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Conserved domains on  [gi|42564134|ref|NP_187996|]
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Metallo-hydrolase/oxidoreductase superfamily protein [Arabidopsis thaliana]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10888664)

uncharacterized member of the MBL fold metallo-hydrolase superfamily, which is most likely a hydrolytic enzyme

Gene Ontology:  GO:0016787
PubMed:  17597585

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 79-291 1.55e-81

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


:

Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 246.62  E-value: 1.55e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134  79 EIVFMGTGTSEGIPRVSCLtnplktCSVCTkATEPgnRNRRLNTSILVRYirpsGTSNILIDCGKFFYHSALRWfptfGL 158
Cdd:cd16279   2 KLTFLGTGTSSGVPVIGCD------CGVCD-SSDP--KNRRLRSSILIET----GGKNILIDTGPDFRQQALRA----GI 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 159 RTLDAVVITHSHADAIGGLDDLRDWTNNVQPHIPIYTAIRDLEVMKKTHYYlvdTSVIIPGAAVSELEFKVIHEDQPFVV 238
Cdd:cd16279  65 RKLDAVLLTHAHADHIHGLDDLRPFNRLQQRPIPVYASEETLDDLKRRFPY---FFAATGGGGVPKLDLHIIEPDEPFTI 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 42564134 239 NDLKITPLPVWHGSNYrSLGFRFGNVCYISDVSDIPEETYPLLKDCDLLIMDA 291
Cdd:cd16279 142 GGLEITPLPVLHGKLP-SLGFRFGDFAYLTDVSEIPEESLEKLRGLDVLILDA 193
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 79-291 1.55e-81

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


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 246.62  E-value: 1.55e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134  79 EIVFMGTGTSEGIPRVSCLtnplktCSVCTkATEPgnRNRRLNTSILVRYirpsGTSNILIDCGKFFYHSALRWfptfGL 158
Cdd:cd16279   2 KLTFLGTGTSSGVPVIGCD------CGVCD-SSDP--KNRRLRSSILIET----GGKNILIDTGPDFRQQALRA----GI 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 159 RTLDAVVITHSHADAIGGLDDLRDWTNNVQPHIPIYTAIRDLEVMKKTHYYlvdTSVIIPGAAVSELEFKVIHEDQPFVV 238
Cdd:cd16279  65 RKLDAVLLTHAHADHIHGLDDLRPFNRLQQRPIPVYASEETLDDLKRRFPY---FFAATGGGGVPKLDLHIIEPDEPFTI 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 42564134 239 NDLKITPLPVWHGSNYrSLGFRFGNVCYISDVSDIPEETYPLLKDCDLLIMDA 291
Cdd:cd16279 142 GGLEITPLPVLHGKLP-SLGFRFGDFAYLTDVSEIPEESLEKLRGLDVLILDA 193
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 79-359 2.52e-55

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 182.02  E-value: 2.52e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134  79 EIVFMGTGTSEGIPRVSCltnplkTCSVCTKAtepGNRNRRLNTSILVRyirpSGTSNILIDCGkffyHSALRWFPTFGL 158
Cdd:COG1235   2 KVTFLGSGSSGGVPQIGC------DCPVCAST---DPRYGRTRSSILVE----ADGTRLLIDAG----PDLREQLLRLGL 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 159 R--TLDAVVITHSHADAIGGLDDLRDWTNnvQPHIPIYTAIRDLEVMKKTHYYLVDTsviipgaAVSELEFKVIHEDQPF 236
Cdd:COG1235  65 DpsKIDAILLTHEHADHIAGLDDLRPRYG--PNPIPVYATPGTLEALERRFPYLFAP-------YPGKLEFHEIEPGEPF 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 237 VVNDLKITPLPVWHGSNyRSLGFRF----GNVCYISDVSDIPEETYPLLKDCDLLIMDALRPDRSSaTHFGLPRALEEVR 312
Cdd:COG1235 136 EIGGLTVTPFPVPHDAG-DPVGYRIedggKKLAYATDTGYIPEEVLELLRGADLLILDATYDDPEP-GHLSNEEALELLA 213

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 42564134 313 KIKPKRTLFTgmmHL----MDHEKVSEELEKLRNTEGldVQLSYDGLRVPI 359
Cdd:COG1235 214 RLGPKRLVLT---HLspdnNDHELDYDELEAALLPAG--VEVAYDGMEIEL 259
PRK02113 PRK02113
MBL fold metallo-hydrolase;
80-357 2.66e-51

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 171.12  E-value: 2.66e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134   80 IVFMGTGTSEGIPRVSCltnplkTCSVCTKAtEPgnRNRRLNTSILVRyirpSGTSNILIDCGKFFYHSALRwfptFGLR 159
Cdd:PRK02113   3 IRILGSGTSTGVPEIGC------TCPVCTSK-DP--RDNRLRTSALVE----TEGARILIDCGPDFREQMLR----LPFG 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134  160 TLDAVVITHSHADAIGGLDDLRD--WTNNVqphiPIYTAIRDLEVMK-KTHYYLVDTSViiPGaaVSELEFKVIHEDQPF 236
Cdd:PRK02113  66 KIDAVLITHEHYDHVGGLDDLRPfcRFGEV----PIYAEQYVAERLRsRMPYCFVEHSY--PG--VPNIPLREIEPDRPF 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134  237 VVNDLKITPLPVWHGsNYRSLGFRFGNVCYISDVSDIPEETYPLLKDCDLLIMDALRPdRSSATHFGLPRALEEVRKIKP 316
Cdd:PRK02113 138 LVNHTEVTPLRVMHG-KLPILGYRIGKMAYITDMLTMPEEEYEQLQGIDVLVMNALRI-APHPTHQSLEEALENIKRIGA 215

