NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446677640|ref|WP_000754986|]
View 

MULTISPECIES: MBL fold metallo-hydrolase [Bacillus]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10870074)

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 10-228 5.31e-100

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: 293.24  E-value: 5.31e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  10 HLYLIDDFDLQHNERTGTYVLLGDD-ITLIETCAAPSLPYILDGLQQLHIDLNEVKNIIVTHVHLDHAGAAGLMMEKCPN 88
Cdd:cd07726    1 GIYLIDLGFLGFPGRIASYLLDGEGrPALIDTGPSSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLAEALPN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  89 ATLYVHSRGARHMIDPTKLILGAKAVYKEDFDKLFDPILPIEEERVHIVQHGDTLQIAeDRILTFYDTPGHAKHHISIHD 168
Cdd:cd07726   81 AKVYVHPRGARHLIDPSKLWASARAVYGDEADRLGGEILPVPEERVIVLEDGETLDLG-GRTLEVIDTPGHAPHHLSFLD 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640 169 SLTNGIFTGDTIGIYYRELadlgVELYLPSTSPSQFQPDAMIASKNHIQSMNVDTIYFGH 228
Cdd:cd07726  160 EESDGLFTGDAAGVRYPEL----DVVGPPSTPPPDFDPEAWLESLDRLLSLKPERIYLTH 215
 
Name Accession Description Interval E-value
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 10-228 5.31e-100

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: 293.24  E-value: 5.31e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  10 HLYLIDDFDLQHNERTGTYVLLGDD-ITLIETCAAPSLPYILDGLQQLHIDLNEVKNIIVTHVHLDHAGAAGLMMEKCPN 88
Cdd:cd07726    1 GIYLIDLGFLGFPGRIASYLLDGEGrPALIDTGPSSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLAEALPN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  89 ATLYVHSRGARHMIDPTKLILGAKAVYKEDFDKLFDPILPIEEERVHIVQHGDTLQIAeDRILTFYDTPGHAKHHISIHD 168
Cdd:cd07726   81 AKVYVHPRGARHLIDPSKLWASARAVYGDEADRLGGEILPVPEERVIVLEDGETLDLG-GRTLEVIDTPGHAPHHLSFLD 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640 169 SLTNGIFTGDTIGIYYRELadlgVELYLPSTSPSQFQPDAMIASKNHIQSMNVDTIYFGH 228
Cdd:cd07726  160 EESDGLFTGDAAGVRYPEL----DVVGPPSTPPPDFDPEAWLESLDRLLSLKPERIYLTH 215
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 11-233 1.71e-22

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: 93.22  E-value: 1.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  11 LYLIDDFDLQHNERTGTYVLLGDD-ITLIETCAAPSLPY-ILDGLQQLHIDlneVKNIIVTHVHLDHAGAAGLMMEKCpN 88
Cdd:COG0491    1 VYVLPGGTPGAGLGVNSYLIVGGDgAVLIDTGLGPADAEaLLAALAALGLD---IKAVLLTHLHPDHVGGLAALAEAF-G 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  89 ATLYVHSRGARHMIDPTKLILGAKAVYKEDfdklfdpilpieeervHIVQHGDTLQIAEDRIlTFYDTPGHAKHHISIHD 168
Cdd:COG0491   77 APVYAHAAEAEALEAPAAGALFGREPVPPD----------------RTLEDGDTLELGGPGL-EVIHTPGHTPGHVSFYV 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446677640 169 SLTNGIFTGDTIGIYyreladlgvelYLPSTSPSQFQPDAMIASKNHIQSMNVDTIYFGHYGASS 233
Cdd:COG0491  140 PDEKVLFTGDALFSG-----------GVGRPDLPDGDLAQWLASLERLLALPPDLVIPGHGPPTT 193
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 27-228 3.24e-16

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: 75.28  E-value: 3.24e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640    27 TYVLLGDDITLIETCAAPSLPyILDGLQQLhiDLNEVKNIIVTHVHLDHAGAAGLMMEKcPNATLYVHSRGARHMIDPTK 106
Cdd:smart00849   3 YLVRDDGGAILIDTGPGEAED-LLAELKKL--GPKKIDAIILTHGHPDHIGGLPELLEA-PGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640   107 LILGAKAVYKEdfdklfdpilpieEERVHIVQHGDTLQIAEDRIlTFYDTPGHAKHHISIHDSLTNGIFTGDTIGIYYRE 186
Cdd:smart00849  79 LLGELGAEAEP-------------APPDRTLKDGDELDLGGGEL-EVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDG 144

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 446677640   187 LADLGvelylpstsPSQFQPDAMIASKNHIQSMNVDTIYFGH 228
Cdd:smart00849 145 RTLVD---------GGDAAASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
27-228 2.08e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 73.56  E-value: 2.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640   27 TYVLLGDDITLIETCAAPSLPYILDgLQQLHIDLNEVKNIIVTHVHLDHAGAAGLMMEKCPNATlYVHSRGARHMIDPtk 106
Cdd:pfam00753   9 YLIEGGGGAVLIDTGGSAEAALLLL-LAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPV-IVVAEEARELLDE-- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  107 lilgakaVYKEDFDKLFDPILPIEEERVHIVQHGDTLQIAEDRILTFYDTPGHAKHHISIHDSLTNGIFTGDTIGIYYRE 186
Cdd:pfam00753  85 -------ELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 446677640  187 LADLGVELYLPSTSPSQfqpDAMIASKNHIQSMNVDTIYFGH 228
Cdd:pfam00753 158 RLDLPLGGLLVLHPSSA---ESSLESLLKLAKLKAAVIVPGH 196
PRK11921 PRK11921
anaerobic nitric oxide reductase flavorubredoxin;
28-157 1.90e-07

anaerobic nitric oxide reductase flavorubredoxin;


