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Conserved domains on  [gi|1375311714|gb|PTK57624|]
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MBL fold metallo-hydrolase [Staphylococcus haemolyticus]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10870184)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 8-195 2.15e-75

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: 225.99  E-value: 2.15e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714   8 SVLASGSTGNATYVESDKGSLLVDVGLTGKKMEDLFSQIDRNIKDLNGILVTHEHSDHIKGLGVLARKYGLPIYANENTW 87
Cdd:cd07733     1 SVLASGSKGNCTYLETEDGKLLIDAGLSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  88 KAIEKKDSKIPMDQKFIFNPYETKSIAGFDIESFNVSHDAIDPQFYIFHNNYKKFTMITDtgyvsdrmkgmiqgsdafmf 167
Cdd:cd07733    81 RAMERKVGLIDVDQKQIFEPGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTD-------------------- 140

                         170       180
                  ....*....|....*....|....*...
gi 1375311714 168 esnhdvdmlrmcrypwkTKQRILSDMGH 195
Cdd:cd07733   141 -----------------LKQRILSDRGH 151
 
Name Accession Description Interval E-value
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 8-195 2.15e-75

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: 225.99  E-value: 2.15e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714   8 SVLASGSTGNATYVESDKGSLLVDVGLTGKKMEDLFSQIDRNIKDLNGILVTHEHSDHIKGLGVLARKYGLPIYANENTW 87
Cdd:cd07733     1 SVLASGSKGNCTYLETEDGKLLIDAGLSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  88 KAIEKKDSKIPMDQKFIFNPYETKSIAGFDIESFNVSHDAIDPQFYIFHNNYKKFTMITDtgyvsdrmkgmiqgsdafmf 167
Cdd:cd07733    81 RAMERKVGLIDVDQKQIFEPGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTD-------------------- 140

                         170       180
                  ....*....|....*....|....*...
gi 1375311714 168 esnhdvdmlrmcrypwkTKQRILSDMGH 195
Cdd:cd07733   141 -----------------LKQRILSDRGH 151
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 6-244 1.54e-61

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 194.73  E-value: 1.54e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714   6 RMSVLASGSTG-----------------------NATYVESDKGSLLVDVGLTGKKmedLFSQIDRNIKDLNGILVTHEH 62
Cdd:COG1235     2 KVTFLGSGSSGgvpqigcdcpvcastdprygrtrSSILVEADGTRLLIDAGPDLRE---QLLRLGLDPSKIDAILLTHEH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  63 SDHIKGLGVLARKYG---LPIYANENTWKAIEKKDSKIPMD-----QKFIFNPYETKSIAGFDIESFNVSHDAIDPQFYI 134
Cdd:COG1235    79 ADHIAGLDDLRPRYGpnpIPVYATPGTLEALERRFPYLFAPypgklEFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGYR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714 135 FHNNYKKFTMITDTGYVSDRMKGMIQGSDAFMFESNHDVDmlrmcrypwktkqrilsDMGHVSNEDAGLAMTDVitgNTK 214
Cdd:COG1235   159 IEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATYDDP-----------------EPGHLSNEEALELLARL---GPK 218

                         250       260       270
                  ....*....|....*....|....*....|
gi 1375311714 215 RIYLSHLSQDNNMKDLARMSVSQVLNEHDI 244
Cdd:COG1235   219 RLVLTHLSPDNNDHELDYDELEAALLPAGV 248
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 17-177 3.78e-17

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: 76.82  E-value: 3.78e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714   17 NATYVESDKGSLLVDVGlTGKKMEDLFSQIDRNIKDLNGILVTHEHSDHIKGLGVLARKYGLPIYANENTWKAIEKK--- 93
Cdd:smart00849   1 NSYLVRDDGGAILIDTG-PGEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLlal 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714   94 -----DSKIPMDQKFIFNPYETKSIAGFDIESFNVSHDAIDPQFYIFHNNYKKFTmiTDTGYVSDRMKGMIQGSDAFMFE 168
Cdd:smart00849  80 lgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFT--GDLLFAGGDGRTLVDGGDAAASD 157


                   ....*....
gi 1375311714  169 SNHDVDMLR 177
Cdd:smart00849 158 ALESLLKLL 166
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 52-220 1.15e-16

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: 75.81  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  52 DLNGILVTHEHSDHIKGLGVLARKYGLPIYANENTWKAIEKKDSKIPMDQKF-----IFNPYETKSIA--GFDIESFNVS 124
Cdd:pfam12706  28 PIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLRRNFPYLFLLEHYgvrvhEIDWGESFTVGdgGLTVTATPAR 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714 125 HDAI--------DPQFYIFHNNYKKFTMITDTGYVSDRMKGMIQGSDAFMFESNHDVDMLRMcrypwktkqrilsDMGHV 196
Cdd:pfam12706 108 HGSPrgldpnpgDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLGGADLLLLDGGAWRDDEMI-------------HMGHM 174

                         170       180
                  ....*....|....*....|....
gi 1375311714 197 SNEDAGLAMTDVitgNTKRIYLSH 220
Cdd:pfam12706 175 TPEEAVEAAADL---GARRKVLIH 195
PRK02113 PRK02113
MBL fold metallo-hydrolase;
21-220 2.35e-07

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 50.55  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  21 VESDKGSLLVDVGltgkkmEDLFSQIDRN-IKDLNGILVTHEHSDHIKGLGVL---ARKYGLPIYANENTWKAIEkkdSK 96
Cdd:PRK02113   40 VETEGARILIDCG------PDFREQMLRLpFGKIDAVLITHEHYDHVGGLDDLrpfCRFGEVPIYAEQYVAERLR---SR 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  97 IPMdqKFIFNPYE-TKSIAGFDIE---SFNVSHDAIDPqFYIFHNN-----YKkftmITDTGYVSDrMKGMIQGSdafmF 167
Cdd:PRK02113  111 MPY--CFVEHSYPgVPNIPLREIEpdrPFLVNHTEVTP-LRVMHGKlpilgYR----IGKMAYITD-MLTMPEEE----Y 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1375311714 168 ESNHDVDMLRMcrypwkTKQRILSDMGHVSNEDAGLAMTDVITGNTKRIYLSH 220
Cdd:PRK02113  179 EQLQGIDVLVM------NALRIAPHPTHQSLEEALENIKRIGAKETYLIHMSH 225
 
Name Accession Description Interval E-value
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 8-195 2.15e-75

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: 225.99  E-value: 2.15e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714   8 SVLASGSTGNATYVESDKGSLLVDVGLTGKKMEDLFSQIDRNIKDLNGILVTHEHSDHIKGLGVLARKYGLPIYANENTW 87
Cdd:cd07733     1 SVLASGSKGNCTYLETEDGKLLIDAGLSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  88 KAIEKKDSKIPMDQKFIFNPYETKSIAGFDIESFNVSHDAIDPQFYIFHNNYKKFTMITDtgyvsdrmkgmiqgsdafmf 167
Cdd:cd07733    81 RAMERKVGLIDVDQKQIFEPGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTD-------------------- 140

                         170       180
                  ....*....|....*....|....*...
gi 1375311714 168 esnhdvdmlrmcrypwkTKQRILSDMGH 195
Cdd:cd07733   141 -----------------LKQRILSDRGH 151
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 6-244 1.54e-61

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 194.73  E-value: 1.54e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714   6 RMSVLASGSTG-----------------------NATYVESDKGSLLVDVGLTGKKmedLFSQIDRNIKDLNGILVTHEH 62
Cdd:COG1235     2 KVTFLGSGSSGgvpqigcdcpvcastdprygrtrSSILVEADGTRLLIDAGPDLRE---QLLRLGLDPSKIDAILLTHEH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  63 SDHIKGLGVLARKYG---LPIYANENTWKAIEKKDSKIPMD-----QKFIFNPYETKSIAGFDIESFNVSHDAIDPQFYI 134
Cdd:COG1235    79 ADHIAGLDDLRPRYGpnpIPVYATPGTLEALERRFPYLFAPypgklEFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGYR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714 135 FHNNYKKFTMITDTGYVSDRMKGMIQGSDAFMFESNHDVDmlrmcrypwktkqrilsDMGHVSNEDAGLAMTDVitgNTK 214
Cdd:COG1235   159 IEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATYDDP-----------------EPGHLSNEEALELLARL---GPK 218

                         250       260       270
                  ....*....|....*....|....*....|
gi 1375311714 215 RIYLSHLSQDNNMKDLARMSVSQVLNEHDI 244
Cdd:COG1235   219 RLVLTHLSPDNNDHELDYDELEAALLPAGV 248
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
18-233 2.81e-17

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 78.70  E-value: 2.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  18 ATYVESDKGSLLVDVGltgkkmEDLFSQIDR---NIKDLNGILVTHEHSDHIKGLGVL--ARKYG-----LPIYANENTW 87
Cdd:COG1234    21 SYLLEAGGERLLIDCG------EGTQRQLLRaglDPRDIDAIFITHLHGDHIAGLPGLlsTRSLAgrekpLTIYGPPGTK 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  88 KAIEK----KDSKIPMDQKFI-FNPYETKSIAGFDIESFNVSHDAidPQF-YIFHNNYKKFTMITDTGYvSDRMKGMIQG 161
Cdd:COG1234    95 EFLEAllkaSGTDLDFPLEFHeIEPGEVFEIGGFTVTAFPLDHPV--PAYgYRFEEPGRSLVYSGDTRP-CEALVELAKG 171

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1375311714 162 SDAFMFESNHDVDMLRMCRypwktkqrilsDMGHVSNEDAGLAMTDVitgNTKRIYLSHLSQDnnMKDLARM 233
Cdd:COG1234   172 ADLLIHEATFLDEEAELAK-----------ETGHSTAKEAAELAAEA---GVKRLVLTHFSPR--YDDPEEL 227
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 17-177 3.78e-17

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: 76.82  E-value: 3.78e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714   17 NATYVESDKGSLLVDVGlTGKKMEDLFSQIDRNIKDLNGILVTHEHSDHIKGLGVLARKYGLPIYANENTWKAIEKK--- 93
Cdd:smart00849   1 NSYLVRDDGGAILIDTG-PGEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLlal 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714   94 -----DSKIPMDQKFIFNPYETKSIAGFDIESFNVSHDAIDPQFYIFHNNYKKFTmiTDTGYVSDRMKGMIQGSDAFMFE 168
Cdd:smart00849  80 lgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFT--GDLLFAGGDGRTLVDGGDAAASD 157


                   ....*....
gi 1375311714  169 SNHDVDMLR 177
Cdd:smart00849 158 ALESLLKLL 166
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 20-163 6.49e-17

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: 76.36  E-value: 6.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  20 YVESDKGSLLVDvglTGKkmeDLFSQ-IDRNIKDLNGILVTHEHSDHIKGLG-----VLARKYGLPIYANENTWKAIEKK 93
Cdd:cd16279    39 LIETGGKNILID---TGP---DFRQQaLRAGIRKLDAVLLTHAHADHIHGLDdlrpfNRLQQRPIPVYASEETLDDLKRR 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1375311714  94 DSKIPMDQKF---------IFNPYETKSIAGFDIESFNVSHDAIDPQFYIFhnnyKKFTMITDTGYVSDRMKGMIQGSD 163
Cdd:cd16279   113 FPYFFAATGGggvpkldlhIIEPDEPFTIGGLEITPLPVLHGKLPSLGFRF----GDFAYLTDVSEIPEESLEKLRGLD 187
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 52-220 1.15e-16

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: 75.81  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  52 DLNGILVTHEHSDHIKGLGVLARKYGLPIYANENTWKAIEKKDSKIPMDQKF-----IFNPYETKSIA--GFDIESFNVS 124
Cdd:pfam12706  28 PIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLRRNFPYLFLLEHYgvrvhEIDWGESFTVGdgGLTVTATPAR 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714 125 HDAI--------DPQFYIFHNNYKKFTMITDTGYVSDRMKGMIQGSDAFMFESNHDVDMLRMcrypwktkqrilsDMGHV 196
Cdd:pfam12706 108 HGSPrgldpnpgDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLGGADLLLLDGGAWRDDEMI-------------HMGHM 174

                         170       180
                  ....*....|....*....|....
gi 1375311714 197 SNEDAGLAMTDVitgNTKRIYLSH 220
Cdd:pfam12706 175 TPEEAVEAAADL---GARRKVLIH 195
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 5-119 5.41e-16

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: 74.34  E-value: 5.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714   5 IRMSVLASGSTGNATYVESDKGSLLVDVGLTGKKMEDLFSQIDRNIKDLNGILVTHEHSDHIKGLGVLARKYGLPIYANE 84
Cdd:COG0491     4 LPGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHA 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1375311714  85 NTWKAIEKKDSKIPMDQKFI-----FNPYETKSIAGFDIE 119
Cdd:COG0491    84 AEAEALEAPAAGALFGREPVppdrtLEDGDTLELGGPGLE 123
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 10-93 2.08e-15

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: 72.64  E-value: 2.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  10 LASGSTGNATYVESDKGSLLVDVGLTG--KKMEDLFSQIDRNIKDLNGILVTHEHSDHIKGLGVLARKYGLPIYANENTW 87
Cdd:cd07721     5 LPLLPPVNAYLIEDDDGLTLIDTGLPGsaKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEREA 84


                  ....*.
gi 1375311714  88 KAIEKK 93
Cdd:cd07721    85 PYLEGE 90
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
16-220 2.78e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 69.32  E-value: 2.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  16 GNATYVESDKGSLLVDVGLTGKKM-EDLFSQIDRNIKDLNGILVTHEHSDHIKGLGVLARKYGLPIYANENTWKAIEKKD 94
Cdd:pfam00753   6 VNSYLIEGGGGAVLIDTGGSAEAAlLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  95 SKIPMDQKFIFNPYETKSIAGFDIESFNVSHDAIDPqFYIFHNnykkFTMITDTGYVSDRMKGMIQGSDAFMFESNHDVD 174
Cdd:pfam00753  86 LGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLG-LLVTHG----PGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLD 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1375311714 175 mlrmcrypwkTKQRILSDMGHVSNEDAGLAMTDVITGNTKRIYLSH 220
Cdd:pfam00753 161 ----------LPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 17-140 1.36e-13

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: 68.59  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  17 NATYVESDKGSLLVDVGLTGKKMEDL--------FSQIDRNIKDLNGILVTHEHSDHIKGLGVLARKYGLPIYANENTWK 88
Cdd:cd07714    12 NMYVVEYDDDIIIIDCGLKFPDEDMPgvdyiipdFSYLEENKDKIKGIFITHGHEDHIGALPYLLPELNVPIYATPLTLA 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1375311714  89 AIEKK--DSKIPMDQKF-IFNPYETKSIAGFDIESFNVSHDAID--------PQFYIFH-NNYK 140
Cdd:cd07714    92 LIKKKleEFKLIKKVKLnEIKPGERIKLGDFEVEFFRVTHSIPDsvglaiktPEGTIVHtGDFK 155
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 9-119 1.53e-12

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: 64.61  E-value: 1.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714   9 VLASGSTGNATYV--ESDKGSLLVDVGLTGkkMEDLFSQIDRNIKDLNGILVTHEHSDHIKGLGVLARKYGLPIYANENT 86
Cdd:cd06262     2 RLPVGPLQTNCYLvsDEEGEAILIDPGAGA--LEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEAD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1375311714  87 WKAIEKKD---------SKIPMDQKFIFNPYETKSIAGFDIE 119
Cdd:cd06262    80 AELLEDPElnlaffgggPLPPPEPDILLEDGDTIELGGLELE 121
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
17-136 2.84e-09

mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 56.99  E-value: 2.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  17 NATYVESDKGSLLVDVGLtgkkM---EDL---------FSQIDRNIKDLNGILVTHEHSDHIKGLGVLARKYGLPIYANE 84
Cdd:COG0595    20 NMYVYEYDDDIIIVDCGL----KfpeDEMpgvdlvipdISYLEENKDKIKGIVLTHGHEDHIGALPYLLKELNVPVYGTP 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1375311714  85 NTWKAIEKK--DSKIPMDQKF-IFNPYETKSIAGFDIESFNVSH---D----AID-PQFYIFH 136
Cdd:COG0595    96 LTLALLEAKlkEHGLLKKVKLhVVKPGDRIKFGPFKVEFFRVTHsipDslglAIRtPAGTIVH 158
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 6-125 6.80e-09

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: 53.99  E-value: 6.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714   6 RMSVL-ASGST---GNAT--Y-VESDKGSLLVDVG---LTGkkmedLFSQIDrnIKDLNGILVTHEHSDHIKGLGVL--A 73
Cdd:cd07716     1 KLTVLgCSGSYpgpGGACsgYlLEADGFRILLDCGsgvLSR-----LQRYID--PEDLDAVVLSHLHPDHCADLGVLqyA 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1375311714  74 RKYG--------LPIYANENTWKAIEKKDSkipMDQKFIFNPYE---TKSIAGFDIESFNVSH 125
Cdd:cd07716    74 RRYHprgarkppLPLYGPAGPAERLAALYG---LEDVFDFHPIEpgePLEIGPFTITFFRTVH 133
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 16-129 1.56e-08

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: 53.38  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  16 GNATYVESDKGSLLVDVGLTGKKMEDLFSQIDRNIKD--------------------------LNGILVTHEHSDHIKGL 69
Cdd:cd07732    13 GNCIEVETGGTRILLDFGLPLDPESKYFDEVLDFLELgllpdivglyrdplllgglrseedpsVDAVLLSHAHLDHYGLL 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1375311714  70 GVLARKygLPIYANENTWKAIE----KKDSKIPMDQKFI-FNPYETKSIAGFDIESFNVSHDAID 129
Cdd:cd07732    93 NYLRPD--IPVYMGEATKRILKallpFFGEGDPVPRNIRvFESGKSFTIGDFTVTPYLVDHSAPG 155
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 17-121 2.04e-08

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: 53.06  E-value: 2.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  17 NATYVESDKGSLLVDVGLTGKKMEDLFSQI-DRNIKDLNGILVTHEHSDHIKGLGVLARKyGLPIYANENTwKAIEKKDS 95
Cdd:cd16285    27 NGLIVIDGKGLVLIDTPWTEAQTATLLDWIeKKLGKPVTAAISTHSHDDRTGGIKALNAR-GIPTYATALT-NELAKKEG 104

                          90       100
                  ....*....|....*....|....*.
gi 1375311714  96 KIPMDQKFIFNpyetKSIAGFDIESF 121
Cdd:cd16285   105 KPVPTHSLKGA----LTLGFGPLEVF 126
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 9-169 2.58e-08

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: 52.27  E-value: 2.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714   9 VLASGS-----TGN--ATYVESDKGSLLVDVG-LTGKKMEdlfsQIDRNIKDLNGILVTHEHSDHIKGLG--VLARKYG- 77
Cdd:cd16272     3 FLGTGGavpslTRNtsSYLLETGGTRILLDCGeGTVYRLL----KAGVDPDKLDAIFLSHFHLDHIGGLPtlLFARRYGg 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  78 ----LPIYANENTWKAIEK-KDSKIPMDQK---FIFNPYETKS----IAGFDIESFNVSHdaIDPQF-YIFHNNYKKFTM 144
Cdd:cd16272    79 rkkpLTIYGPKGIKEFLEKlLNFPVEILPLgfpLEIEELEEGGevleLGDLKVEAFPVKH--SVESLgYRIEAEGKSIVY 156

                         170       180
                  ....*....|....*....|....*
gi 1375311714 145 ITDTGYvSDRMKGMIQGSDAFMFES 169
Cdd:cd16272   157 SGDTGP-CENLVELAKGADLLIHEC 180
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 20-156 4.91e-08

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: 52.62  E-value: 4.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  20 YVESDKGSLLVDVGLTG------KKMEdlfsqIDrnIKDLNGILVTHEHSDHIKGL-GVLARKYGLPIYANENtwkAIEK 92
Cdd:cd07713    24 LIETEGKKILFDTGQSGvllhnaKKLG-----ID--LSDIDAVVLSHGHYDHTGGLkALLELNPKAPVYAHPD---AFEP 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1375311714  93 KDSKIPMDQKFIFNPYETKSIAGFDIESFNVSHdAIDPQFYI---------FHNNYKKFTMITDTGYVSDRMK 156
Cdd:cd07713    94 RYSKRGGGKKGIGIGREELEKAGARLVLVEEPT-EIAPGVYLtgeiprvtdFEKGNPGLFVKEDGGLVPDDFE 165
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 11-82 6.89e-08

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 52.88  E-value: 6.89e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1375311714  11 ASGSTGNATYVESDKGSLLVDVGLTGKKMEDLFSQIDRNIKDLNGILVTHEHSDHIKGLGVLARK-YGLPIYA 82
Cdd:COG1236     9 AGEVTGSCYLLETGGTRILIDCGLFQGGKERNWPPFPFRPSDVDAVVLTHAHLDHSGALPLLVKEgFRGPIYA 81
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 20-148 1.51e-07

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: 50.31  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  20 YVESDKGSLLVDVGLTgkkmeDLFSQidRNIKDLNGILVTHEHSDHIKGLGVLARKYGLPIyaneNTWKAIEKKDSKI-- 97
Cdd:cd07736    41 LIEVDGERILLDAGLT-----DLAER--FPPGSIDAILLTHFHMDHVQGLFHLRWGVGDPI----PVYGPPDPQGCADlf 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1375311714  98 ----PMDQKFIFNPYETKSIAGFDIESFNVSHDAidPQF-YIFHNNYKKFTMITDT 148
Cdd:cd07736   110 khpgILDFQPLVAPFQSFELGGLKITPLPLNHSK--PTFgYLLESGGKRLAYLTDT 163
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 20-85 1.56e-07

