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Conserved domains on  [gi|497574458|ref|WP_009888642|]
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MBL fold metallo-hydrolase [Clostridioides difficile]

Protein Classification

COG1237 family protein( domain architecture ID 10003202)

COG1237 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
3-271 1.33e-105

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


:

Pssm-ID: 440850  Cd Length: 273  Bit Score: 307.58  E-value: 1.33e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458   3 RLKIQVLVDNNTYiDRYFVGEPAVSYYIEIDGNRILFDSGYSDVFISNAEKLNIDLGNLTHVVFSHGHNDHTRGIQ-FLE 81
Cdd:COG1237    1 SMKITVLVDNTAG-DEGLLAEHGLSALIETEGKRILFDTGQSDVLLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLPaLLE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458  82 NRydlSTVELISHPNCFIPRKH---GEKSIGAPFSAEEI-KNIFMYNPKDKPFNLSKNCVFLGEIPSINNFEKRAKIGKC 157
Cdd:COG1237   80 LN---PKAPVYAHPDAFEKRYSkrpGGKYIGIPFSREELeKLGARLILVKEPTEIAPGVYLTGEIPRVTDFEKGDPGLYV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458 158 KIGDLWEDDYVLDDSAIVCKTDKGIFIVTGCSHSGICNIVEYAKRVCGDDRVIGILGGFHLFELNN-RLDSTIQYLDKEE 236
Cdd:COG1237  157 KEDGGLVPDPFLDEQALVIKTDKGLVVITGCSHAGIVNILEYAKEVTGGKRIYAVIGGFHLLGASEeRIEKTIEALKELG 236

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 497574458 237 IRMLYPCHCVSFKVKAKMNEIL--NINEVGVGLTISI 271
Cdd:COG1237  237 VEKIYPGHCTGLEAIAALKERFgdRFIELGVGSVIEF 273
 
Name Accession Description Interval E-value
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
3-271 1.33e-105

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 307.58  E-value: 1.33e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458   3 RLKIQVLVDNNTYiDRYFVGEPAVSYYIEIDGNRILFDSGYSDVFISNAEKLNIDLGNLTHVVFSHGHNDHTRGIQ-FLE 81
Cdd:COG1237    1 SMKITVLVDNTAG-DEGLLAEHGLSALIETEGKRILFDTGQSDVLLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLPaLLE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458  82 NRydlSTVELISHPNCFIPRKH---GEKSIGAPFSAEEI-KNIFMYNPKDKPFNLSKNCVFLGEIPSINNFEKRAKIGKC 157
Cdd:COG1237   80 LN---PKAPVYAHPDAFEKRYSkrpGGKYIGIPFSREELeKLGARLILVKEPTEIAPGVYLTGEIPRVTDFEKGDPGLYV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458 158 KIGDLWEDDYVLDDSAIVCKTDKGIFIVTGCSHSGICNIVEYAKRVCGDDRVIGILGGFHLFELNN-RLDSTIQYLDKEE 236
Cdd:COG1237  157 KEDGGLVPDPFLDEQALVIKTDKGLVVITGCSHAGIVNILEYAKEVTGGKRIYAVIGGFHLLGASEeRIEKTIEALKELG 236

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 497574458 237 IRMLYPCHCVSFKVKAKMNEIL--NINEVGVGLTISI 271
Cdd:COG1237  237 VEKIYPGHCTGLEAIAALKERFgdRFIELGVGSVIEF 273
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 5-270 3.74e-87

