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Conserved domains on  [gi|515955084|ref|WP_017385667|]
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MULTISPECIES: MBL fold metallo-hydrolase [Acinetobacter]

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 ...
 4-193 1.83e-118

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: 334.52  E-value: 1.83e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084   4 VKIVPVTAFAQNCSLVWDSETKEAVLIDAGGDASVLKKEVEALGLKVKALWLTHGHLDHAGAVGELAKEWSVPVIGPHKE 83
Cdd:cd07737    1 YQIIPVTPFQQNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  84 DQFWLDMIQEVSARYGFPIPQPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGHVIFYNKNHGLLWTGDVLFKGSIGRTD 163
Cdd:cd07737   81 DKFLLENLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTD 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 515955084 164 FPRGNHDQLIESIKRECFSLPDDTQFISGH 193
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 ...
 4-193 1.83e-118

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: 334.52  E-value: 1.83e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084   4 VKIVPVTAFAQNCSLVWDSETKEAVLIDAGGDASVLKKEVEALGLKVKALWLTHGHLDHAGAVGELAKEWSVPVIGPHKE 83
Cdd:cd07737    1 YQIIPVTPFQQNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  84 DQFWLDMIQEVSARYGFPIPQPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGHVIFYNKNHGLLWTGDVLFKGSIGRTD 163
Cdd:cd07737   81 DKFLLENLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTD 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 515955084 164 FPRGNHDQLIESIKRECFSLPDDTQFISGH 193
Cdd:cd07737  161 FPGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 8-198 9.81e-56

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 176.42  E-value: 9.81e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084   8 PVTAFAQNCSLVWDseTKEAVLIDAGGD---ASVLKKEVEALGLKVKALWLTHGHLDHAGAVGELAKEWSVPVIGPHKED 84
Cdd:COG0491    9 PGAGLGVNSYLIVG--GDGAVLIDTGLGpadAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  85 QFWLDMIQEVSARYgfpipQPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGHVIFYNKNHGLLWTGDVLFKGSIGRTDF 164
Cdd:COG0491   87 EALEAPAAGALFGR-----EPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDL 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 515955084 165 PRGNHDQLIESIKReCFSLPDDTqFISGHGPMST 198
Cdd:COG0491  162 PDGDLAQWLASLER-LLALPPDL-VIPGHGPPTT 193
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 15-193 4.86e-40

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: 134.99  E-value: 4.86e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084    15 NCSLVWDseTKEAVLIDAG-GDASVLKKEVEALGL-KVKALWLTHGHLDHAGAVGELAKEWSVPVIGPHKEDQFWLDMIQ 92
Cdd:smart00849   1 NSYLVRD--DGGAILIDTGpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084    93 EVSARygFPIPQPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGHVIFYNKNHGLLWTGDVLFKGSIGRTDFPRGNHDQL 172
Cdd:smart00849  79 LLGEL--GAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAAS 156

                          170       180
                   ....*....|....*....|.
gi 515955084   173 IESIKRECFSLPDDTQFISGH 193
Cdd:smart00849 157 DALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
9-193 9.49e-32

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 114.39  E-value: 9.49e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084    9 VTAFAQNCSLVWDseTKEAVLIDAGGDAS----VLKKEVEALGLKVKALWLTHGHLDHAGAVGELAKEWSVPVIGPHKED 84
Cdd:pfam00753   1 LGPGQVNSYLIEG--GGGAVLIDTGGSAEaallLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084   85 QFWLD---MIQEVSARYGFPIPQPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGHVIFYNKNHGLLWTGDVLFKGSIGR 161
Cdd:pfam00753  79 RELLDeelGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGR 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 515955084  162 TDFPRGNHDQLIESIKRECFSL------PDDTQFISGH 193
Cdd:pfam00753 159 LDLPLGGLLVLHPSSAESSLESllklakLKAAVIVPGH 196
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 25-207 5.23e-19

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 82.15  E-value: 5.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  25 KEAVLID-----AGGDASVLKKeveaLGLKVKALWLTHGHLDHAGAVGELAKEwsVPVIGphkedqfwlDMIQEVSAryg 99
Cdd:PLN02962  36 KPALLIDpvdktVDRDLSLVKE----LGLKLIYAMNTHVHADHVTGTGLLKTK--LPGVK---------SIISKASG--- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084 100 fpipqpVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGHVIfYNKNHG-------LLWTGDVLFKGSIGRTDFPRGNHDQL 172
Cdd:PLN02962  98 ------SKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVT-YVTGEGpdqpqprMAFTGDALLIRGCGRTDFQGGSSDQL 170

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 515955084 173 IESIKRECFSLPDDTQFISGHG----PMSTIGYEKQFNP 207
Cdd:PLN02962 171 YKSVHSQIFTLPKDTLIYPAHDykgfTVSTVGEEMLYNP 209
 
Name Accession Description Interval E-value
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 4-193 1.83e-118

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: 334.52  E-value: 1.83e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084   4 VKIVPVTAFAQNCSLVWDSETKEAVLIDAGGDASVLKKEVEALGLKVKALWLTHGHLDHAGAVGELAKEWSVPVIGPHKE 83
Cdd:cd07737    1 YQIIPVTPFQQNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  84 DQFWLDMIQEVSARYGFPIPQPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGHVIFYNKNHGLLWTGDVLFKGSIGRTD 163
Cdd:cd07737   81 DKFLLENLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTD 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 515955084 164 FPRGNHDQLIESIKRECFSLPDDTQFISGH 193
Cdd:cd07737  161 FPGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 5-193 3.60e-72

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: 217.15  E-value: 3.60e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084   5 KIVPVTAFAQNCSLVWDsETKEAVLIDAGGDASV-LKKEVEALGLKVKALWLTHGHLDHAGAVGELAKEWSVPVIGpHKE 83
Cdd:cd06262    1 KRLPVGPLQTNCYLVSD-EEGEAILIDPGAGALEkILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYI-HEA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  84 DQFWLDMIQEVSARYGFPIPQPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGHVIFYNKNHGLLWTGDVLFKGSIGRTD 163
Cdd:cd06262   79 DAELLEDPELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTD 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 515955084 164 FPRGNHDQLIESIKRECFSLPDDTQFISGH 193
Cdd:cd06262  159 LPGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 4-209 9.93e-71

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: 214.14  E-value: 9.93e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084   4 VKIVPVTAFAQNCSLVWDSETKEAVLIDAGGDASVLKKEVEALGLKVKALWLTHGHLDHAGAVGELAKEWSVPVIgPHKE 83
Cdd:cd16322    1 VRPFTLGPLQENTYLVADEGGGEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVY-LHPD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  84 DQFWLDMIQEVSARYGFPIPQPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGHVIFYNKNHGLLWTGDVLFKGSIGRTD 163
Cdd:cd16322   80 DLPLYEAADLGAKAFGLGIEPLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRTD 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 515955084 164 FPRGNHDQLIESIKReCFSLPDDTQFISGHGPMSTIGYEKQFNPFV 209
Cdd:cd16322  160 LPGGDPKAMAASLRR-LLTLPDETRVFPGHGPPTTLGEERRTNPFL 204
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 8-198 9.81e-56