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 42564134  317 KRTLFTGMMHLMD-HEKVSEELEKlrnteglDVQLSYDGLRV 357
Cdd:PRK02113 216 KETYLIHMSHHIGlHADVEKELPP-------HVHFAYDGLEI 250
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 136-324 7.72e-27

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 105.08  E-value: 7.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134   136 NILIDCGK-FFYHSALRWFPTFGLRT-LDAVVITHSHADAIGGLDDLRDwtnnvqphipiyTAIRDLEVMKKTHYYLVDT 213
Cdd:pfam12706   2 RILIDPGPdLRQQALPALQPGRLRDDpIDAVLLTHDHYDHLAGLLDLRE------------GRPRPLYAPLGVLAHLRRN 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134   214 SVIIPGAAVSELEFKVIHEDQPFVVND--LKITPLPVWHGSNYRS-------LGFRFGN----VCYISDVSDIPEETYPL 280
Cdd:pfam12706  70 FPYLFLLEHYGVRVHEIDWGESFTVGDggLTVTATPARHGSPRGLdpnpgdtLGFRIEGpgkrVYYAGDTGYFPDEIGER 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 42564134   281 LKDCDLLIMD--ALRPDR-SSATHFGLPRALEEVRKIKPKRTLFTGM 324
Cdd:pfam12706 150 LGGADLLLLDggAWRDDEmIHMGHMTPEEAVEAAADLGARRKVLIHI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 122-293 4.56e-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: 4.56e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134    122 TSILVRYirpsGTSNILIDCGKFFYHSALRWFPTFGLRTLDAVVITHSHADAIGGLDDLRDwtnnvQPHIPIYTAIRDLE 201
Cdd:smart00849   1 NSYLVRD----DGGAILIDTGPGEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLE-----APGAPVYAPEGTAE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134    202 VMKKTHYYLVDTSVIIPGAAVseleFKVIHEDQPFVVNDLKITPLPV---WHGSNyrSLGFRFGNVCYISDVSDIPEETY 278
Cdd:smart00849  72 LLKDLLALLGELGAEAEPAPP----DRTLKDGDELDLGGGELEVIHTpghTPGSI--VLYLPEGKILFTGDLLFAGGDGR 145

                          170
                   ....*....|....*
gi 42564134    279 PLLKDCDLLIMDALR 293
Cdd:smart00849 146 TLVDGGDAAASDALE 160
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 79-291 1.55e-81

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


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 246.62  E-value: 1.55e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134  79 EIVFMGTGTSEGIPRVSCLtnplktCSVCTkATEPgnRNRRLNTSILVRYirpsGTSNILIDCGKFFYHSALRWfptfGL 158
Cdd:cd16279   2 KLTFLGTGTSSGVPVIGCD------CGVCD-SSDP--KNRRLRSSILIET----GGKNILIDTGPDFRQQALRA----GI 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 159 RTLDAVVITHSHADAIGGLDDLRDWTNNVQPHIPIYTAIRDLEVMKKTHYYlvdTSVIIPGAAVSELEFKVIHEDQPFVV 238
Cdd:cd16279  65 RKLDAVLLTHAHADHIHGLDDLRPFNRLQQRPIPVYASEETLDDLKRRFPY---FFAATGGGGVPKLDLHIIEPDEPFTI 141

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 42564134 239 NDLKITPLPVWHGSNYrSLGFRFGNVCYISDVSDIPEETYPLLKDCDLLIMDA 291
Cdd:cd16279 142 GGLEITPLPVLHGKLP-SLGFRFGDFAYLTDVSEIPEESLEKLRGLDVLILDA 193
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 79-359 2.52e-55

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 182.02  E-value: 2.52e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134  79 EIVFMGTGTSEGIPRVSCltnplkTCSVCTKAtepGNRNRRLNTSILVRyirpSGTSNILIDCGkffyHSALRWFPTFGL 158
Cdd:COG1235   2 KVTFLGSGSSGGVPQIGC------DCPVCAST---DPRYGRTRSSILVE----ADGTRLLIDAG----PDLREQLLRLGL 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 159 R--TLDAVVITHSHADAIGGLDDLRDWTNnvQPHIPIYTAIRDLEVMKKTHYYLVDTsviipgaAVSELEFKVIHEDQPF 236
Cdd:COG1235  65 DpsKIDAILLTHEHADHIAGLDDLRPRYG--PNPIPVYATPGTLEALERRFPYLFAP-------YPGKLEFHEIEPGEPF 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 237 VVNDLKITPLPVWHGSNyRSLGFRF----GNVCYISDVSDIPEETYPLLKDCDLLIMDALRPDRSSaTHFGLPRALEEVR 312
Cdd:COG1235 136 EIGGLTVTPFPVPHDAG-DPVGYRIedggKKLAYATDTGYIPEEVLELLRGADLLILDATYDDPEP-GHLSNEEALELLA 213

