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Conserved domains on  [gi|66730449|ref|NP_001019418|]
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endoribonuclease LACTB2 [Rattus norvegicus]

Protein Classification

beta-lactamase-like protein 2( domain architecture ID 14403986)

beta-lactamase-like protein 2 is an endoribonuclease that is involved in the turnover of mitochondrial RNA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 14-203 1.71e-109

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: 314.86  E-value: 1.71e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  14 RVVRVLGCNPGPMTLQGTNTYLVGTGSRRILIDTGEPsVPEYISCLKQALAEFDTA-IQEILVTHWHRDHSGGIVDICKN 92
Cdd:cd07722   1 RVIRILGQNPGPFTLQGTNTYLVGTGKRRILIDTGEG-RPSYIPLLKSVLDSEGNAtISDILLTHWHHDHVGGLPDVLDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  93 IsNDATYCIKKLRRNPQKEEIIGSGEQqYVYIEDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGTT 172
Cdd:cd07722  80 L-RGPSPRVYKFPRPEEDEDPDEDGGD-IHDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGDCVLGHGTA 157

                       170       180       190
                ....*....|....*....|....*....|.
gi 66730449 173 IFEDLSDYMNSLKDLLKVKANIIYPGHGPVI 203
Cdd:cd07722 158 VFEDLAAYMASLKKLLSLGPGRIYPGHGPVI 188
BLACT_WH pfam17778
Beta-lactamase associated winged helix domain; This winged helix domain is found at the ...
 237-284 1.18e-13

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: 63.79  E-value: 1.18e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 66730449   237 SVSELRKMIYKNVPENLHKMAEHNLLLHLRKLEKDGKIFSIASpaKKW 284
Cdd:pfam17778   1 TAMELVKVIYKDVPESLHPAAERGVLAHLEKLEAEGKVVREGD--GKW 46
 
Name Accession Description Interval E-value
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 14-203 1.71e-109

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: 314.86  E-value: 1.71e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  14 RVVRVLGCNPGPMTLQGTNTYLVGTGSRRILIDTGEPsVPEYISCLKQALAEFDTA-IQEILVTHWHRDHSGGIVDICKN 92
Cdd:cd07722   1 RVIRILGQNPGPFTLQGTNTYLVGTGKRRILIDTGEG-RPSYIPLLKSVLDSEGNAtISDILLTHWHHDHVGGLPDVLDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  93 IsNDATYCIKKLRRNPQKEEIIGSGEQqYVYIEDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGTT 172
Cdd:cd07722  80 L-RGPSPRVYKFPRPEEDEDPDEDGGD-IHDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGDCVLGHGTA 157

                       170       180       190
                ....*....|....*....|....*....|.
gi 66730449 173 IFEDLSDYMNSLKDLLKVKANIIYPGHGPVI 203
Cdd:cd07722 158 VFEDLAAYMASLKKLLSLGPGRIYPGHGPVI 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 23-214 8.43e-40

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: 137.90  E-value: 8.43e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  23 PGPMTLQGTNTYLVGTGSRRILIDTGEPsvPEYISCLKQALAEFDTAIQEILVTHWHRDHSGGIVDICKNIsnDATYCI- 101
Cdd:COG0491   7 GTPGAGLGVNSYLIVGGDGAVLIDTGLG--PADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF--GAPVYAh 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 102 ----KKLRRNPQKEEIIGSGEQQYVYIEDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGTTIF--- 174
Cdd:COG0491  83 aaeaEALEAPAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPdlp 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 66730449 175 -EDLSDYMNSLKDLLKVKANIIYPGHGPVIHNAEAKILEYI 214
Cdd:COG0491 163 dGDLAQWLASLERLLALPPDLVIPGHGPPTTAEAIDYLEEL 203
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 32-199 6.59e-33

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: 118.81  E-value: 6.59e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449     32 NTYLVGTGSRRILIDTGEPSVPEYISCLKQALAEfdtAIQEILVTHWHRDHSGGIVDICKnISNDATYC-------IKKL 104
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPK---KIDAIILTHGHPDHIGGLPELLE-APGAPVYApegtaelLKDL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449    105 RRNPQKEEIIGSGEQQYVYIEDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGTTIF------EDLS 178
Cdd:smart00849  77 LALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTlvdggdAAAS 156

                          170       180
                   ....*....|....*....|.
gi 66730449    179 DYMNSLKDLLKVKANIIYPGH 199
Cdd:smart00849 157 DALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
26-199 5.89e-20

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 85.50  E-value: 5.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449    26 MTLQGTNTYLVGTGSRRILIDTG-EPSVPEYISCLKQALAEFDtaIQEILVTHWHRDHSGGIVDICKNISNDATYCIKKL 104
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGgSAEAALLLLLAALGLGPKD--IDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449   105 RRNPQKEEIIGSGEQQYVY-----------IEDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGD--------- 164
Cdd:pfam00753  79 RELLDEELGLAASRLGLPGppvvplppdvvLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDllfageigr 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 66730449   165 --CILGEGTTIF-EDLSDYMNSLKDLLKVKANIIYPGH 199
Cdd:pfam00753 159 ldLPLGGLLVLHpSSAESSLESLLKLAKLKAAVIVPGH 196
BLACT_WH pfam17778
Beta-lactamase associated winged helix domain; This winged helix domain is found at the ...
 237-284 1.18e-13

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: 63.79  E-value: 1.18e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 66730449   237 SVSELRKMIYKNVPENLHKMAEHNLLLHLRKLEKDGKIFSIASpaKKW 284
Cdd:pfam17778   1 TAMELVKVIYKDVPESLHPAAERGVLAHLEKLEAEGKVVREGD--GKW 46
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 45-199 4.14e-08

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 53.69  E-value: 4.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449   45 IDTGEPSV--PEYISCLKQALAEFDTAIQEILVTHWHRDHSGGivdickNISNDATYCIKKLRRNPQKEEIIGSGeqqyV 122
Cdd:PLN02398  95 EDTGTVGVvdPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGG------NLELKARYGAKVIGSAVDKDRIPGID----I 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  123 YIEDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCI--LGEGtTIFEDLSDYM-NSLKDLLKVKANI-IYPG 198
Cdd:PLN02398 165 VLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLfsLSCG-KLFEGTPEQMlSSLQKIISLPDDTnIYCG 243


                 .
gi 66730449  199 H 199
Cdd:PLN02398 244 H 244
 
Name Accession Description Interval E-value
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 14-203 1.71e-109

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: 314.86  E-value: 1.71e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  14 RVVRVLGCNPGPMTLQGTNTYLVGTGSRRILIDTGEPsVPEYISCLKQALAEFDTA-IQEILVTHWHRDHSGGIVDICKN 92
Cdd:cd07722   1 RVIRILGQNPGPFTLQGTNTYLVGTGKRRILIDTGEG-RPSYIPLLKSVLDSEGNAtISDILLTHWHHDHVGGLPDVLDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  93 IsNDATYCIKKLRRNPQKEEIIGSGEQqYVYIEDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGTT 172
Cdd:cd07722  80 L-RGPSPRVYKFPRPEEDEDPDEDGGD-IHDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGDCVLGHGTA 157

                       170       180       190
                ....*....|....*....|....*....|.
gi 66730449 173 IFEDLSDYMNSLKDLLKVKANIIYPGHGPVI 203
Cdd:cd07722 158 VFEDLAAYMASLKKLLSLGPGRIYPGHGPVI 188
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-203 6.81e-55