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 176.42  E-value: 9.81e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084   8 PVTAFAQNCSLVWDseTKEAVLIDAGGD---ASVLKKEVEALGLKVKALWLTHGHLDHAGAVGELAKEWSVPVIGPHKED 84
Cdd:COG0491    9 PGAGLGVNSYLIVG--GDGAVLIDTGLGpadAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  85 QFWLDMIQEVSARYgfpipQPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGHVIFYNKNHGLLWTGDVLFKGSIGRTDF 164
Cdd:COG0491   87 EALEAPAAGALFGR-----EPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDL 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 515955084 165 PRGNHDQLIESIKReCFSLPDDTqFISGHGPMST 198
Cdd:COG0491  162 PDGDLAQWLASLER-LLALPPDL-VIPGHGPPTT 193
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 7-193 7.32e-41

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: 136.82  E-value: 7.32e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084   7 VPVTAFAQN-CSLVWDSETKEAVLIDAGGDASVLKkEVEALGLKVKALWLTHGHLDHAGAVGELAKEW-SVPVIGPHKED 84
Cdd:cd07723    1 VPIPALSDNyIYLIVDEATGEAAVVDPGEAEPVLA-ALEKNGLTLTAILTTHHHWDHTGGNAELKALFpDAPVYGPAEDR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  85 qfwldmiqevsarygfpIPqpvKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGHVIFYNKNHGLLWTGDVLFKGSIGRTDf 164
Cdd:cd07723   80 -----------------IP---GLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGRFF- 138

                        170       180
                 ....*....|....*....|....*....
gi 515955084 165 pRGNHDQLIESIKReCFSLPDDTQFISGH 193
Cdd:cd07723  139 -EGTAEQMYASLQK-LLALPDDTLVYCGH 165
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 15-193 4.86e-40

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: 134.99  E-value: 4.86e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084    15 NCSLVWDseTKEAVLIDAG-GDASVLKKEVEALGL-KVKALWLTHGHLDHAGAVGELAKEWSVPVIGPHKEDQFWLDMIQ 92
Cdd:smart00849   1 NSYLVRD--DGGAILIDTGpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084    93 EVSARygFPIPQPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGHVIFYNKNHGLLWTGDVLFKGSIGRTDFPRGNHDQL 172
Cdd:smart00849  79 LLGEL--GAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAAS 156

                          170       180
                   ....*....|....*....|.
gi 515955084   173 IESIKRECFSLPDDTQFISGH 193
Cdd:smart00849 157 DALESLLKLLKLLPKLVVPGH 177
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 3-178 3.81e-34

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: 120.40  E-value: 3.81e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084   3 QVKIVPVTAFAqNCSLVWDSEtkEAVLIDAG--GDASVLKKEVEALGLK---VKALWLTHGHLDHAGAVGELAKEWSVPV 77
Cdd:cd07721    1 GVYQLPLLPPV-NAYLIEDDD--GLTLIDTGlpGSAKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAALKEAPGAPV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  78 IGpHKEDQFWLD--------MIQEVSARYGFPIP-QPVKVDQWLEGGEVLKLGEDeFEVRFAPGHTPGHVIFYNKNHGLL 148
Cdd:cd07721   78 YA-HEREAPYLEgekpypppVRLGLLGLLSPLLPvKPVPVDRTLEDGDTLDLAGG-LRVIHTPGHTPGHISLYLEEDGVL 155

                        170       180       190
                 ....*....|....*....|....*....|....
gi 515955084 149 WTGDvLFKGSIGRTDFPRG----NHDQLIESIKR 178
Cdd:cd07721  156 IAGD-ALVTVGGELVPPPPpftwDMEEALESLRK 188
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 18-194 2.38e-33

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: 117.89  E-value: 2.38e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  18 LVWDSETKEAVLIDAGGD-ASVLKKEVEALGLKVKALWLTHGHLDHAGAVGELAKEWSVP-VIGPHKEDQFwldmiqevs 95
Cdd:cd07724   16 LVGDPETGEAAVIDPVRDsVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPiVIGEGAPASF--------- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  96 arygfpipqpvkVDQWLEGGEVLKLGEDEFEVRFAPGHTPGHVIFYNKNHGLLWTGDVLFKGSIGRTDFP---RGNHDQL 172
Cdd:cd07724   87 ------------FDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPgeaEGLARQL 154

                        170       180
                 ....*....|....*....|..
gi 515955084 173 IESIKRECFSLPDDTQFISGHG 194
Cdd:cd07724  155 YDSLQRKLLLLPDETLVYPGHD 176
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 12-193 2.94e-32

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: 114.94  E-value: 2.94e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  12 FAQNCSLVWDSETKEAVLIDAGGDASVLKKEVEALGLKVKALWLTHGHLDHAGAVGELAKEWSVPVIGPHKEDQFwldmi 91
Cdd:cd16275   10 MINYSYIIIDKATREAAVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDY----- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  92 qevsarYGFPIPQPVKVdqwlEGGEVLKLGEDEFEVRFAPGHTPGHVIFYNKNHglLWTGDVLFKGSIGRTDFPRGNHDQ 171
Cdd:cd16275   85 ------YGFRCPNLIPL----EDGDTIKIGDTEITCLLTPGHTPGSMCYLLGDS--LFTGDTLFIEGCGRCDLPGGDPEE 152

                        170       180
                 ....*....|....*....|..
gi 515955084 172 LIESIKRECFSLPDDTQFISGH 193
Cdd:cd16275  153 MYESLQRLKKLPPPNTRVYPGH 174
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
9-193 9.49e-32

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 114.39  E-value: 9.49e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084    9 VTAFAQNCSLVWDseTKEAVLIDAGGDAS----VLKKEVEALGLKVKALWLTHGHLDHAGAVGELAKEWSVPVIGPHKED 84
Cdd:pfam00753   1 LGPGQVNSYLIEG--GGGAVLIDTGGSAEaallLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084   85 QFWLD---MIQEVSARYGFPIPQPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGHVIFYNKNHGLLWTGDVLFKGSIGR 161
Cdd:pfam00753  79 RELLDeelGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGR 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 515955084  162 TDFPRGNHDQLIESIKRECFSL------PDDTQFISGH 193
Cdd:pfam00753 159 LDLPLGGLLVLHPSSAESSLESllklakLKAAVIVPGH 196
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 24-178 1.63e-24

uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 95.00  E-value: 1.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  24 TKEAVLIDAG-GDASvLKKEVEALGLK-VKALwLTHGHLDHAGAVGELAKEWSvpvigpHKEDQFWL---DMIQEVSARY 98
Cdd:cd07712   17 RDRALLIDTGlGIGD-LKEYVRTLTDLpLLVV-ATHGHFDHIGGLHEFEEVYV------HPADAEILaapDNFETLTWDA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  99 GFPIPQPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGHVIFYNKNHGLLWTGDVLFKGSIgRTDFPRGNHDQLIESIKR 178
Cdd:cd07712   89 ATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVYDGPL-IMDLPHSDLDDYLASLEK 167
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 25-178 2.71e-20