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: 260.25  E-value: 3.74e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458   5 KIQVLVDNNTYiDRYFVGEPAVSYYIEIDGNRILFDSGYSDVFISNAEKLNIDLGNLTHVVFSHGHNDHTRGI-QFLENR 83
Cdd:cd07713    1 KITVLVDNTAG-DEGLLAEHGLSLLIETEGKKILFDTGQSGVLLHNAKKLGIDLSDIDAVVLSHGHYDHTGGLkALLELN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458  84 ydlSTVELISHPNCFIPRKH---GEKSIGAPFSAEEIKNIFMYNPKDKPFNLSKNCVFLGEIPSINNFEKRAKIGKCKIG 160
Cdd:cd07713   80 ---PKAPVYAHPDAFEPRYSkrgGGKKGIGIGREELEKAGARLVLVEEPTEIAPGVYLTGEIPRVTDFEKGNPGLFVKED 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458 161 DLWEDDYVLDDSAIVCKTDKGIFIVTGCSHSGICNIVEYAKRVCGDDRVIGILGGFHLFELN-NRLDSTIQYLDKEEIRM 239
Cdd:cd07713  157 GGLVPDDFEDEQALVIDTKKGLVVITGCSHAGIVNILEHAKKLTGGDKIYAVIGGFHLVGASeERIEKTIAALKELGVEK 236

                        250       260       270
                 ....*....|....*....|....*....|...
gi 497574458 240 LYPCHCVSFKVKAKMNEIL--NINEVGVGLTIS 270
Cdd:cd07713  237 IYPGHCTGFKAIAALKEALgdKFIPLGVGTVIE 269
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
22-89 1.31e-07

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 50.83  E-value: 1.31e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458   22 GEPAVSYYIEIDGNRILFDSGYSDVFISNAE--KLNIDLGNLTHVVFSHGHNDHTRGIQFLENRYDLSTV 89
Cdd:pfam00753   3 PGQVNSYLIEGGGGAVLIDTGGSAEAALLLLlaALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVI 72
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 27-121 3.05e-07

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: 49.47  E-value: 3.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458    27 SYYIEIDGNRILFDSGYSDVFISNAEKLNIDLGNLTHVVFSHGHNDHTRGIQFLENRYDlstVELISHPNCFIPRKHGEK 106
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPG---APVYAPEGTAELLKDLLA 78

                           90
                   ....*....|....*
gi 497574458   107 SIGAPFSAEEIKNIF 121
Cdd:smart00849  79 LLGELGAEAEPAPPD 93
 
Name Accession Description Interval E-value
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
3-271 1.33e-105

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 307.58  E-value: 1.33e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458   3 RLKIQVLVDNNTYiDRYFVGEPAVSYYIEIDGNRILFDSGYSDVFISNAEKLNIDLGNLTHVVFSHGHNDHTRGIQ-FLE 81
Cdd:COG1237    1 SMKITVLVDNTAG-DEGLLAEHGLSALIETEGKRILFDTGQSDVLLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLPaLLE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458  82 NRydlSTVELISHPNCFIPRKH---GEKSIGAPFSAEEI-KNIFMYNPKDKPFNLSKNCVFLGEIPSINNFEKRAKIGKC 157
Cdd:COG1237   80 LN---PKAPVYAHPDAFEKRYSkrpGGKYIGIPFSREELeKLGARLILVKEPTEIAPGVYLTGEIPRVTDFEKGDPGLYV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458 158 KIGDLWEDDYVLDDSAIVCKTDKGIFIVTGCSHSGICNIVEYAKRVCGDDRVIGILGGFHLFELNN-RLDSTIQYLDKEE 236
Cdd:COG1237  157 KEDGGLVPDPFLDEQALVIKTDKGLVVITGCSHAGIVNILEYAKEVTGGKRIYAVIGGFHLLGASEeRIEKTIEALKELG 236

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 497574458 237 IRMLYPCHCVSFKVKAKMNEIL--NINEVGVGLTISI 271
Cdd:COG1237  237 VEKIYPGHCTGLEAIAALKERFgdRFIELGVGSVIEF 273
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 5-270 3.74e-87

