD 85
Cdd:COG0491    9 PGAGLGVNSYLIVGGD--GAVLIDTGLGpadAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYA-HAAE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  86 NFWLQGlENQSQMFGFPlckAFEPNTWLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFSEQARLAFVGDVLFNGAIGRTDF 165
Cdd:COG0491   86 AEALEA-PAAGALFGRE---PVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDL 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 515628354 166 PQGDFNTLIASIKtKLWPLGSDVtFVPGHGPEST 199
Cdd:COG0491  162 PDGDLAQWLASLE-RLLALPPDL-VIPGHGPPTT 193
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 16-194 2.49e-38

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: 130.75  E-value: 2.49e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354    16 NCSIVWCDEtmEGIVVDPG-GDVQQLAAIIEELGVKVVN-LVLTHGHLDHVGGTVPLAEILKVEIVGPHKADNFWLQGLE 93
Cdd:smart00849   1 NSYLVRDDG--GAILIDTGpGEAEDLLAELKKLGPKKIDaIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354    94 NQSQMFGFPlcKAFEPNTWLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFSEQARLAFVGDVLFNGAIGRTDFPQGDFNTL 173
Cdd:smart00849  79 LLGELGAEA--EPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAAS 156

                          170       180
                   ....*....|....*....|.
gi 515628354   174 IASIKTKLWPLGSDVTFVPGH 194
Cdd:smart00849 157 DALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
13-194 1.36e-29

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 109.00  E-value: 1.36e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   13 FSQNCSIVWCDEtmEGIVVDPGGDV-QQLAAIIEELGVK---VVNLVLTHGHLDHVGGTVPLAEILKVEIVGPHKADNFW 88
Cdd:pfam00753   4 GQVNSYLIEGGG--GAVLIDTGGSAeAALLLLLAALGLGpkdIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAREL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   89 LQGLENQSQMFGF---PLCKAFEPNTWLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFSEQARLAFVGDVLFNGAIGRTDF 165
Cdd:pfam00753  82 LDEELGLAASRLGlpgPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDL 161

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 515628354  166 PQGDFNTLIASIKTKLWPLGSDV------TFVPGH 194
Cdd:pfam00753 162 PLGGLLVLHPSSAESSLESLLKLaklkaaVIVPGH 196
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 29-208 1.01e-20

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 86.78  E-value: 1.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  29 IVVDP-GGDVQQLAAIIEELGVKVVNLVLTHGHLDHVGGTvplaEILKVEIVGPHKAdnfwlqglenQSQMFGfplCKAf 107
Cdd:PLN02962  39 LLIDPvDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGT----GLLKTKLPGVKSI----------ISKASG---SKA- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354 108 epNTWLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFS------EQARLAFVGDVLFNGAIGRTDFPQGDFNTLIASIKTKL 181
Cdd:PLN02962 101 --DLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTgegpdqPQPRMAFTGDALLIRGCGRTDFQGGSSDQLYKSVHSQI 178

                        170       180       190
                 ....*....|....*....|....*....|.
gi 515628354 182 WPLGSDVTFVPGHGPE----STFGRERASNP 208
Cdd:PLN02962 179 FTLPKDTLIYPAHDYKgftvSTVGEEMLYNP 209
SoxH_rel_PQQ_1 TIGR04558
quinoprotein relay system zinc metallohydrolase 1; By homology, members are Zn ...
 13-196 5.10e-12

quinoprotein relay system zinc metallohydrolase 1; By homology, members are Zn metallohydrolases in the same family as the SoxH protein associated with sulfate metabolism, Bacillus cereus beta-lactamase II (see PDB:1bc2), and, more distantly, hydroxyacylglutathione hydrolase (glyoxalase II). All members occur in genomes with both PQQ biosynthesis and a PQQ-dependent (quinoprotein) dehydrogenase that has a motif of two consecutive Cys residues (see TIGR03075). The Cys-Cys motif is associated with electron transfer by specialized cytochromes such as c551. All these genomes also include a fusion protein (TIGR04557) whose domains resemble SoxY and SoxZ from thiosulfate oxidation. A conserved Cys in this fusion protein aligns to the Cys residue in SoxY that carries sulfur cycle intermediates. In many genomes, the genes for PQQ biosynthesis enzymes, PQQ-dependent enzymes, their associated cytochromes, and members of this family are clustered. Note that one to three closely related Zn metallohydrolases may occur; this family represents a specific clade among them. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275351 [Multi-domain]  Cd Length: 285  Bit Score: 63.44  E-value: 5.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   13 FSQN--CSIVWCD--ETMEG-IVVDPGGDV---QQLAAIIEELGVK-VVNLVLTHGHLDHVGGT-----VPLA------E 72
Cdd:TIGR04558  25 FSRAngGNIVNTAfiVTDEGvIVIDTGPSRrygEQLRAAIAQVTGKpVRRVLNTHHHPDHFLGNqafadVPIAalpatiA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   73 ILKVEivGPHKADNF------WLQGLENQSqmfgfplckafePNTWLEEGdKVTFGNQVIDVIHTPGHTPGHVVLFSEQA 146
Cdd:TIGR04558 105 GIRAE--GDAYADNMyrlvgdWMRGTEPVP------------PNEALEAG-PLTIGGRRLELLALSGHTGADLVILDEAT 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 515628354  147 RLAFVGDVLFNGAIGRTdfPQGDFNTLIASIKtKLWPLGSDVTfVPGHGP 196
Cdd:TIGR04558 170 GVLFAGDLVFLDRAPTT--PHADLADWLASLD-RLEALPAKVL-VPGHGP 215
 
Name Accession Description Interval E-value
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 5-194 5.12e-120

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: 338.37  E-value: 5.12e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   5 YQVVPVTSFSQNCSIVWCDETMEGIVVDPGGDVQQLAAIIEELGVKVVNLVLTHGHLDHVGGTVPLAEILKVEIVGPHKA 84
Cdd:cd07737    1 YQIIPVTPFQQNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  85 DNFWLQGLENQSQMFGFPLCKAFEPNTWLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFSEQARLAFVGDVLFNGAIGRTD 164
Cdd:cd07737   81 DKFLLENLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTD 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 515628354 165 FPQGDFNTLIASIKTKLWPLGSDVTFVPGH 194
Cdd:cd07737  161 FPGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 7-194 1.41e-65

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: 200.59  E-value: 1.41e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   7 VVPVTSFSQNCSIVWcDETMEGIVVDPGGD-VQQLAAIIEELGVKVVNLVLTHGHLDHVGGTVPLAEILKVEIVGpHKAD 85
Cdd:cd06262    2 RLPVGPLQTNCYLVS-DEEGEAILIDPGAGaLEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYI-HEAD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  86 NFWLQGLENQSQMFGFPLCKAFEPNTWLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFSEQARLAFVGDVLFNGAIGRTDF 165
Cdd:cd06262   80 AELLEDPELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDL 159

