NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|7705793|ref|NP_057111|]
View 

endoribonuclease LACTB2 [Homo sapiens]

Protein Classification

beta-lactamase-like protein 2( domain architecture ID 14403984)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 5.15e-113

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: 323.72  E-value: 5.15e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   14 RVVRVLGCNPGPMTLQGTNTYLVGTGPRRILIDTGEPaIPEYISCLKQALTEFNTA-IQEIVVTHWHRDHSGGIGDICKS 92
Cdd:cd07722   1 RVIRILGQNPGPFTLQGTNTYLVGTGKRRILIDTGEG-RPSYIPLLKSVLDSEGNAtISDILLTHWHHDHVGGLPDVLDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   93 INnDTTYCIKKLPRNPQREEIIGNGEQqYVYLKDGDVIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGTT 172
Cdd:cd07722  80 LR-GPSPRVYKFPRPEEDEDPDEDGGD-IHDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGDCVLGHGTA 157

                       170       180       190
                ....*....|....*....|....*....|.
gi 7705793  173 VFEDLYDYMNSLKELLKIKADIIYPGHGPVI 203
Cdd:cd07722 158 VFEDLAAYMASLKKLLSLGPGRIYPGHGPVI 188
BLACT_WH super family cl38958
Beta-lactamase associated winged helix domain; This winged helix domain is found at the ...
 237-284 1.18e-04

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


The actual alignment was detected with superfamily member pfam17778:

Pssm-ID: 407650  Cd Length: 46  Bit Score: 38.75  E-value: 1.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 7705793    237 TVMELVKIIYKNTPENLHEMAKHNLLLHLKKLEKEGKIFSntDPDKKW 284
Cdd:pfam17778   1 TAMELVKVIYKDVPESLHPAAERGVLAHLEKLEAEGKVVR--EGDGKW 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 5.15e-113

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: 323.72  E-value: 5.15e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   14 RVVRVLGCNPGPMTLQGTNTYLVGTGPRRILIDTGEPaIPEYISCLKQALTEFNTA-IQEIVVTHWHRDHSGGIGDICKS 92
Cdd:cd07722   1 RVIRILGQNPGPFTLQGTNTYLVGTGKRRILIDTGEG-RPSYIPLLKSVLDSEGNAtISDILLTHWHHDHVGGLPDVLDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   93 INnDTTYCIKKLPRNPQREEIIGNGEQqYVYLKDGDVIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGTT 172
Cdd:cd07722  80 LR-GPSPRVYKFPRPEEDEDPDEDGGD-IHDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGDCVLGHGTA 157

                       170       180       190
                ....*....|....*....|....*....|.
gi 7705793  173 VFEDLYDYMNSLKELLKIKADIIYPGHGPVI 203
Cdd:cd07722 158 VFEDLAAYMASLKKLLSLGPGRIYPGHGPVI 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 23-230 2.61e-37

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 131.74  E-value: 2.61e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   23 PGPMTLQGTNTYLVGTGPRRILIDTGEPaiPEYISCLKQALTEFNTAIQEIVVTHWHRDHSGGIGDICKSIN-------N 95
Cdd:COG0491   7 GTPGAGLGVNSYLIVGGDGAVLIDTGLG--PADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGapvyahaA 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   96 DTTYCIKKLPRNPQREEIIgngeQQYVYLKDGDVIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGTTvFE 175
Cdd:COG0491  85 EAEALEAPAAGALFGREPV----PPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVG-RP 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  176 DLYD-----YMNSLKELLKIKADIIYPGHGPVIHNAEAKiqqyishrniREQQILTLFRE 230
Cdd:COG0491 160 DLPDgdlaqWLASLERLLALPPDLVIPGHGPPTTAEAID----------YLEELLAALGE 209
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 32-199 3.79e-35

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: 124.97  E-value: 3.79e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793      32 NTYLVGTGPRRILIDTGEPAIPEYISCLKQALTEfntAIQEIVVTHWHRDHSGGIGDIcKSINNDTTYC-------IKKL 104
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPK---KIDAIILTHGHPDHIGGLPEL-LEAPGAPVYApegtaelLKDL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793     105 PRNPQREEIIGNGEQQYVYLKDGDVIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGT------TVFEDLY 178
Cdd:smart00849  77 LALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDgrtlvdGGDAAAS 156

                          170       180
                   ....*....|....*....|.
gi 7705793     179 DYMNSLKELLKIKADIIYPGH 199
Cdd:smart00849 157 DALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
26-199 2.81e-20

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 86.27  E-value: 2.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793     26 MTLQGTNTYLVGTGPRRILIDTGEPAIPEYISCLKQALTEfNTAIQEIVVTHWHRDHSGGIGDICKSINNDTTYCIKKLP 105
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLG-PKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793    106 RNPQREEIIGNGEQQYVY-----------LKDGDVIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGD---------- 164
Cdd:pfam00753  80 ELLDEELGLAASRLGLPGppvvplppdvvLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDllfageigrl 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 7705793    165 -CILGEGTTVF-EDLYDYMNSLKELLKIKADIIYPGH 199
Cdd:pfam00753 160 dLPLGGLLVLHpSSAESSLESLLKLAKLKAAVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 62-199 9.29e-09

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 55.62  E-value: 9.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793    62 ALTEFNTAIQEIVVTHWHRDHSGGIGDIcksinnDTTYCIKKLPRNPQREEIIGNGeqqyVYLKDGDVIKTEGATLRVLY 141
Cdd:PLN02398 114 ALSRKNRNLTYILNTHHHYDHTGGNLEL------KARYGAKVIGSAVDKDRIPGID----IVLKDGDKWMFAGHEVLVME 183

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7705793   142 TPGHTDDHMALLLEEENAIFSGDCI-------LGEGTTvfEDLYdymNSLKELLKIKADI-IYPGH 199
Cdd:PLN02398 184 TPGHTRGHISFYFPGSGAIFTGDTLfslscgkLFEGTP--EQML---SSLQKIISLPDDTnIYCGH 244
BLACT_WH pfam17778
Beta-lactamase associated winged helix domain; This winged helix domain is found at the ...
 237-284 1.18e-04

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: 38.75  E-value: 1.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 7705793    237 TVMELVKIIYKNTPENLHEMAKHNLLLHLKKLEKEGKIFSntDPDKKW 284
Cdd:pfam17778   1 TAMELVKVIYKDVPESLHPAAERGVLAHLEKLEAEGKVVR--EGDGKW 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 5.15e-113

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: 323.72  E-value: 5.15e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   14 RVVRVLGCNPGPMTLQGTNTYLVGTGPRRILIDTGEPaIPEYISCLKQALTEFNTA-IQEIVVTHWHRDHSGGIGDICKS 92
Cdd:cd07722   1 RVIRILGQNPGPFTLQGTNTYLVGTGKRRILIDTGEG-RPSYIPLLKSVLDSEGNAtISDILLTHWHHDHVGGLPDVLDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   93 INnDTTYCIKKLPRNPQREEIIGNGEQqYVYLKDGDVIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGTT 172
Cdd:cd07722  80 LR-GPSPRVYKFPRPEEDEDPDEDGGD-IHDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGDCVLGHGTA 157