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: 260.25  E-value: 3.74e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458   5 KIQVLVDNNTYiDRYFVGEPAVSYYIEIDGNRILFDSGYSDVFISNAEKLNIDLGNLTHVVFSHGHNDHTRGI-QFLENR 83
Cdd:cd07713    1 KITVLVDNTAG-DEGLLAEHGLSLLIETEGKKILFDTGQSGVLLHNAKKLGIDLSDIDAVVLSHGHYDHTGGLkALLELN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458  84 ydlSTVELISHPNCFIPRKH---GEKSIGAPFSAEEIKNIFMYNPKDKPFNLSKNCVFLGEIPSINNFEKRAKIGKCKIG 160
Cdd:cd07713   80 ---PKAPVYAHPDAFEPRYSkrgGGKKGIGIGREELEKAGARLVLVEEPTEIAPGVYLTGEIPRVTDFEKGNPGLFVKED 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458 161 DLWEDDYVLDDSAIVCKTDKGIFIVTGCSHSGICNIVEYAKRVCGDDRVIGILGGFHLFELN-NRLDSTIQYLDKEEIRM 239
Cdd:cd07713  157 GGLVPDDFEDEQALVIDTKKGLVVITGCSHAGIVNILEHAKKLTGGDKIYAVIGGFHLVGASeERIEKTIAALKELGVEK 236

                        250       260       270
                 ....*....|....*....|....*....|...
gi 497574458 240 LYPCHCVSFKVKAKMNEIL--NINEVGVGLTIS 270
Cdd:cd07713  237 IYPGHCTGFKAIAALKEALgdKFIPLGVGTVIE 269
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 27-95 5.34e-08

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 52.59  E-value: 5.34e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497574458  27 SYYIEIDGNRILFDSGYSdvFISNAEKLNIDLGNLTHVVFSHGHNDHTRGIQFLENRYDLSTVELISHP 95
Cdd:COG1235   37 SILVEADGTRLLIDAGPD--LREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYGPNPIPVYATP 103
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
22-89 1.31e-07

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 50.83  E-value: 1.31e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458   22 GEPAVSYYIEIDGNRILFDSGYSDVFISNAE--KLNIDLGNLTHVVFSHGHNDHTRGIQFLENRYDLSTV 89
Cdd:pfam00753   3 PGQVNSYLIEGGGGAVLIDTGGSAEAALLLLlaALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVI 72
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 27-121 3.05e-07

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: 49.47  E-value: 3.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458    27 SYYIEIDGNRILFDSGYSDVFISNAEKLNIDLGNLTHVVFSHGHNDHTRGIQFLENRYDlstVELISHPNCFIPRKHGEK 106
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPG---APVYAPEGTAELLKDLLA 78

                           90
                   ....*....|....*
gi 497574458   107 SIGAPFSAEEIKNIF 121
Cdd:smart00849  79 LLGELGAEAEPAPPD 93
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 27-96 1.35e-06

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: 48.15  E-value: 1.35e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497574458  27 SYYIEIDGNRILFDSGYSDV----FISNAEKLNIDLgnlTHVVFSHGHNDHTRGIQFLENRYDlstVELISHPN 96
Cdd:COG0491   17 SYLIVGGDGAVLIDTGLGPAdaeaLLAALAALGLDI---KAVLLTHLHPDHVGGLAALAEAFG---APVYAHAA 84
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 19-106 1.68e-06

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 47.96  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458  19 YFVGEPAVSYYIeIDGNR--ILFDSGYS----DVFISNAEKLNIDLGNLTHVVFSHGHNDHTRGIQFLENRYDLSTV--- 89
Cdd:cd16280   15 YYVGNKWVSAWA-IDTGDglILIDALNNneaaDLIVDGLEKLGLDPADIKYILITHGHGDHYGGAAYLKDLYGAKVVmse 93

                         90       100
                 ....*....|....*....|.
gi 497574458  90 ----ELISHPNCFIPRKHGEK 106
Cdd:cd16280   94 adwdMMEEPPEEGDNPRWGPP 114
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 22-74 5.51e-06

uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. Members of this bacterial subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 45.51  E-value: 5.51e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 497574458  22 GEPAVSYYIEIDGNRILFDSGySDVFiSNAEKLnIDLGNLTHVVFSHGHNDHT 74
Cdd:cd07716   15 GGACSGYLLEADGFRILLDCG-SGVL-SRLQRY-IDPEDLDAVVLSHLHPDHC 64
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
27-77 5.85e-06