Pssm-ID: 237023 [Multi-domain]  Cd Length: 394  Bit Score: 52.00  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  28 YVLLGDDITLIETCAAPSLPYILDGLQQlHIDLNEVKNIIVTHVHLDHAGAAGLMMEKCPNATLYVHSRGARHMidptkl 107
Cdd:PRK11921  36 YLIKDEKTVLIDTVWQPFAKEFVENLKK-EIDLDKIDYIVANHGEIDHSGALPELMKEIPDTPIYCTKNGAKSL------ 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446677640 108 ilgaKAVYKEDFDklfdpilpieeerVHIVQHGDTLQIaEDRILTFYDTP 157
Cdd:PRK11921 109 ----KGHYHQDWN-------------FVVVKTGDRLEI-GSNELIFIEAP 140
 
Name Accession Description Interval E-value
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 10-228 5.31e-100

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: 293.24  E-value: 5.31e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  10 HLYLIDDFDLQHNERTGTYVLLGDD-ITLIETCAAPSLPYILDGLQQLHIDLNEVKNIIVTHVHLDHAGAAGLMMEKCPN 88
Cdd:cd07726    1 GIYLIDLGFLGFPGRIASYLLDGEGrPALIDTGPSSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLAEALPN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  89 ATLYVHSRGARHMIDPTKLILGAKAVYKEDFDKLFDPILPIEEERVHIVQHGDTLQIAeDRILTFYDTPGHAKHHISIHD 168
Cdd:cd07726   81 AKVYVHPRGARHLIDPSKLWASARAVYGDEADRLGGEILPVPEERVIVLEDGETLDLG-GRTLEVIDTPGHAPHHLSFLD 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640 169 SLTNGIFTGDTIGIYYRELadlgVELYLPSTSPSQFQPDAMIASKNHIQSMNVDTIYFGH 228
Cdd:cd07726  160 EESDGLFTGDAAGVRYPEL----DVVGPPSTPPPDFDPEAWLESLDRLLSLKPERIYLTH 215
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 11-233 1.71e-22

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: 93.22  E-value: 1.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  11 LYLIDDFDLQHNERTGTYVLLGDD-ITLIETCAAPSLPY-ILDGLQQLHIDlneVKNIIVTHVHLDHAGAAGLMMEKCpN 88
Cdd:COG0491    1 VYVLPGGTPGAGLGVNSYLIVGGDgAVLIDTGLGPADAEaLLAALAALGLD---IKAVLLTHLHPDHVGGLAALAEAF-G 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  89 ATLYVHSRGARHMIDPTKLILGAKAVYKEDfdklfdpilpieeervHIVQHGDTLQIAEDRIlTFYDTPGHAKHHISIHD 168
Cdd:COG0491   77 APVYAHAAEAEALEAPAAGALFGREPVPPD----------------RTLEDGDTLELGGPGL-EVIHTPGHTPGHVSFYV 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446677640 169 SLTNGIFTGDTIGIYyreladlgvelYLPSTSPSQFQPDAMIASKNHIQSMNVDTIYFGHYGASS 233
Cdd:COG0491  140 PDEKVLFTGDALFSG-----------GVGRPDLPDGDLAQWLASLERLLALPPDLVIPGHGPPTT 193
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 27-228 4.52e-22

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: 91.90  E-value: 4.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  27 TYVLLGDDITLIETCAAPSLPYILDGLQQLHIDLNEVKNIIVTHVHLDHAGAAGLMMEKcPNATLYVHSRGARHMIDPTK 106
Cdd:cd07721   14 YLIEDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEA-PGAPVYAHEREAPYLEGEKP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640 107 LILGAKAVYKedfdKLFDPILPIEEERVHI-VQHGDTLQIAEDriLTFYDTPGHAKHHISIHDSLTNGIFTGDTigiyyr 185
Cdd:cd07721   93 YPPPVRLGLL----GLLSPLLPVKPVPVDRtLEDGDTLDLAGG--LRVIHTPGHTPGHISLYLEEDGVLIAGDA------ 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446677640 186 eLADLGVELYLPstsPSQFQPD--AMIASKNHIQSMNVDTIYFGH 228
Cdd:cd07721  161 -LVTVGGELVPP---PPPFTWDmeEALESLRKLAELDPEVLAPGH 201
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 27-228 3.24e-16

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: 75.28  E-value: 3.24e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640    27 TYVLLGDDITLIETCAAPSLPyILDGLQQLhiDLNEVKNIIVTHVHLDHAGAAGLMMEKcPNATLYVHSRGARHMIDPTK 106
Cdd:smart00849   3 YLVRDDGGAILIDTGPGEAED-LLAELKKL--GPKKIDAIILTHGHPDHIGGLPELLEA-PGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640   107 LILGAKAVYKEdfdklfdpilpieEERVHIVQHGDTLQIAEDRIlTFYDTPGHAKHHISIHDSLTNGIFTGDTIGIYYRE 186
Cdd:smart00849  79 LLGELGAEAEP-------------APPDRTLKDGDELDLGGGEL-EVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDG 144

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 446677640   187 LADLGvelylpstsPSQFQPDAMIASKNHIQSMNVDTIYFGH 228
Cdd:smart00849 145 RTLVD---------GGDAAASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
27-228 2.08e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 73.56  E-value: 2.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640   27 TYVLLGDDITLIETCAAPSLPYILDgLQQLHIDLNEVKNIIVTHVHLDHAGAAGLMMEKCPNATlYVHSRGARHMIDPtk 106
Cdd:pfam00753   9 YLIEGGGGAVLIDTGGSAEAALLLL-LAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPV-IVVAEEARELLDE-- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  107 lilgakaVYKEDFDKLFDPILPIEEERVHIVQHGDTLQIAEDRILTFYDTPGHAKHHISIHDSLTNGIFTGDTIGIYYRE 186
Cdd:pfam00753  85 -------ELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 446677640  187 LADLGVELYLPSTSPSQfqpDAMIASKNHIQSMNVDTIYFGH 228
Cdd:pfam00753 158 RLDLPLGGLLVLHPSSA---ESSLESLLKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 41-228 4.85e-15