                       170       180       190
                ....*....|....*....|....*....|.
gi 7705793  173 VFEDLYDYMNSLKELLKIKADIIYPGHGPVI 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 8.14e-58

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: 183.46  E-value: 8.14e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   14 RVVRVLGCNPGPMTLQGTNTYLVGTGPRRILIDTGePAIPEYISCLKQALTEFNtaIQEIVVTHWHRDHSGGIGDIcksi 93
Cdd:cd16278   1 GVRRVLAPNPSPMTLDGTNTYLLGAPDGVVVIDPG-PDDPAHLDALLAALGGGR--VSAILVTHTHRDHSPGAARL---- 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   94 nndttyciKKLPRNPqreeIIGNGEQQYVY----------LKDGDVIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSG 163
Cdd:cd16278  74 --------AERTGAP----VRAFGPHRAGGqdtdfapdrpLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTG 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 7705793  164 DCILGEGTTVFE----DLYDYMNSLKELLKIKADIIYPGHGPVI 203
Cdd:cd16278 142 DHVMGWSTTVIAppdgDLGDYLASLERLLALDDRLLLPGHGPPI 185
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 23-230 2.61e-37

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 131.74  E-value: 2.61e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   23 PGPMTLQGTNTYLVGTGPRRILIDTGEPaiPEYISCLKQALTEFNTAIQEIVVTHWHRDHSGGIGDICKSIN-------N 95
Cdd:COG0491   7 GTPGAGLGVNSYLIVGGDGAVLIDTGLG--PADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGapvyahaA 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   96 DTTYCIKKLPRNPQREEIIgngeQQYVYLKDGDVIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGTTvFE 175
Cdd:COG0491  85 EAEALEAPAAGALFGREPV----PPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVG-RP 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  176 DLYD-----YMNSLKELLKIKADIIYPGHGPVIHNAEAKiqqyishrniREQQILTLFRE 230
Cdd:COG0491 160 DLPDgdlaqWLASLERLLALPPDLVIPGHGPPTTAEAID----------YLEELLAALGE 209
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 32-199 3.79e-35

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: 124.97  E-value: 3.79e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793      32 NTYLVGTGPRRILIDTGEPAIPEYISCLKQALTEfntAIQEIVVTHWHRDHSGGIGDIcKSINNDTTYC-------IKKL 104
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPK---KIDAIILTHGHPDHIGGLPEL-LEAPGAPVYApegtaelLKDL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793     105 PRNPQREEIIGNGEQQYVYLKDGDVIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGT------TVFEDLY 178
Cdd:smart00849  77 LALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDgrtlvdGGDAAAS 156

                          170       180
                   ....*....|....*....|.
gi 7705793     179 DYMNSLKELLKIKADIIYPGH 199
Cdd:smart00849 157 DALESLLKLLKLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 30-199 4.01e-34

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: 122.39  E-value: 4.01e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   30 GTNTYLVGTGPRR-ILIDTGEPAIPEyiscLKQALTEFNTAIQEIVVTHWHRDHSGGIGDICKS------INNDTTYCIK 102
Cdd:cd06262   9 QTNCYLVSDEEGEaILIDPGAGALEK----ILEAIEELGLKIKAILLTHGHFDHIGGLAELKEApgapvyIHEADAELLE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  103 KLPRNPQRE-EIIGNGEQQYVYLKDGDVIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCIL--GEGTTVFE--DL 177
Cdd:cd06262  85 DPELNLAFFgGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFagSIGRTDLPggDP 164

                       170       180
                ....*....|....*....|....
gi 7705793  178 YDYMNSLKELLKIKAD--IIYPGH 199
Cdd:cd06262 165 EQLIESIKKLLLLLPDdtVVYPGH 188
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 23-209 1.28e-32

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: 118.56  E-value: 1.28e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   23 PGPMTLQGTNTYLVGTGPRRILIDTGePAIPEYISCLKQALTEFNTAIQEI---VVTHWHRDHSGGIGDICKSiNNDTTY 99
Cdd:cd07725   7 PLPGPLGHVNVYLLRDGDETTLIDTG-LATEEDAEALWEGLKELGLKPSDIdrvLLTHHHPDHIGLAGKLQEK-SGATVY 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  100 CIKKLPrnpqreeiigngeqqyvyLKDGDVIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGT-------- 171
Cdd:cd07725  85 ILDVTP------------------VKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLPKITpnvslwav 146

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 7705793  172 TVFEDLYDYMNSLKELLKIKADIIYPGHGPVIHNAEAK 209
Cdd:cd07725 147 RVEDPLGAYLESLDKLEKLDVDLAYPGHGGPIKDPKAR 184
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 34-199 5.21e-29

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: 108.32  E-value: 5.21e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   34 YLVGTGPRR--ILIDTGEPAIpeyiscLKQALTEFNTAIQEIVVTHWHRDHSGGIGDICKSINNDTTYCikklprnPQRE 111
Cdd:cd07723  12 YLIVDEATGeaAVVDPGEAEP------VLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYG-------PAED 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  112 EIIGNGEQqyvyLKDGDVIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDC--ILG-----EGTtvFEDLYDymnSL 184
Cdd:cd07723  79 RIPGLDHP----VKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTlfSGGcgrffEGT--AEQMYA---SL 149

                       170
                ....*....|....*.
gi 7705793  185 KELLKIKADI-IYPGH 199
Cdd:cd07723 150 QKLLALPDDTlVYCGH 165
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 32-200 3.48e-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: 107.31  E-value: 3.48e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   32 NTYLVGTGPRRILIDTGEPAIPEYIsclKQALTEFNTAIQE---IVVTHWHRDHSGGIGDICKSIN-------NDTTYCI 101
Cdd:cd07721  12 NAYLIEDDDGLTLIDTGLPGSAKRI---LKALRELGLSPKDirrILLTHGHIDHIGSLAALKEAPGapvyaheREAPYLE 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  102 KKLPRNPQREEIIGNGEQQYV---------YLKDGDVIKTEGAtLRVLYTPGHTDDHMALLLEEENAIFSGDCILGEGTT 172
Cdd:cd07721  89 GEKPYPPPVRLGLLGLLSPLLpvkpvpvdrTLEDGDTLDLAGG-LRVIHTPGHTPGHISLYLEEDGVLIAGDALVTVGGE 167

                       170       180       190
                ....*....|....*....|....*....|....*
gi 7705793  173 VF-------EDLYDYMNSLKELLKIKADIIYPGHG 200
Cdd:cd07721 168 LVpppppftWDMEEALESLRKLAELDPEVLAPGHG 202
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 33-199 2.93e-24