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 46.34  E-value: 5.85e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 497574458  27 SYYIEIDGNRILFDSGYSdvFISNAEKLNIDLGNLTHVVFSHGHNDHTRGI 77
Cdd:COG1234   21 SYLLEAGGERLLIDCGEG--TQRQLLRAGLDPRDIDAIFITHLHGDHIAGL 69
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 27-73 9.86e-06

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 45.29  E-value: 9.86e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 497574458  27 SYYIEIDGNRILFD---SGYSDVFISNAEKLNiDLGNLTHVVFSHGHNDH 73
Cdd:COG2220   13 TFLIETGGKRILIDpvfSGRASPVNPLPLDPE-DLPKIDAVLVTHDHYDH 61
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 28-130 1.40e-05

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: 44.90  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458  28 YYIEIDGNRILFDSGYS---DVFISNAEKLNIDLGNLTHVVFSHGHNDHTRGIQFLENRYDlstVELISHPNCfIPRKHG 104
Cdd:cd07721   14 YLIEDDDGLTLIDTGLPgsaKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPG---APVYAHERE-APYLEG 89

                         90       100
                 ....*....|....*....|....*.
gi 497574458 105 EKSIGAPFSAEEIKNIFMYNPKDKPF 130
Cdd:cd07721   90 EKPYPPPVRLGLLGLLSPLLPVKPVP 115
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 25-159 2.41e-05

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: 43.79  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458  25 AVSYYIEIDGNRILFDSGYSDVFisNAEKLNIDLGNLTHVVFSHGHNDHTrgiqflenrYDLSTVELISHPNcfiPRKHG 104
Cdd:cd16272   17 TSSYLLETGGTRILLDCGEGTVY--RLLKAGVDPDKLDAIFLSHFHLDHI---------GGLPTLLFARRYG---GRKKP 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 497574458 105 EKSIGAPFSAEEIKNI--FMYNPKDKPFNLskncvflgEIPSINNFEKRAKIGKCKI 159
Cdd:cd16272   83 LTIYGPKGIKEFLEKLlnFPVEILPLGFPL--------EIEELEEGGEVLELGDLKV 131
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 24-82 4.74e-05

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: 43.74  E-value: 4.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497574458  24 PAVSYYIEIDGNRILFDSGYSDVFISNA---------------------EKLNIDLGNLTHVVFSHGHNDHTRGIQFLEN 82
Cdd:cd07729   31 PVYAYLIEHPEGTILVDTGFHPDAADDPgglelafppgvteeqtleeqlARLGLDPEDIDYVILSHLHFDHAGGLDLFPN 110
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 27-74 5.45e-05

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


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 42.83  E-value: 5.45e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 497574458  27 SYYIEIDGNRILFDSG----YSDVFISNAEKLNIDLGNLTHVVFSHGHNDHT 74
Cdd:cd16295   14 CYLLETGGKRILLDCGlfqgGKELEELNNEPFPFDPKEIDAVILTHAHLDHS 65
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 27-74 5.71e-05

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


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 42.89  E-value: 5.71e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 497574458  27 SYYIEIDGNRILFDSGYSdvFISNAEKLNIDLGNLTHVVFSHGHNDHT 74
Cdd:cd07719   20 STLVVVGGRVYLVDAGSG--VVRRLAQAGLPLGDLDAVFLTHLHSDHV 65
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 27-77 1.31e-04

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 42.87  E-value: 1.31e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 497574458  27 SYYIEIDGNRILFDSG-YSDVFISNAEKLNIDLGNLTHVVFSHGHNDHTRGI 77
Cdd:COG1236   16 CYLLETGGTRILIDCGlFQGGKERNWPPFPFRPSDVDAVVLTHAHLDHSGAL 67
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 27-86 1.66e-04