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: 72.32  E-value: 4.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  41 CAAPSLPYILDGLQQLHIDlneVKNIIVTHVHLDHAGAAGLMMEKcPNATLYVHSRGARHMIDPtklilgakavykEDFD 120
Cdd:cd06262   27 PGAGALEKILEAIEELGLK---IKAILLTHGHFDHIGGLAELKEA-PGAPVYIHEADAELLEDP------------ELNL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640 121 KLFDPILPIEEERVHIVQHGDTLQIAEDRIlTFYDTPGHAKHHISIHDSLTNGIFTGDTIgiyyreLADLGVELYLPSTS 200
Cdd:cd06262   91 AFFGGGPLPPPEPDILLEDGDTIELGGLEL-EVIHTPGHTPGSVCFYIEEEGVLFTGDTL------FAGSIGRTDLPGGD 163

                        170       180       190
                 ....*....|....*....|....*....|
gi 446677640 201 PSQfqpdaMIASKNHIQSMNVD--TIYFGH 228
Cdd:cd06262  164 PEQ-----LIESIKKLLLLLPDdtVVYPGH 188
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 14-157 1.84e-14

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: 71.75  E-value: 1.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  14 IDDFDLQHNERTGT----YVLLGDDITLIETCAAPSLPYILDGLQQLhIDLNEVKNIIVTHVHLDHAGAAGLMMEKCPNA 89
Cdd:cd07709   17 LRLFEGEYPTPRGTsynsYLIKDEKTALIDTVKEPFFDEFLENLEEV-IDPRKIDYIVVNHQEPDHSGSLPELLELAPNA 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446677640  90 TLYVHSRGARHMIDptklilgakavykedfdklfdpILPIEEERVHIVQHGDTLQIAeDRILTFYDTP 157
Cdd:cd07709   96 KIVCSKKAARFLKH----------------------FYPGIDERFVVVKDGDTLDLG-KHTLKFIPAP 140
NorV COG0426
Flavorubredoxin [Energy production and conversion];
14-157 1.44e-13

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 70.63  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  14 IDDFDLQHNERTGT----YVLLGDDITLIETCAAPSLPYILDGLQQlHIDLNEVKNIIVTHVHLDHAGAAGLMMEKCPNA 89
Cdd:COG0426   19 RRLFEGEYPTPRGTtynsYLIVDEKTALIDTVGESFFEEFLENLSK-VIDPKKIDYIIVNHQEPDHSGSLPELLELAPNA 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446677640  90 TLYVHSRGARHMIDptklilgakavykedfdklfdpILPIEEERVHIVQHGDTLQIAeDRILTFYDTP 157
Cdd:COG0426   98 KIVCSKKAARFLPH----------------------FYGIPDFRFIVVKEGDTLDLG-GHTLQFIPAP 142
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 49-228 1.57e-11

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: 63.00  E-value: 1.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  49 ILDGLQQLHIDLNEVKNIIVTHVHLDHAGAAGLmmekCPNATLYVHSRGARHMIDPtkliLGAKAVYKEDFDKLFDpilP 128
Cdd:cd07729   75 LEEQLARLGLDPEDIDYVILSHLHFDHAGGLDL----FPNATIIVQRAELEYATGP----DPLAAGYYEDVLALDD---D 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640 129 IEEERVHIVqHGDTlQIAEDriLTFYDTPGHAKHHISIHDSLTNG--IFTGDTigIYYRELADLGVELYLPSTspsqfqP 206
Cdd:cd07729  144 LPGGRVRLV-DGDY-DLFPG--VTLIPTPGHTPGHQSVLVRLPEGtvLLAGDA--AYTYENLEEGRPPGINYD------P 211

                        170       180
                 ....*....|....*....|....*
gi 446677640 207 DAMIASKNHIQSM---NVDTIYFGH 228
Cdd:cd07729  212 EAALASLERLKALaerEGARVIPGH 236
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 49-180 3.59e-11

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: 60.55  E-value: 3.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  49 ILDGLQQLHIDLnevKNIIVTHVHLDHAGAAGLMMEKCPNATLYVHSRGARHMIDptklilgakavykedfdklfdpilp 128
Cdd:cd07723   33 VLAALEKNGLTL---TAILTTHHHWDHTGGNAELKALFPDAPVYGPAEDRIPGLD------------------------- 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446677640 129 ieeervHIVQHGDTLQIAEDRIlTFYDTPGHAKHHISIHDSLTNGIFTGDTI 180
Cdd:cd07723   85 ------HPVKDGDEIKLGGLEV-KVLHTPGHTLGHICYYVPDEPALFTGDTL 129
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 28-237 2.62e-10

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: 58.85  E-value: 2.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  28 YVL-LGDDITLIETcaAPSLPY----ILDGLQQLHIDLNEVKNIIVTHVHLDHAGAAGLMMEKcpnatlyvhsRGARHMI 102
Cdd:cd07725   18 YLLrDGDETTLIDT--GLATEEdaeaLWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEK----------SGATVYI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640 103 DPTKlilgakavykedfdklfdpilpieeervhIVQHGDTLQIAEDRiLTFYDTPGHAKHHISIHDSLTNGIFTGDTIGI 182
Cdd:cd07725   86 LDVT-----------------------------PVKDGDKIDLGGLR-LKVIETPGHTPGHIVLYDEDRRELFVGDAVLP 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446677640 183 YYReladLGVELYlpstSPSQFQP-DAMIASKNHIQSMNVDTIYFGHYGASSNVTE 237
Cdd:cd07725  136 KIT----PNVSLW----AVRVEDPlGAYLESLDKLEKLDVDLAYPGHGGPIKDPKA 183
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-161 1.16e-09