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: 84.85  E-value: 2.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  25 KEAVLIDAGGDASV--LKKEVEALGL---KVKALWLTHGHLDHAGAVGELAKEWSVPVIG------PHKED--------- 84
Cdd:cd07726   25 GRPALIDTGPSSSVprLLAALEALGIapeDVDYIILTHIHLDHAGGAGLLAEALPNAKVYvhprgaRHLIDpsklwasar 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  85 QFWLDMIQevsaRYGFPIpQPVKVDQW--LEGGEVLKLGEDEFEVRFAPGHTPGHVIFYNKNHGLLWTGDVlFKGSIGRT 162
Cdd:cd07726  105 AVYGDEAD----RLGGEI-LPVPEERVivLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDA-AGVRYPEL 178

                        170       180
                 ....*....|....*....|....
gi 515955084 163 DFPRGNH--------DQLIESIKR 178
Cdd:cd07726  179 DVVGPPStpppdfdpEAWLESLDR 202
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 15-198 1.06e-19

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 83.00  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  15 NCSLVwdsETKEAVL-IDAGGDASV---LKKEVEAL-GLKVKALWLTHGHLDH---AGAVGELAkewsVPVIGPHK---- 82
Cdd:cd16282   16 NIGFI---VGDDGVVvIDTGASPRLaraLLAAIRKVtDKPVRYVVNTHYHGDHtlgNAAFADAG----APIIAHENtree 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  83 ----EDQFWLDMiqEVSARYGFPIPQPVKVDQWLEGGEVLKLGEDEFEVR-FAPGHTPGHVIFYNKNHGLLWTGDVLFKG 157
Cdd:cd16282   89 laarGEAYLELM--RRLGGDAMAGTELVLPDRTFDDGLTLDLGGRTVELIhLGPAHTPGDLVVWLPEEGVLFAGDLVFNG 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 515955084 158 SIgrTDFPRGNHDQLIESIKRecFSLPDDTQFISGHGPMST 198
Cdd:cd16282  167 RI--PFLPDGSLAGWIAALDR--LLALDATVVVPGHGPVGD 203
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 25-207 5.23e-19

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 82.15  E-value: 5.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  25 KEAVLID-----AGGDASVLKKeveaLGLKVKALWLTHGHLDHAGAVGELAKEwsVPVIGphkedqfwlDMIQEVSAryg 99
Cdd:PLN02962  36 KPALLIDpvdktVDRDLSLVKE----LGLKLIYAMNTHVHADHVTGTGLLKTK--LPGVK---------SIISKASG--- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084 100 fpipqpVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGHVIfYNKNHG-------LLWTGDVLFKGSIGRTDFPRGNHDQL 172
Cdd:PLN02962  98 ------SKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVT-YVTGEGpdqpqprMAFTGDALLIRGCGRTDFQGGSSDQL 170

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 515955084 173 IESIKRECFSLPDDTQFISGHG----PMSTIGYEKQFNP 207
Cdd:PLN02962 171 YKSVHSQIFTLPKDTLIYPAHDykgfTVSTVGEEMLYNP 209
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 26-165 2.52e-17

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: 77.49  E-value: 2.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  26 EAVLIDAGGD--ASVLKKEVEALGLK---VKALWLTHGHLDHAGAVGELAKEWSVPVIGphkedqfwldMIQEVSA---- 96
Cdd:cd16310   32 GAILLDGGLEenAALIEQNIKALGFKlsdIKIIINTHAHYDHAGGLAQLKADTGAKLWA----------SRGDRPAleag 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515955084  97 -------RYGFPIPqPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGHVIfynknhgllWTGDVLFKGSIGRTDFP 165
Cdd:cd16310  102 khigdniTQPAPFP-AVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTT---------WSTTVKENGRPLRVVFP 167
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 19-155 1.08e-16

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: 74.87  E-value: 1.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  19 VWDSETKEAVLIDAGGDASV---LKKEVEALGLKVKALWLTHGHLDHAGAVGELAKEWSVPVIGPHKEDQFWLDMIQEVS 95
Cdd:cd07743   12 VYVFGDKEALLIDSGLDEDAgrkIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAFIENPLLEPS 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  96 ARYG-FPIP---------QPVKVDQWLEGGEvLKLGEDEFEVRFAPGHTPGHVIFYNKNhGLLWTGDVLF 155
Cdd:cd07743   92 YLGGaYPPKelrnkflmaKPSKVDDIIEEGE-LELGGVGLEIIPLPGHSFGQIGILTPD-GVLFAGDALF 159
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 26-195 4.48e-16

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: 72.91  E-value: 4.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  26 EAVLIDAG-GDASVLKKEVEAL-GLKVKALWLTHGHLDHAGAVGELAKEWSVPVIGPHKEDQFWLDMiqevsarygfpip 103
Cdd:cd16278   28 GVVVIDPGpDDPAHLDALLAALgGGRVSAILVTHTHRDHSPGAARLAERTGAPVRAFGPHRAGGQDT------------- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084 104 qPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGHVIFYNKNHGLLWTGDVLFKGSigrT---DFPRGNHDQLIESIKR-- 178
Cdd:cd16278   95 -DFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVMGWS---TtviAPPDGDLGDYLASLERll 170

                        170
                 ....*....|....*..
gi 515955084 179 ECfslpDDTQFISGHGP 195
Cdd:cd16278  171 AL----DDRLLLPGHGP 183
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 5-193 4.88e-16

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 74.41  E-value: 4.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084   5 KIVPVTAFAQNCS-LVWDSETKEAVLIDAGGDASVLKKEVEAlGLKVKALWLTHGHLDHAGAVGELAKEWS-VPVIGPHK 82
Cdd:PLN02469   2 KIIPVPCLEDNYAyLIIDESTKDAAVVDPVDPEKVLQAAHEH-GAKIKLVLTTHHHWDHAGGNEKIKKLVPgIKVYGGSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  83 EDqfwldmiqevsarygfpipqpVK--VDQwLEGGEVLKLGED-EFEVRFAPGHTPGHVIFY----NKNHGLLWTGDVLF 155
Cdd:PLN02469  81 DN---------------------VKgcTHP-VENGDKLSLGKDvNILALHTPCHTKGHISYYvtgkEGEDPAVFTGDTLF 138

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 515955084 156 KGSIGRtdFPRGNHDQLIESIKRECFSLPDDTQFISGH 193
Cdd:PLN02469 139 IAGCGK--FFEGTAEQMYQSLCVTLGSLPKPTQVYCGH 174
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 9-193 4.95e-16

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 74.09  E-value: 4.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084   9 VTAFAQNCSLVWDSETKEAVLIDAGGDASVLKKeVEALGLKVKALWLTHGHLDHAGAVGELAKEW-SVPVIGPhkedqfw 87
Cdd:PRK10241   6 IPAFDDNYIWVLNDEAGRCLIVDPGEAEPVLNA-IAENNWQPEAIFLTHHHHDHVGGVKELVEKFpQIVVYGP------- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  88 ldmiQEVsarygfpipQPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGHVIFYnkNHGLLWTGDVLFKGSIGRtdFPRG 167
Cdd:PRK10241  78 ----QET---------QDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF--SKPYLFCGDTLFSGGCGR--LFEG 140