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: 175.76  E-value: 6.81e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  14 RVVRVLGCNPGPMTLQGTNTYLVGTGSRRILIDTGePSVPEYISCLKQALAefDTAIQEILVTHWHRDHSGGIvdickni 93
Cdd:cd16278   1 GVRRVLAPNPSPMTLDGTNTYLLGAPDGVVVIDPG-PDDPAHLDALLAALG--GGRVSAILVTHTHRDHSPGA------- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  94 sndatyciKKLRRNPqKEEIIGSGEQQYVYI----------EDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSG 163
Cdd:cd16278  71 --------ARLAERT-GAPVRAFGPHRAGGQdtdfapdrplADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTG 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 66730449 164 DCILGEGTTIFE----DLSDYMNSLKDLLKVKANIIYPGHGPVI 203
Cdd:cd16278 142 DHVMGWSTTVIAppdgDLGDYLASLERLLALDDRLLLPGHGPPI 185
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 23-214 8.43e-40

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: 137.90  E-value: 8.43e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  23 PGPMTLQGTNTYLVGTGSRRILIDTGEPsvPEYISCLKQALAEFDTAIQEILVTHWHRDHSGGIVDICKNIsnDATYCI- 101
Cdd:COG0491   7 GTPGAGLGVNSYLIVGGDGAVLIDTGLG--PADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF--GAPVYAh 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 102 ----KKLRRNPQKEEIIGSGEQQYVYIEDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGTTIF--- 174
Cdd:COG0491  83 aaeaEALEAPAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPdlp 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 66730449 175 -EDLSDYMNSLKDLLKVKANIIYPGHGPVIHNAEAKILEYI 214
Cdd:COG0491 163 dGDLAQWLASLERLLALPPDLVIPGHGPPTTAEAIDYLEEL 203
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 30-199 4.39e-33

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: 119.70  E-value: 4.39e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  30 GTNTYLVGTGSRR-ILIDTGEPSVPEyiscLKQALAEFDTAIQEILVTHWHRDHSGGIVDICKNisNDATYCI----KKL 104
Cdd:cd06262   9 QTNCYLVSDEEGEaILIDPGAGALEK----ILEAIEELGLKIKAILLTHGHFDHIGGLAELKEA--PGAPVYIheadAEL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 105 RRNPQKEEIIGSGE-----QQYVYIEDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCIL--GEGTTIFE-- 175
Cdd:cd06262  83 LEDPELNLAFFGGGplpppEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFagSIGRTDLPgg 162

                       170       180
                ....*....|....*....|....*.
gi 66730449 176 DLSDYMNSLKDLLKVKAN--IIYPGH 199
Cdd:cd06262 163 DPEQLIESIKKLLLLLPDdtVVYPGH 188
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 32-199 6.59e-33

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: 118.81  E-value: 6.59e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449     32 NTYLVGTGSRRILIDTGEPSVPEYISCLKQALAEfdtAIQEILVTHWHRDHSGGIVDICKnISNDATYC-------IKKL 104
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPK---KIDAIILTHGHPDHIGGLPELLE-APGAPVYApegtaelLKDL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449    105 RRNPQKEEIIGSGEQQYVYIEDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGTTIF------EDLS 178
Cdd:smart00849  77 LALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTlvdggdAAAS 156

                          170       180
                   ....*....|....*....|.
gi 66730449    179 DYMNSLKDLLKVKANIIYPGH 199
Cdd:smart00849 157 DALESLLKLLKLLPKLVVPGH 177
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 23-209 5.57e-29

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: 108.93  E-value: 5.57e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  23 PGPMTLQGTNTYLVGTGSRRILIDTGEPSVPEYISC---LKQALAEFDtAIQEILVTHWHRDHSGGIVDICKniSNDATY 99
Cdd:cd07725   7 PLPGPLGHVNVYLLRDGDETTLIDTGLATEEDAEALwegLKELGLKPS-DIDRVLLTHHHPDHIGLAGKLQE--KSGATV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 100 CIKKLRRnpqkeeiigsgeqqyvyIEDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGT-------- 171
Cdd:cd07725  84 YILDVTP-----------------VKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLPKITpnvslwav 146

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 66730449 172 TIFEDLSDYMNSLKDLLKVKANIIYPGHGPVIHNAEAK 209
Cdd:cd07725 147 RVEDPLGAYLESLDKLEKLDVDLAYPGHGGPIKDPKAR 184
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 32-200 1.42e-28

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: 108.46  E-value: 1.42e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  32 NTYLVGTGSRRILIDTGEP-SVPEYISCLKQALAEFDtAIQEILVTHWHRDHSGGIVDICK--NI-----SNDATYCIKK 103
Cdd:cd07721  12 NAYLIEDDDGLTLIDTGLPgSAKRILKALRELGLSPK-DIRRILLTHGHIDHIGSLAALKEapGApvyahEREAPYLEGE 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 104 LRRNPQKEEIIGSGEQQYV---------YIEDGDLIKTEGAtLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGTTIF 174
Cdd:cd07721  91 KPYPPPVRLGLLGLLSPLLpvkpvpvdrTLEDGDTLDLAGG-LRVIHTPGHTPGHISLYLEEDGVLIAGDALVTVGGELV 169

                       170       180       190
                ....*....|....*....|....*....|...
gi 66730449 175 -------EDLSDYMNSLKDLLKVKANIIYPGHG 200
Cdd:cd07721 170 pppppftWDMEEALESLRKLAELDPEVLAPGHG 202
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 34-199 2.73e-26

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: 101.38  E-value: 2.73e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  34 YLVGTGSRR--ILIDTGEPSVpeyiscLKQALAEFDTAIQEILVTHWHRDHSGGIVDIcKNISNDATycikklrrnpqke 111
Cdd:cd07723  12 YLIVDEATGeaAVVDPGEAEP------VLAALEKNGLTLTAILTTHHHWDHTGGNAEL-KALFPDAP------------- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 112 eIIGSGEQQYVYI----EDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDC--ILGEGtTIFEDLSDYM-NSL 184
Cdd:cd07723  72 -VYGPAEDRIPGLdhpvKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTlfSGGCG-RFFEGTAEQMyASL 149

                       170
                ....*....|....*.
gi 66730449 185 KDLLKVKANI-IYPGH 199
Cdd:cd07723 150 QKLLALPDDTlVYCGH 165
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 30-200 6.34e-23

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: 92.46  E-value: 6.34e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  30 GTNTYLVGTGSRR--ILIDTGEPSVPEYIsclkQALAEFDTAIQEILVTHWHRDHSGGIVDICKNIsnDATYCIKKLrrn 107
Cdd:cd07724  11 GTLSYLVGDPETGeaAVIDPVRDSVDRYL----DLAAELGLKITYVLETHVHADHVSGARELAERT--GAPIVIGEG--- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 108 pqkeeiiGSGEQQYVYIEDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGT--TIFEDLSDYM---- 181
Cdd:cd07724  82 -------APASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVgrPDLPGEAEGLarql 154

                       170       180
                ....*....|....*....|..
gi 66730449 182 -NSLKDLLKVKAN--IIYPGHG 200
Cdd:cd07724 155 yDSLQRKLLLLPDetLVYPGHD 176
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 24-202 6.45e-21

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: 88.17  E-value: 6.45e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  24 GPMtlqGTNTYLVGT--GSRRILIDTGEPSvpeyiSCLKQALAEFDTAIQEILVTHWHRDHSGGIVDIcKNISNDATYCI 101
Cdd:cd16322   7 GPL---QENTYLVADegGGEAVLVDPGDES-----EKLLARFGTTGLTLLYILLTHAHFDHVGGVADL-RRHPGAPVYLH 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 102 K---KLRRNPQKEEIIG--SGEQQY---VYIEDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILgEGTTI 173
Cdd:cd16322  78 PddlPLYEAADLGAKAFglGIEPLPppdRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLF-QGSIG 156

                       170       180       190
                ....*....|....*....|....*....|....*
gi 66730449 174 FEDL--SDY---MNSLKDLLK-VKANIIYPGHGPV 202
Cdd:cd16322 157 RTDLpgGDPkamAASLRRLLTlPDETRVFPGHGPP 191
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
26-199 5.89e-20