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


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 58.10  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  37 LIETCAAPSLPYILDGLQQLHIDLNEVKNIIVTHVHLDHAGAAGLmMEKCPNATLYVHSRGARHMIDPtklilgakavYK 116
Cdd:cd16288   35 LIDTGLESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAA-LKKLTGAKLMASAEDAALLASG----------GK 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446677640 117 EDFDkLFDPILPIEEERV-HIVQHGDTLQIAEdRILTFYDTPGHAK 161
Cdd:cd16288  104 SDFH-YGDDSLAFPPVKVdRVLKDGDRVTLGG-TTLTAHLTPGHTR 147
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 49-165 8.09e-09

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


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 55.35  E-value: 8.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  49 ILDGLQQLHIDLNEVKNIIVTHVHLDHAGAAGLMmekcPNATLYVHSRGARHMIDPtklilgakAVYKEDFDKLFDPILP 128
Cdd:cd07730   70 VAEQLAAGGIDPEDIDAVILSHLHWDHIGGLSDF----PNARLIVGPGAKEALRPP--------GYPSGFLPELLPSDFE 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446677640 129 IEEERVHIVQHGDTLQIAEDRIL------TFY--DTPGHAKHHIS 165
Cdd:cd07730  138 GRLVRWEEDDFLWVPLGPFPRALdlfgdgSLYlvDLPGHAPGHLG 182
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 32-159 9.94e-09

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 55.28  E-value: 9.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  32 GDDITLIETC-AAPSLPYILDGLQQLHIDLNEVKNIIVTHVHLDHAGAAGLMMEKcPNATLYVHSRGARHMIDPTKLILG 110
Cdd:cd16280   30 GDGLILIDALnNNEAADLIVDGLEKLGLDPADIKYILITHGHGDHYGGAAYLKDL-YGAKVVMSEADWDMMEEPPEEGDN 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446677640 111 akavykedfdklFDPILPIEEERVhiVQHGDTLQIAeDRILTFYDTPGH 159
Cdd:cd16280  109 ------------PRWGPPPERDIV--IKDGDTLTLG-DTTITVYLTPGH 142
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-159 7.94e-08

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


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 52.49  E-value: 7.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  37 LIETCAAPSLPYILDGLQQLHIDLNEVKNIIVTHVHLDHAGA-AGLmmEKCPNATLyVHSRGarhmidpTKLILGAKAVY 115
Cdd:cd16309   35 LIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGlAEL--KKATGAQL-VASAA-------DKPLLESGYVG 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446677640 116 KEDFDKLFDPilPIEEERVhiVQHGDTLQIAeDRILTFYDTPGH 159
Cdd:cd16309  105 SGDTKNLQFP--PVRVDRV--IGDGDKVTLG-GTTLTAHLTPGH 143
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 66-197 1.36e-07

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 50.95  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  66 IIVTHVHLDHAGAAGLMMEKCpnatlyvhsrGARhmidptklILGAKAVYKEDFDKLFDPIlpieeervHIVQHGDTLQI 145
Cdd:cd16278   57 ILVTHTHRDHSPGAARLAERT----------GAP--------VRAFGPHRAGGQDTDFAPD--------RPLADGEVIEG 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640 146 AEDRILTFYdTPGHAKHHISIHDSLTNGIFTGDTI---------------GIYYR---ELADLGVELYLP 197
Cdd:cd16278  111 GGLRLTVLH-TPGHTSDHLCFALEDEGALFTGDHVmgwsttviappdgdlGDYLAsleRLLALDDRLLLP 179
PRK11921 PRK11921
anaerobic nitric oxide reductase flavorubredoxin;
28-157 1.90e-07

anaerobic nitric oxide reductase flavorubredoxin;


Pssm-ID: 237023 [Multi-domain]  Cd Length: 394  Bit Score: 52.00  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  28 YVLLGDDITLIETCAAPSLPYILDGLQQlHIDLNEVKNIIVTHVHLDHAGAAGLMMEKCPNATLYVHSRGARHMidptkl 107
Cdd:PRK11921  36 YLIKDEKTVLIDTVWQPFAKEFVENLKK-EIDLDKIDYIVANHGEIDHSGALPELMKEIPDTPIYCTKNGAKSL------ 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446677640 108 ilgaKAVYKEDFDklfdpilpieeerVHIVQHGDTLQIaEDRILTFYDTP 157
Cdd:PRK11921 109 ----KGHYHQDWN-------------FVVVKTGDRLEI-GSNELIFIEAP 140
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 67-228 2.86e-07

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: 49.93  E-value: 2.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  67 IVTHVHLDHAGAAGlMMEKCpnatlYVHSRGARHMIDPTKLILGAKAVYKEDFDKlfdpilpieEERVHIVQHGDTLQIA 146
Cdd:cd07712   47 VATHGHFDHIGGLH-EFEEV-----YVHPADAEILAAPDNFETLTWDAATYSVPP---------AGPTLPLRDGDVIDLG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640 147 eDRILTFYDTPGHAKHHISIHDSLTNGIFTGDTIGiyyrelaDLGVELYLPSTSPSQFqpdamIASKNHIQSM--NVDTI 224
Cdd:cd07712  112 -DRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVY-------DGPLIMDLPHSDLDDY-----LASLEKLSKLpdEFDKV 178


                 ....
gi 446677640 225 YFGH 228
Cdd:cd07712  179 LPGH 182
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 23-180 1.12e-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: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 48.67  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  23 ERTGTYVL-LGDDITLIETCA-----APSLPYI-------LDGLQQLHIDLNEVKNIIVTHVHLDHAG-----AAGLMME 84
Cdd:cd16277   11 ELIHSWLVrTPGRTILVDTGIgndkpRPGPPAFhnlntpyLERLAAAGVRPEDVDYVLCTHLHVDHVGwntrlVDGRWVP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  85 KCPNATLYVHSRGARHMIDPTklilGAKAVYKEDFDklfDPILPIEEE-RVHIVQHGDTLqiaeDRILTFYDTPGHAKHH 163
Cdd:cd16277   91 TFPNARYLFSRAEYDHWSSPD----AGGPPNRGVFE---DSVLPVIEAgLADLVDDDHEI----LDGIRLEPTPGHTPGH 159