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


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 41.09  E-value: 1.66e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497574458  27 SYYIEIDGNRILFDSGYSDVFISNA-EKLNIDLGNLTHVVFSHGHNDHTRGIQFLENRYDL 86
Cdd:cd07733   11 CTYLETEDGKLLIDAGLSGRKITGRlAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNV 71
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 28-77 2.30e-04

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: 41.38  E-value: 2.30e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 497574458  28 YYIEIDGNRILFDSGYSDVFISNAEKL-------NIDLGNLTHVVFSHGHNDHTRGI 77
Cdd:cd07720   52 FLVRTGGRLILVDTGAGGLFGPTAGKLlanlaaaGIDPEDIDDVLLTHLHPDHIGGL 108
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 19-86 3.91e-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: 40.59  E-value: 3.91e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497574458  19 YFVGEPAVSYYIEIDGNRILFDSGYSDVFISNAEK-LNIDLGNLTHVVFSHGHNDHTRGIQFLENRYDL 86
Cdd:cd07743    3 YIPGPTNIGVYVFGDKEALLIDSGLDEDAGRKIRKiLEELGWKLKAIINTHSHADHIGGNAYLQKKTGC 71
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 27-76 4.19e-04

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. 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: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 40.30  E-value: 4.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 497574458  27 SYYIEIDGNRILFDSGYSDVfisnAEKLniDLGNLTHVVFSHGHNDHTRG 76
Cdd:cd07736   39 SALIEVDGERILLDAGLTDL----AERF--PPGSIDAILLTHFHMDHVQG 82
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 5-77 8.97e-04

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: 39.49  E-value: 8.97e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497574458   5 KIQVLVDNNTYI--DRYFVGEPAVSYyIEIDGNRILFDSG---YSDVFISNAEKLNIDLGNLTHVVFSHGHNDHTRGI 77
Cdd:cd07711    1 EVKVLVEGYARRdsDGGFRASSTVTL-IKDGGKNILVDTGtpwDRDLLLKALAEHGLSPEDIDYVVLTHGHPDHIGNL 77
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 14-73 1.24e-03

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: 39.01  E-value: 1.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497574458  14 TYIDRYFVGEPAV--SYYIEIDGNRILFDSGYSDVF--ISNA-EKLNIDLGNLTHVVFSHGHNDH 73
Cdd:cd07726    3 YLIDLGFLGFPGRiaSYLLDGEGRPALIDTGPSSSVprLLAAlEALGIAPEDVDYIILTHIHLDH 67
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 19-80 1.55e-03

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: 39.23  E-value: 1.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497574458  19 YFVGEPAVSYYIeIDGNR--ILFDSGY--SDVFI-SNAEKLNIDLGNLTHVVFSHGHNDHTRGIQFL 80
Cdd:cd16288   15 YYVGTSGLASYL-ITTPQglILIDTGLesSAPMIkANIRKLGFKPSDIKILLNSHAHLDHAGGLAAL 80
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 27-85 2.64e-03

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: 38.04  E-value: 2.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574458  27 SYYIEIDGNR-ILFDSGYSDV--FISNAEKLNIDLgnlTHVVFSHGHNDHTRGIQFLENRYD 85
Cdd:cd06262   12 CYLVSDEEGEaILIDPGAGALekILEAIEELGLKI---KAILLTHGHFDHIGGLAELKEAPG 70
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 33-89 7.91e-03

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 36.76  E-value: 7.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497574458  33 DGNRILFDSGYSDVFISNAEKL-----NIDLGNLTHVVFSHGHNDHTRGIQFLENRYDLSTV 89
Cdd:COG2333   20 DGKTILIDTGPRPSFDAGERVVlpylrALGIRRLDLLVLTHPDADHIGGLAAVLEAFPVGRV 81
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 27-80 8.74e-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: 36.47  E-value: 8.74e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 497574458  27 SYYIEIDGNRILFDSGYSDVfiSNAEKLNIDLGNLTHVVFSHGHNDHTRGIQFL 80
Cdd:cd07740   18 CFHVASEAGRFLIDCGASSL--IALKRAGIDPNAIDAIFITHLHGDHFGGLPFF 69
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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