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 85.50  E-value: 5.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449    26 MTLQGTNTYLVGTGSRRILIDTG-EPSVPEYISCLKQALAEFDtaIQEILVTHWHRDHSGGIVDICKNISNDATYCIKKL 104
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGgSAEAALLLLLAALGLGPKD--IDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449   105 RRNPQKEEIIGSGEQQYVY-----------IEDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGD--------- 164
Cdd:pfam00753  79 RELLDEELGLAASRLGLPGppvvplppdvvLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDllfageigr 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 66730449   165 --CILGEGTTIF-EDLSDYMNSLKDLLKVKANIIYPGH 199
Cdd:pfam00753 159 ldLPLGGLLVLHpSSAESSLESLLKLAKLKAAVIVPGH 196
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 33-199 1.09e-19

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


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 84.85  E-value: 1.09e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  33 TYLVGTGSRRILIDTG-EPSVPEYISCLkQALAEFDTAIQEILVTHWHRDHSGG---IVDICKNisndAT-YC----IKK 103
Cdd:cd07726  18 SYLLDGEGRPALIDTGpSSSVPRLLAAL-EALGIAPEDVDYIILTHIHLDHAGGaglLAEALPN----AKvYVhprgARH 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 104 LRrNPQK-----------------EEIIGSGEQQYVYIEDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCI 166
Cdd:cd07726  93 LI-DPSKlwasaravygdeadrlgGEILPVPEERVIVLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDAA 171

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 66730449 167 ---LGEGTTIFE--------DLSDYMNSLKDLLKVKANIIYPGH 199
Cdd:cd07726 172 gvrYPELDVVGPpstpppdfDPEAWLESLDRLLSLKPERIYLTH 215
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 29-199 4.39e-19

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: 82.68  E-value: 4.39e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  29 QGTNTYLVgTGSRR-ILIDTGEPSVPeyiscLKQALAEFDTAIQEILVTHWHRDHSGGI------------VDICKNISN 95
Cdd:cd07712   7 DRVNIYLL-RGRDRaLLIDTGLGIGD-----LKEYVRTLTDLPLLVVATHGHFDHIGGLhefeevyvhpadAEILAAPDN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  96 DATYCIkklrrNPQKEEIIGSGEqqYVYIEDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDcILGEGTTIFE 175
Cdd:cd07712  81 FETLTW-----DAATYSVPPAGP--TLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGD-VVYDGPLIMD 152

                       170       180       190
                ....*....|....*....|....*....|
gi 66730449 176 ----DLSDYMNSLKDLLKVKANI--IYPGH 199
Cdd:cd07712 153 lphsDLDDYLASLEKLSKLPDEFdkVLPGH 182
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 30-202 2.11e-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: 70.29  E-value: 2.11e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  30 GTNTYLVGTGSRRILIDTGePSvPEYISCLKQALAE-FDTAIQEILVTHWHRDHSGG----------IV---DICKNISN 95
Cdd:cd16282  14 ISNIGFIVGDDGVVVIDTG-AS-PRLARALLAAIRKvTDKPVRYVVNTHYHGDHTLGnaafadagapIIaheNTREELAA 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  96 DATYCIKKLRRnpQKEEIIGSGEQQY--VYIEDGDLIKTEGATLRVLYT-PGHTDDHMALLLEEENAIFSGDCILGEGTT 172
Cdd:cd16282  92 RGEAYLELMRR--LGGDAMAGTELVLpdRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEGVLFAGDLVFNGRIP 169

                       170       180       190
                ....*....|....*....|....*....|..
gi 66730449 173 IFED--LSDYMNSLKDLLKVKANIIYPGHGPV 202
Cdd:cd16282 170 FLPDgsLAGWIAALDRLLALDATVVVPGHGPV 201
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 22-201 6.00e-14

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: 68.77  E-value: 6.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  22 NPGPMTLQGTNTyLVGTGSRRILIDTGepsVPEYISCLKQALAEFDTA---IQEILVTHWHRDHSGGIVDIcknisndat 98
Cdd:cd07711  14 SDGGFRASSTVT-LIKDGGKNILVDTG---TPWDRDLLLKALAEHGLSpedIDYVVLTHGHPDHIGNLNLF--------- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  99 ycikklrrnPQKEEIIGSGEQQYVYIEDgDLIKTEGATL----RVLYTPGHTDDHMALLLEEENA---IFSGDCILGEGT 171
Cdd:cd07711  81 ---------PNATVIVGWDICGDSYDDH-SLEEGDGYEIdenvEVIPTPGHTPEDVSVLVETEKKgtvAVAGDLFEREED 150

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 66730449 172 T--------IFEDLSDYMNSLKDLLKVkANIIYPGHGP 201
Cdd:cd07711 151 LedpilwdpLSEDPELQEESRKRILAL-ADWIIPGHGP 187
BLACT_WH pfam17778
Beta-lactamase associated winged helix domain; This winged helix domain is found at the ...
 237-284 1.18e-13

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: 63.79  E-value: 1.18e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 66730449   237 SVSELRKMIYKNVPENLHKMAEHNLLLHLRKLEKDGKIFSIASpaKKW 284
Cdd:pfam17778   1 TAMELVKVIYKDVPESLHPAAERGVLAHLEKLEAEGKVVREGD--GKW 46
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 34-199 3.32e-12

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: 64.54  E-value: 3.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  34 YLVGTGSRRILIDTGEPsvPEYIS-----------------CLKQALAEFDTAIQEI---LVTHWHRDHSGGIvDICKNi 93
Cdd:cd07729  35 YLIEHPEGTILVDTGFH--PDAADdpgglelafppgvteeqTLEEQLARLGLDPEDIdyvILSHLHFDHAGGL-DLFPN- 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  94 sndAT-YCIKK-----LRRNPQKEEIIGSGEQQYVYIEDGDLIKTEGAT-----LRVLYTPGHTDDHMALL--LEEENAI 160
Cdd:cd07729 111 ---ATiIVQRAeleyaTGPDPLAAGYYEDVLALDDDLPGGRVRLVDGDYdlfpgVTLIPTPGHTPGHQSVLvrLPEGTVL 187

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 66730449 161 FSGDCI-----LGEG-----TTIFEDLSDYMNSLKDLLKVKANIIYPGH 199
Cdd:cd07729 188 LAGDAAytyenLEEGrppgiNYDPEAALASLERLKALAEREGARVIPGH 236
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 59-199 4.60e-11

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: 60.64  E-value: 4.60e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  59 LKQALAEFDTAIQEILVTHWHRDHSGGIVDICKnisndaTYCIKKLrrNPQKEE--IIGSGEQQYV-------------- 122
Cdd:cd07737  36 ILQAIEDLGLTLKKILLTHGHLDHVGGAAELAE------HYGVPII--GPHKEDkfLLENLPEQSQmfgfppaeaftpdr 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 123 YIEDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCIL--GEGTTIFE--DLSDYMNSLKD-LLKVKANI-IY 196
Cdd:cd07737 108 WLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFkgSIGRTDFPggNHAQLIASIKEkLLPLGDDVtFI 187


                ...
gi 66730449 197 PGH 199
Cdd:cd07737 188 PGH 190
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 31-212 1.24e-10

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: 60.19  E-value: 1.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  31 TNTYLVgTGSRRILIDTGEPSV-PEYISCLKQALAefDTAIQEILVTHWHRDHSGGIVDIcknisndatycikkLRRNPQ 109
Cdd:cd07709  32 YNSYLI-KDEKTALIDTVKEPFfDEFLENLEEVID--PRKIDYIVVNHQEPDHSGSLPEL--------------LELAPN 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 110 kEEIIGS-------------GEQQYVYIEDGDLIKTEGATLRVLYTPG-HTDDHMALLLEEENAIFSGDcILG---EGTT 172
Cdd:cd07709  95 -AKIVCSkkaarflkhfypgIDERFVVVKDGDTLDLGKHTLKFIPAPMlHWPDTMVTYDPEDKILFSGD-AFGahgASGE 172