                        170       180
                 ....*....|....*....|....*....
gi 515628354 166 PQGDFNTLIASIKTKLWPLGSDVTFVPGH 194
Cdd:cd06262  160 PGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 6-210 1.45e-61

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: 191.02  E-value: 1.45e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   6 QVVPVTSFSQNCSIVWCDETMEGIVVDPGGDVQQLAAIIEELGVKVVNLVLTHGHLDHVGGTVPLAEILKVEIVgPHKAD 85
Cdd:cd16322    2 RPFTLGPLQENTYLVADEGGGEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVY-LHPDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  86 NFWLQGLENQSQMFGFPLCKAFEPNTWLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFSEQARLAFVGDVLFNGAIGRTDF 165
Cdd:cd16322   81 LPLYEAADLGAKAFGLGIEPLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRTDL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 515628354 166 PQGDFNTLIASIKtKLWPLGSDVTFVPGHGPESTFGRERASNPFV 210
Cdd:cd16322  161 PGGDPKAMAASLR-RLLTLPDETRVFPGHGPPTTLGEERRTNPFL 204
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 9-199 8.14e-55

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: 174.11  E-value: 8.14e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   9 PVTSFSQNCSIVWCDEtmEGIVVDPGGD---VQQLAAIIEELGVKVVNLVLTHGHLDHVGGTVPLAEILKVEIVGpHKAD 85
Cdd:COG0491    9 PGAGLGVNSYLIVGGD--GAVLIDTGLGpadAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYA-HAAE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  86 NFWLQGlENQSQMFGFPlckAFEPNTWLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFSEQARLAFVGDVLFNGAIGRTDF 165
Cdd:COG0491   86 AEALEA-PAAGALFGRE---PVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDL 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 515628354 166 PQGDFNTLIASIKtKLWPLGSDVtFVPGHGPEST 199
Cdd:COG0491  162 PDGDLAQWLASLE-RLLALPPDL-VIPGHGPPTT 193
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 19-195 2.44e-40

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: 135.60  E-value: 2.44e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  19 IVWCDETMEGIVVDPGGD-VQQLAAIIEELGVKVVNLVLTHGHLDHVGGTVPLAEILKVEIVGPHKADnfwlqglenqsq 97
Cdd:cd07724   16 LVGDPETGEAAVIDPVRDsVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGEGAP------------ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  98 mfgfplckAFEPNTWLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFSEQARLAFVGDVLFNGAIGRTDFPQGDF---NTLI 174
Cdd:cd07724   84 --------ASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPGEAEglaRQLY 155

                        170       180
                 ....*....|....*....|.
gi 515628354 175 ASIKTKLWPLGSDVTFVPGHG 195
Cdd:cd07724  156 DSLQRKLLLLPDETLVYPGHD 176
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 16-194 2.49e-38

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: 130.75  E-value: 2.49e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354    16 NCSIVWCDEtmEGIVVDPG-GDVQQLAAIIEELGVKVVN-LVLTHGHLDHVGGTVPLAEILKVEIVGPHKADNFWLQGLE 93
Cdd:smart00849   1 NSYLVRDDG--GAILIDTGpGEAEDLLAELKKLGPKKIDaIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354    94 NQSQMFGFPlcKAFEPNTWLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFSEQARLAFVGDVLFNGAIGRTDFPQGDFNTL 173
Cdd:smart00849  79 LLGELGAEA--EPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAAS 156

                          170       180
                   ....*....|....*....|.
gi 515628354   174 IASIKTKLWPLGSDVTFVPGH 194
Cdd:smart00849 157 DALESLLKLLKLLPKLVVPGH 177
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 8-194 2.37e-36

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: 125.27  E-value: 2.37e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   8 VPVTSFSQN-CSIVWCDETMEGIVVDPGgDVQQLAAIIEELGVKVVNLVLTHGHLDHVGGTVPLAEILK-VEIVGPHKAD 85
Cdd:cd07723    1 VPIPALSDNyIYLIVDEATGEAAVVDPG-EAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPdAPVYGPAEDR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  86 nfwlqglenqsqmfgFPLCkafepNTWLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFSEQARLAFVGDVLFNGAIGRTDf 165
Cdd:cd07723   80 ---------------IPGL-----DHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGRFF- 138

                        170       180
                 ....*....|....*....|....*....
gi 515628354 166 pQGDFNTLIASIKtKLWPLGSDVTFVPGH 194
Cdd:cd07723  139 -EGTAEQMYASLQ-KLLALPDDTLVYCGH 165
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
13-194 1.36e-29

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 109.00  E-value: 1.36e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   13 FSQNCSIVWCDEtmEGIVVDPGGDV-QQLAAIIEELGVK---VVNLVLTHGHLDHVGGTVPLAEILKVEIVGPHKADNFW 88
Cdd:pfam00753   4 GQVNSYLIEGGG--GAVLIDTGGSAeAALLLLLAALGLGpkdIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAREL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   89 LQGLENQSQMFGF---PLCKAFEPNTWLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFSEQARLAFVGDVLFNGAIGRTDF 165
Cdd:pfam00753  82 LDEELGLAASRLGlpgPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDL 161

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 515628354  166 PQGDFNTLIASIKTKLWPLGSDV------TFVPGH 194
Cdd:pfam00753 162 PLGGLLVLHPSSAESSLESLLKLaklkaaVIVPGH 196
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 16-195 9.85e-29

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: 106.54  E-value: 9.85e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  16 NCSIVWCDEtmEGIVVDPG--GDVQQLAAIIEELGVKVVNL---VLTHGHLDHVGGTVPLAEILKVEiVGPHKADNFWLQ 90
Cdd:cd07721   12 NAYLIEDDD--GLTLIDTGlpGSAKRILKALRELGLSPKDIrriLLTHGHIDHIGSLAALKEAPGAP-VYAHEREAPYLE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  91 G---------LENQSQMFGFPLCKAFEPNTWLEEGDKVTFGNQvIDVIHTPGHTPGHVVLFSEQARLAFVGDvLFNGAIG 161
Cdd:cd07721   89 GekpypppvrLGLLGLLSPLLPVKPVPVDRTLEDGDTLDLAGG-LRVIHTPGHTPGHISLYLEEDGVLIAGD-ALVTVGG 166

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 515628354 162 RTDFPQG----DFNTLIASIKtKLwpLGSDV-TFVPGHG 195
Cdd:cd07721  167 ELVPPPPpftwDMEEALESLR-KL--AELDPeVLAPGHG 202
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 12-194 7.80e-28