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: 97.18  E-value: 2.93e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   33 TYLVGTGPRRILIDTG-EPAIPEYISCLkQALTEFNTAIQEIVVTHWHRDHSGGIGDICKSINNDTTYC----IKKLPrN 107
Cdd:cd07726  18 SYLLDGEGRPALIDTGpSSSVPRLLAAL-EALGIAPEDVDYIILTHIHLDHAGGAGLLAEALPNAKVYVhprgARHLI-D 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  108 PQR-----EEIIGNGEQQYVY------------LKDGDVIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCI---L 167
Cdd:cd07726  96 PSKlwasaRAVYGDEADRLGGeilpvpeervivLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDAAgvrY 175

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 7705793  168 GEGTTVFE--------DLYDYMNSLKELLKIKADIIYPGH 199
Cdd:cd07726 176 PELDVVGPpstpppdfDPEAWLESLDRLLSLKPERIYLTH 215
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 30-200 4.06e-24

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: 95.93  E-value: 4.06e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   30 GTNTYLVGTGPRR--ILIDTGEPAIPEYIsclkQALTEFNTAIQEIVVTHWHRDHSGGIGDICKSInnDTTYCIKKLprn 107
Cdd:cd07724  11 GTLSYLVGDPETGeaAVIDPVRDSVDRYL----DLAAELGLKITYVLETHVHADHVSGARELAERT--GAPIVIGEG--- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  108 pqreeiiGNGEQQYVYLKDGDVIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCIL----------GEGTTVFEDL 177
Cdd:cd07724  82 -------APASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFvgdvgrpdlpGEAEGLARQL 154

                       170       180
                ....*....|....*....|....*
gi 7705793  178 YDymnSLKELLKIKAD--IIYPGHG 200
Cdd:cd07724 155 YD---SLQRKLLLLPDetLVYPGHD 176
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 29-199 3.04e-21

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: 88.45  E-value: 3.04e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   29 QGTNTYLVgTGPRR-ILIDTG--EPAIPEYIsclkQALTEFNTaiqEIVVTHWHRDHSGGIG------------DICKSI 93
Cdd:cd07712   7 DRVNIYLL-RGRDRaLLIDTGlgIGDLKEYV----RTLTDLPL---LVVATHGHFDHIGGLHefeevyvhpadaEILAAP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   94 NNDTTYCIKKLPRNPQREEIIGNgeqqyvyLKDGDVIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDcILGEGTTV 173
Cdd:cd07712  79 DNFETLTWDAATYSVPPAGPTLP-------LRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGD-VVYDGPLI 150

                       170       180       190
                ....*....|....*....|....*....|..
gi 7705793  174 FE----DLYDYMNSLKELLKIK--ADIIYPGH 199
Cdd:cd07712 151 MDlphsDLDDYLASLEKLSKLPdeFDKVLPGH 182
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
26-199 2.81e-20

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 86.27  E-value: 2.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793     26 MTLQGTNTYLVGTGPRRILIDTGEPAIPEYISCLKQALTEfNTAIQEIVVTHWHRDHSGGIGDICKSINNDTTYCIKKLP 105
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLG-PKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793    106 RNPQREEIIGNGEQQYVY-----------LKDGDVIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGD---------- 164
Cdd:pfam00753  80 ELLDEELGLAASRLGLPGppvvplppdvvLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDllfageigrl 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 7705793    165 -CILGEGTTVF-EDLYDYMNSLKELLKIKADIIYPGH 199
Cdd:pfam00753 160 dLPLGGLLVLHpSSAESSLESLLKLAKLKAAVIVPGH 196
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 24-202 1.71e-19

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: 84.32  E-value: 1.71e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   24 GPMtlqGTNTYLVGT--GPRRILIDTGEPAipeyiSCLKQALTEFNTAIQEIVVTHWHRDHSGGIGDIcKSINNDTTYCI 101
Cdd:cd16322   7 GPL---QENTYLVADegGGEAVLVDPGDES-----EKLLARFGTTGLTLLYILLTHAHFDHVGGVADL-RRHPGAPVYLH 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  102 K---KLPRNPQREEIIG--NGEQQY---VYLKDGDVIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCILgEGTTV 173
Cdd:cd16322  78 PddlPLYEAADLGAKAFglGIEPLPppdRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLF-QGSIG 156

                       170       180       190
                ....*....|....*....|....*....|....*
gi 7705793  174 FEDL-----YDYMNSLKELLKIKADI-IYPGHGPV 202
Cdd:cd16322 157 RTDLpggdpKAMAASLRRLLTLPDETrVFPGHGPP 191
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 34-199 8.19e-15

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: 72.25  E-value: 8.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   34 YLVGTGPRRILIDTG------------EPAIPEYIS---CLKQALTEFNTAIQEI---VVTHWHRDHSGGIGDICKSinn 95
Cdd:cd07729  35 YLIEHPEGTILVDTGfhpdaaddpgglELAFPPGVTeeqTLEEQLARLGLDPEDIdyvILSHLHFDHAGGLDLFPNA--- 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   96 dTTYCIKK-----LPRNPQREEIIGNGEQQYVYLKDGDVIKTEGAT-----LRVLYTPGHTDDHMALL--LEEENAIFSG 163
Cdd:cd07729 112 -TIIVQRAeleyaTGPDPLAAGYYEDVLALDDDLPGGRVRLVDGDYdlfpgVTLIPTPGHTPGHQSVLvrLPEGTVLLAG 190

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 7705793  164 DCI-----LGEG-----TTVFEDLYDYMNSLKELLKIKADIIYPGH 199
Cdd:cd07729 191 DAAytyenLEEGrppgiNYDPEAALASLERLKALAEREGARVIPGH 236
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 22-201 1.41e-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: 70.31  E-value: 1.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   22 NPGPMTLQGTNTyLVGTGPRRILIDTGEPAIPEYiscLKQALTEFNTA---IQEIVVTHWHRDHSGGIGDICKSINNDTT 98
Cdd:cd07711  14 SDGGFRASSTVT-LIKDGGKNILVDTGTPWDRDL---LLKALAEHGLSpedIDYVVLTHGHPDHIGNLNLFPNATVIVGW 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   99 YCIKKLPRNPQREEIIGngeqqyvYLKDGDViktegatlRVLYTPGHTDDHMALLLEEENA---IFSGDCILGEGTT--- 172
Cdd:cd07711  90 DICGDSYDDHSLEEGDG-------YEIDENV--------EVIPTPGHTPEDVSVLVETEKKgtvAVAGDLFEREEDLedp 154

                       170       180       190
                ....*....|....*....|....*....|....
gi 7705793  173 -----VFEDLYDYMNSLKELLKIkADIIYPGHGP 201
Cdd:cd07711 155 ilwdpLSEDPELQEESRKRILAL-ADWIIPGHGP 187
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 59-199 5.60e-13

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: 66.04  E-value: 5.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   59 LKQALTEFNTAIQEIVVTHWHRDHSGGIGDICKSIN-------NDTTYCIKKLPrnPQREEIIGNGEQQYV---YLKDGD 128
Cdd:cd07737  36 ILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGvpiigphKEDKFLLENLP--EQSQMFGFPPAEAFTpdrWLEEGD 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  129 VIKTEGATLRVLYTPGHTDDHMALLLEEENAIFSGDCIL--GEGTTVF-----EDLydyMNSLKELLKIKAD--IIYPGH 199
Cdd:cd07737 114 TVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFkgSIGRTDFpggnhAQL---IASIKEKLLPLGDdvTFIPGH 190
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 29-209 6.91e-13