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 42564134 313 KIKPKRTLFTgmmHL----MDHEKVSEELEKLRNTEGldVQLSYDGLRVPI 359
Cdd:COG1235 214 RLGPKRLVLT---HLspdnNDHELDYDELEAALLPAG--VEVAYDGMEIEL 259
PRK02113 PRK02113
MBL fold metallo-hydrolase;
80-357 2.66e-51

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 171.12  E-value: 2.66e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134   80 IVFMGTGTSEGIPRVSCltnplkTCSVCTKAtEPgnRNRRLNTSILVRyirpSGTSNILIDCGKFFYHSALRwfptFGLR 159
Cdd:PRK02113   3 IRILGSGTSTGVPEIGC------TCPVCTSK-DP--RDNRLRTSALVE----TEGARILIDCGPDFREQMLR----LPFG 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134  160 TLDAVVITHSHADAIGGLDDLRD--WTNNVqphiPIYTAIRDLEVMK-KTHYYLVDTSViiPGaaVSELEFKVIHEDQPF 236
Cdd:PRK02113  66 KIDAVLITHEHYDHVGGLDDLRPfcRFGEV----PIYAEQYVAERLRsRMPYCFVEHSY--PG--VPNIPLREIEPDRPF 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134  237 VVNDLKITPLPVWHGsNYRSLGFRFGNVCYISDVSDIPEETYPLLKDCDLLIMDALRPdRSSATHFGLPRALEEVRKIKP 316
Cdd:PRK02113 138 LVNHTEVTPLRVMHG-KLPILGYRIGKMAYITDMLTMPEEEYEQLQGIDVLVMNALRI-APHPTHQSLEEALENIKRIGA 215

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 42564134  317 KRTLFTGMMHLMD-HEKVSEELEKlrnteglDVQLSYDGLRV 357
Cdd:PRK02113 216 KETYLIHMSHHIGlHADVEKELPP-------HVHFAYDGLEI 250
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 136-324 7.72e-27

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 105.08  E-value: 7.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134   136 NILIDCGK-FFYHSALRWFPTFGLRT-LDAVVITHSHADAIGGLDDLRDwtnnvqphipiyTAIRDLEVMKKTHYYLVDT 213
Cdd:pfam12706   2 RILIDPGPdLRQQALPALQPGRLRDDpIDAVLLTHDHYDHLAGLLDLRE------------GRPRPLYAPLGVLAHLRRN 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134   214 SVIIPGAAVSELEFKVIHEDQPFVVND--LKITPLPVWHGSNYRS-------LGFRFGN----VCYISDVSDIPEETYPL 280
Cdd:pfam12706  70 FPYLFLLEHYGVRVHEIDWGESFTVGDggLTVTATPARHGSPRGLdpnpgdtLGFRIEGpgkrVYYAGDTGYFPDEIGER 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 42564134   281 LKDCDLLIMD--ALRPDR-SSATHFGLPRALEEVRKIKPKRTLFTGM 324
Cdd:pfam12706 150 LGGADLLLLDggAWRDDEmIHMGHMTPEEAVEAAADLGARRKVLIHI 196
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
79-359 8.15e-23

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 95.65  E-value: 8.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134  79 EIVFMGTGTseGIPRvscltnplktcsvctkatepGNRNrrlNTSILVRYirpsGTSNILIDCGkffyHSALRWFPTFGL 158
Cdd:COG1234   2 KLTFLGTGG--AVPT--------------------PGRA---TSSYLLEA----GGERLLIDCG----EGTQRQLLRAGL 48

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 159 --RTLDAVVITHSHADAIGGLDDLRD--WTNNVQPHIPIYtAIRDLEVMKKTHYYLVDTSVIIPgaavseLEFKVIHEDQ 234
Cdd:COG1234  49 dpRDIDAIFITHLHGDHIAGLPGLLStrSLAGREKPLTIY-GPPGTKEFLEALLKASGTDLDFP------LEFHEIEPGE 121

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 235 PFVVNDLKITPLPVWHGSNyrSLGFRF----GNVCYISDvSDIPEETYPLLKDCDLLIMDALRPDR----------SSAT 300
Cdd:COG1234 122 VFEIGGFTVTAFPLDHPVP--AYGYRFeepgRSLVYSGD-TRPCEALVELAKGADLLIHEATFLDEeaelaketghSTAK 198

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 301 hfglpRALEEVRKIKPKRTLFTgmmHLMDH-EKVSEELEKLRNTEGLDVQLSYDGLRVPI 359
Cdd:COG1234 199 -----EAAELAAEAGVKRLVLT---HFSPRyDDPEELLAEARAVFPGPVELAEDGMVIEL 250
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 79-291 2.51e-18