                        170       180
                 ....*....|....*....|....*.
gi 515955084 168 NHDQLIESIKReCFSLPDDTQFISGH 193
Cdd:PRK10241 141 TASQMYQSLKK-INALPDDTLICCAH 165
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 26-154 7.51e-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: 7.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  26 EAVLIDAG----GDASVLKKEVEALGLK---VKALWLTHGHLDHAGAVGELAKEWSVPVigphkedqfwldMIQEVsary 98
Cdd:cd07725   25 ETTLIDTGlateEDAEALWEGLKELGLKpsdIDRVLLTHHHPDHIGLAGKLQEKSGATV------------YILDV---- 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515955084  99 gfpipQPVKvdqwleGGEVLKLGEDEFEVRFAPGHTPGHVIFYNKNHGLLWTGDVL 154
Cdd:cd07725   89 -----TPVK------DGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAV 133
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 28-214 1.64e-13

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 67.22  E-value: 1.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  28 VLIDAG---GDASVLKKEVEALGLK---VKALWLTHGHLDHAGAVGELAKEWSVPVIGPhKEDqfWlDMIQEVSARYGFP 101
Cdd:cd16280   34 ILIDALnnnEAADLIVDGLEKLGLDpadIKYILITHGHGDHYGGAAYLKDLYGAKVVMS-EAD--W-DMMEEPPEEGDNP 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084 102 I-PQPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGHV--IFYNKNHG-----LLWTGdvlfkgsigrTDFPRGNHDQLI 173
Cdd:cd16280  110 RwGPPPERDIVIKDGDTLTLGDTTITVYLTPGHTPGTLslIFPVKDGGkthraGLWGG----------TGLNTGPNLERR 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515955084 174 ES-------IKRECFSLPDDTqFISGHgPMSTIGYEK----------QFNPFVAGKAG 214
Cdd:cd16280  180 EQyiaslerFKKIAEEAGVDV-FLSNH-PFQDGSLEKrealrnrkpgEPNPFVDGQAW 235
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 24-136 1.78e-13

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: 66.96  E-value: 1.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  24 TKEAVLIDAGGDASV--LKKEVEALGLK---VKALWLTHGHLDHAGAVGELaKEWS----------VPVI-GPHKEDQFW 87
Cdd:cd16288   30 PQGLILIDTGLESSApmIKANIRKLGFKpsdIKILLNSHAHLDHAGGLAAL-KKLTgaklmasaedAALLaSGGKSDFHY 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 515955084  88 LDmiqevsARYGFPipqPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPG 136
Cdd:cd16288  109 GD------DSLAFP---PVKVDRVLKDGDRVTLGGTTLTAHLTPGHTRG 148
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 27-209 3.94e-13

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: 66.03  E-value: 3.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  27 AVLIDAG--GDASVLKKEVEALGLK---VKALWLTHGHLDHAGAVGELAKEW---------SVPVI--GPHKEDQFwldm 90
Cdd:cd07708   33 NILIDGDmeQNAPMIKANIKKLGFKfsdTKLILISHAHFDHAGGSAEIKKQTgakvmagaeDVSLLlsGGSSDFHY---- 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  91 iqEVSARYGFPipqPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGhvifynknhGLLWT---------GDVLFKGSIGR 161
Cdd:cd07708  109 --ANDSSTYFP---QSTVDRAVHDGERVTLGGTVLTAHATPGHTPG---------CTTWTmtlkdhgkqYQVVFADSLTV 174

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515955084 162 ------TDFPRGNHdqLIESIKREcF----SLPDDTqFISGHGPMSTIGYEKQF------NPFV 209
Cdd:cd07708  175 npgyrlVDNPTYPK--IVEDYRHS-FavveAMRCDI-LLGPHPGVFDMKNKYVLlskgqnNPFV 234
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 56-193 4.10e-13

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 66.79  E-value: 4.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  56 THGHLDHAGAVGELAKEWSVPVIGPHKEDqfwlDMIQ--EVSARYGfpipqpvkvDQWLEGGEvlklgedEFEVRFAPGH 133
Cdd:PLN02398 128 THHHYDHTGGNLELKARYGAKVIGSAVDK----DRIPgiDIVLKDG---------DKWMFAGH-------EVLVMETPGH 187

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084 134 TPGHVIFYNKNHGLLWTGDVLFKGSIGRtdFPRGNHDQLIESIKReCFSLPDDTQFISGH 193
Cdd:PLN02398 188 TRGHISFYFPGSGAIFTGDTLFSLSCGK--LFEGTPEQMLSSLQK-IISLPDDTNIYCGH 244
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 28-136 4.82e-12

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: 63.26  E-value: 4.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  28 VLIDAGGDASV--LKKEVEALGLK---VKALWLTHGHLDHAGAVGELAKEWSVPVigphkedqfwldMIQEVSAR----- 97
Cdd:cd16308   34 ILINTGLAESVplIKKNIQALGFKfkdIKILLTTQAHYDHVGAMAAIKQQTGAKM------------MVDEKDAKvladg 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 515955084  98 ---------YGfPIPQPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPG 136
Cdd:cd16308  102 gksdyemggYG-STFAPVKADKLLHDGDTIKLGGTKLTLLHHPGHTKG 148
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-150 7.41e-12

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


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 62.75  E-value: 7.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  28 VLIDAG--GDASVLKKEVEALGLK---VKALWLTHGHLDHAGAVGELAKEWSVPVI------------GPHKED-QF-WL 88
Cdd:cd16290   34 ILIDGAlpQSAPQIEANIRALGFRledVKLILNSHAHFDHAGGIAALQRDSGATVAaspagaaalrsgGVDPDDpQAgAA 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515955084  89 DmiqevsarygfPIPqPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGhvifynknhGLLWT 150
Cdd:cd16290  114 D-----------PFP-PVAKVRVVADGEVVKLGPLAVTAHATPGHTPG---------GTSWT 154
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 23-136 1.02e-10

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: 59.44  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  23 ETKE-AVLIDAG--GDASVLKKEVEALGL---KVKALWLTHGHLDHAGAVGELAKEWSVPVIGpHKEDQFWLDMIQEVSA 96
Cdd:cd16289   28 KTPDgAVLLDGGmpQAADMLLDNMRALGVapgDLKLILHSHAHADHAGPLAALKRATGARVAA-NAESAVLLARGGSDDI 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 515955084  97 RYG----FPipqPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPG 136
Cdd:cd16289  107 HFGdgitFP---PVQADRIVMDGEVVTLGGVTFTAHFTPGHTPG 147
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-136 1.43e-10

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


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 59.03  E-value: 1.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  28 VLIDAG--GDASVLKKEVEALGLK---VKALWLTHGHLDHAGAVGELAKEWSVPVIGPhKEDQFWLDmiqevSARYG--- 99
Cdd:cd16309   34 ILIDGAmpQSTPLIKDNIKKLGFDvkdVKYLLNTHAHFDHAGGLAELKKATGAQLVAS-AADKPLLE-----SGYVGsgd 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 515955084 100 -----FPipqPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPG 136
Cdd:cd16309  108 tknlqFP---PVRVDRVIGDGDKVTLGGTTLTAHLTPGHSPG 146
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-150 2.65e-10

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: 58.46  E-value: 2.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  28 VLIDAGGDASVLK--KEVEALGLK---VKALWLTHGHLDHAGAVGELAKEwSVPVIGPHKEDQFWLdMIQEVS---ARYG 99
Cdd:cd16311   34 VLVDGGLPESAPKiiANIEALGFRiedVKLILNSHGHIDHAGGLAELQRR-SGALVAASPSAALDL-ASGEVGpddPQYH 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 515955084 100 -FPIPQPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGhvifynknhGLLWT 150
Cdd:cd16311  112 aLPKYPPVKDMRLARDGGQFNVGPVSLTAHATPGHTPG---------GLSWT 154
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 15-156 3.81e-10

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: 57.80  E-value: 3.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  15 NCSLVwdsETK-EAVLIDAG---------G------DASVLKKEVEalglKVKALWLTHGHLDHAGAVGELAKEWSVPVI 78
Cdd:cd07714   12 NMYVV---EYDdDIIIIDCGlkfpdedmpGvdyiipDFSYLEENKD----KIKGIFITHGHEDHIGALPYLLPELNVPIY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  79 GPhkedQFWLDMIQEVSARYGFPIPQPVKVdqwLEGGEVLKLGedEFEVRF------APG------HTPGHVIFYnknhg 146
Cdd:cd07714   85 AT----PLTLALIKKKLEEFKLIKKVKLNE---IKPGERIKLG--DFEVEFfrvthsIPDsvglaiKTPEGTIVH----- 150

                        170
                 ....*....|
gi 515955084 147 llwTGDvlFK 156
Cdd:cd07714  151 ---TGD--FK 155
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-136 5.15e-10

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: 57.36  E-value: 5.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  28 VLIDAGGD--ASVLKKEVEALGLK---VKALWLTHGHLDHAGAVGELAKEWSVPVIG------------PHKED-QFwld 89
Cdd:cd16315   34 VLIDSGTEeaAPLVLANIRKLGFDpkdVRWLLSSHEHFDHVGGLAALQRATGARVAAsaaaapvlesgkPAPDDpQA--- 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 515955084  90 miqevSARYGFPipqPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPG 136
Cdd:cd16315  111 -----GLHEPFP---PVRVDRIVEDGDTVALGSLRLTAHATPGHTPG 149
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 28-155 4.28e-09

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: 53.74  E-value: 4.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  28 VLIDAGGDASVLKKEVEALGlKVKALWLTHGHlDHAGAVgELAKEWSVPVIgPHKEDqfwldmiqeVSARygfpiPQPVK 107
Cdd:cd07727   27 ILVDSPRYSPPLAKRIEALG-GIRYIFLTHRD-DVADHA-KWAERFGAKRI-IHEDD---------VNAV-----TRPDE 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 515955084 108 VDQwLEGGEVLKLGEDeFEVRFAPGHTPGHVIFYNKNHGLLWTGDVLF 155
Cdd:cd07727   89 VIV-LWGGDPWELDPD-LTLIPVPGHTRGSVVLLYKEKGVLFTGDHLA 134
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
15-156 6.90e-09

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 55.07  E-value: 6.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  15 NCSLVwdsETK-EAVLIDAG---------G------DASVLKKEVEalglKVKALWLTHGHLDHAGAVGELAKEWSVPVI 78
Cdd:COG0595   20 NMYVY---EYDdDIIIVDCGlkfpedempGvdlvipDISYLEENKD----KIKGIVLTHGHEDHIGALPYLLKELNVPVY 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  79 GPhkedQFWLDMIQEVSARYGFPIPQPVKVdqwLEGGEVLKLGedEFEVRFAP---------G---HTPGHVIFYnknhg 146
Cdd:COG0595   93 GT----PLTLALLEAKLKEHGLLKKVKLHV---VKPGDRIKFG--PFKVEFFRvthsipdslGlaiRTPAGTIVH----- 158

                        170
                 ....*....|
gi 515955084 147 llwTGDvlFK 156
Cdd:COG0595  159 ---TGD--FK 163
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 18-195 8.25e-08

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 50.28  E-value: 8.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  18 LVWDsetKEAVLIDA---GGDAsvLKKEVEAL-GLKVKALWLTHGHLDHAGAvGELAKEWSVPVIGpHKEDQFWLDMiqe 93
Cdd:cd16276   15 LVTD---KGVIVVDAppsLGEN--LLAAIRKVtDKPVTHVVYSHNHADHIGG-ASIFKDEGATIIA-HEATAELLKR--- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  94 vsarygFPIPQPVKVDQWLEGGEVLKLGEDEFEVR-FAPGHTPGHVIFYNKNHGLLWTGDVL------FKGSIGRTDFP- 165
Cdd:cd16276   85 ------NPDPKRPVPTVTFDDEYTLEVGGQTLELSyFGPNHGPGNIVIYLPKQKVLMAVDLInpgwvpFFNFAGSEDIPg 158

                        170       180       190
                 ....*....|....*....|....*....|.
gi 515955084 166 -RGNHDQLIEsikrecfsLPDDTqFISGHGP 195
Cdd:cd16276  159 yIEALDELLE--------YDFDT-FVGGHGN 180
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 15-158 9.62e-08

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: 50.22  E-value: 9.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  15 NCSLVwdSETKEAVLIDAG----GDASVLKKEVEALGLK-VKALWLTHGHLDHAGAVGELAKEWSVPVIGPHKedqfwld 89
Cdd:cd07722   19 NTYLV--GTGKRRILIDTGegrpSYIPLLKSVLDSEGNAtISDILLTHWHHDHVGGLPDVLDLLRGPSPRVYK------- 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515955084  90 miqeVSARYGFPIPQPVKVDQW-LEGGEVLKLGEDEFEVRFAPGHTPGHVIFYNKNHGLLWTGD-VLFKGS 158
Cdd:cd07722   90 ----FPRPEEDEDPDEDGGDIHdLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGDcVLGHGT 156
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 14-153 1.13e-07

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 50.66  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  14 QNCSLVWDSETKeaVLIDAGGDASVLKKEVEALGLKVKALWLTHGHLDHAGAVGELAKEW---SVPVIGPHkedqfwlDM 90
Cdd:COG1235   35 RSSILVEADGTR--LLIDAGPDLREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYgpnPIPVYATP-------GT 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515955084  91 IQEVSARYG-FPIPQPVKVD-QWLEGGEVLKLGedEFEVRFAPG-HTPGHVIFY---NKNHGLLWTGDV 153
Cdd:COG1235  106 LEALERRFPyLFAPYPGKLEfHEIEPGEPFEIG--GLTVTPFPVpHDAGDPVGYrieDGGKKLAYATDT 172
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 26-152 1.78e-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: 50.24  E-value: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  26 EAVLIDAGGD------ASVLKKEVEALGL-KVKALWLTHGHLDHAGAVGELAKEWSVPVI--GPHKEDQFWLDMIQEVSA 96
Cdd:COG2333   22 KTILIDTGPRpsfdagERVVLPYLRALGIrRLDLLVLTHPDADHIGGLAAVLEAFPVGRVlvSGPPDTSETYERLLEALK 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515955084  97 RYGFPIpqpvkvdQWLEGGEVLKLGEDEFEVrFAPGHTPGH----------VIFYNKNHGLLWTGD 152
Cdd:COG2333  102 EKGIPV-------RPCRAGDTWQLGGVRFEV-LWPPEDLLEgsdennnslvLRLTYGGFSFLLTGD 159
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 44-178 2.15e-07