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: 66.71  E-value: 6.91e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   29 QGTNTYLVGTGPRRILIDTGEPAIPEYISCLKQALtEFNTA-IQEIVVTHWHRDHSGGIGDICKSINNDTTYCIKKLPRN 107
Cdd:cd16310  20 KGIGSYLITSNHGAILLDGGLEENAALIEQNIKAL-GFKLSdIKIIINTHAHYDHAGGLAQLKADTGAKLWASRGDRPAL 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  108 PQREEIIGNGEQQYVY--------LKDGDVIKTEGATLRVLYTPGHTDD----HMALLLEEENAIFSGDCILGEGTTVFE 175
Cdd:cd16310  99 EAGKHIGDNITQPAPFpavkvdriLGDGEKIKLGDITLTATLTPGHTKGcttwSTTVKENGRPLRVVFPCSLSVAGNVLV 178

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 7705793  176 D-------LYDYMNSLKELLKIKADIIYPGHgPVIHNAEAK 209
Cdd:cd16310 179 GnktyptiVEDYRASFARLRAMKADIVLTSH-PEVADLLAR 218
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 31-203 8.40e-13

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: 66.36  E-value: 8.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   31 TNTYLVgTGPRRILIDTG-EPAIPEYISCLKQALTEfnTAIQEIVVTHWHRDHSGGIGDICKSINNDTTYCIKK----LP 105
Cdd:cd07709  32 YNSYLI-KDEKTALIDTVkEPFFDEFLENLEEVIDP--RKIDYIVVNHQEPDHSGSLPELLELAPNAKIVCSKKaarfLK 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  106 rnpqreEIIGNGEQQYVYLKDGDVIKTEGATLRVLYTPG-HTDDHMALLLEEENAIFSGDcILG---EGTTVFED----L 177
Cdd:cd07709 109 ------HFYPGIDERFVVVKDGDTLDLGKHTLKFIPAPMlHWPDTMVTYDPEDKILFSGD-AFGahgASGELFDDevedY 181

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 7705793  178 YDYM----------------NSLKELLKIKADIIYPGHGPVI 203
Cdd:cd07709 182 LEEArryyanimgpfskqvrKALEKLEALDIKMIAPSHGPIW 223
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 30-202 2.06e-12

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: 64.89  E-value: 2.06e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   30 GTNTYLVGTGPRRILIDTGepAIPEYISCLKQALTEFNTA-IQEIVVTHWHRDHSGG-----------IG--DICKSINN 95
Cdd:cd16282  14 ISNIGFIVGDDGVVVIDTG--ASPRLARALLAAIRKVTDKpVRYVVNTHYHGDHTLGnaafadagapiIAheNTREELAA 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   96 DTTYCIKKLPRNPqrEEIIGNGEQQY--VYLKDGDVIKTEGATLRVLYT-PGHTDDHMALLLEEENAIFSGDCILGEGTT 172
Cdd:cd16282  92 RGEAYLELMRRLG--GDAMAGTELVLpdRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEGVLFAGDLVFNGRIP 169

                       170       180       190
                ....*....|....*....|....*....|..
gi 7705793  173 VFED--LYDYMNSLKELLKIKADIIYPGHGPV 202
Cdd:cd16282 170 FLPDgsLAGWIAALDRLLALDATVVVPGHGPV 201
NorV COG0426
Flavorubredoxin [Energy production and conversion];
27-214 5.27e-12

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 65.24  E-value: 5.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   27 TLQGT--NTYLVgTGPRRILIDT-GEPAIPEYISCLKQALtefntAIQEI---VVTHWHRDHSGGIGDICKSINNDTTYC 100
Cdd:COG0426  28 TPRGTtyNSYLI-VDEKTALIDTvGESFFEEFLENLSKVI-----DPKKIdyiIVNHQEPDHSGSLPELLELAPNAKIVC 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  101 IKK----LPrnpqreEIIGNGEQQYVYLKDGDVIKTEGATLRVLYTPG-HTDDHMALLLEEENAIFSGDcILGE---GTT 172
Cdd:COG0426 102 SKKaarfLP------HFYGIPDFRFIVVKEGDTLDLGGHTLQFIPAPMlHWPDTMFTYDPEDKILFSGD-AFGShgaSDE 174

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7705793  173 VFEDLYD--------------YMNS-------LKELLKIKADIIYPGHGPVIHNaeaKIQQYI 214
Cdd:COG0426 175 LFDDEVDehleeearryyaniMMPFskqvlkaLKKVRGLDIDMIAPSHGPIWRG---NPKEIL 234
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 73-199 1.13e-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: 59.09  E-value: 1.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   73 IVVTHWHRDHSGGIGDICKsinndttycIKKLPRNPQREEIIGNGEQ--QYVYLKDGDVIKTEGATLRVLYTPGHTDDHM 150
Cdd:cd16275  51 ILLTHSHFDHVNLVEPLLA---------KYDAPVYMSKEEIDYYGFRcpNLIPLEDGDTIKIGDTEITCLLTPGHTPGSM 121

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7705793  151 ALLLeeENAIFSGDcilgegtTVF--------------EDLYDYMNSLKELLKIKAdIIYPGH 199
Cdd:cd16275 122 CYLL--GDSLFTGD-------TLFiegcgrcdlpggdpEEMYESLQRLKKLPPPNT-RVYPGH 174
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 43-205 5.25e-09

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: 55.58  E-value: 5.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   43 ILIDTGEPAipeyiSCLKQALTEFNTAIQE-----IVVTHWHRDHSGGIGDICKSINNDTT--YCIKKLPRNPQREEIIG 115
Cdd:cd07710  30 IIIDTLESA-----EAAKAALELFRKHTGDkpvkaIIYTHSHPDHFGGAGGFVEEEDSGKVpiIAPEGFMEEAVSENVLA 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  116 -----------------NGEQQYVYLKDG--------------DVIKTEGATLRV-------LYTPGHTDDHMALLLEEE 157
Cdd:cd07710 105 gnamsrraayqfgallpKGEKGQVGAGLGpglstgtvgfipptITITETGETLTIdgvelefQHAPGEAPDEMMVWLPDY 184

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7705793  158 NAIFSGDCILGegttVFEDLY-----------DYMNSLKELLKIKADIIYPGHGPVIHN 205
Cdd:cd07710 185 KVLFCADNVYH----TFPNLYtlrgakyrdalAWAKSLDEAISLKAEVLFPSHTWPVWG 239
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 62-199 9.29e-09

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 55.62  E-value: 9.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793    62 ALTEFNTAIQEIVVTHWHRDHSGGIGDIcksinnDTTYCIKKLPRNPQREEIIGNGeqqyVYLKDGDVIKTEGATLRVLY 141
Cdd:PLN02398 114 ALSRKNRNLTYILNTHHHYDHTGGNLEL------KARYGAKVIGSAVDKDRIPGID----IVLKDGDKWMFAGHEVLVME 183