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 173 IFED-LSDYMNSLKD----------------LLKVKA---NIIYPGHGPVIHNAEAKILE 212
Cdd:cd07709 173 LFDDeVEDYLEEARRyyanimgpfskqvrkaLEKLEAldiKMIAPSHGPIWRKDPGEIID 232
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 23-166 2.34e-10

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


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 59.48  E-value: 2.34e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  23 PGPMTLqGTNTYLVGTGSRRILIDTG-----EPSVPEYISCLKQA---LAEFDTaiqeILVTHWHRDHSGGIVDicknis 94
Cdd:cd07720  42 PDPVET-SVNAFLVRTGGRLILVDTGagglfGPTAGKLLANLAAAgidPEDIDD----VLLTHLHPDHIGGLVD------ 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  95 ND-------ATYCIKKLR----RNPQKEEIIGSGEQQYVYI--------EDGDLIKTEGATL---RVLYTPGHTDDHMAL 152
Cdd:cd07720 111 AGgkpvfpnAEVHVSEAEwdfwLDDANAAKAPEGAKRFFDAardrlrpyAAAGRFEDGDEVLpgiTAVPAPGHTPGHTGY 190

                       170
                ....*....|....*.
gi 66730449 153 LLE--EENAIFSGDCI 166
Cdd:cd07720 191 RIEsgGERLLIWGDIV 206
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 73-199 5.87e-10

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: 57.16  E-value: 5.87e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  73 ILVTHWHRDHSGGIVDICKnisndatycikklRRNPQ----KEEIIGSGEQ--QYVYIEDGDLIKTEGATLRVLYTPGHT 146
Cdd:cd16275  51 ILLTHSHFDHVNLVEPLLA-------------KYDAPvymsKEEIDYYGFRcpNLIPLEDGDTIKIGDTEITCLLTPGHT 117

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 147 DDHMALLLeeENAIFSGD--CILGEGTTIF-----EDLSDYMNSLKDLLKVKAnIIYPGH 199
Cdd:cd16275 118 PGSMCYLL--GDSLFTGDtlFIEGCGRCDLpggdpEEMYESLQRLKKLPPPNT-RVYPGH 174
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 29-209 2.20e-09

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: 56.69  E-value: 2.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  29 QGTNTYLVGTGSRRILIDTGEPSVPEYISCLKQALaEFDTA-IQEILVTHWHRDHSGGIVDICKNISNDATYCIKKLRR- 106
Cdd:cd16310  20 KGIGSYLITSNHGAILLDGGLEENAALIEQNIKAL-GFKLSdIKIIINTHAHYDHAGGLAQLKADTGAKLWASRGDRPAl 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 107 ---NPQKEEIIGSGEQQYVYIE----DGDLIKTEGATLRVLYTPGHTDD----HMALLLEEENAIFSGDCILGEGTTIFE 175
Cdd:cd16310  99 eagKHIGDNITQPAPFPAVKVDrilgDGEKIKLGDITLTATLTPGHTKGcttwSTTVKENGRPLRVVFPCSLSVAGNVLV 178

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 66730449 176 D-------LSDYMNSLKDLLKVKANIIYPGHgPVIHNAEAK 209
Cdd:cd16310 179 GnktyptiVEDYRASFARLRAMKADIVLTSH-PEVADLLAR 218
NorV COG0426
Flavorubredoxin [Energy production and conversion];
27-212 5.27e-09

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 56.38  E-value: 5.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  27 TLQGT--NTYLVgTGSRRILIDTGEPSV-PEYISCLKQALAefDTAIQEILVTHWHRDHSGGIVDICKNISNdAT-YCIK 102
Cdd:COG0426  28 TPRGTtyNSYLI-VDEKTALIDTVGESFfEEFLENLSKVID--PKKIDYIIVNHQEPDHSGSLPELLELAPN-AKiVCSK 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 103 K----LRrnpqkeEIIGSGEQQYVYIEDGDLIKTEGATLRVLYTPG-HTDDHMALLLEEENAIFSGDcILGE---GTTIF 174
Cdd:COG0426 104 KaarfLP------HFYGIPDFRFIVVKEGDTLDLGGHTLQFIPAPMlHWPDTMFTYDPEDKILFSGD-AFGShgaSDELF 176

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 66730449 175 EDLSD--------------YMNS-------LKDLLKVKANIIYPGHGPVIHNAEAKILE 212
Cdd:COG0426 177 DDEVDehleeearryyaniMMPFskqvlkaLKKVRGLDIDMIAPSHGPIWRGNPKEILD 235
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 25-146 2.99e-08

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: 53.33  E-value: 2.99e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  25 PMTLQGtNTYLVGTG----------SRRILIDTGEPSVPEYISCLKQALAEFDTAIQEILVTHWHRDHSGGIVDICK--- 91
Cdd:cd16313   7 PFQIYG-NTYYVGTGgisavlitspQGHILIDGGFPKSPEQIAASIRQLGFKLEDVKYILSSHDHWDHAGGIAALQKltg 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66730449  92 --NISNDATycIKKLRR-NPQKEEIIGSGEQQYV------YIEDGDLIKTEGATLRVLYTPGHT 146
Cdd:cd16313  86 aqVLASPAT--VAVLRSgSMGKDDPQFGGLTPMPpvasvrAVRDGEVVKLGPLAVTAHATPGHT 147
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 45-199 4.14e-08

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 53.69  E-value: 4.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449   45 IDTGEPSV--PEYISCLKQALAEFDTAIQEILVTHWHRDHSGGivdickNISNDATYCIKKLRRNPQKEEIIGSGeqqyV 122
Cdd:PLN02398  95 EDTGTVGVvdPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGG------NLELKARYGAKVIGSAVDKDRIPGID----I 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  123 YIEDGDLIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCI--LGEGtTIFEDLSDYM-NSLKDLLKVKANI-IYPG 198
Cdd:PLN02398 165 VLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLfsLSCG-KLFEGTPEQMlSSLQKIISLPDDTnIYCG 243


                 .
gi 66730449  199 H 199
Cdd:PLN02398 244 H 244
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 70-202 4.72e-08

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


Pssm-ID: 293793 [Multi-domain]  Cd Length: 219  Bit Score: 52.55  E-value: 4.72e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  70 IQEILVTHWHRDHSGGIvDICKNI-----SNDATYcikKLRRNPQKEEIIGSGEQQYVYIEDGDLIKT---EGAT----- 136
Cdd:cd07707  59 VTEVINTHFHTDRAGGN-AYLKERgaktvSTALTR---DLAKSEWAEIVAFTRKGLPEYPDLGYELPDgvlDGDFnlqfg 134

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66730449 137 -LRVLYT-PGHTDDHMALLLEEENAIFsGDCILGE---GTTIFEDLSDYMNSLKDLLKV--KANIIYPGHGPV 202
Cdd:cd07707 135 kVEAFYPgPAHTPDNIVVYFPQENVLY-GGCIIKEtdlGNVADADVKEWPTSIERLKKRyrNIKAVIPGHGEV 206
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 27-201 6.41e-08

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


Pssm-ID: 293862 [Multi-domain]  Cd Length: 212  Bit Score: 51.90  E-value: 6.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  27 TLQGT----NTYLVGTGSRRILIDT--GEPSVPEYISCLKQalaEFDTAIQEILVTHWHRDHSGGIVDICKN----ISND 96
Cdd:cd16304  18 LFNGTpvpsNGLIVETSKGVVLIDTpwDDEQTEELLDWIKK---KLKKPVTLAIVTHAHDDRIGGIKALQKRgipvYSTK 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  97 ATycIKKLRRNpqkeeiiGSGEQQYVyIEDGDLIKTEGATLRVLYT-PGHTDDHMALLLEEENAIFSGdCIL------GE 169
Cdd:cd16304  95 LT--AQLAKKQ-------GYPSPDGI-LKDDTTLKFGNTKIETFYPgEGHTADNIVVWLPQSKILFGG-CLVksleakDL 163