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: 103.39  E-value: 7.80e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  12 SFSQNCSIVWCDETMEGIVVDPGGDVQQLAAIIEELGVKVVNLVLTHGHLDHVGGTVPLAEILKVEIvgphkadnfWLQG 91
Cdd:cd16275    9 PMINYSYIIIDKATREAAVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPV---------YMSK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  92 LEnqSQMFGFPlCKAFEPntwLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFSEQaRLaFVGDVLFNGAIGRTDFPQGD-- 169
Cdd:cd16275   80 EE--IDYYGFR-CPNLIP---LEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGD-SL-FTGDTLFIEGCGRCDLPGGDpe 151

                        170       180
                 ....*....|....*....|....*....
gi 515628354 170 --FNTL--IASIktklwpLGSDVTFVPGH 194
Cdd:cd16275  152 emYESLqrLKKL------PPPNTRVYPGH 174
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 29-194 5.48e-27

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: 101.55  E-value: 5.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  29 IVVDPGGDVQQLAAIIEELGVKVVNLVLTHGHLDHVGGtvplaeILKVEIVGPHKADNFWLQGLENQSQMFGFPLC---K 105
Cdd:cd07712   21 LLIDTGLGIGDLKEYVRTLTDLPLLVVATHGHFDHIGG------LHEFEEVYVHPADAEILAAPDNFETLTWDAATysvP 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354 106 AFEPNTWLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFSEQARLAFVGDVLFNGAIgRTDFPQGDFNTLIASIKtKLWPLG 185
Cdd:cd07712   95 PAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVYDGPL-IMDLPHSDLDDYLASLE-KLSKLP 172

                        170
                 ....*....|
gi 515628354 186 SDVTFV-PGH 194
Cdd:cd07712  173 DEFDKVlPGH 182
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 29-196 6.08e-24

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 94.55  E-value: 6.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  29 IVVDPGGDVQQLAAIIEEL----GVKVVNLVLTHGHLDHVGGTVPLAEiLKVEIVGPHKADNFWLQGLENQSQMFGFPLC 104
Cdd:cd16282   27 VVIDTGASPRLARALLAAIrkvtDKPVRYVVNTHYHGDHTLGNAAFAD-AGAPIIAHENTREELAARGEAYLELMRRLGG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354 105 KAFE------PNTWLEEGDKVTFGNQVIDVIHT-PGHTPGHVVLFSEQARLAFVGDVLFNGAIgrTDFPQGDFNTLIASI 177
Cdd:cd16282  106 DAMAgtelvlPDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEGVLFAGDLVFNGRI--PFLPDGSLAGWIAAL 183

                        170       180
                 ....*....|....*....|
gi 515628354 178 KtklWPLGSDVT-FVPGHGP 196
Cdd:cd16282  184 D---RLLALDATvVVPGHGP 200
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 29-197 1.65e-21

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: 87.16  E-value: 1.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  29 IVVDPG-GDVQQLAAIIEEL-GVKVVNLVLTHGHLDHVGGTVPLAEILKVEIVGPHKADNFWLQGlenqsqmfgfplckA 106
Cdd:cd16278   30 VVIDPGpDDPAHLDALLAALgGGRVSAILVTHTHRDHSPGAARLAERTGAPVRAFGPHRAGGQDT--------------D 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354 107 FEPNTWLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFSEQARLAFVGDVLFNGAigrT---DFPQGDFNTLIASIKtKLWP 183
Cdd:cd16278   96 FAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVMGWS---TtviAPPDGDLGDYLASLE-RLLA 171

                        170
                 ....*....|....
gi 515628354 184 LGsDVTFVPGHGPE 197
Cdd:cd16278  172 LD-DRLLLPGHGPP 184
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 29-208 1.01e-20

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 86.78  E-value: 1.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  29 IVVDP-GGDVQQLAAIIEELGVKVVNLVLTHGHLDHVGGTvplaEILKVEIVGPHKAdnfwlqglenQSQMFGfplCKAf 107
Cdd:PLN02962  39 LLIDPvDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGT----GLLKTKLPGVKSI----------ISKASG---SKA- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354 108 epNTWLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFS------EQARLAFVGDVLFNGAIGRTDFPQGDFNTLIASIKTKL 181
Cdd:PLN02962 101 --DLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTgegpdqPQPRMAFTGDALLIRGCGRTDFQGGSSDQLYKSVHSQI 178

                        170       180       190
                 ....*....|....*....|....*....|.
gi 515628354 182 WPLGSDVTFVPGHGPE----STFGRERASNP 208
Cdd:PLN02962 179 FTLPKDTLIYPAHDYKgftvSTVGEEMLYNP 209
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 25-142 4.66e-17

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 76.85  E-value: 4.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  25 TMEGIVV----DPGGDVQQLAAIIEELGVK---VVNLVLTHGHLDHVGGTVPLAEILKVEIVGPHKADNFWLQGLENQSQ 97
Cdd:cd16280   29 TGDGLILidalNNNEAADLIVDGLEKLGLDpadIKYILITHGHGDHYGGAAYLKDLYGAKVVMSEADWDMMEEPPEEGDN 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 515628354  98 MFGFPLckaFEPNTWLEEGDKVTFGNQVIDVIHTPGHTPGHVVLF 142
Cdd:cd16280  109 PRWGPP---PERDIVIKDGDTLTLGDTTITVYLTPGHTPGTLSLI 150
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 6-162 1.96e-15

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 72.87  E-value: 1.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   6 QVVPVTSFSQNCSIVWCDE-TMEGIVVDPGgDVQQLAAIIEELGVKVVNLVLTHGHLDHVGGTVPLAEILK-VEIVGPHK 83
Cdd:PLN02469   2 KIIPVPCLEDNYAYLIIDEsTKDAAVVDPV-DPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPgIKVYGGSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  84 aDNfwLQGLENQsqmfgfplckafepntwLEEGDKVTFGNQV-IDVIHTPGHTPGHVVLF----SEQARLAFVGDVLFNG 158
Cdd:PLN02469  81 -DN--VKGCTHP-----------------VENGDKLSLGKDVnILALHTPCHTKGHISYYvtgkEGEDPAVFTGDTLFIA 140


                 ....
gi 515628354 159 AIGR 162
Cdd:PLN02469 141 GCGK 144
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 29-204 7.06e-15