                        170       180
                 ....*....|....*....|.
gi 446677640 164 ISIHdsLTNG----IFTGDTI 180
Cdd:cd16277  160 VSVE--LESGgeraLFTGDVM 178
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 49-166 1.24e-06

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


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 47.97  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  49 ILDGLQQLHIDLNEVKNIIVTHVHLDHAGAAGLMmekcPNATLYVHSrgarhmidptklilgAKAVYKEDFDKLFDpilp 128
Cdd:cd07711   47 LLKALAEHGLSPEDIDYVVLTHGHPDHIGNLNLF----PNATVIVGW---------------DICGDSYDDHSLEE---- 103

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446677640 129 ieeervhivqhGDTLQIAEDriLTFYDTPGHAKHHISI 166
Cdd:cd07711  104 -----------GDGYEIDEN--VEVIPTPGHTPEDVSV 128
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 25-180 2.50e-06

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: 47.14  E-value: 2.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  25 TGTYVL-LGDDITLIET-----CAAPSLPYILDGLQQLHIDlnevkNIIVTHVHLDHAGAAGLMMEKCPNATLYVHsrga 98
Cdd:cd07722   18 TNTYLVgTGKRRILIDTgegrpSYIPLLKSVLDSEGNATIS-----DILLTHWHHDHVGGLPDVLDLLRGPSPRVY---- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  99 rhmidptklilgaKAVYKEDFDKLFDPILPIeeervHIVQHGDTLQIaEDRILTFYDTPGHAKHHISIHDSLTNGIFTGD 178
Cdd:cd07722   89 -------------KFPRPEEDEDPDEDGGDI-----HDLQDGQVFKV-EGATLRVIHTPGHTTDHVCFLLEEENALFTGD 149


                 ..
gi 446677640 179 TI 180
Cdd:cd07722  150 CV 151
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-160 2.53e-06

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


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 47.73  E-value: 2.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  37 LIETCAAPSLPYILDGLQQLHIDLNEVKNIIVTHVHLDHAGAAGLMMEkcpnATlyvhsrGARHMIDPTklilgAKAVYK 116
Cdd:cd16315   35 LIDSGTEEAAPLVLANIRKLGFDPKDVRWLLSSHEHFDHVGGLAALQR----AT------GARVAASAA-----AAPVLE 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446677640 117 EDFDKLFDP----ILPIEEERV-HIVQHGDTLQIAEDRiLTFYDTPGHA 160
Cdd:cd16315  100 SGKPAPDDPqaglHEPFPPVRVdRIVEDGDTVALGSLR-LTAHATPGHT 147
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 63-238 3.45e-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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 47.18  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  63 VKNIIVTHVHLDHAGAAGLMMEKcpNATLYVHSRGARHMIDPTKLILGAKAVYKEDFDKLFDPILPieeerVHIVQHGDT 142
Cdd:cd16282   53 VRYVVNTHYHGDHTLGNAAFADA--GAPIIAHENTREELAARGEAYLELMRRLGGDAMAGTELVLP-----DRTFDDGLT 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640 143 LQIAEDRILTFYDTPGHAKHHISIHDSLTNGIFTGDtigIYYRELADlgvelYLPSTSPSqfqpdAMIASKNHIQSMNVD 222
Cdd:cd16282  126 LDLGGRTVELIHLGPAHTPGDLVVWLPEEGVLFAGD---LVFNGRIP-----FLPDGSLA-----GWIAALDRLLALDAT 192

                        170
                 ....*....|....*.
gi 446677640 223 TIYFGHyGASSNVTEV 238
Cdd:cd16282  193 VVVPGH-GPVGDKADL 207
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 19-234 4.01e-06

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 47.92  E-value: 4.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  19 LQHNERTGTyVLLGDditliETCAAPslpyILDGLQQLHIDLNEVKNiivTHVHLDHAGAaglmmekcpNATLyvhsrGA 98
Cdd:PLN02398  91 LLHDEDTGT-VGVVD-----PSEAVP----VIDALSRKNRNLTYILN---THHHYDHTGG---------NLEL-----KA 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  99 RHmidptklilGAKAVYKE-DFDKLfdPILPIeeervhIVQHGDTLQIAEDRILTFyDTPGHAKHHISIHDSLTNGIFTG 177
Cdd:PLN02398 144 RY---------GAKVIGSAvDKDRI--PGIDI------VLKDGDKWMFAGHEVLVM-ETPGHTRGHISFYFPGSGAIFTG 205

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446677640 178 DTIgiyyreladlgveLYLPSTSPSQFQPDAMIASKNHIQSMNVDT-IYFGHYGASSN 234
Cdd:PLN02398 206 DTL-------------FSLSCGKLFEGTPEQMLSSLQKIISLPDDTnIYCGHEYTLSN 250
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 66-180 5.24e-06

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: 46.24  E-value: 5.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  66 IIVTHVHLDHAGAAGLMMEKcPNATLYVHSrgarhmidptklilGAKAVYkedFDKLFDpilpieeervhivqHGDTLQI 145
Cdd:cd07724   52 VLETHVHADHVSGARELAER-TGAPIVIGE--------------GAPASF---FDRLLK--------------DGDVLEL 99

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446677640 146 aEDRILTFYDTPGHAKHHISIHDSLTNGIFTGDTI 180
Cdd:cd07724  100 -GNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTL 133
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 45-159 7.87e-06

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


Pssm-ID: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 46.52  E-value: 7.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  45 SLPYILDGLQQLHIDLNEVKNIIVTHVHLDHAGAAGlMMEKCPNATLYVHSRGARHMIDPTKlilgakavYKEDFDKLFD 124
Cdd:cd16312   43 SAPLIIANIEALGFRIEDVKLILNSHAHWDHAGGIA-ALQKASGATVAASAHGAQVLQSGTN--------GKDDPQYQAK 113