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: 81.90  E-value: 2.51e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134  79 EIVFMGTGTSEGIPRVSCltnplkTCSVCTKATEpGNRNRRLNTSILVRyirpSGTSNILIDCGkfFYHSALRWFPTfgl 158
Cdd:cd07736   2 KLTFLGTGDAGGVPVYGC------DCSACQRARQ-DPSYRRRPCSALIE----VDGERILLDAG--LTDLAERFPPG--- 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 159 rTLDAVVITHSHADAIGGLDDLRdWTNNvqPHIPIY-----TAIRDLevmkKTHyylvdtsviiPGAavseLEFKVIHED 233
Cdd:cd07736  66 -SIDAILLTHFHMDHVQGLFHLR-WGVG--DPIPVYgppdpQGCADL----FKH----------PGI----LDFQPLVAP 123

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42564134 234 -QPFVVNDLKITPLPVWHGSNyrSLGFRF----GNVCYISDVSDIPEETYPLLKD--CDLLIMDA 291
Cdd:cd07736 124 fQSFELGGLKITPLPLNHSKP--TFGYLLesggKRLAYLTDTLGLPEETLEFLKQqqPDVLVLDC 186
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 122-293 4.56e-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: 4.56e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134    122 TSILVRYirpsGTSNILIDCGKFFYHSALRWFPTFGLRTLDAVVITHSHADAIGGLDDLRDwtnnvQPHIPIYTAIRDLE 201
Cdd:smart00849   1 NSYLVRD----DGGAILIDTGPGEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLE-----APGAPVYAPEGTAE 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134    202 VMKKTHYYLVDTSVIIPGAAVseleFKVIHEDQPFVVNDLKITPLPV---WHGSNyrSLGFRFGNVCYISDVSDIPEETY 278
Cdd:smart00849  72 LLKDLLALLGELGAEAEPAPP----DRTLKDGDELDLGGGELEVIHTpghTPGSI--VLYLPEGKILFTGDLLFAGGDGR 145

                          170
                   ....*....|....*
gi 42564134    279 PLLKDCDLLIMDALR 293
Cdd:smart00849 146 TLVDGGDAAASDALE 160
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 119-301 5.98e-11

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 61.12  E-value: 5.98e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 119 RLNTSILVRyirpSGTSNILIDCGKffyhSALRWFPTFGL--RTLDAVVITHSHADAIGGLD----DLRDWTNNVQPhIP 192
Cdd:cd07740  14 RLNTCFHVA----SEAGRFLIDCGA----SSLIALKRAGIdpNAIDAIFITHLHGDHFGGLPffllDAQFVAKRTRP-LT 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 193 IY----TAIRDLEVMKkthyylvdtsVIIPGAAVS----ELEFKVIHEDQPFVVNDLKITPLPVWHGSNYRSLGFRFGN- 263
Cdd:cd07740  85 IAgppgLRERLRRAME----------ALFPGSSKVprrfDLEVIELEPGEPTTLGGVTVTAFPVVHPSGALPLALRLEAa 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 42564134 264 ---VCYISDvSDIPEETYPLLKDCDLLIMDALRPDRSSATH 301
Cdd:cd07740 155 grvLAYSGD-TEWTDALVPLARGADLFICECYFFEKKVPGH 194
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 132-291 1.05e-10

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: 59.76  E-value: 1.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 132 SGTSNILIDCGkffyHSAL----RWFPtfgLRTLDAVVITHSHAD--A-IGGLDDLRDW--TNNVQPHIPIYTAIRDLEV 202
Cdd:cd07716  25 ADGFRILLDCG----SGVLsrlqRYID---PEDLDAVVLSHLHPDhcAdLGVLQYARRYhpRGARKPPLPLYGPAGPAER 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 203 MKKTHYYLvdtsviipgaavSELEFKVIHEDQPFVVNDLKITPLPVWHGSNyrSLGFRF----GNVCYISDvSDIPEETY 278
Cdd:cd07716  98 LAALYGLE------------DVFDFHPIEPGEPLEIGPFTITFFRTVHPVP--CYAMRIedggKVLVYTGD-TGYCDELV 162

                       170
                ....*....|...
gi 42564134 279 PLLKDCDLLIMDA 291
Cdd:cd07716 163 EFARGADLLLCEA 175
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 119-261 1.54e-10

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: 59.84  E-value: 1.54e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 119 RLNTSILVRYirpsGTSNILIDCGKFFYHSALRWfpTFGLRTLDAVVITHSHADAIGGLDDL--RDWTNNVQPHIPIY-- 194
Cdd:cd07719  16 RAGPSTLVVV----GGRVYLVDAGSGVVRRLAQA--GLPLGDLDAVFLTHLHSDHVADLPALllTAWLAGRKTPLPVYgp 89

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42564134 195 ----------TAIRDLEVMKKTHYYLVDTSVIIPGAAVSELEF-KVIHEDqpfvvNDLKITPLPVWHGSNYRSLGFRF 261
Cdd:cd07719  90 pgtralvdglLAAYALDIDYRARIGDEGRPDPGALVEVHEIAAgGVVYED-----DGVKVTAFLVDHGPVPPALAYRF 162
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 123-231 2.18e-10