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 50.22  E-value: 1.56e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1375311714  20 YVESDKGSLLVDVGLTGKKMEDLFSQIDRNIKDLNGILVTHEHSDHIKGLGVLARKYGLPIYANEN 85
Cdd:cd07743    13 YVFGDKEALLIDSGLDEDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKI 78
PRK02113 PRK02113
MBL fold metallo-hydrolase;
21-220 2.35e-07

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 50.55  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  21 VESDKGSLLVDVGltgkkmEDLFSQIDRN-IKDLNGILVTHEHSDHIKGLGVL---ARKYGLPIYANENTWKAIEkkdSK 96
Cdd:PRK02113   40 VETEGARILIDCG------PDFREQMLRLpFGKIDAVLITHEHYDHVGGLDDLrpfCRFGEVPIYAEQYVAERLR---SR 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  97 IPMdqKFIFNPYE-TKSIAGFDIE---SFNVSHDAIDPqFYIFHNN-----YKkftmITDTGYVSDrMKGMIQGSdafmF 167
Cdd:PRK02113  111 MPY--CFVEHSYPgVPNIPLREIEpdrPFLVNHTEVTP-LRVMHGKlpilgYR----IGKMAYITD-MLTMPEEE----Y 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1375311714 168 ESNHDVDMLRMcrypwkTKQRILSDMGHVSNEDAGLAMTDVITGNTKRIYLSH 220
Cdd:PRK02113  179 EQLQGIDVLVM------NALRIAPHPTHQSLEEALENIKRIGAKETYLIHMSH 225
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 17-92 2.93e-07

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


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 49.81  E-value: 2.93e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1375311714  17 NATYVESDKGSLLVDVGLTGKKMEDLFSQIDRNIKDLNGILVTHEHSDHIKGLGVLARKY-GLPIYANENTWKAIEK 92
Cdd:cd07739    17 TSTLIYGETEAVLVDAQFTRADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAFpDAKVVATPAVVAHIKA 93
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 11-92 3.90e-07

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 49.49  E-value: 3.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  11 ASGSTGNATYVESDKGSLLVDVGLT---GKKMEDLFSQI-DRNIKDLngiLVTHEHSDHIKGLGVLARKyGLPIYANENT 86
Cdd:cd16282    10 GGGFISNIGFIVGDDGVVVIDTGASprlARALLAAIRKVtDKPVRYV---VNTHYHGDHTLGNAAFADA-GAPIIAHENT 85


                  ....*.
gi 1375311714  87 WKAIEK 92
Cdd:cd16282    86 REELAA 91
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 43-223 5.81e-07

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: 49.37  E-value: 5.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  43 FSQIDRnikdlngILVTHEHSDHIKGL-GVLA------RKYGLPIYANENTWKAIEK----KDSKIPMDQKFI---FNPY 108
Cdd:cd07717    48 PSKIDR-------IFITHLHGDHILGLpGLLStmsllgRTEPLTIYGPKGLKEFLETllrlSASRLPYPIEVHelePDPG 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714 109 ETKSIAGFDIESFNVSHDaIDPQFYIFHNNyKKFTMITDTGYvSDRMKGMIQGSDAFMFESNHDVDMLRMCRypwktkqr 188
Cdd:cd07717   121 LVFEDDGFTVTAFPLDHR-VPCFGYRFEEG-RKIAYLGDTRP-CEGLVELAKGADLLIHEATFLDDDAEKAK-------- 189

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1375311714 189 ilsDMGHVSNEDAGLAMTDVitgNTKRIYLSHLSQ 223
Cdd:cd07717   190 ---ETGHSTAKQAAEIAKKA---GVKKLVLTHFSA 218
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 16-153 7.71e-07

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 48.76  E-value: 7.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  16 GNATY-VESDKGSLLVDVGLTGKKMEDLFSQIDR-NIKDLNGILVTHEHSDHI--KGLGVLARKyGLPIYANENTWKAIE 91
Cdd:COG2220    10 GHATFlIETGGKRILIDPVFSGRASPVNPLPLDPeDLPKIDAVLVTHDHYDHLddATLRALKRT-GATVVAPLGVAAWLR 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1375311714  92 KKDskipMDQKFIFNPYETKSIAGFDIESFNVSHDAIDPQF-------YIFHNNYKKFTMITDTGYVSD 153
Cdd:COG2220    89 AWG----FPRVTELDWGESVELGGLTVTAVPARHSSGRPDRngglwvgFVIETDGKTIYHAGDTGYFPE 153
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 17-105 1.57e-06

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


Pssm-ID: 293862 [Multi-domain]  Cd Length: 212  Bit Score: 47.66  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  17 NATYVESDKGSLLVDVGLTGKKMEDLFSQIDRNI-KDLNGILVTHEHSDHIKGLGVLaRKYGLPIYANENTWKAIEKK-- 93
Cdd:cd16304    27 NGLIVETSKGVVLIDTPWDDEQTEELLDWIKKKLkKPVTLAIVTHAHDDRIGGIKAL-QKRGIPVYSTKLTAQLAKKQgy 105

                          90
                  ....*....|....*
gi 1375311714  94 ---DSKIPMDQKFIF 105
Cdd:cd16304   106 pspDGILKDDTTLKF 120
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 15-86 2.30e-06