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446677640 125 PILPIEE-ERVHIVQHGDTLQIAEDRiLTFYDTPGH 159
Cdd:cd16312  114 PVVHVAKvAKVKEVGEGDTLKVGPLR-LTAHMTPGH 148
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 49-228 9.29e-06

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: 45.80  E-value: 9.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  49 ILDGLQQLHIDLnevKNIIVTHVHLDHAGAAGLMMEKcPNATLYVHSRGARHMIDPTkliLGAKAVYKEdFDKLFDPILP 128
Cdd:cd16322   36 LLARFGTTGLTL---LYILLTHAHFDHVGGVADLRRH-PGAPVYLHPDDLPLYEAAD---LGAKAFGLG-IEPLPPPDRL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640 129 IEeervhivqHGDTLQIAEdriLTF--YDTPGHAKHHISIHDSLTNGIFTGD-----TIGIYYRELADlgvelylpstsp 201
Cdd:cd16322  108 LE--------DGQTLTLGG---LEFkvLHTPGHSPGHVCFYVEEEGLLFSGDllfqgSIGRTDLPGGD------------ 164

                        170       180
                 ....*....|....*....|....*...
gi 446677640 202 sqfqPDAMIASKNHIQSMNVDT-IYFGH 228
Cdd:cd16322  165 ----PKAMAASLRRLLTLPDETrVFPGH 188
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 32-180 9.68e-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: 46.00  E-value: 9.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  32 GDDITLIET----CAAPSLPYILDGLQQLHIDLNEVKNIIVTHVHLDHAGaaGLMMEK----CPNATLYVHSRGARHMID 103
Cdd:cd07720   57 GGRLILVDTgaggLFGPTAGKLLANLAAAGIDPEDIDDVLLTHLHPDHIG--GLVDAGgkpvFPNAEVHVSEAEWDFWLD 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640 104 PtklilGAKAVYKEDFDKLFDPIlpieEERVHIVQHGDTLqIAEDRIL---TFYDTPGHAKHHISIH-----DSLtngIF 175
Cdd:cd07720  135 D-----ANAAKAPEGAKRFFDAA----RDRLRPYAAAGRF-EDGDEVLpgiTAVPAPGHTPGHTGYRiesggERL---LI 201


                 ....*
gi 446677640 176 TGDTI 180
Cdd:cd07720  202 WGDIV 206
PRK05452 PRK05452
anaerobic nitric oxide reductase flavorubredoxin; Provisional
 53-157 1.07e-05

anaerobic nitric oxide reductase flavorubredoxin; Provisional


Pssm-ID: 235475 [Multi-domain]  Cd Length: 479  Bit Score: 46.68  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  53 LQQL--HIDLNEVKNIIVTHVHLDHAGAAGLMMEKCPNATLYVHSRGarhmIDPtklILGAKAVYKEDFdklfdpilpie 130
Cdd:PRK05452  60 VQNLrnEIDLADIDYIVINHAEEDHAGALTELMAQIPDTPIYCTANA----IDS---INGHHHHPEWNF----------- 121

                         90       100
                 ....*....|....*....|....*..
gi 446677640 131 eervHIVQHGDTLQIAEDRILTFYDTP 157
Cdd:PRK05452 122 ----NVVKTGDTLDIGNGKQLIFVETP 144
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 53-183 1.19e-05

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: 44.84  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  53 LQQLHIDLNEVKNIIVTHVHLDHAGAAGLMMEKcPNATLYVHSRGARHmidptklilgakavYKEDFdklfdpilpieeE 132
Cdd:cd16275   38 LAKLNELGLTLTGILLTHSHFDHVNLVEPLLAK-YDAPVYMSKEEIDY--------------YGFRC------------P 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446677640 133 RVHIVQHGDTLQIAEDRIlTFYDTPGHAKHHISIHdsLTNGIFTGDTIGIY 183
Cdd:cd16275   91 NLIPLEDGDTIKIGDTEI-TCLLTPGHTPGSMCYL--LGDSLFTGDTLFIE 138
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 53-109 3.72e-05

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


Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 44.54  E-value: 3.72e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446677640  53 LQQLHIDLNEVKNIIVTHVHLDHAGaaGLMmeKCPNATLYVHSRGARHMIDPTKLIL 109
Cdd:cd07742   71 IEALGFDPSDVRHIVLTHLDLDHAG--GLA--DFPHATVHVHAAELDAATSPRTRYE 123
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 37-159 7.73e-05

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: 43.30  E-value: 7.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  37 LIETCAAPSLPYILDGLQQLHIDLNEVKNIIVTHVHLDHAGAAGLmMEKCPNATLYVHSRGArhmidptKLILGAKAVYK 116
Cdd:cd07708   35 LIDGDMEQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAE-IKKQTGAKVMAGAEDV-------SLLLSGGSSDF 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446677640 117 EDFDKLFDPILPIEEERvhIVQHGDTLQIAeDRILTFYDTPGH 159
Cdd:cd07708  107 HYANDSSTYFPQSTVDR--AVHDGERVTLG-GTVLTAHATPGH 146
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 ...
 45-160 2.02e-04

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: 42.34  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  45 SLPYILDGLQQLHIDLNEVKNIIVTHVHLDHAG--AAglmMEKCPNATLYVHSRGARhmidptklILGAKAVYKED--FD 120
Cdd:cd16290   43 SAPQIEANIRALGFRLEDVKLILNSHAHFDHAGgiAA---LQRDSGATVAASPAGAA--------ALRSGGVDPDDpqAG 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446677640 121 KLfDPILPIEEERVhiVQHGDTLQIAEDRIlTFYDTPGHA 160
Cdd:cd16290  112 AA-DPFPPVAKVRV--VADGEVVKLGPLAV-TAHATPGHT 147
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 53-182 2.35e-04

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 42.06  E-value: 2.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  53 LQQLHIDLNEVKNIIVTHVHLDHAGAAGLMmekcpnatlyvhsrgarhmidpTKLILGAKaVYKEDFDKLfdpilpieEE 132
Cdd:PLN02469  37 LQAAHEHGAKIKLVLTTHHHWDHAGGNEKI----------------------KKLVPGIK-VYGGSLDNV--------KG 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446677640 133 RVHIVQHGDTLQIAED-RILTFYdTPGHAKHHISIHDSLTNG----IFTGDTIGI 182
Cdd:PLN02469  86 CTHPVENGDKLSLGKDvNILALH-TPCHTKGHISYYVTGKEGedpaVFTGDTLFI 139
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 49-94 2.82e-04

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: 41.84  E-value: 2.82e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 446677640  49 ILDGLQQLHIDLNEVKNIIVTHVHLDHAGaaGLM--MEKCPNATLYVH 94
Cdd:cd07713   42 LLHNAKKLGIDLSDIDAVVLSHGHYDHTG--GLKalLELNPKAPVYAH 87
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 49-180 2.88e-04

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: 41.00  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  49 ILDGLQQLHIdlnEVKNIIVTHVHLDHAGAAGLMmekcpnatlyvhsrgARHMIDPtklILGAkavYKED---FDKL--- 122
Cdd:cd07737   36 ILQAIEDLGL---TLKKILLTHGHLDHVGGAAEL---------------AEHYGVP---IIGP---HKEDkflLENLpeq 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446677640 123 -----FDPILPIEEERvhIVQHGDTLQIAEDRILTFYdTPGHAKHHISIHDSLTNGIFTGDTI 180
Cdd:cd07737   92 sqmfgFPPAEAFTPDR--WLEEGDTVTVGNLTLEVLH-CPGHTPGHVVFFNRESKLAIVGDVL 151
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 26-161 2.96e-04

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: 41.67  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  26 GTYVLL-GDDITLIETCAAPSLPYILDGLQQLHIDLNEVKNIIVTHVHLDHAGAAGlMMEKCPNATLYVhSRGarhmiDP 104
Cdd:cd16310   23 GSYLITsNHGAILLDGGLEENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLA-QLKADTGAKLWA-SRG-----DR 95

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446677640 105 TKLILGakavyKEDFDKLFDPIlPIEEERV-HIVQHGDTLQIAEDRiLTFYDTPGHAK 161
Cdd:cd16310   96 PALEAG-----KHIGDNITQPA-PFPAVKVdRILGDGEKIKLGDIT-LTATLTPGHTK 146
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 44-180 4.22e-04

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


Pssm-ID: 293839  Cd Length: 252  Bit Score: 41.33  E-value: 4.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  44 PSLPYILDGLQQLHIDLNEVKNIIVTHVHLDHAGAA------GLMMEKCPNATLYVHSRGARHMIDPTKLilgAKAVYKE 117
Cdd:cd16281   76 HSEHSLLKSLARLGLSPEDITDVILTHLHFDHCGGAtradddGLVELLFPNATYWVQKRHWEWALNPNPR---ERASFLP 152

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446677640 118 DFdklfdpILPIEEE-RVHIVQHGDTLqIAEDRILTFYD--TPGHAkhHISIHDSLTNGIFTGDTI 180
Cdd:cd16281  153 EN------IEPLEESgRLKLIDGSDAE-LGPGIRFHLSDghTPGQM--LPEISTPGGTVVFAADLI 209
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 11-161 5.57e-04

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


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 40.92  E-value: 5.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  11 LYLIDDFDLqhnertGTYVLLGDD-ITLIETCAAPSLPYILDGLQQLHIDLNEVKNIIVTHVHLDHAGAAGlMMEKCPNA 89
Cdd:cd16308   14 LYYVGTYDL------ACYLIVTPKgNILINTGLAESVPLIKKNIQALGFKFKDIKILLTTQAHYDHVGAMA-AIKQQTGA 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446677640  90 TLYVHSRGARHMIDPtklilGAKAVYKEDFDKLFDPILPieEERVHivqHGDTLQIAEDRIlTFYDTPGHAK 161
Cdd:cd16308   87 KMMVDEKDAKVLADG-----GKSDYEMGGYGSTFAPVKA--DKLLH---DGDTIKLGGTKL-TLLHHPGHTK 147
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-161 5.79e-04

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


Pssm-ID: 293865  Cd Length: 255  Bit Score: 40.89  E-value: 5.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  37 LIETCAAPSLPYILDGLQQLHIDLNEVKNIIVTHVHLDHAGAAGLMMEKCpnatlyvhsrGARHMI---DPTKLILGAKA 113
Cdd:cd16307   35 LINSNLESSVPQIKASIEKLGFKFSDTKILLISHAHFDHAAGSALIKRET----------HAKYMVmdgDVDVVESGGKS 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446677640 114 vykeDFDKLFDPILPIEEERVHIVQH-GDTLQIAeDRILTFYDTPGHAK 161
Cdd:cd16307  105 ----DFFYGNDPSTYFPPAHVDKVLHdGEQVELG-GTVLTAHLTAGHTK 148
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 62-198 7.61e-04

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 39.82  E-value: 7.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  62 EVKNIIVTHVHLDHAGAAGLMMEKcPNATLYVhSRGARHMIDPTKL---ILGAKAVYKEDFDKlfdpILPIEEERVHIVQ 138
Cdd:cd07743   45 KLKAIINTHSHADHIGGNAYLQKK-TGCKVYA-PKIEKAFIENPLLepsYLGGAYPPKELRNK----FLMAKPSKVDDII 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640 139 HGDTLQIAEDRiLTFYDTPGHAKHHISIhdsLT-NGI-FTGDTI---------GIYY-----------RELADLGVELYL 196
Cdd:cd07743  119 EEGELELGGVG-LEIIPLPGHSFGQIGI---LTpDGVlFAGDALfgeevlekyGIPFlydveeqletlEKLEELDADYYV 194