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: 49.91  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  44 EALGLK---VKALWLTHGHLDHAGAVGELAK-EWSVpvigpHKED-QFWLDMIqevsARYGFPIPQPVKVDQWLEGGEVL 118
Cdd:cd07729   80 ARLGLDpedIDYVILSHLHFDHAGGLDLFPNaTIIV-----QRAElEYATGPD----PLAAGYYEDVLALDDDLPGGRVR 150

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084 119 KLGEDE-----FEVRFAPGHTPGH--VIFYNKNHGLLWTGDVL-FKGSIGRTDFPRGNHD--QLIESIKR 178
Cdd:cd07729  151 LVDGDYdlfpgVTLIPTPGHTPGHqsVLVRLPEGTVLLAGDAAyTYENLEEGRPPGINYDpeAALASLER 220
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-136 3.20e-07

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


Pssm-ID: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 49.50  E-value: 3.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  28 VLIDAGGD--ASVLKKEVEALGLK---VKALWLTHGHLDHAGAVGELAKEWSVPVIG------------PHKEDQFWLDm 90
Cdd:cd16314   34 ILIDGGTDkaAPLIEANIRALGFRpedVRYIVSSHEHFDHAGGIARLQRATGAPVVArepaattlergrSDRSDPQFLV- 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 515955084  91 iqevsaryGFPIPqPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPG 136
Cdd:cd16314  113 --------VEKFP-PVASVQRIGDGEVLRVGPLALTAHATPGHTPG 149
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 15-122 3.76e-07

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


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 48.03  E-value: 3.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  15 NCSLVwdSETKEAVLIDAGGDASVLKKEVEALGLK---VKALWLTHGHLDHAGAVGELAKEWSVPVIGPHKedqfwldmi 91
Cdd:cd07733   10 NCTYL--ETEDGKLLIDAGLSGRKITGRLAEIGRDpedIDAILVTHEHADHIKGLGVLARKYNVPIYATAG--------- 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 515955084  92 qevSARYGFPIPQPVKVDQ--WLEGGEVLKLGE 122
Cdd:cd07733   79 ---TLRAMERKVGLIDVDQkqIFEPGETFSIGD 108
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 28-150 5.17e-07

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: 48.71  E-value: 5.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  28 VLIDAGGDAS--VLKKEVEALGLK---VKALWLTHGHLDHAGAVGELAKEWSVPVI-GPHKEDQFWLDMIQEVSARY-GF 100
Cdd:cd16313   34 ILIDGGFPKSpeQIAASIRQLGFKledVKYILSSHDHWDHAGGIAALQKLTGAQVLaSPATVAVLRSGSMGKDDPQFgGL 113

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 515955084 101 PIPQPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPGhvifynknhGLLWT 150
Cdd:cd16313  114 TPMPPVASVRAVRDGEVVKLGPLAVTAHATPGHTTG---------GTSWT 154
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-136 1.49e-06

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


Pssm-ID: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 47.67  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  28 VLIDAG--GDASVLKKEVEALGLK---VKALWLTHGHLDHAGAVGELAKEWSVPVIG------------PHKED-QFWLD 89
Cdd:cd16312   34 VLLDGAlpQSAPLIIANIEALGFRiedVKLILNSHAHWDHAGGIAALQKASGATVAAsahgaqvlqsgtNGKDDpQYQAK 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 515955084  90 MIQEVsarygfpiPQPVKVDQWLEGgEVLKLGEDEFEVRFAPGHTPG 136
Cdd:cd16312  114 PVVHV--------AKVAKVKEVGEG-DTLKVGPLRLTAHMTPGHTPG 151
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
7-152 1.49e-06

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 47.50  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084   7 VPVTAFAQNCSLVWDSETKeaVLIDAGGDASVLKKEVEALGLKVKALWLTHGHLDHAGAVGELAKEWS-------VPVIG 79
Cdd:COG1234   12 VPTPGRATSSYLLEAGGER--LLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSlagrekpLTIYG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  80 PHKEDQFWLDMIQEVSARYGFPIpqpvKVdQWLEGGEVLKLGedEFEVRFAPG-HT----------PGHVIFYnknhgll 148
Cdd:COG1234   90 PPGTKEFLEALLKASGTDLDFPL----EF-HEIEPGEVFEIG--GFTVTAFPLdHPvpaygyrfeePGRSLVY------- 155


                 ....
gi 515955084 149 wTGD 152
Cdd:COG1234  156 -SGD 158
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 49-173 1.52e-06

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


Pssm-ID: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 46.84  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  49 KVKALWLTHGHLDHAGAVGELAKEWSVpVIGphkEDQFWLDMIQEVSARYGFPIPQPVKVdqwLEGGEVLKLGedEFEVR 128
Cdd:cd07732   75 SVDAVLLSHAHLDHYGLLNYLRPDIPV-YMG---EATKRILKALLPFFGEGDPVPRNIRV---FESGKSFTIG--DFTVT 145

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515955084 129 F------APG------HTPGHVIFYnknhgllwTGDVLFKGSIGRT-----DFPRGNHDQLI 173
Cdd:cd07732  146 PylvdhsAPGayafliEAPGKRIFY--------TGDFRFHGRKPELteafvEKAPKNIDVLL 199
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 15-196 2.19e-06

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: 46.42  E-value: 2.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  15 NCSLVWDSETKeaVLIDAGG--DASVLKKEVEALGLK---VKALWLTHGHLDHAGAVG--ELAKewsvpvigphkedqfW 87
Cdd:cd07711   23 TVTLIKDGGKN--ILVDTGTpwDRDLLLKALAEHGLSpedIDYVVLTHGHPDHIGNLNlfPNAT---------------V 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  88 LDMIQEVSARYGFpipqpvkvDQWLEGGEVLKlgEDEFEVRFAPGHTPGHVIF--YNKNHGL-LWTGDvLFKGSIG---R 161
Cdd:cd07711   86 IVGWDICGDSYDD--------HSLEEGDGYEI--DENVEVIPTPGHTPEDVSVlvETEKKGTvAVAGD-LFEREEDledP 154

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 515955084 162 TDFPRGNHD--QLIESIKReCFSLPDdtqFI-SGHGPM 196
Cdd:cd07711  155 ILWDPLSEDpeLQEESRKR-ILALAD---WIiPGHGPP 188
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 25-118 5.89e-06

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 44.82  E-value: 5.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  25 KEAVLIDAGGDASVLKKEV----EALG-LKVKALWLTHGHLDHAGAVGELAKEWSVPVI---GPHKEDQFWLDMIQEVsA 96
Cdd:cd07731   19 GKTILIDTGPRDSFGEDVVvpylKARGiKKLDYLILTHPDADHIGGLDAVLKNFPVKEVympGVTHTTKTYEDLLDAI-K 97

                         90       100
                 ....*....|....*....|....*
gi 515955084  97 RYGFPIPQPVKVDQWLEGG---EVL 118
Cdd:cd07731   98 EKGIPVTPCKAGDRWQLGGvsfEVL 122
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-136 1.14e-05