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: 47.07  E-value: 2.30e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1375311714  15 TGNATYVESDKGSLLVDVGLT-GKKMEDL--FSQIDRNIKDLNGILVTHEHSDHIKGLGVLARK-YGLPIYANENT 86
Cdd:cd16295    11 TGSCYLLETGGKRILLDCGLFqGGKELEElnNEPFPFDPKEIDAVILTHAHLDHSGRLPLLVKEgFRGPIYATPAT 86
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 16-90 2.88e-06

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 47.11  E-value: 2.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  16 GNATYVESDKGSLLVDVGL---TGKKMEDLFSQI--DRNIKdlnGILVTHEHSDHIKGLGVLA---RKYGLPIYANENTW 87
Cdd:cd07710    18 SNMTFIEGDTGLIIIDTLEsaeAAKAALELFRKHtgDKPVK---AIIYTHSHPDHFGGAGGFVeeeDSGKVPIIAPEGFM 94


                  ...
gi 1375311714  88 KAI 90
Cdd:cd07710    95 EEA 97
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 17-82 2.89e-06

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


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 47.34  E-value: 2.89e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1375311714  17 NATYVESDKGSLLVDVGLT--GKKMEDLFSQIDRNIKDLNGILVTHEHSDHIKGLGVLARKYGLPIYA 82
Cdd:cd16290    23 SAVLITSPQGLILIDGALPqsAPQIEANIRALGFRLEDVKLILNSHAHFDHAGGIAALQRDSGATVAA 90
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 18-92 2.91e-06

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


Pssm-ID: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 47.19  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  18 ATYVESDKGSLLVDvGLTGKKMedlfSQIDRNIK-------DLNGILVTHEHSDHIKGLGVLARKYGLPIYANENTWKAI 90
Cdd:cd16314    24 ALLVTSDAGHILID-GGTDKAA----PLIEANIRalgfrpeDVRYIVSSHEHFDHAGGIARLQRATGAPVVAREPAATTL 98


                  ..
gi 1375311714  91 EK 92
Cdd:cd16314    99 ER 100
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 11-141 3.06e-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) 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: 46.48  E-value: 3.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  11 ASGSTGNA---TYVESDKGSLLVDVG---LTGKKMEdlfsQIDRNikDLNGILVTHEHSDHIKGLG--------VLARKY 76
Cdd:cd07740     8 AFGSGGRLntcFHVASEAGRFLIDCGassLIALKRA----GIDPN--AIDAIFITHLHGDHFGGLPfflldaqfVAKRTR 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1375311714  77 GLPIYANENTWKAIEK-------KDSKIPmdQKF-----IFNPYETKSIAGFDIESFNVSHDAIDPQFYIFHNNYKK 141
Cdd:cd07740    82 PLTIAGPPGLRERLRRamealfpGSSKVP--RRFdleviELEPGEPTTLGGVTVTAFPVVHPSGALPLALRLEAAGR 156
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
20-155 4.17e-06

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 46.80  E-value: 4.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  20 YVESDKGSLLVDVGlTGKKMEDLFSQIDRNIKDLNGILVTHEHSDHIKGL-GVLARKYGLPIYANENTWkaiEKKDSKIP 98
Cdd:COG1237    26 LIETEGKRILFDTG-QSDVLLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLpALLELNPKAPVYAHPDAF---EKRYSKRP 101

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  99 mDQKFIFNPYETKSI--AGFDiesFNVSHDA--IDPQFYI---------FHNNYKKFTMITDTGYVSDRM 155
Cdd:COG1237   102 -GGKYIGIPFSREELekLGAR---LILVKEPteIAPGVYLtgeiprvtdFEKGDPGLYVKEDGGLVPDPF 167
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 16-76 6.29e-06

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: 46.39  E-value: 6.29e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1375311714  16 GNATYVESDKG-SLLVDVGltGKKMEDLFSQI------DRNIKDLNGILVTHEHSDHIKGLGVLARKY 76
Cdd:COG2333    11 GDAILIRTPDGkTILIDTG--PRPSFDAGERVvlpylrALGIRRLDLLVLTHPDADHIGGLAAVLEAF 76
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 13-91 8.01e-06

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


Pssm-ID: 293868  Cd Length: 252  Bit Score: 45.90  E-value: 8.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  13 GSTGNATY-VESDKGSLLVDVGLtgkkmEDLFSQIDRNIK-------DLNGILVTHEHSDHIKGLGVLARKYGLPIYANE 84
Cdd:cd16310    18 GTKGIGSYlITSNHGAILLDGGL-----EENAALIEQNIKalgfklsDIKIIINTHAHYDHAGGLAQLKADTGAKLWASR 92


                  ....*..
gi 1375311714  85 NTWKAIE 91
Cdd:cd16310    93 GDRPALE 99
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 10-84 9.04e-06

uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 45.42  E-value: 9.04e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1375311714  10 LASGSTGNATYVESDKGS---LLVDvglTGKKMEDLFSQIDRNIKDLNGILVTHEHSDHIKGLGVLARKYGLPIYANE 84
Cdd:cd16322     4 FTLGPLQENTYLVADEGGgeaVLVD---PGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHP 78
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 16-97 1.07e-05

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: 44.82  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  16 GNATYVESDKGSLLVDVGLTGKKMED-LFSQI-DRNIKDLNGILVTHEHSDHIKGL-GVLAR---------KYGLPIYAN 83
Cdd:cd07731    10 GDAILIQTPGKTILIDTGPRDSFGEDvVVPYLkARGIKKLDYLILTHPDADHIGGLdAVLKNfpvkevympGVTHTTKTY 89