                 ..
gi 446677640 197 PS 198
Cdd:cd07743  195 PG 196
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 44-108 8.44e-04

cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; MBL-fold metallo-hydrolase domain; CPSF3 (also known as cleavage and polyadenylation specificity factor 73 kDa subunit/CPSF-73) functions as a 3' endonuclease in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and in 3' end processing of metazoan histone pre-mRNAs. This subgroup also contains the yeast homolog of CPSF-73, Ysh1/Brr5 which has roles in mRNA and snoRNA synthesis. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain, and a RMMBL domain (RNA-metabolizing metallo-beta-lactamase). 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: 293850  Cd Length: 194  Bit Score: 39.88  E-value: 8.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446677640  44 PSLPYiLDglqqlHIDLNEVKNIIVTHVHLDHAGAAGLMMEKCPnatlyvhSRGARHMIDPTKLI 108
Cdd:cd16292   40 ASLPF-FD-----EIDLSEIDLLLITHFHLDHCGALPYFLQKTN-------FKGRVFMTHPTKAI 91
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 58-178 1.34e-03

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


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 39.36  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  58 IDLNEVKNIIVTHVHLDHAGAAGLMMEKCPNATLYvhsrgarhMIDPTKLILG------AKaVYKEDFDKLFDPILPIEE 131
Cdd:cd16295   47 FDPKEIDAVILTHAHLDHSGRLPLLVKEGFRGPIY--------ATPATKDLAElllldsAK-IQEEEAEHPPAEPLYTEE 117

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640 132 E------RVHIVQHGDTLQIAEDRILTFYDTpGhakhHI----SIHDSLTNGI---FTGD 178
Cdd:cd16295  118 DvekalkHFRPVEYGEPFEIGPGVKVTFYDA-G----HIlgsaSVELEIGGGKrilFSGD 172
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 58-178 1.92e-03

Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; CPSF3 (cleavage and polyadenylation specificity factor subunit 3; also known as cleavage and polyadenylation specificity factor 73 kDa subunit, CPSF-73) and CPSF2 (also known as cleavage and polyadenylation specificity factor 100 kDa subunit /CPSF-100) are components of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. CPSF3 functions as a 3' endonuclease. Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)), and Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74) are subunits of Integrator, a metazoan-specific multifunctional protein complex composed of 14 subunits. Integrator has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. 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: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 38.85  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  58 IDLNEVKNIIVTHVHLDHAGAAGLMMEkcpnatlYVHSRGARHMIDPTKLILgakAVYKEDFDKLFDPILP--------- 128
Cdd:cd07734   45 LLPPEIDAILISHFHLDHCGALPYLFR-------GFIFRGPIYATHPTVALG---RLLLEDYVKSAERIGQdqslytped 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446677640 129 IEEERVHI--VQHGDTLQIAEDRILTFYDT---PGHAKHHISIHdsLTNGIFTGD 178
Cdd:cd07734  115 IEEALKHIvpLGYGQSIDLFPALSLTAYNAghvLGAAMWEIQIY--GEKLVYTGD 167
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 53-179 4.26e-03

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


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 37.63  E-value: 4.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  53 LQQLHIDLNEVKNIIVTHVHLDHAGaaGLMMekcpnatlYVHSRGARHMIDPTKLIlGAKAVyKEDFDKLFDPILPIEEE 132
Cdd:cd16272   41 LLKAGVDPDKLDAIFLSHFHLDHIG--GLPT--------LLFARRYGGRKKPLTIY-GPKGI-KEFLEKLLNFPVEILPL 108

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446677640 133 R----VHIVQHGDTLQIAEDRILTFYDTPgHAKHHISIHDSLTNGI--FTGDT 179
Cdd:cd16272  109 GfpleIEELEEGGEVLELGDLKVEAFPVK-HSVESLGYRIEAEGKSivYSGDT 160
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
49-179 6.20e-03

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 37.48  E-value: 6.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  49 ILDGLQQLHIDLNEVKNIIVTHVHLDH-AGAAGLMMekcpnaTLYVHSRGAR-HMIDPTKLILGAKAVYKEDFDKLFDPI 126
Cdd:COG1234   39 TQRQLLRAGLDPRDIDAIFITHLHGDHiAGLPGLLS------TRSLAGREKPlTIYGPPGTKEFLEALLKASGTDLDFPL 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446677640 127 lpieeeRVHIVQHGDTLQIaEDRILTFYDTpghaKHHIsihDSL-----TNGI---FTGDT 179
Cdd:COG1234  113 ------EFHEIEPGEVFEI-GGFTVTAFPL----DHPV---PAYgyrfeEPGRslvYSGDT 159
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 48-168 6.24e-03

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. 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: 293814  Cd Length: 249  Bit Score: 37.62  E-value: 6.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446677640  48 YILDGLQQLHIDLNEVKNIIVTHVHLDHAGaaGLMMEK-------CPNATLYVHSRGARHMIDPTKLilgAKAVYKEDFd 120
Cdd:cd07728   81 SIEESLAELGLTPEDIDYVLMTHLHFDHAS--GLTKVKgeqlvsvFPNATIYVSEIEWEEMRNPNIR---SKNTYWKEN- 154

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 446677640 121 klFDPIlpieEERVHIVQhgDTLQIAEDriLTFYDTPGHAKHH--ISIHD 168
Cdd:cd07728  155 --WEPI----EDQVKTFS--DEIEIVPG--ITMIHTGGHSDGHsiIEIEQ 194
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 41-77 6.64e-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: 37.24  E-value: 6.64e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446677640  41 CAAPSLPyildGLQQLHIDLNEVKNIIVTHVHLDHAG 77
Cdd:cd07740   32 CGASSLI----ALKRAGIDPNAIDAIFITHLHGDHFG 64
 
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