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: 60.26  E-value: 2.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 123 SILVRYirPSGTsNILIDCGKFFYHSA-----LRWFPTFGLRTLDAVVITHSHADAIGGLDDLRD-------WTNNVQPH 190
Cdd:COG2333  13 AILIRT--PDGK-TILIDTGPRPSFDAgervvLPYLRALGIRRLDLLVLTHPDADHIGGLAAVLEafpvgrvLVSGPPDT 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 42564134 191 IPIYTAIRDLEVMKKTHYYLVDTSVIIPgaaVSELEFKVIH 231
Cdd:COG2333  90 SETYERLLEALKEKGIPVRPCRAGDTWQ---LGGVRFEVLW 127
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 116-291 4.67e-10

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: 58.04  E-value: 4.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 116 RNRRLNTSILVRyirpSGTSNILIDCGKFFYHSALRwfptFGL--RTLDAVVITHSHADAIGGLDDL---RDWTNNVQPh 190
Cdd:cd16272  12 SLTRNTSSYLLE----TGGTRILLDCGEGTVYRLLK----AGVdpDKLDAIFLSHFHLDHIGGLPTLlfaRRYGGRKKP- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 191 IPIYtairdleVMKKTHYYLvdTSVIIPGAAVSELEFKVIHEDQP-----FVVNDLKITPLPVWHGSnyRSLGFRF---- 261
Cdd:cd16272  83 LTIY-------GPKGIKEFL--EKLLNFPVEILPLGFPLEIEELEeggevLELGDLKVEAFPVKHSV--ESLGYRIeaeg 151

                       170       180       190
                ....*....|....*....|....*....|
gi 42564134 262 GNVCYISDvSDIPEETYPLLKDCDLLIMDA 291
Cdd:cd16272 152 KSIVYSGD-TGPCENLVELAKGADLLIHEC 180
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 136-273 4.40e-09

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: 55.37  E-value: 4.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 136 NILIDCGKFFYHSALRWFPTFGLrTLDAVVITHSHADAIGGLDDLRDWTNnvqphIPIYTAIRDLEVMKKTHYYLvdtSV 215
Cdd:cd06262  22 AILIDPGAGALEKILEAIEELGL-KIKAILLTHGHFDHIGGLAELKEAPG-----APVYIHEADAELLEDPELNL---AF 92

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 42564134 216 IIPGAAVSELEFKVIHEDQPFVVNDLKITPLPV-WHGSnyrslgfrfGNVCYISDVSDI 273
Cdd:cd06262  93 FGGGPLPPPEPDILLEDGDTIELGGLELEVIHTpGHTP---------GSVCFYIEEEGV 142
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
116-318 1.12e-08

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 54.68  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134   116 RNRRLNTSILVRyirpSGTSNILIDCG------KFFYHSALRwfptFGLRTLDAVVITHSHADAIGGLDDLRDWTNnvqp 189
Cdd:pfam00753   1 LGPGQVNSYLIE----GGGGAVLIDTGgsaeaaLLLLLAALG----LGPKDIDAVILTHGHFDHIGGLGELAEATD---- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134   190 hIPIYTAIRDLEVMKKTHYYLVDTSVIIPGAAVSELE---FKVIHEDQPFVVNDLKITPLPVwHGSNYRSLGFRFGNVCY 266
Cdd:pfam00753  69 -VPVIVVAEEARELLDEELGLAASRLGLPGPPVVPLPpdvVLEEGDGILGGGLGLLVTHGPG-HGPGHVVVYYGGGKVLF 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 42564134   267 ISDVSdIPEETYPLlkdcDLLIMDALRPDRSSATHFGlpRALEEVRKIKPKR 318
Cdd:pfam00753 147 TGDLL-FAGEIGRL----DLPLGGLLVLHPSSAESSL--ESLLKLAKLKAAV 191
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 116-291 3.65e-08

Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; 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. 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. 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; this subgroup includes the short form (ELAC1). Only the short form exists in bacteria. 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: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 53.61  E-value: 3.65e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 116 RNRRLnTSILVRYirpsGTSNILIDCG-----KFFYHSalrwfptFGLRTLDAVVITHSHADAIGGLDDL---RDwTNNV 187
Cdd:cd07717  13 PERNL-SSIALRL----EGELWLFDCGegtqrQLLRAG-------LSPSKIDRIFITHLHGDHILGLPGLlstMS-LLGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 188 QPHIPIY--TAIRDlevmkkthyyLVDTSVIIPGAAVS-ELEFKVIHEDQPFVVND--LKITPLPVWHGsnYRSLGFRF- 261
Cdd:cd07717  80 TEPLTIYgpKGLKE----------FLETLLRLSASRLPyPIEVHELEPDPGLVFEDdgFTVTAFPLDHR--VPCFGYRFe 147

                       170       180       190
                ....*....|....*....|....*....|..
gi 42564134 262 -G-NVCYISDVSDiPEETYPLLKDCDLLIMDA 291
Cdd:cd07717 148 eGrKIAYLGDTRP-CEGLVELAKGADLLIHEA 178
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 128-270 4.58e-07