                          90
                  ....*....|....
gi 1375311714  84 ENTWKAIEKKDSKI 97
Cdd:cd07731    90 EDLLDAIKEKGIPV 103
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 46-86 1.28e-05

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: 44.37  E-value: 1.28e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1375311714  46 IDRNIKDLNGILVTHEHSDHIKGLGVLARKYG-LPIYANENT 86
Cdd:cd07723    37 LEKNGLTLTAILTTHHHWDHTGGNAELKALFPdAPVYGPAED 78
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 40-84 1.42e-05

Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; Bacillus amyloliquefaciens BaeB may play a role in the synthesis of the antibiotic polyketide bacillaene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293833 [Multi-domain]  Cd Length: 174  Bit Score: 44.45  E-value: 1.42e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1375311714  40 EDLFSQIDRNIKDLNGILVTHEHSDHIKGLGVLARKYGLPIYANE 84
Cdd:cd16275    35 EKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSK 79
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 51-97 1.23e-04

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 42.19  E-value: 1.23e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1375311714  51 KDLNGILVTHEHSDHIKGLGVLARKYGLPIYANENTWKAIEKKDSKI 97
Cdd:cd16280    60 ADIKYILITHGHGDHYGGAAYLKDLYGAKVVMSEADWDMMEEPPEEG 106
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 11-132 1.72e-04

cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; MBL-fold metallo-hydrolase domain; CPSF2, also known as cleavage and polyadenylation specificity factor 100 kDa subunit (CPSF-100), is a component of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. This subgroup includes Ydh1p, the yeast homolog of CPSF2. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain. 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: 293851  Cd Length: 199  Bit Score: 41.35  E-value: 1.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  11 ASGSTGNATYVESDKGSLLVDVGLTGKKMEDLFSQIDRNIKDLNGILVTHEHSDHIKGLGVLARKYGL--PIYANENTWK 88
Cdd:cd16293     7 AGDESPLCYLLEIDDVTILLDCGWDESFDMEYLESLKRIAPTIDAVLLSHPDLEHLGALPYLVGKLGLtcPVYATLPVHK 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1375311714  89 aiekkdskipMDQKFIFNPYETKSIAGfDIESFnvSHDAIDPQF 132
Cdd:cd16293    87 ----------MGRMFMYDLYQSRGLEE-DFNLF--TLDDVDEAF 117
IND_BlaB-like_MBL-B1 cd16299
IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 17-127 3.47e-04

IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded metallo-beta-lactamases Chryseobacterium indologenes IND-1, IND-2, and IND-7, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB, Chryseobacterium gleum CGB-1, and Empedobacter brevis EBR-1. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293857  Cd Length: 212  Bit Score: 40.89  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  17 NATYVESDKGSLLVDVGLTGKKMEDLFSQI-DRNIKDLNGILVTHEHSDHIKGLGVLARKyGLPIYANENTwKAIEKKDS 95
Cdd:cd16299    27 NAMYLVTKKGVILFDTPWDKDQYQPLLDSIrKKHNLPVIAVIATHSHEDRAGGLGYFNKI-GIPTYATAMT-NSILKKEN 104

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1375311714  96 KipMDQKFIFNPYETKSIAG--FDIESFNVSHDA 127
Cdd:cd16299   105 K--PQATYLIETDKTYKIGGekFVVYFFGEGHTA 136
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 17-84 4.97e-04

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 39.97  E-value: 4.97e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1375311714  17 NATYVESDKGSLLVDVGL----TGKKMEDLFSQIDRNIKDLNGILVTHEHSDHIKGLGVLARKYGLPIYANE 84
Cdd:cd07725    16 NVYLLRDGDETTLIDTGLateeDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGATVYILD 87
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 16-82 7.84e-04

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


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 40.02  E-value: 7.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  16 GNATYV----------ESDKGSLLVDVGltgkkMEDLFSQIDRNI-------KDLNGILVTHEHSDHIKGLGVLARKYGL 78
Cdd:cd16315    12 GNTYYVgtcgisailiTGDDGHVLIDSG-----TEEAAPLVLANIrklgfdpKDVRWLLSSHEHFDHVGGLAALQRATGA 86


                  ....
gi 1375311714  79 PIYA 82
Cdd:cd16315    87 RVAA 90
IMP_DIM-like_MBL-B1 cd16301
IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 16-109 9.89e-04

IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the acquired MBLs IMP-1(a beta-lactamase that is active on imipenem), DIM-1 (Dutch imipenemase), GIM-1 (German imipenemase), KHM-1 (Kyorin Health Science MBL 1), SIM-1 (Seoul imipenemase), and TMB-1 (Tripoli metallo-beta-lactamase). IMP-1, DIM-1, GIM-1, SIM-1, and TMB-1 are Class 1 integron-mediated MBLs, KMH-1 is plasmid-mediated. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of acquired MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293859 [Multi-domain]  Cd Length: 215  Bit Score: 39.57  E-value: 9.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  16 GNATYVESDKGSLLVDVGLTGKKMEDLFSQIDRNIKDLNGILVTHEHSDHIKGLGVLARKyGLPIYANENTwKAIEKKDS 95
Cdd:cd16301    29 ANGLVVVDGKEAYLIDTPWSESDTEKLVEWIKAQGLTLKASISTHFHEDRTGGIGYLNSH-SIPTYASELT-NQLLKKNG 106

                          90
                  ....*....|....
gi 1375311714  96 KIPMDQKFIFNPYE 109
Cdd:cd16301   107 KELATHSFSGDEFW 120
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 14-81 1.08e-03

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: 39.04  E-value: 1.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1375311714  14 STGNAtyVESDKGSLLVDVGL-TGKKmedlFSQIDRNIKDLNGILVTHEHSDHIKGLGVLA-------RKYGLPIY 81
Cdd:cd07719    18 GPSTL--VVVGGRVYLVDAGSgVVRR----LAQAGLPLGDLDAVFLTHLHSDHVADLPALLltawlagRKTPLPVY 87
VIM_type_MBL-B1 cd16303
VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona ...
 17-98 1.32e-03

VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona integron-encoded metallo-beta-lactamase)-type MBLs are integron-associated and are widely distributed acquired MBLs. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of VIM-type MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293861 [Multi-domain]  Cd Length: 218  Bit Score: 39.07  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  17 NATYVESDKGSLLVDVGLTGKKMEDLFSQIDRNIK-DLNGILVTHEHSDHIKGLGVLaRKYGLPIYANENTWKAIEKKDS 95
Cdd:cd16303    29 NGLIVRDGDELLLIDTAWGAKNTAALLAEIEKQIGlPVTRAVSTHFHDDRVGGVDVL-RAAGVATYASPSTRRLAEAEGN 107


                  ...
gi 1375311714  96 KIP 98
Cdd:cd16303   108 EIP 110
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 55-82 1.41e-03

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 38.63  E-value: 1.41e-03
                          10        20
                  ....*....|....*....|....*...
gi 1375311714  55 GILVTHEHSDHIKGLGVLARKYGLPIYA 82
Cdd:cd16278    56 AILVTHTHRDHSPGAARLAERTGAPVRA 83
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 47-81 1.53e-03

Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Salmonella enterica serovar typhimurium YcbL which has type II hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as glyoxalase II) activity, and has a single metal ion binding site, and Thermus thermophilus TTHA1623 which does not have GLX2 activity and has two metal ion binding sites with a glyoxalase II-type metal coordination. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 38.69  E-value: 1.53e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1375311714  47 DRNIKdLNGILVTHEHSDHIKGLGVLARKYGLPIY 81
Cdd:cd07737    42 DLGLT-LKKILLTHGHLDHVGGAAELAEHYGVPII 75
MUS_TUS_MBL-B1 cd16318
Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; ...
 15-70 1.79e-03

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


Pssm-ID: 293876  Cd Length: 214  Bit Score: 38.48  E-value: 1.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1375311714  15 TGNATYVESDKGSLLVDVGLTGKKMEDLFSQIDRN-IKDLNGILVTHEHSDHIKGLG 70
Cdd:cd16318    25 SSNSMYVLTDEGVILIDTPWDKDQYEPLLEYIRSNhNKEVKWVITTHFHEDRSGGLG 81
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 18-76 2.05e-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: 38.24  E-value: 2.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1375311714  18 ATYV-ESDKGSLLVDVG--LTGKKMEDLFSQIDRNIKDLNGILVTHEHSDHIKGLGVLARKY 76
Cdd:cd07726    17 ASYLlDGEGRPALIDTGpsSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLAEAL 78
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 18-83 2.89e-03

Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of L1- and Pom-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293847  Cd Length: 239  Bit Score: 38.26  E-value: 2.89e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1375311714  18 ATYVESDKGSLLVDVGLtgKKMEDLFSQIDRNI----KDLNGILVTHEHSDHIKGLGVLARKYGLPIYAN 83
Cdd:cd16289    24 ALLVKTPDGAVLLDGGM--PQAADMLLDNMRALgvapGDLKLILHSHAHADHAGPLAALKRATGARVAAN 91
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 18-74 7.60e-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: 36.76  E-value: 7.60e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1375311714  18 ATYVE-SDKGSLLVDVGltgkkmEDLFSQIDRN---------IKDLNGILVTHEHSDHIKGL-GVLAR 74
Cdd:cd07718    19 GILLRiPGDGSILLDCG------EGTLGQLRRHygpeeadevLRNLKCIFISHLHADHHLGLiRLLAE 80
BDS1 COG2015
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary ...
 17-84 7.61e-03

Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441618 [Multi-domain]  Cd Length: 629  Bit Score: 37.51  E-value: 7.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1375311714  17 NATYVESDKGSLLVDVGLTGKKME---DLFSQI--DRNIKdlnGILVTHEHSDHIKG-LGVLA----RKYGLPIYANE 84
Cdd:COG2015   104 NMTFIEGDTGWIVIDPLTSVETAAaalALYRKHlgDRPVK---AVIYTHSHVDHFGGvRGVVDeedvKSGKVPIIAPE 178
PRK11539 PRK11539
ComEC family competence protein; Provisional
 52-82 7.90e-03

ComEC family competence protein; Provisional


Pssm-ID: 236924 [Multi-domain]  Cd Length: 755  Bit Score: 37.67  E-value: 7.90e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1375311714  52 DLNGILVTHEHSDHIKGLGVLARKY-GLPIYA 82
Cdd:PRK11539  551 TPEGIILSHEHLDHRGGLASLLHAWpMAWIRS 582
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 5-69 8.19e-03

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: 36.76  E-value: 8.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1375311714   5 IRMSVlasgstgNATYVESDKGSLLVDVGlTGKKMEDLFSQIDRNIK-------DLNGILVTHEHSDHIKGL 69
Cdd:cd07720    45 VETSV-------NAFLVRTGGRLILVDTG-AGGLFGPTAGKLLANLAaagidpeDIDDVLLTHLHPDHIGGL 108
 
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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