                       170       180       190
                ....*....|....*....|....*....|....
gi 66730449 170 GTTIFEDLSDYMNSLKDLLKV--KANIIYPGHGP 201
Cdd:cd16304 164 GNTADANLKEWPTSIRNVLKRypNAEIVVPGHGE 197
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 30-199 1.01e-07

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 50.99  E-value: 1.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  30 GTNTYLVGTGSRR-ILIDTG-EPSVPEYIsclKQALAEFDTAIQEILVTHWHRDHSGGIVDI-----CKNIS--NDATYC 100
Cdd:cd07743   7 PTNIGVYVFGDKEaLLIDSGlDEDAGRKI---RKILEELGWKLKAIINTHSHADHIGGNAYLqkktgCKVYApkIEKAFI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 101 ikklrRNPQKEEIIGSG-----EQQY-----------VYIEDGDlIKTEGATLRVLYTPGHTDDHMALLLEEeNAIFSGD 164
Cdd:cd07743  84 -----ENPLLEPSYLGGayppkELRNkflmakpskvdDIIEEGE-LELGGVGLEIIPLPGHSFGQIGILTPD-GVLFAGD 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 66730449 165 CILGEGT------TIFEDLSDYMNSLKDLLKVKANIIYPGH 199
Cdd:cd07743 157 ALFGEEVlekygiPFLYDVEEQLETLEKLEELDADYYVPGH 197
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 29-200 1.62e-07

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 51.40  E-value: 1.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  29 QGTNTYLVGTGSRRILIDTGEPSVPEY-----ISCLK-QALAEFDTAIqeilVTHWHRDHSGGIVDICKNISNDATYCIK 102
Cdd:COG2333  10 QGDAILIRTPDGKTILIDTGPRPSFDAgervvLPYLRaLGIRRLDLLV----LTHPDADHIGGLAAVLEAFPVGRVLVSG 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 103 KLRRNPQKEEIIGSGEQ---QYVYIEDGDLIKTEGATLRVLYTPGHTDDH-------MALLLE--EENAIFSGDCilgeG 170
Cdd:COG2333  86 PPDTSETYERLLEALKEkgiPVRPCRAGDTWQLGGVRFEVLWPPEDLLEGsdennnsLVLRLTygGFSFLLTGDA----E 161

                       170       180       190
                ....*....|....*....|....*....|.
gi 66730449 171 TTIFEDLSDYMNSLK-DLLKVkaniiyPGHG 200
Cdd:COG2333 162 AEAEAALLARGPDLKaDVLKV------PHHG 186
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 34-185 3.20e-07

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 50.28  E-value: 3.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  34 YLVGTGSRRILIDTGEPSVPEYIscLKQALAE--FDTA-IQEILVTHWHRDHSGGiVDICKNISN--------DATYcik 102
Cdd:cd16280  25 WAIDTGDGLILIDALNNNEAADL--IVDGLEKlgLDPAdIKYILITHGHGDHYGG-AAYLKDLYGakvvmseaDWDM--- 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 103 kLRRNPQKEEIIGSGE--QQYVYIEDGDLIKTEGATLRVLYTPGHTDDHMALLLEEEN------AIFSGdcilGEG---T 171
Cdd:cd16280  99 -MEEPPEEGDNPRWGPppERDIVIKDGDTLTLGDTTITVYLTPGHTPGTLSLIFPVKDggkthrAGLWG----GTGlntG 173

                       170
                ....*....|....
gi 66730449 172 TIFEDLSDYMNSLK 185
Cdd:cd16280 174 PNLERREQYIASLE 187
PRK11921 PRK11921
anaerobic nitric oxide reductase flavorubredoxin;
32-244 3.87e-07

anaerobic nitric oxide reductase flavorubredoxin;


Pssm-ID: 237023 [Multi-domain]  Cd Length: 394  Bit Score: 50.85  E-value: 3.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449   32 NTYLVgTGSRRILIDT-GEPSVPEYISCLKQalaEFD-TAIQEILVTHWHRDHSGGIVDICKNISNDATYC----IKKLR 105
Cdd:PRK11921  34 NSYLI-KDEKTVLIDTvWQPFAKEFVENLKK---EIDlDKIDYIVANHGEIDHSGALPELMKEIPDTPIYCtkngAKSLK 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  106 RNPQKE---EIIGSGEQqyVYIEDGDLIKTEGATLrvlytpgHTDDHMALLLEEENAIFSGDCiLGE---GTTIFEDLSD 179
Cdd:PRK11921 110 GHYHQDwnfVVVKTGDR--LEIGSNELIFIEAPML-------HWPDSMFTYLTGDNILFSNDA-FGQhyaSELMYNDLVD 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  180 YMNSLKDLLKVKANI------------------------IYPGHGPVIHNAEAKILE-YISHRNNREEQIITVFRDNLEE 234
Cdd:PRK11921 180 QGELYQEAIKYYANIltpfsplvikkieeilslnlpvdmICPSHGVIWRDNPLQIVEkYLEWAANYQENQVTILYDTMWN 259

                        250
                 ....*....|
gi 66730449  235 SfsvseLRKM 244
Cdd:PRK11921 260 S-----TRRM 264
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 35-171 4.73e-07

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 49.82  E-value: 4.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449   35 LVGTGSRRILIDTGEpSVPeyiscLKQALAEFDTAIQEILVTHWHRDHSGGIVDICKNISNDATYcikklrrNPQkeEII 114
Cdd:PRK10241  17 LNDEAGRCLIVDPGE-AEP-----VLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVY-------GPQ--ETQ 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66730449  115 GSGEQQYVyiEDGDLIKTEGATLRVLYTPGHTDDHMALL----LEEENAIFSGDC-ILGEGT 171
Cdd:PRK10241  82 DKGTTQVV--KDGETAFVLGHEFSVFATPGHTLGHICYFskpyLFCGDTLFSGGCgRLFEGT 141
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 30-146 5.76e-07

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: 49.40  E-value: 5.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  30 GTNTYLVGTGSRRILIDTGEPSVPEYISCLKQALAeFDTA-IQEILVTHWHRDHSGGIVDICKniSNDATYcIKKLRRNP 108
Cdd:cd16309  21 GLGVFLITTPEGHILIDGAMPQSTPLIKDNIKKLG-FDVKdVKYLLNTHAHFDHAGGLAELKK--ATGAQL-VASAADKP 96

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 66730449 109 QKEE-IIGSGEQQYV---------YIEDGDLIKTEGATLRVLYTPGHT 146
Cdd:cd16309  97 LLESgYVGSGDTKNLqfppvrvdrVIGDGDKVTLGGTTLTAHLTPGHS 144
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 33-166 5.78e-07

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 49.44  E-value: 5.78e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  33 TYLVGTGSRRILIDTG-----EPSVPEYISCLKQ----ALAEFDTAIQEI---LVTHWHRDHSGGivdickNISND---- 96
Cdd:cd16277  15 SWLVRTPGRTILVDTGigndkPRPGPPAFHNLNTpyleRLAAAGVRPEDVdyvLCTHLHVDHVGW------NTRLVdgrw 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  97 ------ATYCIkklrrnPQKE-----EIIGSGEQQYVYIEDG----------DLIkTEGATL----RVLYTPGHTDDHMA 151
Cdd:cd16277  89 vptfpnARYLF------SRAEydhwsSPDAGGPPNRGVFEDSvlpvieaglaDLV-DDDHEIldgiRLEPTPGHTPGHVS 161

                       170
                ....*....|....*..
gi 66730449 152 LLLE--EENAIFSGDCI 166
Cdd:cd16277 162 VELEsgGERALFTGDVM 178
MUS_TUS_MBL-B1 cd16318
Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; ...
 31-199 8.67e-07

Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded MBLs Myroides odoratimimus MUS-1 and related MBLs. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293876  Cd Length: 214  Bit Score: 48.88  E-value: 8.67e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  31 TNTYLVGTGSRRILIDTgeP-SVPEYISCLKQALAEFDTAIQEILVTHWHRDHSGGIVDICKNISNDATYC----IKKLR 105
Cdd:cd16318  26 SNSMYVLTDEGVILIDT--PwDKDQYEPLLEYIRSNHNKEVKWVITTHFHEDRSGGLGYFNSIGAQTYTYAltneILKER 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 106 RNPQKEEIIGSgEQQYVYIEDgdliktegaTLRVLYT-PGHTDDHMALLLEEEnAIFSGDCIL--GEGTTI-------FE 175
Cdd:cd16318 104 NEPQAQFSFNK-EKQFTFGNE---------KLAVYFLgEGHSLDNTVVWFPKE-EVLYGGCLIksAEATTIgniadgnVI 172

                       170       180
                ....*....|....*....|....
gi 66730449 176 DLSDYMNSLKDLLKvKANIIYPGH 199
Cdd:cd16318 173 AWPKTIEAVKQKFK-NAKVIIPGH 195
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 30-204 1.36e-06

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: 47.58  E-value: 1.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  30 GTNTYLVGTGSRRILIDTgepsvPEYISCLKQALAEFDtAIQEILVTHwhRDHSGGIVDI-----CKNI--SNDATYcik 102
Cdd:cd07727  14 GAASYLILRPEGNILVDS-----PRYSPPLAKRIEALG-GIRYIFLTH--RDDVADHAKWaerfgAKRIihEDDVNA--- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 103 klrrNPQKEEIIGSGEQQYVYIEDGdliktegatLRVLYTPGHTDDHMALLLEEENAIFSGDCI----LGEGTTIFEDLS 178
Cdd:cd07727  83 ----VTRPDEVIVLWGGDPWELDPD---------LTLIPVPGHTRGSVVLLYKEKGVLFTGDHLawsrRRGWLSAFRYVC 149

                       170       180       190
                ....*....|....*....|....*....|.
gi 66730449 179 DYM-----NSLKDLLKVKANIIYPGHGPVIH 204
Cdd:cd07727 150 WYSwpeqaESVERLADLDFEWVLPGHGRRVH 180
NDM_FIM-like_MBL-B1 cd16300
NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase ...
 31-201 1.57e-06

NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the ISCR-mediated MBLs NDM-1 (NDM (New Delhi metallo-beta-lactamase) and FIM-1 (Florence imipenemase). MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293858  Cd Length: 214  Bit Score: 47.89  E-value: 1.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  31 TNTYLVGTGSRRILIDTG--EPSVPEYISCLKQALAEfdtAIQEILVTHWHRD--------HSGGIVDICKNISNdatyc 100
Cdd:cd16300  27 SNGLIVRDGDRVLLVDTAwtDDQTAQILNWAKQELNL---PVRLAVVTHAHQDkmggmdalHAAGIATYANALSN----- 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 101 ikklRRNPQkeEIIGSGEQQYVYIEDGDLIKTEGatLRVLYT-PGHTDDHMALLLEEENAIFSGDCILGEGTTIFEDLSD 179
Cdd:cd16300  99 ----QLAPQ--EGLVPAQHSLTFAAEPSTAPNFP--LKVFYPgPGHTRDNIVVGIDGTGIAFGGCLIRPSKATSLGNLAD 170

                       170       180
                ....*....|....*....|....*....
gi 66730449 180 -----YMNSLKDLLKV--KANIIYPGHGP 201
Cdd:cd16300 171 adtehWAASARAFGAAfpDASMIVPSHGA 199
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 ...
 25-146 1.67e-06

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: 48.11  E-value: 1.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  25 PMTLQGtNTYLVGTG--------SRR--ILIDTGEP-SVPEYISCLkQALAeFD-TAIQEILVTHWHRDHSGGIVDICKN 92
Cdd:cd16290   7 PFRIHG-NTYYVGTGglsavlitSPQglILIDGALPqSAPQIEANI-RALG-FRlEDVKLILNSHAHFDHAGGIAALQRD 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66730449  93 isNDATYC-----IKKLRR------NPQKEEIIG-SGEQQYVYIEDGDLIKTEGATLRVLYTPGHT 146
Cdd:cd16290  84 --SGATVAaspagAAALRSggvdpdDPQAGAADPfPPVAKVRVVADGEVVKLGPLAVTAHATPGHT 147
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 35-190 1.70e-06

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 47.13  E-value: 1.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  35 LVGTGSRRILIDTGEPSVPEY---ISCLKqalAEFDTAIQEILVTHWHRDHSGGIVDICKNISNDATYCIKKLRRNPQKE 111
Cdd:cd07731  14 LIQTPGKTILIDTGPRDSFGEdvvVPYLK---ARGIKKLDYLILTHPDADHIGGLDAVLKNFPVKEVYMPGVTHTTKTYE 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 112 EIIGSGEQQ---YVYIEDGDLIKTEGATLRVLYTPGHTDDHM-----ALLLEEEN--AIFSGDC-ILGEgttifEDL-SD 179
Cdd:cd07731  91 DLLDAIKEKgipVTPCKAGDRWQLGGVSFEVLSPPKDDYDDLnnnscVLRLTYGGtsFLLTGDAeKEAE-----EELlAS 165

                       170
                ....*....|.
gi 66730449 180 YMNSLKDLLKV 190
Cdd:cd07731 166 GPDLLADVLKV 176
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 32-86 2.10e-06

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


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 46.49  E-value: 2.10e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  32 NTYLVGTGSRRILIDTGepsvpeyISC--LKQALAEFDTA---IQEILVTHWHRDHSGGI 86
Cdd:cd07733  10 NCTYLETEDGKLLIDAG-------LSGrkITGRLAEIGRDpedIDAILVTHEHADHIKGL 62
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 43-205 2.30e-06

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: 47.50  E-value: 2.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  43 ILIDTGEPsvpeyISCLKQALAEFDTAIQE-----ILVTHWHRDHSGGIVDICKNISNDATYCI--KKLRRNPQKEEIIG 115
Cdd:cd07710  30 IIIDTLES-----AEAAKAALELFRKHTGDkpvkaIIYTHSHPDHFGGAGGFVEEEDSGKVPIIapEGFMEEAVSENVLA 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 116 S-----------------GEQQYVYIEDG--------------DLIKTEGATLRV-------LYTPGHTDDHMALLLEEE 157
Cdd:cd07710 105 GnamsrraayqfgallpkGEKGQVGAGLGpglstgtvgfipptITITETGETLTIdgvelefQHAPGEAPDEMMVWLPDY 184

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66730449 158 NAIFSGDCILG--------EGTTIfEDLSDYMNSLKDLLKVKANIIYPGHGPVIHN 205
Cdd:cd07710 185 KVLFCADNVYHtfpnlytlRGAKY-RDALAWAKSLDEAISLKAEVLFPSHTWPVWG 239
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 25-146 2.43e-06

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: 47.54  E-value: 2.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  25 PMTLQGtNTYLVGTGS----------RRILIDTGEPSVPEYISCLKQALAEFDTAIQEILVTHWHRDHSGGIVDI----- 89
Cdd:cd07708   7 PFQIAG-NTYYVGTDDlaaylivtpqGNILIDGDMEQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAEIkkqtg 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66730449  90 CKNISNDATycIKKLRRNPQKEEIIGSGEQQYV-------YIEDGDLIKTEGATLRVLYTPGHT 146
Cdd:cd07708  86 AKVMAGAED--VSLLLSGGSSDFHYANDSSTYFpqstvdrAVHDGERVTLGGTVLTAHATPGHT 147
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 69-201 2.56e-06