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: 48.80  E-value: 4.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 128 YIRpSGTSNILIDCGkffyhsalrwfptFGLRT--------------LDAVVITHSHADAIGGLDDLRDWTNnvqphIPI 193
Cdd:cd07733  13 YLE-TEDGKLLIDAG-------------LSGRKitgrlaeigrdpedIDAILVTHEHADHIKGLGVLARKYN-----VPI 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 194 YTAIRDLEVMKKtHYYLVDTSviipgaavselEFKVIHEDQPFVVNDLKITPLPVWHGSnYRSLGFRFGN----VCYISD 269
Cdd:cd07733  74 YATAGTLRAMER-KVGLIDVD-----------QKQIFEPGETFSIGDFDVESFGVSHDA-ADPVGYRFEEggrrFGMLTD 140


                .
gi 42564134 270 V 270
Cdd:cd07733 141 L 141
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 133-177 4.92e-07

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: 49.76  E-value: 4.92e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 42564134 133 GTSNILIDCGKFF---YHSALRWFP-TFGLRTLDAVVITHSHADAIGGL 177
Cdd:cd16295  20 GGKRILLDCGLFQggkELEELNNEPfPFDPKEIDAVILTHAHLDHSGRL 68
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 131-177 6.52e-07

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 50.57  E-value: 6.52e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 42564134 131 PSGTSNILIDCGKFFYHSALRW--FPtFGLRTLDAVVITHSHADAIGGL 177
Cdd:COG1236  20 ETGGTRILIDCGLFQGGKERNWppFP-FRPSDVDAVVLTHAHLDHSGAL 67
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 223-291 1.53e-06

MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain; Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. 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: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 48.26  E-value: 1.53e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42564134 223 SELEFKVIHEDQPFVVNDLKITPLPVWHGSNyrSLGFRF----GNVCYISDV------SDIPEETYPLLKDCDLLIMDA 291
Cdd:cd07715 121 AAIEFHDLEPGEPFSIGGVTVTTIPLNHPGG--ALGYRIeedgKSVVYATDTehypddGESDEALLEFARGADLLIHDA 197
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 123-231 1.70e-06

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 47.90  E-value: 1.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 123 SILVRyirpSGTSNILIDCGKFFYHSALRWFP---TFGLRTLDAVVITHSHADAIGGLDDLRD-------WTNNVQPHIP 192
Cdd:cd07731  12 AILIQ----TPGKTILIDTGPRDSFGEDVVVPylkARGIKKLDYLILTHPDADHIGGLDAVLKnfpvkevYMPGVTHTTK 87

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 42564134 193 IYTAIRDLEVMKKTHYYLVDTSVIIPgaaVSELEFKVIH 231
Cdd:cd07731  88 TYEDLLDAIKEKGIPVTPCKAGDRWQ---LGGVSFEVLS 123
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 132-231 1.73e-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: 47.91  E-value: 1.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 132 SGTSNILIDCG--KFFYHSALRWF-PTFGLRTLDAVVITHSHADAIGGLDDLRDWTNNvqPHIPIY----TAIRDLEVMK 204
Cdd:cd07722  25 TGKRRILIDTGegRPSYIPLLKSVlDSEGNATISDILLTHWHHDHVGGLPDVLDLLRG--PSPRVYkfprPEEDEDPDED 102

                        90       100
                ....*....|....*....|....*...
gi 42564134 205 KTHY-YLVDTSVIipgaAVSELEFKVIH 231
Cdd:cd07722 103 GGDIhDLQDGQVF----KVEGATLRVIH 126
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 137-240 4.68e-06

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: 46.83  E-value: 4.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 137 ILIDCG-KFFYHSALRWFPTFGLRT--LDAVVITHSHADAIGGLDDLRDWtnnvqPHIPIYTAIRDLEVMKKTHYYLVDT 213
Cdd:cd07721  23 TLIDTGlPGSAKRILKALRELGLSPkdIRRILLTHGHIDHIGSLAALKEA-----PGAPVYAHEREAPYLEGEKPYPPPV 97

                        90       100
                ....*....|....*....|....*..
gi 42564134 214 SVIIPGAAVSELEFKVIHEDQPFVVND 240
Cdd:cd07721  98 RLGLLGLLSPLLPVKPVPVDRTLEDGD 124
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 161-250 9.04e-06

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. 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: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 46.07  E-value: 9.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 161 LDAVVITHSHADAIGGLDDLRdwtnnvqPHIPIYTAirdlevmKKTHYYLVDTSVIIPGAAVSELEFKVIHEDQPFVVND 240
Cdd:cd07732  76 VDAVLLSHAHLDHYGLLNYLR-------PDIPVYMG-------EATKRILKALLPFFGEGDPVPRNIRVFESGKSFTIGD 141

                        90
                ....*....|
gi 42564134 241 LKITPLPVWH 250
Cdd:cd07732 142 FTVTPYLVDH 151
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 122-270 2.01e-05

class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. 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: 293821  Cd Length: 259  Bit Score: 45.67  E-value: 2.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 122 TSILvryIRPSGTSN-ILIDCG-------------KFFYHSALRWFptFGLRTLDAVVITHSHADAIGGL----DDLRDW 183
Cdd:cd07735  18 SSFL---LDPAGSDGdILLDAGtgvgalsleemfnDILFPSQKAAY--ELYQRIRHYLITHAHLDHIAGLpllsPNDGGQ 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 184 TNnvqPHIPIYTAIRDLEVMKKtHYY-------LVDtsviIPGAAVSELEFKVIHEDQPFVVNDLKITPLPVWHGSNYrS 256
Cdd:cd07735  93 RG---SPKTIYGLPETIDALKK-HIFnwviwpdFTS----IPSGKYPYLRLEPIEPEYPIALTGLSVTAFPVSHGVPV-S 163