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


Pssm-ID: 293865  Cd Length: 255  Bit Score: 44.74  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  28 VLIDAGGDASV--LKKEVEALGLK---VKALWLTHGHLDHAGAVGELAKEW---------SVPVI-GPHKEDQFWLDmiq 92
Cdd:cd16307   34 ILINSNLESSVpqIKASIEKLGFKfsdTKILLISHAHFDHAAGSALIKREThakymvmdgDVDVVeSGGKSDFFYGN--- 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 515955084  93 EVSARYgfpipQPVKVDQWLEGGEVLKLGEDEFEVRFAPGHTPG 136
Cdd:cd16307  111 DPSTYF-----PPAHVDKVLHDGEQVELGGTVLTAHLTAGHTKG 149
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 9-163 1.51e-05

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 44.79  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084   9 VTAfaqNCSLVWDSETKeaVLIDAGGDASVLKKEVEALGL---KVKALWLTHGHLDHAGAVGELAKE-WSVPVIGPH--K 82
Cdd:COG1236   12 VTG---SCYLLETGGTR--ILIDCGLFQGGKERNWPPFPFrpsDVDAVVLTHAHLDHSGALPLLVKEgFRGPIYATPatA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  83 E--DQFWLDM--IQEVSARYGfPIPQPVKVDQWLEGGEVLKLGE----DEFEVRFAP-GHTPG--HVifynknhgLLWTG 151
Cdd:COG1236   87 DlaRILLGDSakIQEEEAEAE-PLYTEEDAERALELFQTVDYGEpfeiGGVRVTFHPaGHILGsaQV--------ELEVG 157

                        170
                 ....*....|....
gi 515955084 152 D--VLFKGSIGRTD 163
Cdd:COG1236  158 GkrIVFSGDYGRED 171
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 25-153 1.78e-05

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


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 44.02  E-value: 1.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  25 KEAVLIDAGGD---ASVLKKEVEALGL-KVKALWLTHGHLDHAGAVGELAKEWS-VPVIGPHKedqfWLDMIQEvsarYG 99
Cdd:cd07709   40 EKTALIDTVKEpffDEFLENLEEVIDPrKIDYIVVNHQEPDHSGSLPELLELAPnAKIVCSKK----AARFLKH----FY 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515955084 100 FPIPQPVKVdqwLEGGEVLKLGEDEFEVRFAPG-HTPGHVIFYNKNHGLLWTGDV 153
Cdd:cd07709  112 PGIDERFVV---VKDGDTLDLGKHTLKFIPAPMlHWPDTMVTYDPEDKILFSGDA 163
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 2-157 2.27e-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) 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: 43.64  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084   2 LQVKIV---PVTAFAQNCSLVwdSETKEAVLIDAG---GDASVLKKEVEALGLKVKALWLTHGHLDHAGAVGELAKEW-S 74
Cdd:cd07739    1 LQVDVFtapEISSFPVTSTLI--YGETEAVLVDAQftrADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAFpD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  75 VPVI------------GPHKEDQFWLDMIQEVSARygFPIPQPVKvdqwlegGEVLKLGEDEFEVRfAPGHTPGHvifyn 142
Cdd:cd07739   79 AKVVatpavvahikaqLEPKLAFWGPLLGGNAPAR--LVVPEPLD-------GDTLTLEGHPLEIV-GVGGGDTD----- 143

                        170       180
                 ....*....|....*....|...
gi 515955084 143 kNHGLLW--------TGDVLFKG 157
Cdd:cd07739  144 -DTTYLWipslktvvAGDVVYNG 165
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 9-163 7.05e-05

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 42.06  E-value: 7.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084   9 VTAfaqNCSLVwdsETKEA-VLIDAG---GDASVLKKEVEALGL---KVKALWLTHGHLDHAGAVGELAKE-WSVPVIG- 79
Cdd:cd16295   10 VTG---SCYLL---ETGGKrILLDCGlfqGGKELEELNNEPFPFdpkEIDAVILTHAHLDHSGRLPLLVKEgFRGPIYAt 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  80 -PHKE--DQFWLDM--IQEVSARYGFPIP--------------QPVKVDQWLEggevlkLGEDeFEVRFAP-GHTPG--H 137
Cdd:cd16295   84 pATKDlaELLLLDSakIQEEEAEHPPAEPlyteedvekalkhfRPVEYGEPFE------IGPG-VKVTFYDaGHILGsaS 156

                        170       180
                 ....*....|....*....|....*..
gi 515955084 138 V-IFYNKNHGLLWTGDvlfkgsIGRTD 163
Cdd:cd16295  157 VeLEIGGGKRILFSGD------LGRKN 177
NorV COG0426
Flavorubredoxin [Energy production and conversion];
26-163 7.92e-05

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 42.51  E-value: 7.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  26 EAVLIDAGGD--ASVLKKEVEAL--GLKVKALWLTHGHLDHAGAVGELAKEWS-VPVIGPHKedqfWLDMIQEVSARYGF 100
Cdd:COG0426   43 KTALIDTVGEsfFEEFLENLSKVidPKKIDYIIVNHQEPDHSGSLPELLELAPnAKIVCSKK----AARFLPHFYGIPDF 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515955084 101 PIpQPVKvdqwleGGEVLKLGEDEFEVRFAPG-HTPGHVIFYNKNHGLLWTGDvLFkGSIGRTD 163
Cdd:COG0426  119 RF-IVVK------EGDTLDLGGHTLQFIPAPMlHWPDTMFTYDPEDKILFSGD-AF-GSHGASD 173
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 26-194 1.70e-04

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


Pssm-ID: 293860  Cd Length: 212  Bit Score: 41.08  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  26 EAVLIDAGGDASVLKKEV----EALGLKVKALWLTHGHLDHAGAVGELAKEwSVPVIGPHkedqfwldMIQEVSARYGFP 101
Cdd:cd16302   37 EAVVFDTPTNDSQSEELIdwieNSLKAKVKAVVPTHFHDDCLGGLKAFHRR-GIPSYANQ--------KTIALAKEKGLP 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084 102 IPQPVKVDQwleggEVLKLGEDEFEVR-FAPGHTPGHVIFYnknhglLWTGDVLFKG----SIGRTdfpRGN-------- 168
Cdd:cd16302  108 VPQHGFSDS-----LTLKLGGKKIVCRyFGEGHTKDNIVVY------FPSEKVLFGGcmvkSLGAG---KGNledanvea 173

                        170       180
                 ....*....|....*....|....*.
gi 515955084 169 HDQLIESIKREcfsLPDDTQFISGHG 194
Cdd:cd16302  174 WPKTVEKVKAK---YPDVKIVIPGHG 196
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 15-156 2.01e-04