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 46.81  E-value: 2.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  69 AIQEI-------LV-THWHRDHSGG---IVDIC-KNISNDATYciKKLRRNPQKEEIIGSgeqqyVYIEDGDLIKTEGAT 136
Cdd:cd16276  37 AIRKVtdkpvthVVySHNHADHIGGasiFKDEGaTIIAHEATA--ELLKRNPDPKRPVPT-----VTFDDEYTLEVGGQT 109

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66730449 137 LRVLYT-PGHTDDHMALLLEEENAIFSGDCILGEGTTIF-----EDLSDYMNSLKDLLKVKANIIYPGHGP 201
Cdd:cd16276 110 LELSYFgPNHGPGNIVIYLPKQKVLMAVDLINPGWVPFFnfagsEDIPGYIEALDELLEYDFDTFVGGHGN 180
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 12-86 3.17e-06

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 47.58  E-value: 3.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  12 SSRVVRVLGCNPGPMTLQG------TNTYLVGTGSRRILIDTGePSvpeyISCLKQALAEFDTAIQEILVTHWHRDHSGG 85
Cdd:COG1235  10 SSGGVPQIGCDCPVCASTDprygrtRSSILVEADGTRLLIDAG-PD----LREQLLRLGLDPSKIDAILLTHEHADHIAG 84


                .
gi 66730449  86 I 86
Cdd:COG1235  85 L 85
Sfh-1-like_MBL-B2 cd16305
Serratia fonticola Sfh-I and related metallo-beta-lactamases, subclass B2; MBL-fold ...
 24-207 7.35e-06

Serratia fonticola Sfh-I and related metallo-beta-lactamases, subclass B2; 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. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis.


Pssm-ID: 293863  Cd Length: 226  Bit Score: 46.14  E-value: 7.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  24 GPMTLQGTNTY-----LVGTGSRRILIdTGEPSVPEYISCLKQALAEFDT-AIQEILVTHWHRDHSGGIVDI----CKNI 93
Cdd:cd16305   8 GPLYIVEDKEYvqensMVYIGTDGITI-IGATWTPETAETLEKEIRKVSPlPIKEVINTNYHTDRAGGNAYWktlgASIV 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  94 SNDATYCIKKlrrnPQKEEIIG---SGEQQYVYIED--------GDLiKTEGATLRVLYT-PGHTDDHMALLLEEENAIF 161
Cdd:cd16305  87 STQMTYDLEK----SQWGSIVDftrQGNNKYPNLEKslpdtvypGDF-NLQNGSVRALYLgEAHTEDGIFVYFPAERVLY 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 66730449 162 sGDCILGE--GTTIFEDLSDYMNSLKDLL------KVKANIIYPGHGPVIHNAE 207
Cdd:cd16305 162 -GNCILKEklGNMSFANRTEYPKTLKKLKglieqgELKVESIIAGHDTPIHDVE 214
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 34-146 1.31e-05

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: 45.39  E-value: 1.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  34 YLVGTGSRRILIDTG-EPSVPEYISCLKQaLAeFDTA-IQEILVTHWHRDHSGGIVDIcKNISnDATYCIKKlrrnPQKE 111
Cdd:cd16288  25 YLITTPQGLILIDTGlESSAPMIKANIRK-LG-FKPSdIKILLNSHAHLDHAGGLAAL-KKLT-GAKLMASA----EDAA 96

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 66730449 112 EIIGSGEQQYVY---------------IEDGDLIKTEGATLRVLYTPGHT 146
Cdd:cd16288  97 LLASGGKSDFHYgddslafppvkvdrvLKDGDRVTLGGTTLTAHLTPGHT 146
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
16-86 1.63e-05

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 45.19  E-value: 1.63e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66730449  16 VRVLGCNpGPMTLQGTNT--YLVGTGSRRILIDTGEPSVpeyisclkQALAEFDTAIQE---ILVTHWHRDHSGGI 86
Cdd:COG1234   3 LTFLGTG-GAVPTPGRATssYLLEAGGERLLIDCGEGTQ--------RQLLRAGLDPRDidaIFITHLHGDHIAGL 69
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 35-89 1.96e-05

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; 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 named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 44.39  E-value: 1.96e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66730449  35 LVGTGSRRILIDTGepsvPEyiscLK-QALAEFDTAIQEILVTHWHRDHSGGIVDI 89
Cdd:cd16279  39 LIETGGKNILIDTG----PD----FRqQALRAGIRKLDAVLLTHAHADHIHGLDDL 86
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 41-145 3.16e-05

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: 43.84  E-value: 3.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449    41 RRILIDTGePSVPEYISCLKQALAEFDTAIQEILVTHWHRDHSGGIVDICKnISNDATYCIKK----LRRNPQKEEIIGS 116
Cdd:pfam12706   1 RRILIDPG-PDLRQQALPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDLRE-GRPRPLYAPLGvlahLRRNFPYLFLLEH 78

                          90       100
                  ....*....|....*....|....*....
gi 66730449   117 GEQQYVYIEDGDLIKTEGATLRVLYTPGH 145
Cdd:pfam12706  79 YGVRVHEIDWGESFTVGDGGLTVTATPAR 107
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 30-98 4.69e-05

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 43.65  E-value: 4.69e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66730449   30 GTNTYLVGTGSRRILID---TGEPSVPeyiscLKqaLAEFDTAIqeILVTHWHRDHSGGIVDICKNisNDAT 98
Cdd:PRK00685   7 GHSAFLIETGGKKILIDpfiTGNPLAD-----LK--PEDVKVDY--ILLTHGHGDHLGDTVEIAKR--TGAT 67
IMP_DIM-like_MBL-B1 cd16301
IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 74-202 6.67e-05

IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the acquired MBLs IMP-1(a beta-lactamase that is active on imipenem), DIM-1 (Dutch imipenemase), GIM-1 (German imipenemase), KHM-1 (Kyorin Health Science MBL 1), SIM-1 (Seoul imipenemase), and TMB-1 (Tripoli metallo-beta-lactamase). IMP-1, DIM-1, GIM-1, SIM-1, and TMB-1 are Class 1 integron-mediated MBLs, KMH-1 is plasmid-mediated. 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 acquired MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293859 [Multi-domain]  Cd Length: 215  Bit Score: 43.04  E-value: 6.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  74 LVTHWHRDHSGGI-VDICKNISNDATYCIKKLRRNPQKE---EIIGSGEQQYVyiedGDLIKTegatlrvlYTP--GHTD 147
Cdd:cd16301  70 ISTHFHEDRTGGIgYLNSHSIPTYASELTNQLLKKNGKElatHSFSGDEFWLL----KGKIEV--------FYPgaGHTK 137

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66730449 148 DHMALLLEEENAIFSGdCIL------GEGTTIFEDLSDYMNSLKDLL--KVKANIIYPGHGPV 202
Cdd:cd16301 138 DNLVVWLPKEKILFGG-CLVksleskGLGNTGDASISQWPASAQKVLskYPNAKLVVPGHGKV 199
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 46-199 1.51e-04

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 42.44  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449   46 DTGEPSV--PEYISCLKQALAEFDTAIQEILVTHWHRDHSGGIVDICKNISNDATYcikklrrNPQKEEIIGSGEQqyvy 123
Cdd:PLN02469  21 STKDAAVvdPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVY-------GGSLDNVKGCTHP---- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  124 IEDGDLIkTEGATLRV--LYTPGHTDDHMALLL----EEENAIFSGDC--ILG-----EGTT--IFEDLSDYMNSLKDLL 188
Cdd:PLN02469  90 VENGDKL-SLGKDVNIlaLHTPCHTKGHISYYVtgkeGEDPAVFTGDTlfIAGcgkffEGTAeqMYQSLCVTLGSLPKPT 168