                       170
                ....*....|....*...
gi 42564134 257 LGFRFGN----VCYISDV 270
Cdd:cd07735 164 TAFLIRDggdsFLFFGDT 181
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 133-248 2.83e-05

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: 44.68  E-value: 2.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 133 GTSNILIDCG--KFFYHSALRWFPTFGLRtLDAVVITHSHADAIGGLDDLRDWTNnvqphIPIYTAIRDLEVMKKTHYYL 210
Cdd:COG0491  23 GDGAVLIDTGlgPADAEALLAALAALGLD-IKAVLLTHLHPDHVGGLAALAEAFG-----APVYAHAAEAEALEAPAAGA 96

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 42564134 211 VDTSVIIPgaavselEFKVIHEDQPFVVNDLKITPLPV 248
Cdd:COG0491  97 LFGREPVP-------PDRTLEDGDTLELGGPGLEVIHT 127
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 136-322 3.09e-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: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 44.49  E-value: 3.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 136 NILIDCGKFFYHSALRwfPTFGLRTLDAVVITHSHADaigglddlrdwtnnvqpHipiYTairDLEVM--------KKTH 207
Cdd:cd07741  31 NIHIDPGPGALVRMCR--PKLDPTKLDAIILSHRHLD-----------------H---SN---DANVLieamteggFKKR 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 208 YYLV-------DTSVIIPGAAVSELEFKVIHED-QPFVVNDLKITPLPVWHGSNYrSLGFRFGN----VCYISDVSDIPE 275
Cdd:cd07741  86 GTLLapedalnGEPVVLLYYHRRKLEEIEILEEgDEYELGGIKIEATRHKHSDPT-TYGFIFRTsdkkIGYISDTRYFEE 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 42564134 276 -ETYPllKDCDLLIMDALRPDRS-SATHFGLPRALEEVRKIKPKRTLFT 322
Cdd:cd07741 165 lIEYY--SNCDVLIINVTRPRPRkGVDHLSVEDVEKILKEIKPKLAILT 211
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 136-348 4.32e-05

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 44.14  E-value: 4.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 136 NILIDcgKFFYHSALRWFPT----FGLRTLDAVVITHSHADAiggLDDlrdwtnnvqphipiyTAIRDLevmKKTHyylv 211
Cdd:COG2220  22 RILID--PVFSGRASPVNPLpldpEDLPKIDAVLVTHDHYDH---LDD---------------ATLRAL---KRTG---- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 212 dTSVIIP---GAAVSELEFKVIHE---DQPFVVNDLKITPLPVWHGSNYRSLG--------FRFGNVC--------YISD 269
Cdd:COG2220  75 -ATVVAPlgvAAWLRAWGFPRVTEldwGESVELGGLTVTAVPARHSSGRPDRNgglwvgfvIETDGKTiyhagdtgYFPE 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 270 VSDIPEEtYPLlkdcDLLIM--DALRPdrssatHFGLPRALEEVRKIKPKRTLFT--GMMHLMDHEKVsEELEKLRNTEG 345
Cdd:COG2220 154 MKEIGER-FPI----DVALLpiGAYPF------TMGPEEAAEAARDLKPKVVIPIhyGTFPLLDEDPL-ERFAAALAAAG 221


                ...
gi 42564134 346 LDV 348
Cdd:COG2220 222 VRV 224
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 125-177 2.88e-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: 41.77  E-value: 2.88e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42564134 125 LVRyirpSGTSNILIDCGkffyhSALRWFPTFG--LRTL----------DAVVITHSHADAIGGL 177
Cdd:cd07720  53 LVR----TGGRLILVDTG-----AGGLFGPTAGklLANLaaagidpediDDVLLTHLHPDHIGGL 108
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 160-231 4.93e-04

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: 40.14  E-value: 4.93e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42564134 160 TLDAVVITHSHADAIGGLDDLRDWTnnvqPHIPIYtAIRDLEVMKKTHyYLVDTSVIipgaAVSELEFKVIH 231
Cdd:cd07723  43 TLTAILTTHHHWDHTGGNAELKALF----PDAPVY-GPAEDRIPGLDH-PVKDGDEI----KLGGLEVKVLH 104
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 123-340 1.17e-03

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


Pssm-ID: 293799  Cd Length: 269  Bit Score: 40.30  E-value: 1.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 123 SILVRYirpsGTSNILIDCGK--FFYHSALRwfptFG--LRTLDAVVITHSHADAIGGLDDLRDwtNNvqPHIPIYtaIR 198
Cdd:cd07713  22 SLLIET----EGKKILFDTGQsgVLLHNAKK----LGidLSDIDAVVLSHGHYDHTGGLKALLE--LN--PKAPVY--AH 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 199 DlEVMKKtHYYLVDTSVIIPGAAVSELE---FKVIHEDQPFVVND--LKITPLPVWHGSNYRSLG-FRFGNVCYISDvsD 272
Cdd:cd07713  88 P-DAFEP-RYSKRGGGKKGIGIGREELEkagARLVLVEEPTEIAPgvYLTGEIPRVTDFEKGNPGlFVKEDGGLVPD--D 163