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


Pssm-ID: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 40.95  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  15 NCSLVwdsETKE-AVLIDAG---GDASVLKKEVEALGLK--VKALWLTHGHLDH---AGAVGELAKEWSVPVIGPHKedq 85
Cdd:cd07710   19 NMTFI---EGDTgLIIIDTLesaEAAKAALELFRKHTGDkpVKAIIYTHSHPDHfggAGGFVEEEDSGKVPIIAPEG--- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  86 FWLDMIQEV----------SAR-YGFPIP--QPVKVDQWL-------------------EGGEVLKLGEDEFEVRFAPGH 133
Cdd:cd07710   93 FMEEAVSENvlagnamsrrAAYqFGALLPkgEKGQVGAGLgpglstgtvgfipptititETGETLTIDGVELEFQHAPGE 172

                        170       180
                 ....*....|....*....|...
gi 515955084 134 TPGHVIFYNKNHGLLWTGDVLFK 156
Cdd:cd07710  173 APDEMMVWLPDYKVLFCADNVYH 195
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 23-81 4.56e-04

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 39.79  E-value: 4.56e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515955084  23 ETKEA-VLID---AGGDASVLKKEvealGLKVKALWLTHGHLDHAGAVGELAKEWSVPVIGPH 81
Cdd:PRK00685  14 ETGGKkILIDpfiTGNPLADLKPE----DVKVDYILLTHGHGDHLGDTVEIAKRTGATVIANA 72
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 13-80 6.52e-04

Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 39.04  E-value: 6.52e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515955084  13 AQNCSLVWDSEtkEAVLIDAGGDASVlkkEVEALGLK---VKALWLTHGHLDHAGAVGELAK-------EWSVPVIGP 80
Cdd:cd07719   17 AGPSTLVVVGG--RVYLVDAGSGVVR---RLAQAGLPlgdLDAVFLTHLHSDHVADLPALLLtawlagrKTPLPVYGP 89
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 16-152 7.52e-04

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: 38.78  E-value: 7.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  16 CSLVWDSETKeaVLIDAGGdaSVLKKEVEA--LGLKVKALWLTHGHLDHAGAVGELAKEW-------SVPVIGPhKEDQF 86
Cdd:cd16272   19 SYLLETGGTR--ILLDCGE--GTVYRLLKAgvDPDKLDAIFLSHFHLDHIGGLPTLLFARryggrkkPLTIYGP-KGIKE 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515955084  87 WLDMIQEVSARYgFPIPQPVKVDQWLEGGEVLKLGedEFEVRFAPG-HTPG--HVIFYNKNHGLLWTGD 152
Cdd:cd16272   94 FLEKLLNFPVEI-LPLGFPLEIEELEEGGEVLELG--DLKVEAFPVkHSVEslGYRIEAEGKSIVYSGD 159
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 55-154 1.03e-03

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 38.66  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  55 LTHGHLDHAG----AVGElakEWsVP------VIGPHKEDQFWLDMIQEVSARYGF------PIPQPVKVDQWLEGGEVL 118
Cdd:cd16277   69 CTHLHVDHVGwntrLVDG---RW-VPtfpnarYLFSRAEYDHWSSPDAGGPPNRGVfedsvlPVIEAGLADLVDDDHEIL 144

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 515955084 119 klgeDEFEVRFAPGHTPGHVIFYNKNHG--LLWTGDVL 154
Cdd:cd16277  145 ----DGIRLEPTPGHTPGHVSVELESGGerALFTGDVM 178
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 28-133 1.06e-03

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: 38.44  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084   28 VLIDAGGD----ASVLKKEVEALGLKVKALWLTHGHLDHAGAVGELAKEWSVPVIGPhkedqfwLDMIQEVSARYGFPIP 103
Cdd:pfam12706   3 ILIDPGPDlrqqALPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAP-------LGVLAHLRRNFPYLFL 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 515955084  104 QPVKVDQW--LEGGEVLKLGEDEFEVRFAPGH 133
Cdd:pfam12706  76 LEHYGVRVheIDWGESFTVGDGGLTVTATPAR 107
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 24-151 1.38e-03

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


Pssm-ID: 293862 [Multi-domain]  Cd Length: 212  Bit Score: 38.42  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  24 TKEAVLIDAGGDASVLKKEV----EALGLKVKALWLTHGHLDHAGAVGELAKEwSVPVIGPHKEDQFwldmiqevSARYG 99
Cdd:cd16304   34 SKGVVLIDTPWDDEQTEELLdwikKKLKKPVTLAIVTHAHDDRIGGIKALQKR-GIPVYSTKLTAQL--------AKKQG 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515955084 100 FPIPQPVkvdqwLEGGEVLKLGEDEFEVRFA-PGHTPGHVIFYNKNHGLLWTG 151
Cdd:cd16304  105 YPSPDGI-----LKDDTTLKFGNTKIETFYPgEGHTADNIVVWLPQSKILFGG 152
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
16-62 1.96e-03

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 38.40  E-value: 1.96e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515955084  16 CSLVWDSETKEAVLIDAGGDASVLKKEVEALGLK---------VKALWLTHGHLDH 62
Cdd:COG5212   30 TYLLRPLGSDDYVLLDAGTVVSGLELAEQKGAFKgrqgyvlehIKGYLISHAHLDH 85
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 25-139 4.73e-03

metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. Includes chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1.


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 36.88  E-value: 4.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  25 KEAVLIDAG-GD---ASVLKKEVEALGLKVKALWLTHGHLDHAGAVGELAKEwSVPVigphkedqFWLDMIQEVSARYGF 100
Cdd:cd16285   35 KGLVLIDTPwTEaqtATLLDWIEKKLGKPVTAAISTHSHDDRTGGIKALNAR-GIPT--------YATALTNELAKKEGK 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 515955084 101 PIPQPVkvdqwLEGGEVLKLGedEFEVRF-APGHTPGHVI 139
Cdd:cd16285  106 PVPTHS-----LKGALTLGFG--PLEVFYpGPGHTPDNIV 138
SPM-1-like_MBL-B1-B2-like cd16286
Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; ...
 56-154 7.03e-03

Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; MBL-fold metallo-hydrolase domain; SPM-1 was first identified in a Pseudomonas aeruginosa strain from a paediatric leukaemia patient and is a major clinical problem. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs are most closely related to each other. SPM-1 appears to be a hybrid B1/B2 MBL.


Pssm-ID: 293844 [Multi-domain]  Cd Length: 236  Bit Score: 36.36  E-value: 7.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515955084  56 THGHLDHAGAVGELaKEWSVPVIGP----------HKEDQFWL-------DMIQEVSARYGFPIPQPVKVDQwlegGEVL 118
Cdd:cd16286   72 THFHLDGTGGNEAL-KKRGIPTWGSdltkqlllerGKADRIKAaeflkneDLKRRIESSPPVPPDNVFDLKE----GKVF 146

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 515955084 119 KLGEDEFEVRF-APGHTPGHVIFYNKNHGLLWTGDVL 154
Cdd:cd16286  147 SFGNELVEVSFpGPAHAPDNVVVYFPERKILFGGCMI 183
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 28-80 7.10e-03

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293799  Cd Length: 269  Bit Score: 36.45  E-value: 7.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515955084  28 VLIDAGGDaSVLKKEVEALGL---KVKALWLTHGHLDHAGAVGELAKEWS-VPVIGP 80
Cdd:cd07713   32 ILFDTGQS-GVLLHNAKKLGIdlsDIDAVVLSHGHYDHTGGLKALLELNPkAPVYAH 87
 
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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