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: 69.63  E-value: 7.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  29 IVVDPG----GDVQQLAAIIEELGVKVVN---LVLTHGHLDHVGgtvpLAEILKVEIVGPHKADNFwlqglenqsqmfgf 101
Cdd:cd07725   27 TLIDTGlateEDAEALWEGLKELGLKPSDidrVLLTHHHPDHIG----LAGKLQEKSGATVYILDV-------------- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354 102 plckafepnTWLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFSEQARLAFVGDVLFN-------GAIGRTDFPQGDFNTLI 174
Cdd:cd07725   89 ---------TPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLPkitpnvsLWAVRVEDPLGAYLESL 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 515628354 175 ASIKTklwpLGSDVtFVPGHGPESTFGRER 204
Cdd:cd07725  160 DKLEK----LDVDL-AYPGHGGPIKDPKAR 184
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 41-196 5.43e-13

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: 64.86  E-value: 5.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  41 AAIIEELGVKVVNLVLTHGHLDHVGGtvpLAEILKVEIVGPHKADNFWLQGLENQSQMFGFPLCKafepntwLEEGDKVT 120
Cdd:cd07722   47 SVLDSEGNATISDILLTHWHHDHVGG---LPDVLDLLRGPSPRVYKFPRPEEDEDPDEDGGDIHD-------LQDGQVFK 116

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515628354 121 FGNQVIDVIHTPGHTPGHVVLFSEQARLAFVGD-VLfnGAiGRTDFpqGDFNTLIASIKtKLWPLGSDVTFvPGHGP 196
Cdd:cd07722  117 VEGATLRVIHTPGHTTDHVCFLLEEENALFTGDcVL--GH-GTAVF--EDLAAYMASLK-KLLSLGPGRIY-PGHGP 186
SoxH_rel_PQQ_1 TIGR04558
quinoprotein relay system zinc metallohydrolase 1; By homology, members are Zn ...
 13-196 5.10e-12

quinoprotein relay system zinc metallohydrolase 1; By homology, members are Zn metallohydrolases in the same family as the SoxH protein associated with sulfate metabolism, Bacillus cereus beta-lactamase II (see PDB:1bc2), and, more distantly, hydroxyacylglutathione hydrolase (glyoxalase II). All members occur in genomes with both PQQ biosynthesis and a PQQ-dependent (quinoprotein) dehydrogenase that has a motif of two consecutive Cys residues (see TIGR03075). The Cys-Cys motif is associated with electron transfer by specialized cytochromes such as c551. All these genomes also include a fusion protein (TIGR04557) whose domains resemble SoxY and SoxZ from thiosulfate oxidation. A conserved Cys in this fusion protein aligns to the Cys residue in SoxY that carries sulfur cycle intermediates. In many genomes, the genes for PQQ biosynthesis enzymes, PQQ-dependent enzymes, their associated cytochromes, and members of this family are clustered. Note that one to three closely related Zn metallohydrolases may occur; this family represents a specific clade among them. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275351 [Multi-domain]  Cd Length: 285  Bit Score: 63.44  E-value: 5.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   13 FSQN--CSIVWCD--ETMEG-IVVDPGGDV---QQLAAIIEELGVK-VVNLVLTHGHLDHVGGT-----VPLA------E 72
Cdd:TIGR04558  25 FSRAngGNIVNTAfiVTDEGvIVIDTGPSRrygEQLRAAIAQVTGKpVRRVLNTHHHPDHFLGNqafadVPIAalpatiA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   73 ILKVEivGPHKADNF------WLQGLENQSqmfgfplckafePNTWLEEGdKVTFGNQVIDVIHTPGHTPGHVVLFSEQA 146
Cdd:TIGR04558 105 GIRAE--GDAYADNMyrlvgdWMRGTEPVP------------PNEALEAG-PLTIGGRRLELLALSGHTGADLVILDEAT 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 515628354  147 RLAFVGDVLFNGAIGRTdfPQGDFNTLIASIKtKLWPLGSDVTfVPGHGP 196
Cdd:TIGR04558 170 GVLFAGDLVFLDRAPTT--PHADLADWLASLD-RLEALPAKVL-VPGHGP 215
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 39-160 5.27e-12

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: 62.95  E-value: 5.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  39 QLAAIIEELGVK---VVNLVLTHGHLDHVGGTV--------PLAEIlkveIVgpHKAD-NFWLQGlENQSQM-----FGF 101
Cdd:cd07720   77 KLLANLAAAGIDpedIDDVLLTHLHPDHIGGLVdaggkpvfPNAEV----HV--SEAEwDFWLDD-ANAAKApegakRFF 149

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515628354 102 PLCKA----FEPNTWLEEGDKVTFGnqvIDVIHTPGHTPGH--VVLFSEQARLAFVGDVLFNGAI 160
Cdd:cd07720  150 DAARDrlrpYAAAGRFEDGDEVLPG---ITAVPAPGHTPGHtgYRIESGGERLLIWGDIVHHPAL 211
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 29-154 6.14e-12

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


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 62.51  E-value: 6.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  29 IVVDPGGD--VQQLAAIIEELGVKVVNL---VLTHGHLDHVGGTVPLAEIL---KVeIVGP----HKADnfwLQGLENQS 96
Cdd:cd07726   28 ALIDTGPSssVPRLLAALEALGIAPEDVdyiILTHIHLDHAGGAGLLAEALpnaKV-YVHPrgarHLID---PSKLWASA 103

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515628354  97 -QMFGfplcKAFEPNTW------------LEEGDKVTFGNQVIDVIHTPGHTPGHVVLFSEQARLAFVGDV 154
Cdd:cd07726  104 rAVYG----DEADRLGGeilpvpeervivLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDA 170
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 10-162 1.08e-11

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 62.15  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  10 VTSFSQNCSIVWCDETMEGIVVDPGGDVQQLAAIiEELGVKVVNLVLTHGHLDHVGGTVPL-AEILKVEIVGPHKADNFW 88
Cdd:PRK10241   6 IPAFDDNYIWVLNDEAGRCLIVDPGEAEPVLNAI-AENNWQPEAIFLTHHHHDHVGGVKELvEKFPQIVVYGPQETQDKG 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515628354  89 LQGLenqsqmfgfplckafepntwLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFSEQarLAFVGDVLFNGAIGR 162
Cdd:PRK10241  85 TTQV--------------------VKDGETAFVLGHEFSVFATPGHTLGHICYFSKP--YLFCGDTLFSGGCGR 136
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 27-194 1.49e-11

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: 61.01  E-value: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  27 EGIVVDPGGD---VQQLAAIIEELGVKVVNLVLTHGHLDHVGGTVPLAEILKVEIVGPHKADNFwlqgLENQSQM----F 99
Cdd:cd07743   19 EALLIDSGLDedaGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAF----IENPLLEpsylG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354 100 GFPLCKAFEpNTWLE----------EGDKVTFGNQVIDVIHTPGHTPGHV-VLFSEqaRLAFVGDVLFN-GAIGRTDFPq 167
Cdd:cd07743   95 GAYPPKELR-NKFLMakpskvddiiEEGELELGGVGLEIIPLPGHSFGQIgILTPD--GVLFAGDALFGeEVLEKYGIP- 170

                        170       180       190
                 ....*....|....*....|....*....|
gi 515628354 168 gdFNTLIA-SIKT--KLWPLGSDVtFVPGH 194
Cdd:cd07743  171 --FLYDVEeQLETleKLEELDADY-YVPGH 197
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 2-194 2.54e-11

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 61.78  E-value: 2.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   2 SLKYQVVPVtsFSQNCSIVWCDETMEGI-VVDPggdvQQLAAIIEELGVKVVNLVL---THGHLDHVGGTVPLAEILKVE 77
Cdd:PLN02398  75 SLQIELVPC--LKDNYAYLLHDEDTGTVgVVDP----SEAVPVIDALSRKNRNLTYilnTHHHYDHTGGNLELKARYGAK 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  78 IVGPHKaDNFWLQGLEnqsqmfgfplckafepnTWLEEGDKVTFGNQVIDVIHTPGHTPGHVVLFSEQARLAFVGDVLFN 157
Cdd:PLN02398 149 VIGSAV-DKDRIPGID-----------------IVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFS 210

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 515628354 158 GAIGRtdFPQGDFNTLIASIKtKLWPLGSDVTFVPGH 194
Cdd:PLN02398 211 LSCGK--LFEGTPEQMLSSLQ-KIISLPDDTNIYCGH 244
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 29-156 2.36e-10

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: 57.21  E-value: 2.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  29 IVVDPGGDV--------QQLAAIIEELGvKVVNLVLTHghLDHVGGTVPLAEILKVEIVgPHKADNFWLQGLENQSQmfg 100
Cdd:cd07727   19 LILRPEGNIlvdsprysPPLAKRIEALG-GIRYIFLTH--RDDVADHAKWAERFGAKRI-IHEDDVNAVTRPDEVIV--- 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515628354 101 fplckafepntwLEEGDKVTFGNQViDVIHTPGHTPGHVVLFSEQARLAFVGDVLF 156
Cdd:cd07727   92 ------------LWGGDPWELDPDL-TLIPVPGHTRGSVVLLYKEKGVLFTGDHLA 134
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 29-196 4.44e-10

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 56.83  E-value: 4.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  29 IVVDPGG--DVQQLAAIIEELGVKV--VNLV-LTHGHLDHVGGTV--PLAEIlkveIVGPHKADNFWLqglenqsqmfgf 101
Cdd:cd07711   34 ILVDTGTpwDRDLLLKALAEHGLSPedIDYVvLTHGHPDHIGNLNlfPNATV----IVGWDICGDSYD------------ 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354 102 plckafePNTWLEEGDKVTFGNqvIDVIHTPGHTPGHVVLF---SEQARLAFVGDVLF--NGAIGRTDFPQGDFNT--LI 174
Cdd:cd07711   98 -------DHSLEEGDGYEIDEN--VEVIPTPGHTPEDVSVLvetEKKGTVAVAGDLFEreEDLEDPILWDPLSEDPelQE 168

                        170       180
                 ....*....|....*....|..
gi 515628354 175 ASIKtKLWPLgSDVtFVPGHGP 196
Cdd:cd07711  169 ESRK-RILAL-ADW-IIPGHGP 187
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 20-137 1.05e-09

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: 56.72  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  20 VWCDETMEG-IVVDPG--GDVQQLAAIIEELGVKV--VNLVL-THGHLDHVGGTVPLAEILKVEIVGPhKADNFWLQ--- 90
Cdd:cd16309   24 VFLITTPEGhILIDGAmpQSTPLIKDNIKKLGFDVkdVKYLLnTHAHFDHAGGLAELKKATGAQLVAS-AADKPLLEsgy 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 515628354  91 -GLENQSQMfGFPLCKAfepNTWLEEGDKVTFGNQVIDVIHTPGHTPG 137
Cdd:cd16309  103 vGSGDTKNL-QFPPVRV---DRVIGDGDKVTLGGTTLTAHLTPGHSPG 146
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 29-196 8.55e-09

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: 53.36  E-value: 8.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  29 IVVDPGGDVQQ--LAAIIEELGVKVVNLVLTHGHLDHVGGTVPLAEiLKVEIVGpHKADNFWLQglenqsqmfGFPLCKA 106
Cdd:cd16276   22 IVVDAPPSLGEnlLAAIRKVTDKPVTHVVYSHNHADHIGGASIFKD-EGATIIA-HEATAELLK---------RNPDPKR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354 107 FEPNTWLEEGDKVTFGNQVIDVI-HTPGHTPGHVVLFSEQARLAFVGDVLFNGAIGRTDFPqGDFNT--LIASIKTKL-- 181
Cdd:cd16276   91 PVPTVTFDDEYTLEVGGQTLELSyFGPNHGPGNIVIYLPKQKVLMAVDLINPGWVPFFNFA-GSEDIpgYIEALDELLey 169

                        170
                 ....*....|....*.
gi 515628354 182 -WplgsdVTFVPGHGP 196
Cdd:cd16276  170 dF-----DTFVGGHGN 180
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 40-194 1.32e-08

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: 53.37  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  40 LAAIIEELGVKV--VNLV-LTHGHLDHVGGT--VPLAEIlkveIVgpHKADNFWLQGLENQSQMFGFPLCKAFEPNTWLE 114
Cdd:cd07729   75 LEEQLARLGLDPedIDYViLSHLHFDHAGGLdlFPNATI----IV--QRAELEYATGPDPLAAGYYEDVLALDDDLPGGR 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354 115 ----EGDKVTFGNqvIDVIHTPGHTPGHVVLF--SEQARLAFVGDVLF---NGAIGRTDFPQGDFNTLIASIKT-KLWPL 184
Cdd:cd07729  149 vrlvDGDYDLFPG--VTLIPTPGHTPGHQSVLvrLPEGTVLLAGDAAYtyeNLEEGRPPGINYDPEAALASLERlKALAE 226

                        170
                 ....*....|
gi 515628354 185 GSDVTFVPGH 194
Cdd:cd07729  227 REGARVIPGH 236
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 15-154 3.84e-08

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 52.20  E-value: 3.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  15 QNCSIVWCDETmeGIVVDPGGDvqqLAAIIEELGVKVVNL---VLTHGHLDHVGGTVPLAEIL---KVEIVGPHKAdnfw 88
Cdd:COG1235   35 RSSILVEADGT--RLLIDAGPD---LREQLLRLGLDPSKIdaiLLTHEHADHIAGLDDLRPRYgpnPIPVYATPGT---- 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515628354  89 LQGLENQSQMFGFPLCKAFEPNTwLEEGDKVTFGN---QVIDVIHTPGHTPGhVVLFSEQARLAFVGDV 154
Cdd:COG1235  106 LEALERRFPYLFAPYPGKLEFHE-IEPGEPFEIGGltvTPFPVPHDAGDPVG-YRIEDGGKKLAYATDT 172
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 27-137 2.00e-07

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: 49.86  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  27 EGIVVDPGGDVQQ------LAAIIEELGVKVVN-LVLTHGHLDHVGGTVPLAEILKVE--IVGPHKADNFWLQGLENQSQ 97
Cdd:COG2333   22 KTILIDTGPRPSFdagervVLPYLRALGIRRLDlLVLTHPDADHIGGLAAVLEAFPVGrvLVSGPPDTSETYERLLEALK 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 515628354  98 MFGFPLckafepnTWLEEGDKVTFGNQVIDVIHTPGHTPG 137
Cdd:COG2333  102 EKGIPV-------RPCRAGDTWQLGGVRFEVLWPPEDLLE 134
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 29-137 3.62e-07

BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Bradyrhizobium diazoefficiens BJP-1, Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Caulobacter crescentus Mbl1b. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 49.24  E-value: 3.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  29 IVVDPGGD--VQQLAAIIEELGVKVVN---LVLTHGHLDHVGGtvpLAEILKVE----IVGPHKADNFWLQG-----LEN 94
Cdd:cd16288   34 ILIDTGLEssAPMIKANIRKLGFKPSDikiLLNSHAHLDHAGG---LAALKKLTgaklMASAEDAALLASGGksdfhYGD 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 515628354  95 QSqmFGFPLCKAfepNTWLEEGDKVTFGNQVIDVIHTPGHTPG 137
Cdd:cd16288  111 DS--LAFPPVKV---DRVLKDGDRVTLGGTTLTAHLTPGHTRG 148
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
8-153 6.25e-07

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 48.65  E-value: 6.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   8 VPVTSFSQNCSIVWCDEtmEGIVVDPGGDVQQLaaiIEELGVKVVNL---VLTHGHLDHVGGTVPLAEIL-------KVE 77
Cdd:COG1234   12 VPTPGRATSSYLLEAGG--ERLLIDCGEGTQRQ---LLRAGLDPRDIdaiFITHLHGDHIAGLPGLLSTRslagrekPLT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  78 IVGPHKADNFWLQGLENQSQMFGFPLckAFEPntwLEEGDKVTFGN---QVIDVIHTpghTPGHVVLFSEQAR-LAFVGD 153
Cdd:COG1234   87 IYGPPGTKEFLEALLKASGTDLDFPL--EFHE---IEPGEVFEIGGftvTAFPLDHP---VPAYGYRFEEPGRsLVYSGD 158
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 29-137 6.74e-07

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


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 48.50  E-value: 6.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  29 IVVDPGGD--VQQLAAIIEELGVKV--VNLVLT-HGHLDHVGGtvpLAEILKVE----IVGPHKAdnfwlQGLEN----- 94
Cdd:cd16315   34 VLIDSGTEeaAPLVLANIRKLGFDPkdVRWLLSsHEHFDHVGG---LAALQRATgarvAASAAAA-----PVLESgkpap 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 515628354  95 ---QSQMFgfplcKAFEPNT---WLEEGDKVTFGNQVIDVIHTPGHTPG 137
Cdd:cd16315  106 ddpQAGLH-----EPFPPVRvdrIVEDGDTVALGSLRLTAHATPGHTPG 149
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 29-130 7.03e-07

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 47.51  E-value: 7.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  29 IVVDPGGDVQQLAAII----EELGVKVVN-LVLTHGHLDHVGGtvpLAEILKVeivgpHKADNFWLQGLENQSQMFGFPL 103
Cdd:cd07731   22 ILIDTGPRDSFGEDVVvpylKARGIKKLDyLILTHPDADHIGG---LDAVLKN-----FPVKEVYMPGVTHTTKTYEDLL 93

                         90       100       110
                 ....*....|....*....|....*....|
gi 515628354 104 CKAFEPN---TWLEEGDKVTFGNQVIDVIH 130
Cdd:cd07731   94 DAIKEKGipvTPCKAGDRWQLGGVSFEVLS 123
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 37-137 7.59e-07

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


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 48.31  E-value: 7.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  37 VQQLAAIIEELGVKVVN---LVLTHGHLDHVGGTVPLAEILKVEIVGPHKADNFWLQGLENQSQMFG-----FPLCKAfe 108
Cdd:cd07708   44 APMIKANIKKLGFKFSDtklILISHAHFDHAGGSAEIKKQTGAKVMAGAEDVSLLLSGGSSDFHYANdsstyFPQSTV-- 121

                         90       100
                 ....*....|....*....|....*....
gi 515628354 109 pNTWLEEGDKVTFGNQVIDVIHTPGHTPG 137
Cdd:cd07708  122 -DRAVHDGERVTLGGTVLTAHATPGHTPG 149
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 34-137 9.97e-07

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: 47.85  E-value: 9.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  34 GGDVQQLAAIIEELGVKVVN---LVLTHGHLDHVGGtvpLAEILKVE--IVGPHKADNFWLQ-GLENQSQMFGF-PLCKA 106
Cdd:cd16308   41 AESVPLIKKNIQALGFKFKDikiLLTTQAHYDHVGA---MAAIKQQTgaKMMVDEKDAKVLAdGGKSDYEMGGYgSTFAP 117

                         90       100       110
                 ....*....|....*....|....*....|.
gi 515628354 107 FEPNTWLEEGDKVTFGNQVIDVIHTPGHTPG 137
Cdd:cd16308  118 VKADKLLHDGDTIKLGGTKLTLLHHPGHTKG 148
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 29-153 1.76e-06

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


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 46.49  E-value: 1.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  29 IVVDPG-GDVQQLAAIIEELGvKVVNLVLTHGHLDHVGGTVPLAEILK-------VEIVGPHKADNFWLQGLENQSQMFG 100
Cdd:cd16272   29 ILLDCGeGTVYRLLKAGVDPD-KLDAIFLSHFHLDHIGGLPTLLFARRyggrkkpLTIYGPKGIKEFLEKLLNFPVEILP 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515628354 101 FPLCKAFEPntwLEEGDKVTFGNQVI----DVIHTPGhTPGhVVLFSEQARLAFVGD 153
Cdd:cd16272  108 LGFPLEIEE---LEEGGEVLELGDLKveafPVKHSVE-SLG-YRIEAEGKSIVYSGD 159
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 16-155 1.17e-05

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: 44.80  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  16 NCSIVwcdETMEG-IVVDPGGDVQQLAAIIEE----LGVK-VVNLVLTHGHLDHVGGT---VPLAEILKVEIVGPHK--- 83
Cdd:cd07710   19 NMTFI---EGDTGlIIIDTLESAEAAKAALELfrkhTGDKpVKAIIYTHSHPDHFGGAggfVEEEDSGKVPIIAPEGfme 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  84 ---ADNFWLQGLENQ--SQMFGFPLCK--------------------AFEPNTWLEE-GDKVTFGNQVIDVIHTPGHTPG 137
Cdd:cd07710   96 eavSENVLAGNAMSRraAYQFGALLPKgekgqvgaglgpglstgtvgFIPPTITITEtGETLTIDGVELEFQHAPGEAPD 175

                        170
                 ....*....|....*...
gi 515628354 138 HVVLFSEQARLAFVGDVL 155
Cdd:cd07710  176 EMMVWLPDYKVLFCADNV 193
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 27-137 1.22e-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: 44.75  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  27 EGIVVDPGGD--VQQLAAIIEELGVKVVN---LVLTHGHLDHVGGTVPLAEILKVEIV-----------GPHKADNfwlq 90
Cdd:cd16310   32 GAILLDGGLEenAALIEQNIKALGFKLSDikiIINTHAHYDHAGGLAQLKADTGAKLWasrgdrpaleaGKHIGDN---- 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 515628354  91 glenQSQMFGFPlckAFEPNTWLEEGDKVTFGNQVIDVIHTPGHTPG 137
Cdd:cd16310  108 ----ITQPAPFP---AVKVDRILGDGEKIKLGDITLTATLTPGHTKG 147
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 52-194 1.97e-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: 44.05  E-value: 1.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  52 VNLVL-THGHLDHVGG-----------TVPLAEILKveivgpHKAD-NFWLQGLENQSQMFGfplckAFEPNTW--LEEG 116
Cdd:cd16277   64 VDYVLcTHLHVDHVGWntrlvdgrwvpTFPNARYLF------SRAEyDHWSSPDAGGPPNRG-----VFEDSVLpvIEAG 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354 117 --DKVTFGNQVID---VIHTPGHTPGH--VVLFSEQARLAFVGDVLFNGA-IGRTDFPQG-DFNTLIAsIKTKLWPL--- 184
Cdd:cd16277  133 laDLVDDDHEILDgirLEPTPGHTPGHvsVELESGGERALFTGDVMHHPIqVARPDWSSVfDEDPAQA-AATRRRLLera 211

                        170
                 ....*....|.
gi 515628354 185 -GSDVTFVPGH 194
Cdd:cd16277  212 aDTDTLLFPAH 222
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 29-137 3.01e-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: 43.70  E-value: 3.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  29 IVVD--PGGDVQQLAAIIEELGVKV--VNLVL-THGHLDHVGGTVPLAEILKVEIV-GPHKADNFWL-QGLENQSQMFGF 101
Cdd:cd16313   34 ILIDggFPKSPEQIAASIRQLGFKLedVKYILsSHDHWDHAGGIAALQKLTGAQVLaSPATVAVLRSgSMGKDDPQFGGL 113

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 515628354 102 PLCKAFEPNTWLEEGDKVTFGNQVIDVIHTPGHTPG 137
Cdd:cd16313  114 TPMPPVASVRAVRDGEVVKLGPLAVTAHATPGHTTG 149
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 39-137 6.33e-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: 42.67  E-value: 6.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  39 QLAAIIEELGVKV--VNLVL-THGHLDHVGGtvpLAEILKVE--IVGPHKADNFWLQGLEN-----QSQMF-GFPLCKAF 107
Cdd:cd16311   46 KIIANIEALGFRIedVKLILnSHGHIDHAGG---LAELQRRSgaLVAASPSAALDLASGEVgpddpQYHALpKYPPVKDM 122

                         90       100       110
                 ....*....|....*....|....*....|
gi 515628354 108 EpntWLEEGDKVTFGNQVIDVIHTPGHTPG 137
Cdd:cd16311  123 R---LARDGGQFNVGPVSLTAHATPGHTPG 149
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 24-137 1.17e-04

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: 41.73  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  24 ETMEGIVVDPGGDVQ---QLAAIIEELGVKVVNL---VLTHGHLDHVGgtvPLAEILKVeiVGPHKADN----FWLQGLE 93
Cdd:cd16289   28 KTPDGAVLLDGGMPQaadMLLDNMRALGVAPGDLkliLHSHAHADHAG---PLAALKRA--TGARVAANaesaVLLARGG 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 515628354  94 NQSQMFG----FPLCKAfepNTWLEEGDKVTFGNQVIDVIHTPGHTPG 137
Cdd:cd16289  103 SDDIHFGdgitFPPVQA---DRIVMDGEVVTLGGVTFTAHFTPGHTPG 147
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 44-81 1.77e-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: 41.24  E-value: 1.77e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 515628354  44 IEELGVKVVNLVLTHGHLDHVGGtVP-LAEILKVEIVGP 81
Cdd:cd07714   49 LEENKDKIKGIFITHGHEDHIGA-LPyLLPELNVPIYAT 86
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 38-153 1.85e-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: 41.10  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  38 QQLAAIIEELGVK---VVNLVLTHGHLDHVGGTVPL--AEIlkveIVGPhkadNFWLQGLENQSQMFGFP--LCKAFEPN 110
Cdd:cd07730   68 EDVAEQLAAGGIDpedIDAVILSHLHWDHIGGLSDFpnARL----IVGP----GAKEALRPPGYPSGFLPelLPSDFEGR 139

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515628354 111 TWLEEGDKVT-------------FGNQVIDVIHTPGHTPGHVVLF---SEQARLAFVGD 153
Cdd:cd07730  140 LVRWEEDDFLwvplgpfpraldlFGDGSLYLVDLPGHAPGHLGLLartTSGTWVFLAGD 198
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 29-162 1.89e-04

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 40.76  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   29 IVVDPGGDVQQLAA----IIEELGVKVVNLVLTHGHLDHVGGTVPLAEILKVEIVGPHKAdnfwLQGLENQSQmFGFPLC 104
Cdd:pfam12706   3 ILIDPGPDLRQQALpalqPGRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGV----LAHLRRNFP-YLFLLE 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515628354  105 KAFEPNTWLEEGDKVTFGNQVIDVIHTP---GHTPGHVVLFSEQA---------RLAFVGDV-LFNGAIGR 162
Cdd:pfam12706  78 HYGVRVHEIDWGESFTVGDGGLTVTATParhGSPRGLDPNPGDTLgfriegpgkRVYYAGDTgYFPDEIGE 148
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 23-155 1.93e-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: 293839  Cd Length: 252  Bit Score: 41.33  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  23 DETMEGIVVDPGGDVqqLAAIIEELGVK---VVNLVLTHGHLDHVGGTVPLAEILKVEIVGPhKAdNFWLQGLENQSQMF 99
Cdd:cd16281   66 DPKFRSIYVQHSEHS--LLKSLARLGLSpedITDVILTHLHFDHCGGATRADDDGLVELLFP-NA-TYWVQKRHWEWALN 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354 100 GFPLCKA--FEPN----------TWLEEGDKVTFGNqvIDVIHTPGHTPG--HVVLFSEQARLAFVGDVL 155
Cdd:cd16281  142 PNPRERAsfLPENiepleesgrlKLIDGSDAELGPG--IRFHLSDGHTPGqmLPEISTPGGTVVFAADLI 209
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 36-137 1.98e-04

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


Pssm-ID: 293865  Cd Length: 255  Bit Score: 41.28  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  36 DVQQLAAIIEELGVKVVN---LVLTHGHLDHVGGTVplaeilkvEIVGPHKADNFWLQG----LENQSQM---FGFPLCK 105
Cdd:cd16307   43 SVPQIKASIEKLGFKFSDtkiLLISHAHFDHAAGSA--------LIKRETHAKYMVMDGdvdvVESGGKSdffYGNDPST 114

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 515628354 106 AFEPNT---WLEEGDKVTFGNQVIDVIHTPGHTPG 137
Cdd:cd16307  115 YFPPAHvdkVLHDGEQVELGGTVLTAHLTAGHTKG 149
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 29-135 3.12e-04

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 40.57  E-value: 3.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  29 IVVDP---GGDVQQLAAiiEELGVKVVnlVLTHGHLDHVGGTVPLAEILKVEIVGPHKADNfWL--QGLENQSQM----- 98
Cdd:PRK00685  20 ILIDPfitGNPLADLKP--EDVKVDYI--LLTHGHGDHLGDTVEIAKRTGATVIANAELAN-YLseKGVEKTHPMniggt 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 515628354  99 --FGF---PLCKAFEPNTWLEEGDKVTFGNQVIDVIHTPGHT 135
Cdd:PRK00685  95 veFDGgkvKLTPALHSSSFIDEDGITYLGNPTGFVITFEGKT 136
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
16-81 1.17e-03

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 39.27  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  16 NCSIVWCDETMegIVVD----------PGGDVqqlaaII------EELGVKVVNLVLTHGHLDHVGGtVP-LAEILKVEI 78
Cdd:COG0595   20 NMYVYEYDDDI--IIVDcglkfpedemPGVDL-----VIpdisylEENKDKIKGIVLTHGHEDHIGA-LPyLLKELNVPV 91


                 ...
gi 515628354  79 VGP 81
Cdd:COG0595   92 YGT 94
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 29-137 1.80e-03

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


Pssm-ID: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 38.33  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  29 IVVDpGGDVQ---QLAAIIEELGVK---VVNLVLTHGHLDHVGGTVPLAEILKVEIVGPHKADNFWLQGLENQSQMfGFP 102
Cdd:cd16314   34 ILID-GGTDKaapLIEANIRALGFRpedVRYIVSSHEHFDHAGGIARLQRATGAPVVAREPAATTLERGRSDRSDP-QFL 111

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 515628354 103 LCKAFEPNT---WLEEGDKVTFGNQVIDVIHTPGHTPG 137
Cdd:cd16314  112 VVEKFPPVAsvqRIGDGEVLRVGPLALTAHATPGHTPG 149
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 38-196 2.09e-03

metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B1 MBls include chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1. B2 MBLs have a narrow substrate profile that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis. B2 MBLs include Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I.


Pssm-ID: 293793 [Multi-domain]  Cd Length: 219  Bit Score: 37.91  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  38 QQLAAIIEE-LGVKVVNLVLTHGHLDHVGGTvplaEILKVEIVGPHKAD-NFWLQGLENQSQMFGFPLCKAFEPNTWLEE 115
Cdd:cd07707   45 KELIKEIEKvSQKPVTEVINTHFHTDRAGGN----AYLKERGAKTVSTAlTRDLAKSEWAEIVAFTRKGLPEYPDLGYEL 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354 116 GDKV-----TFGNQVIDVIHT-PGHTPGHVVLFSEQARLAFVGDVLFNGAIGRTDFpqGDFNTLIASIKtKLWPLGSDVT 189
Cdd:cd07707  121 PDGVldgdfNLQFGKVEAFYPgPAHTPDNIVVYFPQENVLYGGCIIKETDLGNVAD--ADVKEWPTSIE-RLKKRYRNIK 197


                 ....*...
gi 515628354 190 FV-PGHGP 196
Cdd:cd07707  198 AViPGHGE 205
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 3-158 2.10e-03

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


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 37.87  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354   3 LKYQVV---PVTSFSQNCSIVWCDEtmEGIVVDPG---GDVQQLAAIIEELGVKVVNLVLTHGHLDHVGGtvpLAEILK- 75
Cdd:cd07739    1 LQVDVFtapEISSFPVTSTLIYGET--EAVLVDAQftrADAERLADWIKASGKTLTTIYITHGHPDHYFG---LEVLLEa 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  76 ---VEIV------------GPHKADNFWLQGLENQSQMFGFPlcKAFEPNTWLEEGDKVtfgnQVIDVIHtpGHTPGHVV 140
Cdd:cd07739   76 fpdAKVVatpavvahikaqLEPKLAFWGPLLGGNAPARLVVP--EPLDGDTLTLEGHPL----EIVGVGG--GDTDDTTY 147

                        170
                 ....*....|....*...
gi 515628354 141 LFSEQARLAFVGDVLFNG 158
Cdd:cd07739  148 LWIPSLKTVVAGDVVYNG 165
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 29-153 7.66e-03

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 36.43  E-value: 7.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515628354  29 IVVDP-----GGDVQQLAAIIEELGvKVVNLVLTHGHLDHVGGTVpLAEILK--VEIVGPHKADNfWLQGLenqsqmfGF 101
Cdd:COG2220   23 ILIDPvfsgrASPVNPLPLDPEDLP-KIDAVLVTHDHYDHLDDAT-LRALKRtgATVVAPLGVAA-WLRAW-------GF 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515628354 102 PLCKAFEPntwleeGDKVTFGNqvIDVIHTPG-HTPGH----------VVLFSEQARLAFVGD 153
Cdd:COG2220   93 PRVTELDW------GESVELGG--LTVTAVPArHSSGRpdrngglwvgFVIETDGKTIYHAGD 147
 
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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