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42564134 273 IPEETYPLLKDCD-LLIMdalrpdrSSATHFGLPRALEEVRKIKPKRTLFT--GMMHLMDH-----EKVSEELEKL 340
Cdd:cd07713 164 FEDEQALVIDTKKgLVVI-------TGCSHAGIVNILEHAKKLTGGDKIYAviGGFHLVGAseeriEKTIAALKEL 232
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 163-269 1.35e-03

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. 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: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 39.70  E-value: 1.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 163 AVVITHSHADAIGGLddlrdwtnnvqPHI------PIYTAIRDLEVMKKthyYLVDTSVIIpgaavsELEFKVIHEDQPF 236
Cdd:cd07714  58 GIFITHGHEDHIGAL-----------PYLlpelnvPIYATPLTLALIKK---KLEEFKLIK------KVKLNEIKPGERI 117

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 42564134 237 VVNDLKITPLPVWHgSNYRSLGFRF----GNVCYISD 269
Cdd:cd07714 118 KLGDFEVEFFRVTH-SIPDSVGLAIktpeGTIVHTGD 153
PRK00055 PRK00055
ribonuclease Z; Reviewed
 79-177 1.37e-03

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 39.78  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134   79 EIVFMGTGTseGIPRvscltnplktcsvctkatepgnRNRRLnTSILVRYirpsGTSNILIDCGKFFYHSALRwfPTFGL 158
Cdd:PRK00055   3 ELTFLGTGS--GVPT----------------------PTRNV-SSILLRL----GGELFLFDCGEGTQRQLLK--TGIKP 51

                         90
                 ....*....|....*....
gi 42564134  159 RTLDAVVITHSHADAIGGL 177
Cdd:PRK00055  52 RKIDKIFITHLHGDHIFGL 70
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
123-194 1.74e-03

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 39.48  E-value: 1.74e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 42564134 123 SILVRYirpsGTSNILIDCG--KFFYHSALRwfptFG--LRTLDAVVITHSHADAIGGLDDLRDwtnnVQPHIPIY 194
Cdd:COG1237  24 SALIET----EGKRILFDTGqsDVLLKNAEK----LGidLSDIDAVVLSHGHYDHTGGLPALLE----LNPKAPVY 87
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 128-229 3.41e-03

metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. Includes chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1.


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 38.42  E-value: 3.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 128 YIRPSGTSnILIDC--GKFFYHSALRWF-PTFGLRtLDAVVITHSHADAIGGLDDLRDwtnnvqPHIPIYTAIRDLEVMK 204
Cdd:cd16285  30 IVIDGKGL-VLIDTpwTEAQTATLLDWIeKKLGKP-VTAAISTHSHDDRTGGIKALNA------RGIPTYATALTNELAK 101

                        90       100
                ....*....|....*....|....*
gi 42564134 205 KtHYYLVDTSVIIPGAAVSELEFKV 229
Cdd:cd16285 102 K-EGKPVPTHSLKGALTLGFGPLEV 125
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 130-231 4.20e-03

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: 38.10  E-value: 4.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134 130 RPSGTSNILIDCGkFFYHSALRWFPTFGLrTLDAVVITHSHADAIGGLDDLRDWTNnvqphIPIYTAIRDLEvmkktHYY 209
Cdd:cd16322  18 DEGGGEAVLVDPG-DESEKLLARFGTTGL-TLLYILLTHAHFDHVGGVADLRRHPG-----APVYLHPDDLP-----LYE 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 42564134 210 LVDTSVIIPGAAV------------------SELEFKVIH 231
Cdd:cd16322  86 AADLGAKAFGLGIeplpppdrlledgqtltlGGLEFKVLH 125
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 80-172 4.48e-03

Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; 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; this eukaryotic subgroup includes short forms (ELAC1) and the C-terminus of long forms including human ELAC2. 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: 293804 [Multi-domain]  Cd Length: 204  Bit Score: 37.91  E-value: 4.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42564134  80 IVFMGTGtsegiprvSCLtnPLKTcsvctkatepgnRNrrlNTSILVRYirpSGTSNILIDCGKFFYHSALRWFPTFG-- 157
Cdd:cd07718   1 VVFLGTG--------SAI--PSKY------------RN---VSGILLRI---PGDGSILLDCGEGTLGQLRRHYGPEEad 52

                        90
                ....*....|....*..
gi 42564134 158 --LRTLDAVVITHSHAD 172
Cdd:cd07718  53 evLRNLKCIFISHLHAD 69
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 128-194 4.94e-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: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 37.90  E-value: 4.94e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42564134 128 YIRPSGTSNILIDCG--KFFYHSALRWFPTFGLrTLDAVVITHSHADAIGGLDDLRDwtnnvQPHIPIY 194
Cdd:cd07743  12 VYVFGDKEALLIDSGldEDAGRKIRKILEELGW-KLKAIINTHSHADHIGGNAYLQK-----KTGCKVY 74
 
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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