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7705793   142 TPGHTDDHMALLLEEENAIFSGDCI-------LGEGTTvfEDLYdymNSLKELLKIKADI-IYPGH 199
Cdd:PLN02398 184 TPGHTRGHISFYFPGSGAIFTGDTLfslscgkLFEGTP--EQML---SSLQKIISLPDDTnIYCGH 244
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 70-202 2.97e-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: 52.93  E-value: 2.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   70 IQEIVVTHWHRDHSGGIgDICKSINNDT--TYCIKKLPRNPQREEIIGNGEQQYVYLKDGDVIKT---EGAT------LR 138
Cdd:cd07707  59 VTEVINTHFHTDRAGGN-AYLKERGAKTvsTALTRDLAKSEWAEIVAFTRKGLPEYPDLGYELPDgvlDGDFnlqfgkVE 137

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  139 VLYT-PGHTDDHMALLLEEENAIFsGDCILGE---GTTVFEDLYDYMNSLKELLKI--KADIIYPGHGPV 202
Cdd:cd07707 138 AFYPgPAHTPDNIVVYFPQENVLY-GGCIIKEtdlGNVADADVKEWPTSIERLKKRyrNIKAVIPGHGEV 206
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 30-204 5.01e-08

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: 51.81  E-value: 5.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   30 GTNTYLVGTGPRRILIDTgepaiPEYISCLKQALTEFNtAIQEIVVTHwhRDHSGG-------IGdiCKSI--NNDTTYc 100
Cdd:cd07727  14 GAASYLILRPEGNILVDS-----PRYSPPLAKRIEALG-GIRYIFLTH--RDDVADhakwaerFG--AKRIihEDDVNA- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  101 ikkLPRNPQREEIIGNGeqqYVYLKDGdviktegatLRVLYTPGHTDDHMALLLEEENAIFSGDCI----LGEGTTVFED 176
Cdd:cd07727  83 ---VTRPDEVIVLWGGD---PWELDPD---------LTLIPVPGHTRGSVVLLYKEKGVLFTGDHLawsrRRGWLSAFRY 147

                       170       180       190
                ....*....|....*....|....*....|...
gi 7705793  177 LYDYM-----NSLKELLKIKADIIYPGHGPVIH 204
Cdd:cd07727 148 VCWYSwpeqaESVERLADLDFEWVLPGHGRRVH 180
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 69-201 7.92e-08

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 51.43  E-value: 7.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   69 AIQEI--------VVTHWHRDHSGGiGDICKS-----INNDTTYciKKLPRNPQREEIIGNgeqqyVYLKDGDVIKTEGA 135
Cdd:cd16276  37 AIRKVtdkpvthvVYSHNHADHIGG-ASIFKDegatiIAHEATA--ELLKRNPDPKRPVPT-----VTFDDEYTLEVGGQ 108

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7705793  136 TLRVLYT-PGHTDDHMALLLEEENAIFSGDCILgEGTTVF------EDLYDYMNSLKELLKIKADIIYPGHGP 201
Cdd:cd16276 109 TLELSYFgPNHGPGNIVIYLPKQKVLMAVDLIN-PGWVPFfnfagsEDIPGYIEALDELLEYDFDTFVGGHGN 180
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 30-199 9.03e-08

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 51.38  E-value: 9.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   30 GTNTYLVGTGPRR-ILIDTGepaIPE-YISCLKQALTEFNTAIQEIVVTHWHRDHSGGIGDIcKSINNDTTYCIKK---L 104
Cdd:cd07743   7 PTNIGVYVFGDKEaLLIDSG---LDEdAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYL-QKKTGCKVYAPKIekaF 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  105 PRNPQREEIIGNGEQQYVYLK---------------DGDVIKTEGATLRVLYTPGHTDDHMALLLEEeNAIFSGDCILGE 169
Cdd:cd07743  83 IENPLLEPSYLGGAYPPKELRnkflmakpskvddiiEEGELELGGVGLEIIPLPGHSFGQIGILTPD-GVLFAGDALFGE 161

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 7705793  170 GttVFED-----LYD---YMNSLKELLKIKADIIYPGH 199
Cdd:cd07743 162 E--VLEKygipfLYDveeQLETLEKLEELDADYYVPGH 197
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 29-148 1.46e-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: 1.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   29 QGTNTYLVGTGPRRILIDTGEPAIPEY-----ISCLKQAltefntAIQEI---VVTHWHRDHSGGIGDICKSINNDTTYC 100
Cdd:COG2333  10 QGDAILIRTPDGKTILIDTGPRPSFDAgervvLPYLRAL------GIRRLdllVLTHPDADHIGGLAAVLEAFPVGRVLV 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 7705793  101 IKKLPRNPQREEIIGNGEQ---QYVYLKDGDVIKTEGATLRVLYTPGHTDD 148
Cdd:COG2333  84 SGPPDTSETYERLLEALKEkgiPVRPCRAGDTWQLGGVRFEVLWPPEDLLE 134
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 27-201 2.48e-07

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: 50.36  E-value: 2.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   27 TLQGT----NTYLVGTGPRRILIDT--GEPAIPEYISCLKQaltEFNTAIQEIVVTHWHRDHSGGIgDICKSINNDttyc 100
Cdd:cd16304  18 LFNGTpvpsNGLIVETSKGVVLIDTpwDDEQTEELLDWIKK---KLKKPVTLAIVTHAHDDRIGGI-KALQKRGIP---- 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  101 IKKLPRNPQREEIIGNGEQQYVyLKDGDVIKTEGATLRVLYT-PGHTDDHMALLLEEENAIFSGdCIL------GEGTTV 173
Cdd:cd16304  90 VYSTKLTAQLAKKQGYPSPDGI-LKDDTTLKFGNTKIETFYPgEGHTADNIVVWLPQSKILFGG-CLVksleakDLGNTA 167

                       170       180       190
                ....*....|....*....|....*....|
gi 7705793  174 FEDLYDYMNSLKELLKI--KADIIYPGHGP 201
Cdd:cd16304 168 DANLKEWPTSIRNVLKRypNAEIVVPGHGE 197
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 41-171 2.66e-07

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 50.59  E-value: 2.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793    41 RRILIDTGEPAiPeyiscLKQALTEFNTAIQEIVVTHWHRDHSGGIGDICKSINNDTTYcikklprNPQreEIIGNGEQQ 120
Cdd:PRK10241  23 RCLIVDPGEAE-P-----VLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVY-------GPQ--ETQDKGTTQ 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 7705793   121 YVylKDGDVIKTEGATLRVLYTPGHTDDHMALL----LEEENAIFSGDC-ILGEGT 171
Cdd:PRK10241  88 VV--KDGETAFVLGHEFSVFATPGHTLGHICYFskpyLFCGDTLFSGGCgRLFEGT 141
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 25-146 3.10e-07