                        170
                 ....*....|.
gi 66730449  189 KVkaniiYPGH 199
Cdd:PLN02469 169 QV-----YCGH 174
PRK05452 PRK05452
anaerobic nitric oxide reductase flavorubredoxin; Provisional
 27-235 1.60e-04

anaerobic nitric oxide reductase flavorubredoxin; Provisional


Pssm-ID: 235475 [Multi-domain]  Cd Length: 479  Bit Score: 42.82  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449   27 TLQGT--NTYLVGTGsRRILIDTGE-PSVPEYISCLKqalAEFDTA-IQEILVTHWHRDHSGGIVDICKNISNDATYC-- 100
Cdd:PRK05452  29 TLRGSsyNSYLIREE-KNVLIDTVDhKFSREFVQNLR---NEIDLAdIDYIVINHAEEDHAGALTELMAQIPDTPIYCta 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  101 -----IKKLRRNPqkeeiigsgEQQYVYIEDGDLIKT-EGATLRVLYTPG-HTDDHMALLLEEENAIFSGDCiLGE---G 170
Cdd:PRK05452 105 naidsINGHHHHP---------EWNFNVVKTGDTLDIgNGKQLIFVETPMlHWPDSMMTYLTGDAVLFSNDA-FGQhycD 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  171 TTIFEDLSDYMNSLKDLLKVKANIIYP------------------------GHGPVIHNAEAKILE-YISHRNNREEQII 225
Cdd:PRK05452 175 EHLFNDEVDQTELFEQCQRYYANILTPfsrlvtpkiteilgfnlpvdmiatSHGVVWRDNPTQIVElYLKWAADYQEDRI 254

                        250
                 ....*....|
gi 66730449  226 TVFRDNLEES 235
Cdd:PRK05452 255 TIFYDTMSNN 264
CphS_ImiS-like_MBL-B2 cd16287
metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas ...
 124-207 2.48e-04

metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I. 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. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis.


Pssm-ID: 293845  Cd Length: 226  Bit Score: 41.65  E-value: 2.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 124 IEDGDLIKTEGaTLRVLYT-PGHTDDHMALLLEEENAIFSGdCILGE--GTTIFEDLSDYMNSLKDLLKVKANIIYP--- 197
Cdd:cd16287 124 VFPGDFNLQNG-SIRAMYLgEAHTKDGIFVYFPAERVLYGN-CILKEnlGNMSFANRTEYPKTLEKLKGLIEQGELKvds 201

                        90
                ....*....|...
gi 66730449 198 ---GHGPVIHNAE 207
Cdd:cd16287 202 iiaGHDTPIHDVG 214
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 31-87 7.83e-04

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 39.55  E-value: 7.83e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 66730449  31 TNTYL-VGTGSRRILIDTGEPSVPEyiscLKQALAEFDtAIQEILVTHWHRDHSGGIV 87
Cdd:cd07740  15 LNTCFhVASEAGRFLIDCGASSLIA----LKRAGIDPN-AIDAIFITHLHGDHFGGLP 67
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
34-136 8.36e-04

Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440850  Cd Length: 273  Bit Score: 40.25  E-value: 8.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  34 YLVGTGSRRILIDTGEPSVpeYISCLKQA---LAEFDTAIqeilVTHWHRDHSGGIVDICKNISNDATYC-----IKKLR 105
Cdd:COG1237  25 ALIETEGKRILFDTGQSDV--LLKNAEKLgidLSDIDAVV----LSHGHYDHTGGLPALLELNPKAPVYAhpdafEKRYS 98

                        90       100       110
                ....*....|....*....|....*....|.
gi 66730449 106 RNPQKEEIIGSGEQQYVYIEDGDLIKTEGAT 136
Cdd:COG1237  99 KRPGGKYIGIPFSREELEKLGARLILVKEPT 129
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 16-90 1.31e-03

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: 38.58  E-value: 1.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  16 VRVLGCN---PGPmtLQGTNTYLVGTGSRRILIDTGE---PSVPEYIsclkqALAEFDTaiqeILVTHWHRDHsggIVDI 89
Cdd:cd07716   2 LTVLGCSgsyPGP--GGACSGYLLEADGFRILLDCGSgvlSRLQRYI-----DPEDLDA----VVLSHLHPDH---CADL 67


                .
gi 66730449  90 C 90
Cdd:cd07716  68 G 68
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-87 1.57e-03

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


Pssm-ID: 293839  Cd Length: 252  Bit Score: 39.02  E-value: 1.57e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66730449  35 LVGTGSRRILIDTG-----EPSVPEYI-----SCLKQALAEFDTAIQEI---LVTHWHRDHSGGIV 87
Cdd:cd16281  47 LIETGGRNILIDTGigdkqDPKFRSIYvqhseHSLLKSLARLGLSPEDItdvILTHLHFDHCGGAT 112
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 30-87 1.95e-03

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


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 38.40  E-value: 1.95e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66730449  30 GTNTYLVGTGSRRILIDTGEPSVpeyisclkQALAEFDTAIQE---ILVTHWHRDHSGGIV 87
Cdd:cd16272  16 NTSSYLLETGGTRILLDCGEGTV--------YRLLKAGVDPDKldaIFLSHFHLDHIGGLP 68
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 34-95 4.19e-03

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


Pssm-ID: 293799  Cd Length: 269  Bit Score: 37.99  E-value: 4.19e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66730449  34 YLVGTGSRRILIDTGEPSVpeyisCLKQA------LAEFDTAIqeilVTHWHRDHSGGIVDICKNISN 95
Cdd:cd07713  23 LLIETEGKKILFDTGQSGV-----LLHNAkklgidLSDIDAVV----LSHGHYDHTGGLKALLELNPK 81
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 32-200 5.34e-03

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


Pssm-ID: 293860  Cd Length: 212  Bit Score: 37.22  E-value: 5.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449  32 NTYLVGTGSRRILIDT--GEPSVPEYISCLKQalaEFDTAIQEILVTHWHRDHSGGIVDICKNisNDATYC----IKKLR 105
Cdd:cd16302  28 NGMIVINGGEAVVFDTptNDSQSEELIDWIEN---SLKAKVKAVVPTHFHDDCLGGLKAFHRR--GIPSYAnqktIALAK 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730449 106 RNPQKEEIIGsgeqqyvyIEDGDLIKTEGATLRVLY-TPGHTDDHMALLLEEENAIFSGdCILGEGTTIFEDLSD----- 179
Cdd:cd16302 103 EKGLPVPQHG--------FSDSLTLKLGGKKIVCRYfGEGHTKDNIVVYFPSEKVLFGG-CMVKSLGAGKGNLEDanvea 173

                       170       180
                ....*....|....*....|....
gi 66730449 180 ---YMNSLKDLLKvKANIIYPGHG 200
Cdd:cd16302 174 wpkTVEKVKAKYP-DVKIVIPGHG 196
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 23-82 8.56e-03

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 36.82  E-value: 8.56e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66730449  23 PGPMTLQ--GTNTYLVGTGSRRILID---TGEPSVPEYISCLKQALAEFDTaiqeILVTHWHRDH 82
Cdd:COG2220   1 PGGMKITwlGHATFLIETGGKRILIDpvfSGRASPVNPLPLDPEDLPKIDA----VLVTHDHYDH 61
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 34-86 9.43e-03

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


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 36.28  E-value: 9.43e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 66730449  34 YLVGTGSRRILIDTGepSVPEYISCLKQALAEFDTAIQEI---LVTHWHRDHSGGI 86
Cdd:cd16295  15 YLLETGGKRILLDCG--LFQGGKELEELNNEPFPFDPKEIdavILTHAHLDHSGRL 68
 
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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