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Conserved domains on  [gi|890048396|emb|CLN97665|]
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hydrolase [Mycobacterium tuberculosis]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 14427473)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme that may have substrate towards phosphotriesters, esters, and/or lactones

CATH:  3.60.15.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  17597585|12177301|11471246|11513844
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 23-197 1.22e-76

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: 230.46  E-value: 1.22e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  23 ASVLLADNPGLLTLDGTNTWVLRGPlsDELVVVDPGPDDDEHLARVAAL---GRIALVLISHRHGDHTSGIDKLVALTGA 99
Cdd:cd16278    2 VRRVLAPNPSPMTLDGTNTYLLGAP--DGVVVIDPGPDDPAHLDALLAAlggGRVSAILVTHTHRDHSPGAARLAERTGA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396 100 PVRAADP------QFLRRDGETLTDGEVIDVAGLTITVLATPGHTADSLSFVL--DDAVLTADTVLGCGTTVIDKEDGSL 171
Cdd:cd16278   80 PVRAFGPhraggqDTDFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALedEGALFTGDHVMGWSTTVIAPPDGDL 159

                        170       180
                 ....*....|....*....|....*.
gi 890048396 172 ADYLESLHRLRGLGRRTVLPGHGPDL 197
Cdd:cd16278  160 GDYLASLERLLALDDRLLLPGHGPPI 185
BLACT_WH super family cl38958
Beta-lactamase associated winged helix domain; This winged helix domain is found at the ...
 230-264 2.92e-03

Beta-lactamase associated winged helix domain; This winged helix domain is found at the C-terminus of some beta lactamase enzymes.


The actual alignment was detected with superfamily member pfam17778:

Pssm-ID: 407650  Cd Length: 46  Bit Score: 34.90  E-value: 2.92e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 890048396  230 TVREVVEHVYLDVDEKLWNAAEWSVQAQLDYLRTR 264
Cdd:pfam17778   1 TAMELVKVIYKDVPESLHPAAERGVLAHLEKLEAE 35
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 23-197 1.22e-76

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: 230.46  E-value: 1.22e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  23 ASVLLADNPGLLTLDGTNTWVLRGPlsDELVVVDPGPDDDEHLARVAAL---GRIALVLISHRHGDHTSGIDKLVALTGA 99
Cdd:cd16278    2 VRRVLAPNPSPMTLDGTNTYLLGAP--DGVVVIDPGPDDPAHLDALLAAlggGRVSAILVTHTHRDHSPGAARLAERTGA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396 100 PVRAADP------QFLRRDGETLTDGEVIDVAGLTITVLATPGHTADSLSFVL--DDAVLTADTVLGCGTTVIDKEDGSL 171
Cdd:cd16278   80 PVRAFGPhraggqDTDFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALedEGALFTGDHVMGWSTTVIAPPDGDL 159

                        170       180
                 ....*....|....*....|....*.
gi 890048396 172 ADYLESLHRLRGLGRRTVLPGHGPDL 197
Cdd:cd16278  160 GDYLASLERLLALDDRLLLPGHGPPI 185
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 31-195 3.66e-37

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: 130.58  E-value: 3.66e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  31 PGLLTLDGTNTWVLRGPlsDELVVVDPGPDDDEH---LARVAALG-RIALVLISHRHGDHTSGIDKLVALTGAPVRA--- 103
Cdd:COG0491    7 GTPGAGLGVNSYLIVGG--DGAVLIDTGLGPADAealLAALAALGlDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAhaa 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396 104 --------ADPQFLRRDG----ETLTDGEVIDVAGLTITVLATPGHTADSLSFVLDD--AVLTADTVLGCGTTVIDKEDG 169
Cdd:COG0491   85 eaealeapAAGALFGREPvppdRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDekVLFTGDALFSGGVGRPDLPDG 164

                        170       180
                 ....*....|....*....|....*.
gi 890048396 170 SLADYLESLHRLRGLGRRTVLPGHGP 195
Cdd:COG0491  165 DLAQWLASLERLLALPPDLVIPGHGP 190
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 40-193 4.41e-26

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: 100.32  E-value: 4.41e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396    40 NTWVLRGPlsDELVVVDPGPDDDEH-LARVAALG--RIALVLISHRHGDHTSGIDKLVALTGAPVRA------------- 103
Cdd:smart00849   1 NSYLVRDD--GGAILIDTGPGEAEDlLAELKKLGpkKIDAIILTHGHPDHIGGLPELLEAPGAPVYApegtaellkdlla 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396   104 -----ADPQFLRRDGETLTDGEVIDVAGLTITVLATPGHTADSLSFVLDD--AVLTADTVL--GCGTTVIDKEDGSLADY 174
Cdd:smart00849  79 llgelGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEgkILFTGDLLFagGDGRTLVDGGDAAASDA 158

                          170
                   ....*....|....*....
gi 890048396   175 LESLHRLRGLGRRTVLPGH 193
Cdd:smart00849 159 LESLLKLLKLLPKLVVPGH 177
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 42-193 2.94e-22

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


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 92.21  E-value: 2.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396   42 WVLRGPlSDELVVVDPGpDDDEHLARVAALG-RIALVLISHRHGDHTSGIDKLVALTGAPVRAADPQFLRRDGETLTDGE 120
Cdd:TIGR03413  13 WLLHDP-DGQAAVVDPG-EAEPVLDALEARGlTLTAILLTHHHHDHVGGVAELLEAFPAPVYGPAEERIPGITHPVKDGD 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 890048396  121 VIDVAGLTITVLATPGHTADSLSFVLDD--AVLTADTV--LGCGTTVidkeDGSLADYLESLHRLRGLGRRT-VLPGH 193
Cdd:TIGR03413  91 TVTLGGLEFEVLAVPGHTLGHIAYYLPDspALFCGDTLfsAGCGRLF----EGTPEQMYDSLQRLAALPDDTlVYCAH 164
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
34-193 3.67e-12

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 63.54  E-value: 3.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396   34 LTLDGTNTWVLRGPlsDELVVVDPGPDDDEhlARVAALGRIAL-------VLISHRHGDHTSGIDKLVALTGAPVRAAD- 105
Cdd:pfam00753   1 LGPGQVNSYLIEGG--GGAVLIDTGGSAEA--ALLLLLAALGLgpkdidaVILTHGHFDHIGGLGELAEATDVPVIVVAe 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  106 ----------------------PQFLRRDGETLTDGEVIDVAGLTITVLATPGHTADSLSFVLDDA--VLTADTVLGCGT 161
Cdd:pfam00753  77 earelldeelglaasrlglpgpPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGkvLFTGDLLFAGEI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 890048396  162 TVIDKE--------DGSLADYLESLHRLRGLGRRTVLPGH 193
Cdd:pfam00753 157 GRLDLPlggllvlhPSSAESSLESLLKLAKLKAAVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 54-193 3.35e-07

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 50.61  E-value: 3.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  54 VVDPgpddDEHLARVAALGR----IALVLISHRHGDHTSGIDKLVALTGAPV--RAADPQFLRRDGETLTDGEVIDVAGL 127
Cdd:PLN02398 102 VVDP----SEAVPVIDALSRknrnLTYILNTHHHYDHTGGNLELKARYGAKVigSAVDKDRIPGIDIVLKDGDKWMFAGH 177

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 890048396 128 TITVLATPGHTADSLSFVL--DDAVLTADTV--LGCGTTVidkeDGSLADYLESLHRLRGLGRRT-VLPGH 193
Cdd:PLN02398 178 EVLVMETPGHTRGHISFYFpgSGAIFTGDTLfsLSCGKLF----EGTPEQMLSSLQKIISLPDDTnIYCGH 244
BLACT_WH pfam17778
Beta-lactamase associated winged helix domain; This winged helix domain is found at the ...
 230-264 2.92e-03

Beta-lactamase associated winged helix domain; This winged helix domain is found at the C-terminus of some beta lactamase enzymes.


Pssm-ID: 407650  Cd Length: 46  Bit Score: 34.90  E-value: 2.92e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 890048396  230 TVREVVEHVYLDVDEKLWNAAEWSVQAQLDYLRTR 264
Cdd:pfam17778   1 TAMELVKVIYKDVPESLHPAAERGVLAHLEKLEAE 35
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 23-197 1.22e-76

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: 230.46  E-value: 1.22e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  23 ASVLLADNPGLLTLDGTNTWVLRGPlsDELVVVDPGPDDDEHLARVAAL---GRIALVLISHRHGDHTSGIDKLVALTGA 99
Cdd:cd16278    2 VRRVLAPNPSPMTLDGTNTYLLGAP--DGVVVIDPGPDDPAHLDALLAAlggGRVSAILVTHTHRDHSPGAARLAERTGA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396 100 PVRAADP------QFLRRDGETLTDGEVIDVAGLTITVLATPGHTADSLSFVL--DDAVLTADTVLGCGTTVIDKEDGSL 171
Cdd:cd16278   80 PVRAFGPhraggqDTDFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALedEGALFTGDHVMGWSTTVIAPPDGDL 159

                        170       180
                 ....*....|....*....|....*.
gi 890048396 172 ADYLESLHRLRGLGRRTVLPGHGPDL 197
Cdd:cd16278  160 GDYLASLERLLALDDRLLLPGHGPPI 185
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 27-195 4.32e-40

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: 137.28  E-value: 4.32e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  27 LADNPGLLTLDGTNTWVL-RGPlsdELVVVDPG---PDDDEHLARV---AALGRIALVLISHRHGDHTSGIDKLVAL-TG 98
Cdd:cd07722    6 LGQNPGPFTLQGTNTYLVgTGK---RRILIDTGegrPSYIPLLKSVldsEGNATISDILLTHWHHDHVGGLPDVLDLlRG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  99 APVRA---------ADPQFLRRDGETLTDGEVIDVAGLTITVLATPGHTADSLSFVL--DDAVLTADTVLGCGTTVIdkE 167
Cdd:cd07722   83 PSPRVykfprpeedEDPDEDGGDIHDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLeeENALFTGDCVLGHGTAVF--E 160

                        170       180
                 ....*....|....*....|....*...
gi 890048396 168 DgsLADYLESLHRLRGLGRRTVLPGHGP 195
Cdd:cd07722  161 D--LAAYMASLKKLLSLGPGRIYPGHGP 186
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 31-195 3.66e-37

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: 130.58  E-value: 3.66e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  31 PGLLTLDGTNTWVLRGPlsDELVVVDPGPDDDEH---LARVAALG-RIALVLISHRHGDHTSGIDKLVALTGAPVRA--- 103
Cdd:COG0491    7 GTPGAGLGVNSYLIVGG--DGAVLIDTGLGPADAealLAALAALGlDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAhaa 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396 104 --------ADPQFLRRDG----ETLTDGEVIDVAGLTITVLATPGHTADSLSFVLDD--AVLTADTVLGCGTTVIDKEDG 169
Cdd:COG0491   85 eaealeapAAGALFGREPvppdRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDekVLFTGDALFSGGVGRPDLPDG 164

                        170       180
                 ....*....|....*....|....*.
gi 890048396 170 SLADYLESLHRLRGLGRRTVLPGHGP 195
Cdd:COG0491  165 DLAQWLASLERLLALPPDLVIPGHGP 190
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 42-193 1.82e-32

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: 116.79  E-value: 1.82e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  42 WVLRGPLSDELVVVDPGpDDDEHLARVAALG-RIALVLISHRHGDHTSGIDKLVALTG-APVRAADPQFLRRDGETLTDG 119
Cdd:cd07723   12 YLIVDEATGEAAVVDPG-EAEPVLAALEKNGlTLTAILTTHHHWDHTGGNAELKALFPdAPVYGPAEDRIPGLDHPVKDG 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 890048396 120 EVIDVAGLTITVLATPGHTADSLSFVLDD--AVLTADT--VLGCGTTVidkeDGSLADYLESLHRLRGLGRRT-VLPGH 193
Cdd:cd07723   91 DEIKLGGLEVKVLHTPGHTLGHICYYVPDepALFTGDTlfSGGCGRFF----EGTAEQMYASLQKLLALPDDTlVYCGH 165
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 38-193 1.20e-28

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: 107.37  E-value: 1.20e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  38 GTNTWVLRGPlSDELVVVDPGPDDDEHLARV--AALGRIALVLISHRHGDHTSGIDKLVALTGAPVRA--ADPQFLRRDG 113
Cdd:cd06262    9 QTNCYLVSDE-EGEAILIDPGAGALEKILEAieELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIheADAELLEDPE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396 114 E-----------------TLTDGEVIDVAGLTITVLATPGHTADSLSFVLDD--AVLTADTVLGCGTTVIDKEDGSLADY 174
Cdd:cd06262   88 LnlaffgggplpppepdiLLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEegVLFTGDTLFAGSIGRTDLPGGDPEQL 167

                        170       180
                 ....*....|....*....|.
gi 890048396 175 LESLHRLRGL--GRRTVLPGH 193
Cdd:cd06262  168 IESIKKLLLLlpDDTVVYPGH 188
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 49-193 7.08e-27

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: 102.23  E-value: 7.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  49 SDELVVVDPGPDDDEHLARVAALG-RIALVLISHRHGDHTSGIDKLVALTGAPV-----RAADPQFLRRDGETLTDGEVI 122
Cdd:cd16275   22 TREAAVVDPAWDIEKILAKLNELGlTLTGILLTHSHFDHVNLVEPLLAKYDAPVymskeEIDYYGFRCPNLIPLEDGDTI 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 890048396 123 DVAGLTITVLATPGHTADSLSFVLDDAVLTADTVL--GCGTTviDKEDGSLADYLESLHRLRGL--GRRTVLPGH 193
Cdd:cd16275  102 KIGDTEITCLLTPGHTPGSMCYLLGDSLFTGDTLFieGCGRC--DLPGGDPEEMYESLQRLKKLppPNTRVYPGH 174
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 40-193 4.41e-26

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: 100.32  E-value: 4.41e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396    40 NTWVLRGPlsDELVVVDPGPDDDEH-LARVAALG--RIALVLISHRHGDHTSGIDKLVALTGAPVRA------------- 103
Cdd:smart00849   1 NSYLVRDD--GGAILIDTGPGEAEDlLAELKKLGpkKIDAIILTHGHPDHIGGLPELLEAPGAPVYApegtaellkdlla 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396   104 -----ADPQFLRRDGETLTDGEVIDVAGLTITVLATPGHTADSLSFVLDD--AVLTADTVL--GCGTTVIDKEDGSLADY 174
Cdd:smart00849  79 llgelGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEgkILFTGDLLFagGDGRTLVDGGDAAASDA 158

                          170
                   ....*....|....*....
gi 890048396   175 LESLHRLRGLGRRTVLPGH 193
Cdd:smart00849 159 LESLLKLLKLLPKLVVPGH 177
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 38-194 2.50e-25

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: 98.24  E-value: 2.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  38 GTNTWVLRGPLSDELVVVDPGPDD-DEHLARVAALG-RIALVLISHRHGDHTSGIDKLVALTGAPV---RAADPQFlrrD 112
Cdd:cd07724   11 GTLSYLVGDPETGEAAVIDPVRDSvDRYLDLAAELGlKITYVLETHVHADHVSGARELAERTGAPIvigEGAPASF---F 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396 113 GETLTDGEVIDVAGLTITVLATPGHTADSLSFVLDD--AVLTADTVL--GCGTTVIDKEDGSLADYL-ESLHRLRGL--G 185
Cdd:cd07724   88 DRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDpdAVFTGDTLFvgDVGRPDLPGEAEGLARQLyDSLQRKLLLlpD 167


                 ....*....
gi 890048396 186 RRTVLPGHG 194
Cdd:cd07724  168 ETLVYPGHD 176
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 39-194 2.88e-22

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: 90.44  E-value: 2.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  39 TNTWVLRGPlsDELVVVDPGPDDDE-------HLARV-AALGRIALVLISHRHGDHTSGIDKLVALTGAPVRAADPqflr 110
Cdd:cd07725   15 VNVYLLRDG--DETTLIDTGLATEEdaealweGLKELgLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGATVYILDV---- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396 111 rdgETLTDGEVIDVAGLTITVLATPGHTADSLSFVLDDA--VLTADTVLG----CGTTVIDKEDGSLADYLESLHRLRGL 184
Cdd:cd07725   89 ---TPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRreLFVGDAVLPkitpNVSLWAVRVEDPLGAYLESLDKLEKL 165

                        170
                 ....*....|
gi 890048396 185 GRRTVLPGHG 194
Cdd:cd07725  166 DVDLAYPGHG 175
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 42-193 2.94e-22

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


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 92.21  E-value: 2.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396   42 WVLRGPlSDELVVVDPGpDDDEHLARVAALG-RIALVLISHRHGDHTSGIDKLVALTGAPVRAADPQFLRRDGETLTDGE 120
Cdd:TIGR03413  13 WLLHDP-DGQAAVVDPG-EAEPVLDALEARGlTLTAILLTHHHHDHVGGVAELLEAFPAPVYGPAEERIPGITHPVKDGD 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 890048396  121 VIDVAGLTITVLATPGHTADSLSFVLDD--AVLTADTV--LGCGTTVidkeDGSLADYLESLHRLRGLGRRT-VLPGH 193
Cdd:TIGR03413  91 TVTLGGLEFEVLAVPGHTLGHIAYYLPDspALFCGDTLfsAGCGRLF----EGTPEQMYDSLQRLAALPDDTlVYCAH 164
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 33-194 3.60e-19

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: 82.65  E-value: 3.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  33 LLTLDGTNTWVLRGPlsDELVVVDPG-PDDDEHLARVAA-----LGRIALVLISHRHGDHTSGIDKLVALTGAPV----- 101
Cdd:cd07721    5 LPLLPPVNAYLIEDD--DGLTLIDTGlPGSAKRILKALRelglsPKDIRRILLTHGHIDHIGSLAALKEAPGAPVyaher 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396 102 -----------------------RAADPQFLRRDGETLTDGEVIDVAGlTITVLATPGHTADSLSFVL--DDAVLTADTV 156
Cdd:cd07721   83 eapylegekpypppvrlgllgllSPLLPVKPVPVDRTLEDGDTLDLAG-GLRVIHTPGHTPGHISLYLeeDGVLIAGDAL 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 890048396 157 lgcgTTVIDKEDGS-------LADYLESLHRLRGLGRRTVLPGHG 194
Cdd:cd07721  162 ----VTVGGELVPPpppftwdMEEALESLRKLAELDPEVLAPGHG 202
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 40-195 7.47e-16

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: 73.92  E-value: 7.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  40 NTWVLRGPLSDELVVVDPGPDDDEHLARVAALG-RIALVLISHRHGDHTSGIDKLVALTGAPV---------RAADPQFL 109
Cdd:cd16322   12 NTYLVADEGGGEAVLVDPGDESEKLLARFGTTGlTLLYILLTHAHFDHVGGVADLRRHPGAPVylhpddlplYEAADLGA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396 110 RRDG----------ETLTDGEVIDVAGLTITVLATPGHTADSLSFVLDD--AVLTADtVLGCGTtvIDKEDGSLADY--- 174
Cdd:cd16322   92 KAFGlgieplpppdRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEegLLFSGD-LLFQGS--IGRTDLPGGDPkam 168

                        170       180
                 ....*....|....*....|..
gi 890048396 175 LESLHRLRGLGRRT-VLPGHGP 195
Cdd:cd16322  169 AASLRRLLTLPDETrVFPGHGP 190
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 37-193 4.60e-14

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: 68.42  E-value: 4.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  37 DGTNTWVLRGplSDELVVVDPG---PDDDEHLARVAALGriALVLISHRHGDHTSGI-------------DKLVALTGAP 100
Cdd:cd07712    7 DRVNIYLLRG--RDRALLIDTGlgiGDLKEYVRTLTDLP--LLVVATHGHFDHIGGLhefeevyvhpadaEILAAPDNFE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396 101 VRAADPQFLRRDGET----LTDGEVIDVAGLTITVLATPGHTADSLSFV-LDDAVLTADTVLGCGTTVIDKEDGSLADYL 175
Cdd:cd07712   83 TLTWDAATYSVPPAGptlpLRDGDVIDLGDRQLEVIHTPGHTPGSIALLdRANRLLFSGDVVYDGPLIMDLPHSDLDDYL 162

                        170       180
                 ....*....|....*....|
gi 890048396 176 ESLHRLRGLGR--RTVLPGH 193
Cdd:cd07712  163 ASLEKLSKLPDefDKVLPGH 182
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 40-195 5.50e-14

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: 68.75  E-value: 5.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  40 NTWVLRGPL-------------SDELVVVDPGPDD---DEHLARVAAL--GRIALVLISHRHGDHTSG------------ 89
Cdd:cd16282    1 GVYALIGPDgggfisnigfivgDDGVVVIDTGASPrlaRALLAAIRKVtdKPVRYVVNTHYHGDHTLGnaafadagapii 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  90 ----IDKLVALTGAPVRAADPQFLRRDGE---------TLTDGEVIDVAGLTITVLAT-PGHTADSLSFVLDDA--VLTA 153
Cdd:cd16282   81 ahenTREELAARGEAYLELMRRLGGDAMAgtelvlpdrTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEgvLFAG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 890048396 154 DTVLGCGTTVIDkeDGSLADYLESLHRLRGLGRRTVLPGHGP 195
Cdd:cd16282  161 DLVFNGRIPFLP--DGSLAGWIAALDRLLALDATVVVPGHGP 200
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 49-184 5.50e-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: 66.84  E-value: 5.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  49 SDELVVVDPG-PDDDEHL--ARVAALG----RIALVLISHRHGDHTSGIDKLVALTGAPV--RAADPQFLRRDGE----- 114
Cdd:cd16280   30 GDGLILIDALnNNEAADLivDGLEKLGldpaDIKYILITHGHGDHYGGAAYLKDLYGAKVvmSEADWDMMEEPPEegdnp 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396 115 ----------TLTDGEVIDVAGLTITVLATPGHTADSLSFVLD----DAVLTADTVLGCGTTVIDKEDgSLADYLESLHR 180
Cdd:cd16280  110 rwgppperdiVIKDGDTLTLGDTTITVYLTPGHTPGTLSLIFPvkdgGKTHRAGLWGGTGLNTGPNLE-RREQYIASLER 188


                 ....
gi 890048396 181 LRGL 184
Cdd:cd16280  189 FKKI 192
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-143 8.13e-13

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: 66.22  E-value: 8.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  49 SDELVVVDPGPDD--DEHLARVAALG----RIALVLISHRHGDHTSGIDKLVALTGAPVRA---------------ADPQ 107
Cdd:cd16315   30 DDGHVLIDSGTEEaaPLVLANIRKLGfdpkDVRWLLSSHEHFDHVGGLAALQRATGARVAAsaaaapvlesgkpapDDPQ 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 890048396 108 F--------LRRDGeTLTDGEVIDVAGLTITVLATPGHTADSLS 143
Cdd:cd16315  110 AglhepfppVRVDR-IVEDGDTVALGSLRLTAHATPGHTPGALS 152
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
34-193 3.67e-12

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 63.54  E-value: 3.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396   34 LTLDGTNTWVLRGPlsDELVVVDPGPDDDEhlARVAALGRIAL-------VLISHRHGDHTSGIDKLVALTGAPVRAAD- 105
Cdd:pfam00753   1 LGPGQVNSYLIEGG--GGAVLIDTGGSAEA--ALLLLLAALGLgpkdidaVILTHGHFDHIGGLGELAEATDVPVIVVAe 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  106 ----------------------PQFLRRDGETLTDGEVIDVAGLTITVLATPGHTADSLSFVLDDA--VLTADTVLGCGT 161
Cdd:pfam00753  77 earelldeelglaasrlglpgpPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGkvLFTGDLLFAGEI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 890048396  162 TVIDKE--------DGSLADYLESLHRLRGLGRRTVLPGH 193
Cdd:pfam00753 157 GRLDLPlggllvlhPSSAESSLESLLKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 41-193 1.19e-11

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 62.16  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  41 TWVLRGPL--------SDELVVVDPGPDDDEHLARVAALG----RIALVLISHRHGDHTSGIDKLVALTGA--------- 99
Cdd:cd07743    1 TYYIPGPTnigvyvfgDKEALLIDSGLDEDAGRKIRKILEelgwKLKAIINTHSHADHIGGNAYLQKKTGCkvyapkiek 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396 100 -----------------PVRAADPQFLRRDG----ETLTDGEVIdVAGLTITVLATPGHTADSLSFVLDDAVL-TADTVL 157
Cdd:cd07743   81 afienpllepsylggayPPKELRNKFLMAKPskvdDIIEEGELE-LGGVGLEIIPLPGHSFGQIGILTPDGVLfAGDALF 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 890048396 158 GCGttVIDKEDGSL----ADYLESLHRLRGLGRRTVLPGH 193
Cdd:cd07743  160 GEE--VLEKYGIPFlydvEEQLETLEKLEELDADYYVPGH 197
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 41-193 7.45e-11

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: 60.20  E-value: 7.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  41 TWVLRGPlsDELVVVDPGPDD--DEHLARVAALG----RIALVLISHRHGDHTSGIDKLV-ALTGAPV----RAA----D 105
Cdd:cd07726   18 SYLLDGE--GRPALIDTGPSSsvPRLLAALEALGiapeDVDYIILTHIHLDHAGGAGLLAeALPNAKVyvhpRGArhliD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396 106 P-------------QFLRRDGE----------TLTDGEVIDVAGLTITVLATPGHTADSLSFVLD--DAVLTADT----- 155
Cdd:cd07726   96 PsklwasaravygdEADRLGGEilpvpeerviVLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEesDGLFTGDAagvry 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 890048396 156 -----VLGCGTT--VIDkedgsLADYLESLHRLRGLGRRTVLPGH 193
Cdd:cd07726  176 peldvVGPPSTPppDFD-----PEAWLESLDRLLSLKPERIYLTH 215
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 53-200 2.99e-10

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: 59.11  E-value: 2.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  53 VVVDPGPDDDEHL--ARVAALG----RIALVLISHRHGDHTSGIDKLVALTGAPVRAA---------------DPQFLRR 111
Cdd:cd16313   34 ILIDGGFPKSPEQiaASIRQLGfkleDVKYILSSHDHWDHAGGIAALQKLTGAQVLASpatvavlrsgsmgkdDPQFGGL 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396 112 DG-------ETLTDGEVIDVAGLTITVLATPGHTADSLSFVLD--DAVLTADTVLGCGTTVIDKEDGS-------LADYL 175
Cdd:cd16313  114 TPmppvasvRAVRDGEVVKLGPLAVTAHATPGHTTGGTSWTWQscEQGRCANMVFADSLTAVSADGYRfsahpavLADVE 193

                        170       180
                 ....*....|....*....|....*
gi 890048396 176 ESLHRLRGLGRRTVLPGHgPDLLDL 200
Cdd:cd16313  194 QSIAAVEKLACDILVSAH-PEFSDM 217
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 ...
 24-143 3.38e-10

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


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 58.90  E-value: 3.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  24 SVLLADNPGLLTLDGTNtwvlrgPLSDELVvvdpgpdddehLARVAALG----RIALVLISHRHGDHTSGIDKLVALTGA 99
Cdd:cd16290   24 AVLITSPQGLILIDGAL------PQSAPQI-----------EANIRALGfrleDVKLILNSHAHFDHAGGIAALQRDSGA 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 890048396 100 PVRA---------------ADPQFLR-------RDGETLTDGEVIDVAGLTITVLATPGHTADSLS 143
Cdd:cd16290   87 TVAAspagaaalrsggvdpDDPQAGAadpfppvAKVRVVADGEVVKLGPLAVTAHATPGHTPGGTS 152
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 27-148 1.63e-09

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: 56.78  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  27 LADNPGLLTLDGTNTWVLRGPlsDELVVVDPG-PDDDEHL-ARVAALG----RIALVLISHRHGDHTSGIDKLVALTGAP 100
Cdd:cd07708   10 IAGNTYYVGTDDLAAYLIVTP--QGNILIDGDmEQNAPMIkANIKKLGfkfsDTKLILISHAHFDHAGGSAEIKKQTGAK 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396 101 VRA--ADPQFLRR---------DGETLT-----------DGEVIDVAGLTITVLATPGHTADSLSFVLDD 148
Cdd:cd07708   88 VMAgaEDVSLLLSggssdfhyaNDSSTYfpqstvdravhDGERVTLGGTVLTAHATPGHTPGCTTWTMTL 157
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 42-193 7.27e-09

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 54.91  E-value: 7.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  42 WVLRGPlsDELVVVDPGPDDDEH--------------------LARVAALG----RIALVLISHRHGDHTSGIDKLV--- 94
Cdd:cd07729   35 YLIEHP--EGTILVDTGFHPDAAddpgglelafppgvteeqtlEEQLARLGldpeDIDYVILSHLHFDHAGGLDLFPnat 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  95 ----------ALTGAPVRAADPQFLRRDGETLTDGEVI------DVAGlTITVLATPGHTADSLSFVLD----DAVLTAD 154
Cdd:cd07729  113 iivqraeleyATGPDPLAAGYYEDVLALDDDLPGGRVRlvdgdyDLFP-GVTLIPTPGHTPGHQSVLVRlpegTVLLAGD 191

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 890048396 155 TV---LGCGTTVIDKEDGSLADYLESLHRLRGLGRR---TVLPGH 193
Cdd:cd07729  192 AAytyENLEEGRPPGINYDPEAALASLERLKALAERegaRVIPGH 236
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 53-193 1.89e-08

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: 52.94  E-value: 1.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  53 VVVDPGPDDDEHLARVAALG-RIALVLISHRHGDHTSGIDKLVALTGAPV---RAADPQFLRRDGET------------- 115
Cdd:cd07737   25 AVIDPGGDADKILQAIEDLGlTLKKILLTHGHLDHVGGAAELAEHYGVPIigpHKEDKFLLENLPEQsqmfgfppaeaft 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396 116 ----LTDGEVIDVAGLTITVLATPGHT---------ADSLSFVLDdaVLTADTVlgcGTTviDKEDGSLADYLESLHR-L 181
Cdd:cd07737  105 pdrwLEEGDTVTVGNLTLEVLHCPGHTpghvvffnrESKLAIVGD--VLFKGSI---GRT--DFPGGNHAQLIASIKEkL 177

                        170
                 ....*....|...
gi 890048396 182 RGLGRR-TVLPGH 193
Cdd:cd07737  178 LPLGDDvTFIPGH 190
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 20-194 3.79e-08

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: 52.71  E-value: 3.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  20 TDTASVLLADNPGLLTLDGtntwvlrGPLSDELVVvdpgpdddehLARVAALG----RIALVLISHRHGDHTSGIDKLVA 95
Cdd:cd16288   20 SGLASYLITTPQGLILIDT-------GLESSAPMI----------KANIRKLGfkpsDIKILLNSHAHLDHAGGLAALKK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  96 LTGAP--VRAADPQFLRRDG-------------------ETLTDGEVIDVAGLTITVLATPGHTADSLSF---VLDDA-- 149
Cdd:cd16288   83 LTGAKlmASAEDAALLASGGksdfhygddslafppvkvdRVLKDGDRVTLGGTTLTAHLTPGHTRGCTTWtmtVKDDGkv 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 890048396 150 --VLTAD--TVLGcGTTVIDKED--GSLADYLESLHRLRGLGRRTVLPGHG 194
Cdd:cd16288  163 yqVVFADslTVNP-GYKLVGNPTypGIAEDYRHSFATLRALQCDIFLASHA 212
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 29-195 6.49e-08

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


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 51.43  E-value: 6.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  29 DNPGLLTLDGTNTwVLRGPlsDELVVVDPG-PDDDEHLarVAALGRIAL-------VLISHRHGDHTSGID------KLV 94
Cdd:cd07711   13 DSDGGFRASSTVT-LIKDG--GKNILVDTGtPWDRDLL--LKALAEHGLspedidyVVLTHGHPDHIGNLNlfpnatVIV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  95 ALTGAPVRAADPQFLRRDGETLTDGevidvagltITVLATPGHTADSLSFVLDDAVLtaDTVLGCG---TTVIDKEDGSL 171
Cdd:cd07711   88 GWDICGDSYDDHSLEEGDGYEIDEN---------VEVIPTPGHTPEDVSVLVETEKK--GTVAVAGdlfEREEDLEDPIL 156

                        170       180       190
                 ....*....|....*....|....*....|.
gi 890048396 172 ----ADYLESL--HRLRGLGRRTVL-PGHGP 195
Cdd:cd07711  157 wdplSEDPELQeeSRKRILALADWIiPGHGP 187
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 65-144 1.16e-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: 51.43  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  65 LARVAALG----RIALVLISHRHGDHTSGIDKLVALTGAPVRA---------------ADPQFLR-------RDGETLTD 118
Cdd:cd16314   48 EANIRALGfrpeDVRYIVSSHEHFDHAGGIARLQRATGAPVVArepaattlergrsdrSDPQFLVvekfppvASVQRIGD 127

                         90       100
                 ....*....|....*....|....*.
gi 890048396 119 GEVIDVAGLTITVLATPGHTADSLSF 144
Cdd:cd16314  128 GEVLRVGPLALTAHATPGHTPGGTSW 153
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 66-147 1.37e-07

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


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 51.32  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  66 ARVAALG----RIALVLISHRHGDHTSGIDKLVALTGAP--VRAADPQFLRRDG-------------------ETLTDGE 120
Cdd:cd16308   49 KNIQALGfkfkDIKILLTTQAHYDHVGAMAAIKQQTGAKmmVDEKDAKVLADGGksdyemggygstfapvkadKLLHDGD 128

                         90       100
                 ....*....|....*....|....*..
gi 890048396 121 VIDVAGLTITVLATPGHTADSLSFVLD 147
Cdd:cd16308  129 TIKLGGTKLTLLHHPGHTKGSCSFLFD 155
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 53-202 1.49e-07

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: 50.91  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  53 VVVDPGPDDDEHL--ARVAALG----RIALVLISHRHGDHTSGIDKLVALTGAPVRAADPQF------LRRDGET----- 115
Cdd:cd16310   34 ILLDGGLEENAALieQNIKALGfklsDIKIIINTHAHYDHAGGLAQLKADTGAKLWASRGDRpaleagKHIGDNItqpap 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396 116 ---------LTDGEVIDVAGLTITVLATPGHT--ADSLSFVLDDAVLTADTVLGCGTTV-----IDKED--GSLADYLES 177
Cdd:cd16310  114 fpavkvdriLGDGEKIKLGDITLTATLTPGHTkgCTTWSTTVKENGRPLRVVFPCSLSVagnvlVGNKTypTIVEDYRAS 193

                        170       180
                 ....*....|....*....|....*
gi 890048396 178 LHRLRGLGRRTVLPGHgPDLLDLEA 202
Cdd:cd16310  194 FARLRAMKADIVLTSH-PEVADLLA 217
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 50-148 2.17e-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: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  50 DELVVVDPGPDDDEHLARVAA-LGRIALVLISHRHGDHTSGIDKLV-------------ALTGAPVRAADPQFLRRDG-- 113
Cdd:COG1235   44 GTRLLIDAGPDLREQLLRLGLdPSKIDAILLTHEHADHIAGLDDLRprygpnpipvyatPGTLEALERRFPYLFAPYPgk 123

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 890048396 114 ---ETLTDGEVIDVAGLTITVLATPGHTADSLSFVLDD 148
Cdd:COG1235  124 lefHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGYRIED 161
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 54-193 3.35e-07

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 50.61  E-value: 3.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  54 VVDPgpddDEHLARVAALGR----IALVLISHRHGDHTSGIDKLVALTGAPV--RAADPQFLRRDGETLTDGEVIDVAGL 127
Cdd:PLN02398 102 VVDP----SEAVPVIDALSRknrnLTYILNTHHHYDHTGGNLELKARYGAKVigSAVDKDRIPGIDIVLKDGDKWMFAGH 177

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 890048396 128 TITVLATPGHTADSLSFVL--DDAVLTADTV--LGCGTTVidkeDGSLADYLESLHRLRGLGRRT-VLPGH 193
Cdd:PLN02398 178 EVLVMETPGHTRGHISFYFpgSGAIFTGDTLfsLSCGKLF----EGTPEQMLSSLQKIISLPDDTnIYCGH 244
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 65-144 4.73e-07

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: 49.60  E-value: 4.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  65 LARVAALG----RIALVLISHRHGDHTSGIDKLVALTGAPVRAA---------------DPQFLR-------RDGETLTD 118
Cdd:cd16311   48 IANIEALGfrieDVKLILNSHGHIDHAGGLAELQRRSGALVAASpsaaldlasgevgpdDPQYHAlpkyppvKDMRLARD 127

                         90       100
                 ....*....|....*....|....*.
gi 890048396 119 GEVIDVAGLTITVLATPGHTADSLSF 144
Cdd:cd16311  128 GGQFNVGPVSLTAHATPGHTPGGLSW 153
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 42-190 6.63e-07

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 49.05  E-value: 6.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  42 WVLRGPlSDELVVVDPGpDDDEHLARVAALGRI-ALVLISHRHGDHTSGIDKLVAlTGAPVRAADPQFLRRDGET--LTD 118
Cdd:PRK10241  15 WVLNDE-AGRCLIVDPG-EAEPVLNAIAENNWQpEAIFLTHHHHDHVGGVKELVE-KFPQIVVYGPQETQDKGTTqvVKD 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 890048396 119 GEVIDVAGLTITVLATPGHTADSLSFVLDDAVLTADTVL--GCGTTVidkeDGSLADYLESLHRLRGLGRRTVL 190
Cdd:PRK10241  92 GETAFVLGHEFSVFATPGHTLGHICYFSKPYLFCGDTLFsgGCGRLF----EGTASQMYQSLKKINALPDDTLI 161
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 27-148 3.50e-06

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: 46.73  E-value: 3.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  27 LADNPGLLTLDGTNTWVLRGPlsDELVVVDPG-PDDDEHL-----ARVAALGRIALVLISHRHGDHTSGIDKLVALTGAP 100
Cdd:cd16289   10 IADHTWYIGTESLTALLVKTP--DGAVLLDGGmPQAADMLldnmrALGVAPGDLKLILHSHAHADHAGPLAALKRATGAR 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 890048396 101 V--RAADPQFLRRDG------------------ETLTDGEVIDVAGLTITVLATPGHTADSLSFVLDD 148
Cdd:cd16289   88 VaaNAESAVLLARGGsddihfgdgitfppvqadRIVMDGEVVTLGGVTFTAHFTPGHTPGSTSWTWTD 155
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 53-149 7.04e-06

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: 45.38  E-value: 7.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396   53 VVVDPGPDDDEHLARV-----AALGRIALVLISHRHGDHTSGIDKLVALTGAPVRAADP---------QFLRRDGE---- 114
Cdd:pfam12706   3 ILIDPGPDLRQQALPAlqpgrLRDDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGvlahlrrnfPYLFLLEHygvr 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 890048396  115 --TLTDGEVIDVAGLTITVLATP----------GHTADSLSFVLDDA 149
Cdd:pfam12706  83 vhEIDWGESFTVGDGGLTVTATParhgsprgldPNPGDTLGFRIEGP 129
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 65-138 9.83e-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: 45.75  E-value: 9.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  65 LARVAALG----RIALVLISHRHGDHTSGIDKLVALTGAPVRAA---------------DPQFLR---------RDGETL 116
Cdd:cd16312   48 IANIEALGfrieDVKLILNSHAHWDHAGGIAALQKASGATVAASahgaqvlqsgtngkdDPQYQAkpvvhvakvAKVKEV 127

                         90       100
                 ....*....|....*....|..
gi 890048396 117 TDGEVIDVAGLTITVLATPGHT 138
Cdd:cd16312  128 GEGDTLKVGPLRLTAHMTPGHT 149
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 65-163 1.11e-05

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: 45.55  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  65 LARVAALG----RIALVLISHRHGDHTSGIDKLVALTGAPV--RAADPQFLR-----------------RDGETLTDGEV 121
Cdd:cd16309   48 KDNIKKLGfdvkDVKYLLNTHAHFDHAGGLAELKKATGAQLvaSAADKPLLEsgyvgsgdtknlqfppvRVDRVIGDGDK 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 890048396 122 IDVAGLTITVLATPGHTADSLSF---VLDDAVLTADTVLGCGTTV 163
Cdd:cd16309  128 VTLGGTTLTAHLTPGHSPGCTSWtttVKDTAGPPREVLFFCSATV 172
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 35-195 1.19e-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: 45.17  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  35 TLDGT--NTWVLRGplsDELVVVDPGPDD--DEHLARVAA---LGRIALVLISHRHGDHTSGIDKLVALT-GAPV----R 102
Cdd:cd07709   26 TPRGTsyNSYLIKD---EKTALIDTVKEPffDEFLENLEEvidPRKIDYIVVNHQEPDHSGSLPELLELApNAKIvcskK 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396 103 AAD--PQFLRRDGE---TLTDGEVIDVAGLTITVLATPG-HTADSL-SFVLDDAVL-TAD--TVLGCGTTVIDKEDGSLA 172
Cdd:cd07709  103 AARflKHFYPGIDErfvVVKDGDTLDLGKHTLKFIPAPMlHWPDTMvTYDPEDKILfSGDafGAHGASGELFDDEVEDYL 182

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 890048396 173 DYLESLH----------------RLRGLGRRTVLPGHGP 195
Cdd:cd07709  183 EEARRYYanimgpfskqvrkaleKLEALDIKMIAPSHGP 221
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 63-194 2.60e-05

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: 43.72  E-value: 2.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  63 EHLA-RVAALGRIALVLISHRhgDHTSGIDKLVALTGAPV--RAADPQFLRRDGE--TLTDGEVIDVAGlTITVLATPGH 137
Cdd:cd07727   36 PPLAkRIEALGGIRYIFLTHR--DDVADHAKWAERFGAKRiiHEDDVNAVTRPDEviVLWGGDPWELDP-DLTLIPVPGH 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 890048396 138 TADSLSFVLDD--AVLTADTVlgcgTTVIDKEDGSLADY---------LESLHRLRGLGRRTVLPGHG 194
Cdd:cd07727  113 TRGSVVLLYKEkgVLFTGDHL----AWSRRRGWLSAFRYvcwyswpeqAESVERLADLDFEWVLPGHG 176
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
50-155 3.55e-05

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 44.03  E-value: 3.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  50 DELVVVDPGPDDDEHLARV-AALGRIALVLISHRHGDHTSGID---KLVALTG--APVR----AADPQFLRR-------- 111
Cdd:COG1234   28 GERLLIDCGEGTQRQLLRAgLDPRDIDAIFITHLHGDHIAGLPgllSTRSLAGreKPLTiygpPGTKEFLEAllkasgtd 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 890048396 112 -----DGETLTDGEVIDVAGLTITVLATPgHTADSLSFVLDDA----VLTADT 155
Cdd:COG1234  108 ldfplEFHEIEPGEVFEIGGFTVTAFPLD-HPVPAYGYRFEEPgrslVYSGDT 159
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 27-160 6.08e-05

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 43.21  E-value: 6.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  27 LADNPGLLTLDGTntwvlrgplSDELVVVDPgPDDDEHLARVAALG-RIALVLISHRHGDHTSGIDKLVAL-TGAPVRAA 104
Cdd:PLN02469   9 LEDNYAYLIIDES---------TKDAAVVDP-VDPEKVLQAAHEHGaKIKLVLTTHHHWDHAGGNEKIKKLvPGIKVYGG 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 890048396 105 ---------DPQflrRDGETLTDGEVIDvagltITVLATPGHTADSLSFVL------DDAVLTADT--VLGCG 160
Cdd:PLN02469  79 sldnvkgctHPV---ENGDKLSLGKDVN-----ILALHTPCHTKGHISYYVtgkegeDPAVFTGDTlfIAGCG 143
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 38-137 9.49e-05

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 42.60  E-value: 9.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  38 GTNTWVLRgpLSDELVVVDP-----GPDDDEHLARVAALGRIALVLISHRHGDHTSG-IDKLVALTGAPVRA--ADPQFL 109
Cdd:COG2220   10 GHATFLIE--TGGKRILIDPvfsgrASPVNPLPLDPEDLPKIDAVLVTHDHYDHLDDaTLRALKRTGATVVAplGVAAWL 87

                         90       100       110
                 ....*....|....*....|....*....|..
gi 890048396 110 RRDG----ETLTDGEVIDVAGLTITvlATPGH 137
Cdd:COG2220   88 RAWGfprvTELDWGESVELGGLTVT--AVPAR 117
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 53-155 2.22e-04

uncharacterized bacterial subgroup of Ribonuclease Z, short form; 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. Members of this bacterial 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: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 40.89  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  53 VVVDPGPDDDEHLARVAALGRIALVLISHRHGDHTSGIDKL-VALTGAPVRAA-----------DPQFLRR--------D 112
Cdd:cd07716   30 ILLDCGSGVLSRLQRYIDPEDLDAVVLSHLHPDHCADLGVLqYARRYHPRGARkpplplygpagPAERLAAlygledvfD 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 890048396 113 GETLTDGEVIDVAGLTITVLATPgHTADSLSFVLDDA----VLTADT 155
Cdd:cd07716  110 FHPIEPGEPLEIGPFTITFFRTV-HPVPCYAMRIEDGgkvlVYTGDT 155
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 53-193 5.91e-04

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 40.17  E-value: 5.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  53 VVVDP-GPDDDEHLARVAALG-RIALVLISHRHGDHTSGIDKLValTGAP-VRAADPQFLRRDGETLTD-GEVIDVAGLT 128
Cdd:PLN02962  39 LLIDPvDKTVDRDLSLVKELGlKLIYAMNTHVHADHVTGTGLLK--TKLPgVKSIISKASGSKADLFVEpGDKIYFGDLY 116

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 890048396 129 ITVLATPGHTADSLSFVLDDA--------VLTADTVL--GCGTTviDKEDGSLADYLESLH-RLRGLGRRTVL-PGH 193
Cdd:PLN02962 117 LEVRATPGHTAGCVTYVTGEGpdqpqprmAFTGDALLirGCGRT--DFQGGSSDQLYKSVHsQIFTLPKDTLIyPAH 191
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 34-90 7.20e-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: 39.55  E-value: 7.20e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 890048396  34 LTLDGTNTWVLRG---------PLSDELVVVDPGPDDDEHLARVA-ALGRIALVLISHRHGDHTSGI 90
Cdd:cd16272    1 LTFLGTGGAVPSLtrntssyllETGGTRILLDCGEGTVYRLLKAGvDPDKLDAIFLSHFHLDHIGGL 67
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 37-194 1.10e-03

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


Pssm-ID: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 39.41  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  37 DGTNTWVLRGPlsDELVVVDPGpDDDEHLARVAALGR-------IALVLISHRHGDHTSGI-----------------DK 92
Cdd:cd07710   16 DLSNMTFIEGD--TGLIIIDTL-ESAEAAKAALELFRkhtgdkpVKAIIYTHSHPDHFGGAggfveeedsgkvpiiapEG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  93 LVALTGAPVRAADPQFLRR----------DGE----------------------TLT---DGEVIDVAGLTITVLATPGH 137
Cdd:cd07710   93 FMEEAVSENVLAGNAMSRRaayqfgallpKGEkgqvgaglgpglstgtvgfippTITiteTGETLTIDGVELEFQHAPGE 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 890048396 138 TADSLSFVLDD--AVLTADTVLGC--------GTTVIDkedgsLADYLESLHRLRGLGRRTVLPGHG 194
Cdd:cd07710  173 APDEMMVWLPDykVLFCADNVYHTfpnlytlrGAKYRD-----ALAWAKSLDEAISLKAEVLFPSHT 234
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 41-193 2.91e-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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 38.02  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  41 TWVLRGPLSDELVVVDPGPDDDEHLARV-AALGRIALVLISHRHGDHTSGID-------------KLVALTGAPVRAADP 106
Cdd:cd07730   50 TPRVPERLYRTPVPLEVEEDVAEQLAAGgIDPEDIDAVILSHLHWDHIGGLSdfpnarlivgpgaKEALRPPGYPSGFLP 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396 107 QFLRRDGETLTDGEVIDVAGLT----------------ITVLATPGHTADSL---------SFVLddavLTADTVLGCGT 161
Cdd:cd07730  130 ELLPSDFEGRLVRWEEDDFLWVplgpfpraldlfgdgsLYLVDLPGHAPGHLgllarttsgTWVF----LAGDACHHRIG 205

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 890048396 162 ---------TVIDKEDGSLADYLESLHRLRGLGRR---TVLPGH 193
Cdd:cd07730  206 llrpspllpLPDLDDGADREAARETLARLRELDAApdvRVVLAH 249
BLACT_WH pfam17778
Beta-lactamase associated winged helix domain; This winged helix domain is found at the ...
 230-264 2.92e-03

Beta-lactamase associated winged helix domain; This winged helix domain is found at the C-terminus of some beta lactamase enzymes.


Pssm-ID: 407650  Cd Length: 46  Bit Score: 34.90  E-value: 2.92e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 890048396  230 TVREVVEHVYLDVDEKLWNAAEWSVQAQLDYLRTR 264
Cdd:pfam17778   1 TAMELVKVIYKDVPESLHPAAERGVLAHLEKLEAE 35
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 53-154 2.93e-03

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: 38.30  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 890048396  53 VVVDPGPDDDEHLAR---VAAL-----GRIALVLISHRHGDHTSGIDKLVA-------LTGAPVRAADP-----QFLRRD 112
Cdd:COG2333   24 ILIDTGPRPSFDAGErvvLPYLralgiRRLDLLVLTHPDADHIGGLAAVLEafpvgrvLVSGPPDTSETyerllEALKEK 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 890048396 113 G---ETLTDGEVIDVAGLTITVLATPGHT-------ADSLSFVLDD----AVLTAD 154
Cdd:COG2333  104 GipvRPCRAGDTWQLGGVRFEVLWPPEDLlegsdenNNSLVLRLTYggfsFLLTGD 159
 
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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