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


Pssm-ID: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 50.25  E-value: 3.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   25 PMTLQGtNTYLVGTG---------PR-RILIDTGEPAIPEYISCLKQALTEFNTAIQEIVVTHWHRDHSGGIGDICKSIN 94
Cdd:cd16313   7 PFQIYG-NTYYVGTGgisavlitsPQgHILIDGGFPKSPEQIAASIRQLGFKLEDVKYILSSHDHWDHAGGIAALQKLTG 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7705793   95 NDTTYCIKKLPrnPQREEIIGNGEQQYVYL------------KDGDVIKTEGATLRVLYTPGHT 146
Cdd:cd16313  86 AQVLASPATVA--VLRSGSMGKDDPQFGGLtpmppvasvravRDGEVVKLGPLAVTAHATPGHT 147
MUS_TUS_MBL-B1 cd16318
Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; ...
 31-199 3.32e-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: 50.04  E-value: 3.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   31 TNTYLVGTGPRRILIDTgepaiP----EYISCLKQALTEFNTAIQEIVVTHWHRDHSGGIGDICKSINNDTTYCIKK--- 103
Cdd:cd16318  26 SNSMYVLTDEGVILIDT-----PwdkdQYEPLLEYIRSNHNKEVKWVITTHFHEDRSGGLGYFNSIGAQTYTYALTNeil 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  104 LPRNPQREEIIGNGEQQYVYLKDGDVIKTEGAtlrvlytpGHTDDHMALLLEEEnAIFSGDCIL--GEGTTV-------F 174
Cdd:cd16318 101 KERNEPQAQFSFNKEKQFTFGNEKLAVYFLGE--------GHSLDNTVVWFPKE-EVLYGGCLIksAEATTIgniadgnV 171

                       170       180
                ....*....|....*....|....*
gi 7705793  175 EDLYDYMNSLKELLKiKADIIYPGH 199
Cdd:cd16318 172 IAWPKTIEAVKQKFK-NAKVIIPGH 195
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 35-148 4.44e-07

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 49.05  E-value: 4.44e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   35 LVGTGPRRILIDTGEPAIPEY---ISCLKQaltEFNTAIQEIVVTHWHRDHSGGIGDICKSINNDTTYCIKKLPRNPQRE 111
Cdd:cd07731  14 LIQTPGKTILIDTGPRDSFGEdvvVPYLKA---RGIKKLDYLILTHPDADHIGGLDAVLKNFPVKEVYMPGVTHTTKTYE 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 7705793  112 EI---IGNGEQQYVYLKDGDVIKTEGATLRVLYTPGHTDD 148
Cdd:cd07731  91 DLldaIKEKGIPVTPCKAGDRWQLGGVSFEVLSPPKDDYD 130
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 23-166 2.38e-06

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


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 47.54  E-value: 2.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   23 PGPMTLqGTNTYLVGTGPRRILIDTG-----EPAIPEYISCLKQA-LT-EfntAIQEIVVTHWHRDHSGGIgdicksINN 95
Cdd:cd07720  42 PDPVET-SVNAFLVRTGGRLILVDTGagglfGPTAGKLLANLAAAgIDpE---DIDDVLLTHLHPDHIGGL------VDA 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   96 DttyciKKL--PR--------------NPQREEIIGNGEQQYVY--------LKDGDVIKTEGATL---RVLYTPGHTDD 148
Cdd:cd07720 112 G-----GKPvfPNaevhvseaewdfwlDDANAAKAPEGAKRFFDaardrlrpYAAAGRFEDGDEVLpgiTAVPAPGHTPG 186

                       170       180
                ....*....|....*....|
gi 7705793  149 HMALLLE--EENAIFSGDCI 166
Cdd:cd07720 187 HTGYRIEsgGERLLIWGDIV 206
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 2.64e-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: 47.73  E-value: 2.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   25 PMTLQGtNTYLVGT-GPRRILIDTGE-------------PAIPEYISCLKQALTEfntaIQEIVVTHWHRDHSGGIGDIC 90
Cdd:cd16290   7 PFRIHG-NTYYVGTgGLSAVLITSPQglilidgalpqsaPQIEANIRALGFRLED----VKLILNSHAHFDHAGGIAALQ 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7705793   91 K---------SINNDTTYCIKKLPRNPQREEIIG-NGEQQYVYLKDGDVIKTEGATLRVLYTPGHT 146
Cdd:cd16290  82 RdsgatvaasPAGAAALRSGGVDPDDPQAGAADPfPPVAKVRVVADGEVVKLGPLAVTAHATPGHT 147
Sfh-1-like_MBL-B2 cd16305
Serratia fonticola Sfh-I and related metallo-beta-lactamases, subclass B2; MBL-fold ...
 53-215 3.01e-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: 47.30  E-value: 3.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   53 PEYISCLKQALTEFNT-AIQEIVVTHWHRDHSGG------IGdiCKSINNDTTYCIKKlprnPQREEIIG---NGEQQYV 122
Cdd:cd16305  41 PETAETLEKEIRKVSPlPIKEVINTNYHTDRAGGnaywktLG--ASIVSTQMTYDLEK----SQWGSIVDftrQGNNKYP 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  123 YLKD--------GDvIKTEGATLRVLYT-PGHTDDHMALLLEEENAIFsGDCILGE--GTTVFEDLYDYMNSLKELL--- 188
Cdd:cd16305 115 NLEKslpdtvypGD-FNLQNGSVRALYLgEAHTEDGIFVYFPAERVLY-GNCILKEklGNMSFANRTEYPKTLKKLKgli 192

                       170       180       190
                ....*....|....*....|....*....|
gi 7705793  189 ---KIKADIIYPGHGPVIHNAEAkIQQYIS 215
Cdd:cd16305 193 eqgELKVESIIAGHDTPIHDVEL-IDHYLT 221
PRK11921 PRK11921
anaerobic nitric oxide reductase flavorubredoxin;
32-215 3.24e-06

anaerobic nitric oxide reductase flavorubredoxin;


Pssm-ID: 237023 [Multi-domain]  Cd Length: 394  Bit Score: 47.76  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793    32 NTYLVGTGpRRILIDT-GEPAIPEYISCLKQaltEFN-TAIQEIVVTHWHRDHSGGIGDICKSINNDTTYCIKKlprnpQ 109
Cdd:PRK11921  34 NSYLIKDE-KTVLIDTvWQPFAKEFVENLKK---EIDlDKIDYIVANHGEIDHSGALPELMKEIPDTPIYCTKN-----G 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   110 REEIIGNGEQ--QYVYLKDGDVIKTEGATLRVLYTPG-HTDDHMALLLEEENAIFSGDCiLGE---GTTVFEDLYDYMNS 183
Cdd:PRK11921 105 AKSLKGHYHQdwNFVVVKTGDRLEIGSNELIFIEAPMlHWPDSMFTYLTGDNILFSNDA-FGQhyaSELMYNDLVDQGEL 183

                        170       180       190
                 ....*....|....*....|....*....|..
gi 7705793   184 LKELLKIKADIIYPGHGPVIhnaeAKIQQYIS 215
Cdd:PRK11921 184 YQEAIKYYANILTPFSPLVI----KKIEEILS 211
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 34-213 5.63e-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: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 46.42  E-value: 5.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   34 YLVGTGPRRILIDTGEPAIPEYIscLKQALTE--FNTA-IQEIVVTHWHRDHSGGigdicksinndTTYcIKKLPrNP-- 108
Cdd:cd16280  25 WAIDTGDGLILIDALNNNEAADL--IVDGLEKlgLDPAdIKYILITHGHGDHYGG-----------AAY-LKDLY-GAkv 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  109 -----------QREEIIGNGE-----QQYVYLKDGDVIKTEGATLRVLYTPGHTDDHMALLLEEEN------AIFSGdci 166
Cdd:cd16280  90 vmseadwdmmeEPPEEGDNPRwgpppERDIVIKDGDTLTLGDTTITVYLTPGHTPGTLSLIFPVKDggkthrAGLWG--- 166

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 7705793  167 lGEG---TTVFEDLYDYMNSLKELLKIK----ADIIYPGHgPVIHNAEAKIQQY 213
Cdd:cd16280 167 -GTGlntGPNLERREQYIASLERFKKIAeeagVDVFLSNH-PFQDGSLEKREAL 218
CphS_ImiS-like_MBL-B2 cd16287
metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas ...
 70-207 8.19e-06

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: 45.88  E-value: 8.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   70 IQEIVVTHWHRDHSGG------IG----------DICKSINND-TTYCIKKLPRNPQREEIIGNgeqqyvYLKDGDVIKT 132
Cdd:cd16287  59 INEVINTNYHTDRAGGnaywktLGakivatqmtyDLQKSQWGSiVNFTRQGNNKYPNLEKSLPD------TVFPGDFNLQ 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  133 EGaTLRVLYT-PGHTDDHMALLLEEENAIFSGdCILGE--GTTVFEDLYDYMNSLKELLKIKADIIYP------GHGPVI 203
Cdd:cd16287 133 NG-SIRAMYLgEAHTKDGIFVYFPAERVLYGN-CILKEnlGNMSFANRTEYPKTLEKLKGLIEQGELKvdsiiaGHDTPI 210


                ....
gi 7705793  204 HNAE 207
Cdd:cd16287 211 HDVG 214
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 25-146 8.77e-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: 46.00  E-value: 8.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   25 PMTLQGtNTYLVGTG---------PR-RILIDTGEPAIPEYISCLKQALTEFNTAIQEIVVTHWHRDHSGGIGDI----- 89
Cdd:cd07708   7 PFQIAG-NTYYVGTDdlaaylivtPQgNILIDGDMEQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAEIkkqtg 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7705793   90 CKSINNDTTycIKKLPRNPQREEIIGNGEQQYV-------YLKDGDVIKTEGATLRVLYTPGHT 146
Cdd:cd07708  86 AKVMAGAED--VSLLLSGGSSDFHYANDSSTYFpqstvdrAVHDGERVTLGGTVLTAHATPGHT 147
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
16-180 1.01e-05

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 45.96  E-value: 1.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   16 VRVLGCNpGPMTLQGTNT--YLVGTGPRRILIDTGEPAIPEyiscLKQALTEFNtAIQEIVVTHWHRDHSGGIGDICKSI 93
Cdd:COG1234   3 LTFLGTG-GAVPTPGRATssYLLEAGGERLLIDCGEGTQRQ----LLRAGLDPR-DIDAIFITHLHGDHIAGLPGLLSTR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   94 NND------TTYCikklPRNPQR--EEIIGNGEQQYVY------LKDGDVIKTEGATLRVLYTPgHTDDHMALLLEEENA 159
Cdd:COG1234  77 SLAgrekplTIYG----PPGTKEflEALLKASGTDLDFplefheIEPGEVFEIGGFTVTAFPLD-HPVPAYGYRFEEPGR 151

                       170       180
                ....*....|....*....|...
gi 7705793  160 I--FSGDcilgegTTVFEDLYDY 180
Cdd:COG1234 152 SlvYSGD------TRPCEALVEL 168
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 32-87 2.23e-05

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: 43.41  E-value: 2.23e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7705793   32 NTYLVGTGPRRILIDTGepaipeyISC--LKQALTEFNTA---IQEIVVTHWHRDHSGGIG 87
Cdd:cd07733  10 NCTYLETEDGKLLIDAG-------LSGrkITGRLAEIGRDpedIDAILVTHEHADHIKGLG 63
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 31-208 2.75e-05

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 44.50  E-value: 2.75e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   31 TNTYLVGTGPRRILIDTGepaipeyISCLKQALTEFN--TAIQEIVVTHWHRDHSGGIGDICKSINND--TTYC----IK 102
Cdd:COG1235  35 RSSILVEADGTRLLIDAG-------PDLREQLLRLGLdpSKIDAILLTHEHADHIAGLDDLRPRYGPNpiPVYAtpgtLE 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  103 KLPRNPQREEIIGNGEQQYVYLKDGDVIKTEGATLRVLYTPGHTDDHMALLLEEENAIFsgdCILGegttvfeDLYDYMN 182
Cdd:COG1235 108 ALERRFPYLFAPYPGKLEFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGYRIEDGGKKL---AYAT-------DTGYIPE 177

                       170       180       190
                ....*....|....*....|....*....|....*
gi 7705793  183 SLKELLKiKADII---------YPGHgpvIHNAEA 208
Cdd:COG1235 178 EVLELLR-GADLLildatyddpEPGH---LSNEEA 208
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 126-166 4.02e-05

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 43.67  E-value: 4.02e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 7705793  126 DGDVIkTEGatLRVLYTPGHTDDHMALLLE--EENAIFSGDCI 166
Cdd:cd16277 139 DDHEI-LDG--IRLEPTPGHTPGHVSVELEsgGERALFTGDVM 178
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 35-89 4.87e-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: 43.23  E-value: 4.87e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7705793   35 LVGTGPRRILIDTGepaiPE-YISCLKQALTEfntaIQEIVVTHWHRDHSGGIGDI 89
Cdd:cd16279  39 LIETGGKNILIDTG----PDfRQQALRAGIRK----LDAVLLTHAHADHIHGLDDL 86
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 5.14e-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: 43.42  E-value: 5.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   74 VVTHWHRDHSGGIGDI-CKSINNDTTYCIKKLPRNPQRE----EIIGNgeqQYVYLKDgdviKTEgatlrVLYT-PGHTD 147
Cdd:cd16301  70 ISTHFHEDRTGGIGYLnSHSIPTYASELTNQLLKKNGKElathSFSGD---EFWLLKG----KIE-----VFYPgAGHTK 137

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7705793  148 DHMALLLEEENAIFSGdCIL------GEGTTVFEDLYDYMNSLKELL--KIKADIIYPGHGPV 202
Cdd:cd16301 138 DNLVVWLPKEKILFGG-CLVksleskGLGNTGDASISQWPASAQKVLskYPNAKLVVPGHGKV 199
VIM_type_MBL-B1 cd16303
VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona ...
 25-201 5.65e-05

VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona integron-encoded metallo-beta-lactamase)-type MBLs are integron-associated and are widely distributed acquired MBLs. 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. This subgroup of VIM-type 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: 293861 [Multi-domain]  Cd Length: 218  Bit Score: 43.31  E-value: 5.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   25 PMTLQGTNTYLVGTGPRRILIDTGEPAIpEYISCLKQALTEFNTAIQEIVVTHWHRDHSGGIgDICKSiNNDTTYCikkL 104
Cdd:cd16303  22 DGAVYPSNGLIVRDGDELLLIDTAWGAK-NTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGV-DVLRA-AGVATYA---S 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  105 PRNPQREEIIGNGEQQYVYL---KDGDVIKTegATLRVLYT-PGHTDDHMALLLEEENAIFSGdCILGE------GTTVF 174
Cdd:cd16303  96 PSTRRLAEAEGNEIPTHSLEglsSSGDAVRF--GPVELFYPgAAHSTDNLVVYVPSARVLYGG-CAVRElsstsaGNVAD 172

                       170       180
                ....*....|....*....|....*....
gi 7705793  175 EDLYDYMNSLKELLK--IKADIIYPGHGP 201
Cdd:cd16303 173 ADLAEWPTSIERIQKhyPEAEFVIPGHGL 201
BLACT_WH pfam17778
Beta-lactamase associated winged helix domain; This winged helix domain is found at the ...
 237-284 1.18e-04

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: 38.75  E-value: 1.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 7705793    237 TVMELVKIIYKNTPENLHEMAKHNLLLHLKKLEKEGKIFSntDPDKKW 284
Cdd:pfam17778   1 TAMELVKVIYKDVPESLHPAAERGVLAHLEKLEAEGKVVR--EGDGKW 46
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 41-165 6.33e-04

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


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 40.33  E-value: 6.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   41 RRILIDTG--------EPAIPEYISCLKQALTEFNTA-------------IQEIVVTHWHRDHSGGIGD------ICksi 93
Cdd:cd07730  34 GKILFDLGyrkdfeeyTPRVPERLYRTPVPLEVEEDVaeqlaaggidpedIDAVILSHLHWDHIGGLSDfpnarlIV--- 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   94 NNDTTYCIKK-----------LPRNPQREEI-----------IGNGEQQYVYLKDGDVIktegatlrVLYTPGHTDDHMA 151
Cdd:cd07730 111 GPGAKEALRPpgypsgflpelLPSDFEGRLVrweeddflwvpLGPFPRALDLFGDGSLY--------LVDLPGHAPGHLG 182

                       170
                ....*....|....*..
gi 7705793  152 LLLEEENAIF---SGDC 165
Cdd:cd07730 183 LLARTTSGTWvflAGDA 199
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 41-145 7.00e-04

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 39.99  E-value: 7.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793     41 RRILIDTGePAIPEYISCLKQALTEFNTAIQEIVVTHWHRDHSGGIGDICKsINNDTTYCIKK----LPRNPQREEIIGN 116
Cdd:pfam12706   1 RRILIDPG-PDLRQQALPALQPGRLRDDPIDAVLLTHDHYDHLAGLLDLRE-GRPRPLYAPLGvlahLRRNFPYLFLLEH 78

                          90       100
                  ....*....|....*....|....*....
gi 7705793    117 GEQQYVYLKDGDVIKTEGATLRVLYTPGH 145
Cdd:pfam12706  79 YGVRVHEIDWGESFTVGDGGLTVTATPAR 107
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
34-136 1.07e-03

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 39.87  E-value: 1.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   34 YLVGTGPRRILIDTGEPAIpeYISCLKQA---LTEfntaIQEIVVTHWHRDHSGGIGDICKsINNDTT-YC-----IKKL 104
Cdd:COG1237  25 ALIETEGKRILFDTGQSDV--LLKNAEKLgidLSD----IDAVVLSHGHYDHTGGLPALLE-LNPKAPvYAhpdafEKRY 97

                        90       100       110
                ....*....|....*....|....*....|..
gi 7705793  105 PRNPQREEIIGNGEQQYVYLKDGDVIKTEGAT 136
Cdd:COG1237  98 SKRPGGKYIGIPFSREELEKLGARLILVKEPT 129
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 31-86 1.88e-03

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 38.39  E-value: 1.88e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 7705793   31 TNTYL-VGTGPRRILIDTGEPAIPEyiscLKQALTEFNtAIQEIVVTHWHRDHSGGI 86
Cdd:cd07740  15 LNTCFhVASEAGRFLIDCGASSLIA----LKRAGIDPN-AIDAIFITHLHGDHFGGL 66
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 16-90 2.74e-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: 37.81  E-value: 2.74e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7705793   16 VRVLGCN---PGPmtLQGTNTYLVGTGPRRILIDTGEPAIPEYisclkQALTEFNtAIQEIVVTHWHRDHsggIGDIC 90
Cdd:cd07716   2 LTVLGCSgsyPGP--GGACSGYLLEADGFRILLDCGSGVLSRL-----QRYIDPE-DLDAVVLSHLHPDH---CADLG 68
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 34-136 4.75e-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: 4.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   34 YLVGTGPRRILIDTG-EPAIpeyiscLKQA------LTEfntaIQEIVVTHWHRDHSGGIGDICKSINNDTTYC-----I 101
Cdd:cd07713  23 LLIETEGKKILFDTGqSGVL------LHNAkklgidLSD----IDAVVLSHGHYDHTGGLKALLELNPKAPVYAhpdafE 92

                        90       100       110
                ....*....|....*....|....*....|....*
gi 7705793  102 KKLPRNPQREEIIGNGEqQYVYLKDGDVIKTEGAT 136
Cdd:cd07713  93 PRYSKRGGGKKGIGIGR-EELEKAGARLVLVEEPT 126
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 32-200 6.72e-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: 36.84  E-value: 6.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793   32 NTYLVGTGPRRILIDT--GEPAIPEYISCLKQaltEFNTAIQEIVVTHWHRDHSGGIGDICKsiNNDTTYCIKKLPRNPQ 109
Cdd:cd16302  28 NGMIVINGGEAVVFDTptNDSQSEELIDWIEN---SLKAKVKAVVPTHFHDDCLGGLKAFHR--RGIPSYANQKTIALAK 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7705793  110 REEIigngEQQYVYLKDGDVIKTEGATLRVLY-TPGHTDDHMALLLEEENAIFSGdCIL-----GEGTTVFEDLYDYMNS 183
Cdd:cd16302 103 EKGL----PVPQHGFSDSLTLKLGGKKIVCRYfGEGHTKDNIVVYFPSEKVLFGG-CMVkslgaGKGNLEDANVEAWPKT 177

                       170
                ....*....|....*....
gi 7705793  184 LKELLKIKAD--IIYPGHG 200
Cdd:cd16302 178 VEKVKAKYPDvkIVIPGHG 196
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH