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Conserved domains on  [gi|446444982|ref|WP_000522837|]
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MULTISPECIES: MBL fold metallo-hydrolase [Bacillus]

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 ...
 6-193 1.43e-71

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: 216.36  E-value: 1.43e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982   6 SVLASGSTGNMLYVGTDEKKLLVDAGLSGKATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYANEKTW 85
Cdd:cd07733    1 SVLASGSKGNCTYLETEDGKLLIDAGLSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  86 NAMEHLIGNIPTEQKFIFSVGDVKTFGDIEVESFGVSHDAAEPMFYAFHNNNRKLALITDtgyvsdrmkgvikganafvf 165
Cdd:cd07733   81 RAMERKVGLIDVDQKQIFEPGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTD-------------------- 140

                        170       180
                 ....*....|....*....|....*...
gi 446444982 166 esnhdvemlrmgrypwsIKRRILSDVGH 193
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 ...
 6-193 1.43e-71

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: 216.36  E-value: 1.43e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982   6 SVLASGSTGNMLYVGTDEKKLLVDAGLSGKATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYANEKTW 85
Cdd:cd07733    1 SVLASGSKGNCTYLETEDGKLLIDAGLSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  86 NAMEHLIGNIPTEQKFIFSVGDVKTFGDIEVESFGVSHDAAEPMFYAFHNNNRKLALITDtgyvsdrmkgvikganafvf 165
Cdd:cd07733   81 RAMERKVGLIDVDQKQIFEPGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTD-------------------- 140

                        170       180
                 ....*....|....*....|....*...
gi 446444982 166 esnhdvemlrmgrypwsIKRRILSDVGH 193
Cdd:cd07733  141 -----------------LKQRILSDRGH 151
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 3-250 4.14e-62

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 195.88  E-value: 4.14e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982   3 LHFSVLASGSTG-----------------------NMLYVGTDEKKLLVDAGLSGKAteaLFKQAELNINDVSGILVTHE 59
Cdd:COG1235    1 MKVTFLGSGSSGgvpqigcdcpvcastdprygrtrSSILVEADGTRLLIDAGPDLRE---QLLRLGLDPSKIDAILLTHE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  60 HSDHIKGLGVLARKY---DLPVYANEKTWNAMEHLIGNIPTE-----QKFIFSVGDVKTFGDIEVESFGVSHDAAEPMFY 131
Cdd:COG1235   78 HADHIAGLDDLRPRYgpnPIPVYATPGTLEALERRFPYLFAPypgklEFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982 132 AFHNNNRKLALITDTGYVSDRMKGVIKGANAFVFESNHDVEmlrmgrYPwsikrrilsdvGHVCNEDAALAMADVItdeT 211
Cdd:COG1235  158 RIEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATYDDP------EP-----------GHLSNEEALELLARLG---P 217

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 446444982 212 KHIYLAHLSLDNNMKELARMSVSQVLEEKGFGV---GESFEI 250
Cdd:COG1235  218 KRLVLTHLSPDNNDHELDYDELEAALLPAGVEVaydGMEIEL 259
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 15-175 8.92e-18

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: 78.36  E-value: 8.92e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982    15 NMLYVGTDEKKLLVDAGLsGKATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYANEKTWNAMEHLI-- 92
Cdd:smart00849   1 NSYLVRDDGGAILIDTGP-GEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLal 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982    93 ------GNIPTEQKFIFSVGDVKTFGDIEVESFGVSHDAAEPMFYAFHnnNRKLALITDTGYVSDRMKGVIKGANAFVFE 166
Cdd:smart00849  80 lgelgaEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLP--EGKILFTGDLLFAGGDGRTLVDGGDAAASD 157


                   ....*....
gi 446444982   167 SNHDVEMLR 175
Cdd:smart00849 158 ALESLLKLL 166
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 26-177 1.63e-14

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: 70.03  E-value: 1.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982   26 LLVDAGLSGKATEALFKQ-AELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYANEKTwnaMEHLIGNIP-------- 96
Cdd:pfam12706   3 ILIDPGPDLRQQALPALQpGRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGV---LAHLRRNFPylfllehy 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982   97 TEQKFIFSVGDVKTFGD--IEVESFGVSHDAA--------EPMFYAFHNNNRKLALITDTGYVSDRMKGVIKGANAFVFE 166
Cdd:pfam12706  80 GVRVHEIDWGESFTVGDggLTVTATPARHGSPrgldpnpgDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLGGADLLLLD 159

                         170
                  ....*....|...
gi 446444982  167 SN--HDVEMLRMG 177
Cdd:pfam12706 160 GGawRDDEMIHMG 172
PRK02113 PRK02113
MBL fold metallo-hydrolase;
19-218 8.73e-06

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 45.93  E-value: 8.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  19 VGTDEKKLLVDAGLSGKAtEALFkqaeLNINDVSGILVTHEHSDHIKGLGVL---ARKYDLPVYANEKTWNAM------- 88
Cdd:PRK02113  40 VETEGARILIDCGPDFRE-QMLR----LPFGKIDAVLITHEHYDHVGGLDDLrpfCRFGEVPIYAEQYVAERLrsrmpyc 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  89 --EHL---IGNIPTEQkfifsVGDVKTF--GDIEVESFGVSHDAAEPMFYAFHnnnrKLALITDTGYVSDRMKGVIKGAN 161
Cdd:PRK02113 115 fvEHSypgVPNIPLRE-----IEPDRPFlvNHTEVTPLRVMHGKLPILGYRIG----KMAYITDMLTMPEEEYEQLQGID 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446444982 162 AFVFESnhdvemLRMGRYPwsikrrilsdvGHVCNEDAALAMADVITDETKHIYLAH 218
Cdd:PRK02113 186 VLVMNA------LRIAPHP-----------THQSLEEALENIKRIGAKETYLIHMSH 225
 
Name Accession Description Interval E-value
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 6-193 1.43e-71

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: 216.36  E-value: 1.43e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982   6 SVLASGSTGNMLYVGTDEKKLLVDAGLSGKATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYANEKTW 85
Cdd:cd07733    1 SVLASGSKGNCTYLETEDGKLLIDAGLSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  86 NAMEHLIGNIPTEQKFIFSVGDVKTFGDIEVESFGVSHDAAEPMFYAFHNNNRKLALITDtgyvsdrmkgvikganafvf 165
Cdd:cd07733   81 RAMERKVGLIDVDQKQIFEPGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTD-------------------- 140

                        170       180
                 ....*....|....*....|....*...
gi 446444982 166 esnhdvemlrmgrypwsIKRRILSDVGH 193
Cdd:cd07733  141 -----------------LKQRILSDRGH 151
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 3-250 4.14e-62

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 195.88  E-value: 4.14e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982   3 LHFSVLASGSTG-----------------------NMLYVGTDEKKLLVDAGLSGKAteaLFKQAELNINDVSGILVTHE 59
Cdd:COG1235    1 MKVTFLGSGSSGgvpqigcdcpvcastdprygrtrSSILVEADGTRLLIDAGPDLRE---QLLRLGLDPSKIDAILLTHE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  60 HSDHIKGLGVLARKY---DLPVYANEKTWNAMEHLIGNIPTE-----QKFIFSVGDVKTFGDIEVESFGVSHDAAEPMFY 131
Cdd:COG1235   78 HADHIAGLDDLRPRYgpnPIPVYATPGTLEALERRFPYLFAPypgklEFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982 132 AFHNNNRKLALITDTGYVSDRMKGVIKGANAFVFESNHDVEmlrmgrYPwsikrrilsdvGHVCNEDAALAMADVItdeT 211
Cdd:COG1235  158 RIEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATYDDP------EP-----------GHLSNEEALELLARLG---P 217

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 446444982 212 KHIYLAHLSLDNNMKELARMSVSQVLEEKGFGV---GESFEI 250
Cdd:COG1235  218 KRLVLTHLSPDNNDHELDYDELEAALLPAGVEVaydGMEIEL 259
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
22-220 6.20e-21

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 88.71  E-value: 6.20e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  22 DEKKLLVDAGlSGkaTEALFKQAELNINDVSGILVTHEHSDHIKGLGVLA-------RKYDLPVYANEKTWNAMEHLIGN 94
Cdd:COG1234   27 GGERLLIDCG-EG--TQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLstrslagREKPLTIYGPPGTKEFLEALLKA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  95 IPTEQKF-----IFSVGDVKTFGDIEVESFGVSHdAAEPMFYAFHNNNRKLALITDTGYvSDRMKGVIKGANAFVFESNH 169
Cdd:COG1234  104 SGTDLDFplefhEIEPGEVFEIGGFTVTAFPLDH-PVPAYGYRFEEPGRSLVYSGDTRP-CEALVELAKGADLLIHEATF 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446444982 170 DVEMLRMGRypwsikrrilsDVGHVCNEDAA--LAMADVitdetKHIYLAHLS 220
Cdd:COG1234  182 LDEEAELAK-----------ETGHSTAKEAAelAAEAGV-----KRLVLTHFS 218
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 15-175 8.92e-18

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: 78.36  E-value: 8.92e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982    15 NMLYVGTDEKKLLVDAGLsGKATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYANEKTWNAMEHLI-- 92
Cdd:smart00849   1 NSYLVRDDGGAILIDTGP-GEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLal 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982    93 ------GNIPTEQKFIFSVGDVKTFGDIEVESFGVSHDAAEPMFYAFHnnNRKLALITDTGYVSDRMKGVIKGANAFVFE 166
Cdd:smart00849  80 lgelgaEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLP--EGKILFTGDLLFAGGDGRTLVDGGDAAASD 157


                   ....*....
gi 446444982   167 SNHDVEMLR 175
Cdd:smart00849 158 ALESLLKLL 166
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 15-117 5.91e-15

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: 71.65  E-value: 5.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  15 NMLYVGTDEKKLLVDAGLSGKATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYANEKTWNAMEH---- 90
Cdd:COG0491   16 NSYLIVGGDGAVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEApaag 95

                         90       100
                 ....*....|....*....|....*...
gi 446444982  91 -LIGNIPTEQKFIFSVGDVKTFGDIEVE 117
Cdd:COG0491   96 aLFGREPVPPDRTLEDGDTLELGGPGLE 123
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 26-177 1.63e-14

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: 70.03  E-value: 1.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982   26 LLVDAGLSGKATEALFKQ-AELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYANEKTwnaMEHLIGNIP-------- 96
Cdd:pfam12706   3 ILIDPGPDLRQQALPALQpGRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGV---LAHLRRNFPylfllehy 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982   97 TEQKFIFSVGDVKTFGD--IEVESFGVSHDAA--------EPMFYAFHNNNRKLALITDTGYVSDRMKGVIKGANAFVFE 166
Cdd:pfam12706  80 GVRVHEIDWGESFTVGDggLTVTATPARHGSPrgldpnpgDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLGGADLLLLD 159

                         170
                  ....*....|...
gi 446444982  167 SN--HDVEMLRMG 177
Cdd:pfam12706 160 GGawRDDEMIHMG 172
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 17-159 2.80e-14

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: 69.42  E-value: 2.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  17 LYVGTDEKKLLVDAGlsgkaTEalFKQAEL--NINDVSGILVTHEHSDHIKGLG-----VLARKYDLPVYANEKTWNAM- 88
Cdd:cd16279   38 ILIETGGKNILIDTG-----PD--FRQQALraGIRKLDAVLLTHAHADHIHGLDdlrpfNRLQQRPIPVYASEETLDDLk 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  89 --------EHLIGNIPTEQKFIFSVGDVKTFGDIEVESFGVSHDaaePMF-YAFhnnnR--KLALITDTGYVSDRMKGVI 157
Cdd:cd16279  111 rrfpyffaATGGGGVPKLDLHIIEPDEPFTIGGLEITPLPVLHG---KLPsLGF----RfgDFAYLTDVSEIPEESLEKL 183


                 ..
gi 446444982 158 KG 159
Cdd:cd16279  184 RG 185
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 15-117 7.55e-14

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: 68.08  E-value: 7.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  15 NMLYVGTDEKK-LLVDAGLSgkATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYANEKTWNAMEHLIG 93
Cdd:cd06262   11 NCYLVSDEEGEaILIDPGAG--ALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAELLEDPEL 88

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446444982  94 N---------IPTEQKFIFSVGDVKTFGDIEVE 117
Cdd:cd06262   89 NlaffgggplPPPEPDILLEDGDTIELGGLELE 121
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
14-165 9.04e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 68.16  E-value: 9.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982   14 GNMLYVGTDEKKLLVDAGLSG-KATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYANEKTWNAMEHLI 92
Cdd:pfam00753   6 VNSYLIEGGGGAVLIDTGGSAeAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982   93 GN-------IPTEQKFIFSVGDVKTFGDI---EVESFGVSHDAAE-PMFYAFHNNNRKLALITDTGYVSDRMKGVIKGAN 161
Cdd:pfam00753  86 LGlaasrlgLPGPPVVPLPPDVVLEEGDGilgGGLGLLVTHGPGHgPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPLGG 165


                  ....
gi 446444982  162 AFVF 165
Cdd:pfam00753 166 LLVL 169
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 8-82 8.57e-13

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: 65.32  E-value: 8.57e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446444982   8 LASGSTGNMLYVGTDEKKLLVDAGLSGKAT--EALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYANE 82
Cdd:cd07721    5 LPLLPPVNAYLIEDDDGLTLIDTGLPGSAKriLKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYAHE 81
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 9-168 2.24e-11

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 61.12  E-value: 2.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982   9 ASGSTG---NMLYVGTDEKKLLVDAGLSgkaTEALFKQAELNINDVSGILVTHEHSDHIKGLG--------VLARKYDLP 77
Cdd:cd07740    8 AFGSGGrlnTCFHVASEAGRFLIDCGAS---SLIALKRAGIDPNAIDAIFITHLHGDHFGGLPfflldaqfVAKRTRPLT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  78 VYANE--KTW--NAMEHLI-GNIPTEQKFIFSV-----GDVKTFGDIEVESFGVSHDAAEPMFYAFHNNNRK-LALITDT 146
Cdd:cd07740   85 IAGPPglRERlrRAMEALFpGSSKVPRRFDLEVielepGEPTTLGGVTVTAFPVVHPSGALPLALRLEAAGRvLAYSGDT 164

                        170       180
                 ....*....|....*....|..
gi 446444982 147 GYVsDRMKGVIKGANAFVFESN 168
Cdd:cd07740  165 EWT-DALVPLARGADLFICECY 185
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 15-134 1.71e-10

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: 59.73  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  15 NMLYVGTDEKKLLVDAGLS-------GKA-----TEALFKqaelNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYANE 82
Cdd:cd07714   12 NMYVVEYDDDIIIIDCGLKfpdedmpGVDyiipdFSYLEE----NKDKIKGIFITHGHEDHIGALPYLLPELNVPIYATP 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446444982  83 KTWNAMEHLI---GNIPTEQKFIFSVGDVKTFGDIEVESFGVSHDAAEPMFYAFH 134
Cdd:cd07714   88 LTLALIKKKLeefKLIKKVKLNEIKPGERIKLGDFEVEFFRVTHSIPDSVGLAIK 142
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 21-167 2.08e-10

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


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 58.22  E-value: 2.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  21 TDEKKLLVDAGlSGkATEALfkQAELNINDVSGILVTHEHSDHIKGLGVL--ARKYD--------LPVYANEKTWNAMEH 90
Cdd:cd07716   25 ADGFRILLDCG-SG-VLSRL--QRYIDPEDLDAVVLSHLHPDHCADLGVLqyARRYHprgarkppLPLYGPAGPAERLAA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  91 LIGNIPTEQKFIFSVGDVKTFGDIEVESFGVSH--DAaepmfYAFH--NNNRKLALITDTGYvSDRMKGVIKGANAFVFE 166
Cdd:cd07716  101 LYGLEDVFDFHPIEPGEPLEIGPFTITFFRTVHpvPC-----YAMRieDGGKVLVYTGDTGY-CDELVEFARGADLLLCE 174


                 .
gi 446444982 167 S 167
Cdd:cd07716  175 A 175
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
15-134 7.68e-10

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 58.92  E-value: 7.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  15 NMLYVGTDEKKLLVDAGLsgkateaLFKQAEL---------------NINDVSGILVTHEHSDHIKGLGVLARKYDLPVY 79
Cdd:COG0595   20 NMYVYEYDDDIIIVDCGL-------KFPEDEMpgvdlvipdisyleeNKDKIKGIVLTHGHEDHIGALPYLLKELNVPVY 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446444982  80 ANEKTwNAM------EHligNIPTEQKF-IFSVGDVKTFGDIEVESFGVSHDAAEPMFYAFH 134
Cdd:COG0595   93 GTPLT-LALleaklkEH---GLLKKVKLhVVKPGDRIKFGPFKVEFFRVTHSIPDSLGLAIR 150
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 22-239 9.72e-10

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: 57.46  E-value: 9.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  22 DEKKLLVDAGlsgKATEALFKQAELNINDVSGILVTHEHSDHIKGL-GVLA------RKYDLPVYANEKTWNAMEHLI-- 92
Cdd:cd07717   25 EGELWLFDCG---EGTQRQLLRAGLSPSKIDRIFITHLHGDHILGLpGLLStmsllgRTEPLTIYGPKGLKEFLETLLrl 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  93 --GNIPTEQKFI---FSVGDVKTFGDIEVESFGVSHDaAEPMFYAFHnNNRKLALITDTGYvSDRMKGVIKGANAFVFES 167
Cdd:cd07717  102 saSRLPYPIEVHelePDPGLVFEDDGFTVTAFPLDHR-VPCFGYRFE-EGRKIAYLGDTRP-CEGLVELAKGADLLIHEA 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446444982 168 NHDVEMLRMGRypwsikrrilsDVGHVCNEDAA-LA-MADVitdetKHIYLAHLSldnnmkelARMSVSQVLEE 239
Cdd:cd07717  179 TFLDDDAEKAK-----------ETGHSTAKQAAeIAkKAGV-----KKLVLTHFS--------ARYKDPEELLK 228
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 13-114 2.08e-08

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: 53.61  E-value: 2.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  13 TGNMLYVGT----------DEKKLLVDAGL--SGKATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYA 80
Cdd:cd16310   11 VDNIYYVGTkgigsylitsNHGAILLDGGLeeNAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQLKADTGAKLWA 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446444982  81 NEKTWNAME---HLIGNI-------PTEQKFIFSVGDVKTFGDI 114
Cdd:cd16310   91 SRGDRPALEagkHIGDNItqpapfpAVKVDRILGDGEKIKLGDI 134
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 13-91 2.29e-08

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: 52.85  E-value: 2.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  13 TGNMLYVGTDEKKLLVDAGLS-GKATEALFKQAEL--NINDVSGILVTHEHSDHIKGLGVLARK-YDLPVYANEKTWNAM 88
Cdd:cd16295   11 TGSCYLLETGGKRILLDCGLFqGGKELEELNNEPFpfDPKEIDAVILTHAHLDHSGRLPLLVKEgFRGPIYATPATKDLA 90


                 ...
gi 446444982  89 EHL 91
Cdd:cd16295   91 ELL 93
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 21-167 3.32e-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: 51.88  E-value: 3.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  21 TDEKKLLVDAGlSGKATEALfkQAELNINDVSGILVTHEHSDHIKGLG--VLARKYD-----LPVYANEKTWNAMEHLIG 93
Cdd:cd16272   24 TGGTRILLDCG-EGTVYRLL--KAGVDPDKLDAIFLSHFHLDHIGGLPtlLFARRYGgrkkpLTIYGPKGIKEFLEKLLN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  94 NIPTEQKFIFSV--------GDVKTFGDIEVESFGVSHdAAEPMFYAFHNNNRKLALITDTGYvSDRMKGVIKGANAFVF 165
Cdd:cd16272  101 FPVEILPLGFPLeieeleegGEVLELGDLKVEAFPVKH-SVESLGYRIEAEGKSIVYSGDTGP-CENLVELAKGADLLIH 178


                 ..
gi 446444982 166 ES 167
Cdd:cd16272  179 EC 180
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 12-164 4.24e-08

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: 51.75  E-value: 4.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  12 STGNMLYVGtdEKKLLVDAGlSGkATEALFkQAELNINDVSGILVTHEHSDHIKGLGVLA-------RKYDLPVYA---- 80
Cdd:cd07719   18 GPSTLVVVG--GRVYLVDAG-SG-VVRRLA-QAGLPLGDLDAVFLTHLHSDHVADLPALLltawlagRKTPLPVYGppgt 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  81 ---NEKTWNAMEHLI-------GNIPTEQKFIFSV------GDVKTFGDIEVESFGVSHDAAEPMF-YAFHNNNRKLALI 143
Cdd:cd07719   93 ralVDGLLAAYALDIdyrarigDEGRPDPGALVEVheiaagGVVYEDDGVKVTAFLVDHGPVPPALaYRFDTPGRSVVFS 172

                        170       180
                 ....*....|....*....|.
gi 446444982 144 TDTGYvSDRMKGVIKGANAFV 164
Cdd:cd07719  173 GDTGP-SENLIELAKGADLLV 192
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 ...
 14-80 5.60e-08

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: 52.35  E-value: 5.60e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446444982  14 GNMLYVGT----------DEKKLLVDAGL--SGKATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYA 80
Cdd:cd16290   12 GNTYYVGTgglsavlitsPQGLILIDGALpqSAPQIEANIRALGFRLEDVKLILNSHAHFDHAGGIAALQRDSGATVAA 90
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 38-117 7.02e-08

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: 51.00  E-value: 7.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  38 EALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYANEKTWNAMEHLIGNIPTeqkfiFSVGDVKTFGDIEVE 117
Cdd:cd16275   35 EKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDYYGFRCPNLIP-----LEDGDTIKIGDTEIT 109
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 11-82 1.04e-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: 50.99  E-value: 1.04e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446444982  11 GSTgNMLYVGTDEKK-LLVDAGLSGKATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYANE 82
Cdd:cd07743    6 GPT-NIGVYVFGDKEaLLIDSGLDEDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPK 77
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 12-200 1.28e-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: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 50.65  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  12 STGNMLYvGTDEKKLLVDAGLSgkateAL--FKQAELNINDVSGILVTHEHSDH---------------IKGLGVLArky 74
Cdd:cd07741   19 ASGGIWI-ELNGKNIHIDPGPG-----ALvrMCRPKLDPTKLDAIILSHRHLDHsndanvlieamteggFKKRGTLL--- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  75 dLPVYANEKTwNAMEHLIGNIPTEQKFIFSVGDVKTFGDIEVESFGVSHDAAEPMFYAFHNNNRKLALITDTGYvSDRMK 154
Cdd:cd07741   90 -APEDALNGE-PVVLLYYHRRKLEEIEILEEGDEYELGGIKIEATRHKHSDPTTYGFIFRTSDKKIGYISDTRY-FEELI 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446444982 155 GVIKGANAFVfesnhdVEMLRMGRYPWsikrrilsdVGHVCNEDAA 200
Cdd:cd07741  167 EYYSNCDVLI------INVTRPRPRKG---------VDHLSVEDVE 197
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-80 1.62e-07

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 51.73  E-value: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982   1 MGLHFSVLASGSTGNMLYVGTDEKKLLVDAGLSGKATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARK-YDLPVY 79
Cdd:COG1236    1 MKLTFLGAAGEVTGSCYLLETGGTRILIDCGLFQGGKERNWPPFPFRPSDVDAVVLTHAHLDHSGALPLLVKEgFRGPIY 80


                 .
gi 446444982  80 A 80
Cdd:COG1236   81 A 81
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 50-125 2.15e-07

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: 49.92  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  50 DVSGILVTHEHSDHIKGLGVLARkyDLPVYANEKTWNAMEHL----IGNIPTEQKFI-FSVGDVKTFGDIEVESFGVSHD 124
Cdd:cd07732   75 SVDAVLLSHAHLDHYGLLNYLRP--DIPVYMGEATKRILKALlpffGEGDPVPRNIRvFESGKSFTIGDFTVTPYLVDHS 152


                 .
gi 446444982 125 A 125
Cdd:cd07732  153 A 153
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 14-120 3.60e-07

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: 49.89  E-value: 3.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  14 GNMLYVGT----------DEKKLLVDAGL--SGKATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYAN 81
Cdd:cd16314   12 GNTWYVGTcgisallvtsDAGHILIDGGTdkAAPLIEANIRALGFRPEDVRYIVSSHEHFDHAGGIARLQRATGAPVVAR 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446444982  82 EKTWNAMEHLIGNIPTEQKFIFS----VGDVKTFGDIEVESFG 120
Cdd:cd16314   92 EPAATTLERGRSDRSDPQFLVVEkfppVASVQRIGDGEVLRVG 134
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 15-82 3.85e-07

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: 49.22  E-value: 3.85e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446444982  15 NMLYVGTDEKKLLVDAGL----SGKATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYANE 82
Cdd:cd07725   16 NVYLLRDGDETTLIDTGLateeDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGATVYILD 87
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 17-154 5.53e-07

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: 49.54  E-value: 5.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  17 LYVGTDEKKLLVDAGLSGkateALFKQAE-LNIN--DVSGILVTHEHSDHIKGL-GVLARKYDLPVYAN----EKTWNAM 88
Cdd:cd07713   23 LLIETEGKKILFDTGQSG----VLLHNAKkLGIDlsDIDAVVLSHGHYDHTGGLkALLELNPKAPVYAHpdafEPRYSKR 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446444982  89 EHLIGNIPTEQK--------FIFSVGDVKTFGDIEVesFGVShdaaePMFYAFHNNNRKLALITDTGYVSDRMK 154
Cdd:cd07713   99 GGGKKGIGIGREelekagarLVLVEEPTEIAPGVYL--TGEI-----PRVTDFEKGNPGLFVKEDGGLVPDDFE 165
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 21-206 7.23e-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: 7.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  21 TDEKKLLVDAGLSGKAteALFKQAELNINDVSG---ILVTHEHSDHI--KGLGVLARKyDLPVYANEKTWNAMEHL-IGN 94
Cdd:COG2220   18 TGGKRILIDPVFSGRA--SPVNPLPLDPEDLPKidaVLVTHDHYDHLddATLRALKRT-GATVVAPLGVAAWLRAWgFPR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  95 IpteqkFIFSVGDVKTFGDIEVESFGVSH-------DAAEPMFYAFHNNNRKLALITDTGYVSDrMKGVIKGANAfvfes 167
Cdd:COG2220   95 V-----TELDWGESVELGGLTVTAVPARHssgrpdrNGGLWVGFVIETDGKTIYHAGDTGYFPE-MKEIGERFPI----- 163

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446444982 168 nhDVEMLRMGRYPWsikrrilsdvgHVCNEDAALAMADV 206
Cdd:COG2220  164 --DVALLPIGAYPF-----------TMGPEEAAEAARDL 189
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
17-153 7.77e-07

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 49.11  E-value: 7.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  17 LYVGTDEKKLLVDAGlsgkATEALFKQAE-LNIN--DVSGILVTHEHSDHIKGL-GVLARKYDLPVYA-----NEKTWNA 87
Cdd:COG1237   25 ALIETEGKRILFDTG----QSDVLLKNAEkLGIDlsDIDAVVLSHGHYDHTGGLpALLELNPKAPVYAhpdafEKRYSKR 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  88 MEHLIGNIPTEQK--------FIFSVGDVK------TFGDIevesfgvshdaaePMFYAFHNNNRKLALITDTGYVSDRM 153
Cdd:COG1237  101 PGGKYIGIPFSREeleklgarLILVKEPTEiapgvyLTGEI-------------PRVTDFEKGDPGLYVKEDGGLVPDPF 167
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 11-115 2.20e-06

Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; CPSF3 (cleavage and polyadenylation specificity factor subunit 3; also known as cleavage and polyadenylation specificity factor 73 kDa subunit, CPSF-73) and CPSF2 (also known as cleavage and polyadenylation specificity factor 100 kDa subunit /CPSF-100) are components of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. CPSF3 functions as a 3' endonuclease. Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)), and Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74) are subunits of Integrator, a metazoan-specific multifunctional protein complex composed of 14 subunits. Integrator has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 46.94  E-value: 2.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  11 GSTGNMLYVGTDEKKLLVDAGLS-GKAT-EALFKQAELNINDVSGILVTHEHSDHIKGLGVLAR--KYDLPVYANEKTWN 86
Cdd:cd07734    8 EVGRSCFLVEFKGRTVLLDCGMNpGKEDpEACLPQFELLPPEIDAILISHFHLDHCGALPYLFRgfIFRGPIYATHPTVA 87

                         90       100
                 ....*....|....*....|....*....
gi 446444982  87 AMEHLIGNIPTEQKFIFSVGDVKTFGDIE 115
Cdd:cd07734   88 LGRLLLEDYVKSAERIGQDQSLYTPEDIE 116
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 28-117 2.47e-06

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: 46.30  E-value: 2.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  28 VDAGLSGKATEALfKQAELNIndvSGILVTHEHSDHIKGLGVLARKY-DLPVYANEKtwnamehliGNIPTEQKFIfSVG 106
Cdd:cd07723   25 VDPGEAEPVLAAL-EKNGLTL---TAILTTHHHWDHTGGNAELKALFpDAPVYGPAE---------DRIPGLDHPV-KDG 90

                         90
                 ....*....|.
gi 446444982 107 DVKTFGDIEVE 117
Cdd:cd07723   91 DEIKLGGLEVK 101
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-117 5.66e-06

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 46.42  E-value: 5.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  14 GNMLYVG----------TDEKKLLVDAGLSGKATEALF---KQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYA 80
Cdd:cd16280   12 DNLYYVGnkwvsawaidTGDGLILIDALNNNEAADLIVdglEKLGLDPADIKYILITHGHGDHYGGAAYLKDLYGAKVVM 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446444982  81 NEKTWNAMEHLIGNIPTEQKFI-FSV------GDVKTFGDIEVE 117
Cdd:cd16280   92 SEADWDMMEEPPEEGDNPRWGPpPERdivikdGDTLTLGDTTIT 135
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 18-84 6.84e-06

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


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 45.80  E-value: 6.84e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  18 YVGTDE---KKLLVDaglSGKATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYANEKT 84
Cdd:cd16322   14 YLVADEgggEAVLVD---PGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDD 80
PRK02113 PRK02113
MBL fold metallo-hydrolase;
19-218 8.73e-06

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 45.93  E-value: 8.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  19 VGTDEKKLLVDAGLSGKAtEALFkqaeLNINDVSGILVTHEHSDHIKGLGVL---ARKYDLPVYANEKTWNAM------- 88
Cdd:PRK02113  40 VETEGARILIDCGPDFRE-QMLR----LPFGKIDAVLITHEHYDHVGGLDDLrpfCRFGEVPIYAEQYVAERLrsrmpyc 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  89 --EHL---IGNIPTEQkfifsVGDVKTF--GDIEVESFGVSHDAAEPMFYAFHnnnrKLALITDTGYVSDRMKGVIKGAN 161
Cdd:PRK02113 115 fvEHSypgVPNIPLRE-----IEPDRPFlvNHTEVTPLRVMHGKLPILGYRIG----KMAYITDMLTMPEEEYEQLQGID 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446444982 162 AFVFESnhdvemLRMGRYPwsikrrilsdvGHVCNEDAALAMADVITDETKHIYLAH 218
Cdd:PRK02113 186 VLVMNA------LRIAPHP-----------THQSLEEALENIKRIGAKETYLIHMSH 225
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 15-84 1.26e-05

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: 44.97  E-value: 1.26e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446444982  15 NMLYVGTDEKKLLVDAGLSGKATEALFKQAELNIN-DVSGILVTHEHSDHIKGLGVLARKyDLPVYANEKT 84
Cdd:cd16285   27 NGLIVIDGKGLVLIDTPWTEAQTATLLDWIEKKLGkPVTAAISTHSHDDRTGGIKALNAR-GIPTYATALT 96
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 17-90 2.38e-05

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293814  Cd Length: 249  Bit Score: 44.56  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  17 LYVGTDEKKLLVDAGL-SGKATEALFKQ-------------AELNI--NDVSGILVTHEHSDHIKGLGVLARKYDLPV-- 78
Cdd:cd07728   46 ILIQYQGKNYLIDAGIgNGKLTEKQKRNfgvteessieeslAELGLtpEDIDYVLMTHLHFDHASGLTKVKGEQLVSVfp 125

                         90
                 ....*....|....*.
gi 446444982  79 ----YANEKTWNAMEH 90
Cdd:cd07728  126 natiYVSEIEWEEMRN 141
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 26-150 2.68e-05

class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293821  Cd Length: 259  Bit Score: 44.51  E-value: 2.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  26 LLVDAG----------LSGKATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLA---------RKydlPVYANEKTWN 86
Cdd:cd07735   31 ILLDAGtgvgalsleeMFNDILFPSQKAAYELYQRIRHYLITHAHLDHIAGLPLLSpndggqrgsPK---TIYGLPETID 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446444982  87 AM-EHL--------IGNIPT-EQKFI----FSVGDVKTFGDIEVESFGVSHDAAEPMFYAFHNNNRKLALITDTGYVS 150
Cdd:cd07735  108 ALkKHIfnwviwpdFTSIPSgKYPYLrlepIEPEYPIALTGLSVTAFPVSHGVPVSTAFLIRDGGDSFLFFGDTGPDS 185
PRK00055 PRK00055
ribonuclease Z; Reviewed
 22-200 6.01e-05

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 43.25  E-value: 6.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  22 DEKKLLVDAGlsgKATEALFKQAELNINDVSGILVTHEHSDHIKGL-GVLA------RKYDLPVYA---NEKTWNAMEHL 91
Cdd:PRK00055  28 GGELFLFDCG---EGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLpGLLStrslsgRTEPLTIYGpkgIKEFVETLLRA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  92 -------------IGNIPTEQKFIFSV------GDVKTFGDIEVEsfgvSHDAAEP-MFYAFHNNNRKLALITDTGYvSD 151
Cdd:PRK00055 105 sgslgyriaekdkPGKLDAEKLKALGVppgplfGKLKRGEDVTLE----DGRIINPaDVLGPPRKGRKVAYCGDTRP-CE 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446444982 152 RMKGVIKGANAFVFESNHDVEMLRMGRypwsikrrilsDVGHVCNEDAA 200
Cdd:PRK00055 180 ALVELAKGADLLVHEATFGDEDEELAK-----------EYGHSTARQAA 217
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 4-90 7.13e-05

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 42.55  E-value: 7.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982   4 HFSVLASGSTGNMLYVGTDEKKLLVDAGLSGKATEALFKQAElNIND--VSGILVTHEHSDHIKGLGVLARKyDLPVYAN 81
Cdd:cd16282    5 LIGPDGGGFISNIGFIVGDDGVVVIDTGASPRLARALLAAIR-KVTDkpVRYVVNTHYHGDHTLGNAAFADA-GAPIIAH 82


                 ....*....
gi 446444982  82 EKTWNAMEH 90
Cdd:cd16282   83 ENTREELAA 91
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 21-92 7.83e-05

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: 42.48  E-value: 7.83e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446444982  21 TDEKKLLVDAG--LSGKATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKY-DLPVYANEKtwnAMEHLI 92
Cdd:cd07726   23 GEGRPALIDTGpsSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLAEALpNAKVYVHPR---GARHLI 94
VIM_type_MBL-B1 cd16303
VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona ...
 15-131 9.08e-05

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


Pssm-ID: 293861 [Multi-domain]  Cd Length: 218  Bit Score: 42.54  E-value: 9.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  15 NMLYVGTDEKKLLVDAGLSGKATEALFKQAELNIN-DVSGILVTHEHSDHIKGLGVLaRKYDLPVYANEKTWNAMEHLIG 93
Cdd:cd16303   29 NGLIVRDGDELLLIDTAWGAKNTAALLAEIEKQIGlPVTRAVSTHFHDDRVGGVDVL-RAAGVATYASPSTRRLAEAEGN 107

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446444982  94 NIPTEQ-KFIFSVGDVKTFGDIEVESFGVSHDAAEPMFY 131
Cdd:cd16303  108 EIPTHSlEGLSSSGDAVRFGPVELFYPGAAHSTDNLVVY 146
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 15-84 1.05e-04

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: 42.27  E-value: 1.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446444982  15 NMLYVGTDEKKLLVDAGLSGKATEALFKQAELNIN-DVSGILVTHEHSDHIKGLGVLaRKYDLPVYANEKT 84
Cdd:cd16304   27 NGLIVETSKGVVLIDTPWDDEQTEELLDWIKKKLKkPVTLAIVTHAHDDRIGGIKAL-QKRGIPVYSTKLT 96
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 17-146 1.07e-04

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 41.84  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  17 LYVGTDEKKLLVDAGLSGKATEalfkqaeLNINDVSGILVTHEHSDHIKGL-----GVLARkydLPVYA---NEKTWNAM 88
Cdd:cd07736   40 ALIEVDGERILLDAGLTDLAER-------FPPGSIDAILLTHFHMDHVQGLfhlrwGVGDP---IPVYGppdPQGCADLF 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446444982  89 EH--LIGNIPTEQKFifsvgDVKTFGDIEVESFGVSHdaAEPMF-YAFHNNNRKLALITDT 146
Cdd:cd07736  110 KHpgILDFQPLVAPF-----QSFELGGLKITPLPLNH--SKPTFgYLLESGGKRLAYLTDT 163
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 14-80 1.33e-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: 42.34  E-value: 1.33e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446444982  14 GNMLYVGT----------DEKKLLVDAGLSGKATEALFKQAEL--NINDVSGILVTHEHSDHIKGLGVLARKYDLPVYA 80
Cdd:cd16315   12 GNTYYVGTcgisailitgDDGHVLIDSGTEEAAPLVLANIRKLgfDPKDVRWLLSSHEHFDHVGGLAALQRATGARVAA 90
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 19-79 1.85e-04

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 41.36  E-value: 1.85e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446444982  19 VGTDEKKLLVDAGLSGKATEALFKQA--ELNINDVSGILVTHEHSDHIKGL-GVLARKYD--LPVY 79
Cdd:cd07722   23 VGTGKRRILIDTGEGRPSYIPLLKSVldSEGNATISDILLTHWHHDHVGGLpDVLDLLRGpsPRVY 88
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 15-67 2.58e-04

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


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 41.38  E-value: 2.58e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  15 NMLYVGTDEKKLLVDAGL-------SGKATEALfKQAELNINDVSGILVTHEHSDHIKGL 67
Cdd:cd07720   50 NAFLVRTGGRLILVDTGAgglfgptAGKLLANL-AAAGIDPEDIDDVLLTHLHPDHIGGL 108
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 18-96 3.41e-04

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 40.93  E-value: 3.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  18 YVGTDEKKLLVDAGLSGKATEALFK-QAELNINDVSGILVTHEHSDHIKGLGVLARKY-DLPVYANEKTWNAMEHLIGNI 95
Cdd:cd07709   35 YLIKDEKTALIDTVKEPFFDEFLENlEEVIDPRKIDYIVVNHQEPDHSGSLPELLELApNAKIVCSKKAARFLKHFYPGI 114


                 .
gi 446444982  96 P 96
Cdd:cd07709  115 D 115
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 26-117 3.98e-04

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


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 40.56  E-value: 3.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  26 LLVDAGLSGKATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKY-DLPVYANEKTWNAMEH------------LI 92
Cdd:cd07739   28 VLVDAQFTRADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAFpDAKVVATPAVVAHIKAqlepklafwgplLG 107

                         90       100
                 ....*....|....*....|....*
gi 446444982  93 GNIPTEqkfiFSVGDVKTFGDIEVE 117
Cdd:cd07739  108 GNAPAR----LVVPEPLDGDTLTLE 128
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 51-80 7.94e-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: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 39.40  E-value: 7.94e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 446444982  51 VSGILVTHEHSDHIKGLGVLARKYDLPVYA 80
Cdd:cd16278   54 VSAILVTHTHRDHSPGAARLAERTGAPVRA 83
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 7-64 7.98e-04

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


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 39.49  E-value: 7.98e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982   7 VLASGSTgnmLYVGTDEKKLLVDAGLSGKATEALFKQAELNI--NDVSGILVTHEHSDHI 64
Cdd:cd07711   18 FRASSTV---TLIKDGGKNILVDTGTPWDRDLLLKALAEHGLspEDIDYVVLTHGHPDHI 74
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 18-81 9.50e-04

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 39.41  E-value: 9.50e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446444982  18 YVGTDEKKLLVDAGLSGKATEALfKQAELNInDVsgILVTHEHSDHIKGLGVLARKYDLPVYAN 81
Cdd:PRK00685  12 LIETGGKKILIDPFITGNPLADL-KPEDVKV-DY--ILLTHGHGDHLGDTVEIAKRTGATVIAN 71
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 22-117 1.05e-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: 39.07  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  22 DEKKL--LVDAGlsGKAtEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYANEKtwnAMEHLIGNIPTEQ 99
Cdd:cd07737   19 EETKEaaVIDPG--GDA-DKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHK---EDKFLLENLPEQS 92

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446444982 100 K-FIFSV------------GDVKTFGDIEVE 117
Cdd:cd07737   93 QmFGFPPaeaftpdrwleeGDTVTVGNLTLE 123
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 3-123 1.53e-03

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


Pssm-ID: 293860  Cd Length: 212  Bit Score: 38.77  E-value: 1.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982   3 LHFSVLASGSTG-----NMLYVGTDEKkLLVDAGLSGKATEAL--FKQAELNInDVSGILVTHEHSDHIKGLGVLARKYd 75
Cdd:cd16302   12 VHVSYLETETFGkvpcnGMIVINGGEA-VVFDTPTNDSQSEELidWIENSLKA-KVKAVVPTHFHDDCLGGLKAFHRRG- 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446444982  76 LPVYANEKTWN-AMEHligNIPTEQKF-----IFSVGDVKtfgdIEVESFGVSH 123
Cdd:cd16302   89 IPSYANQKTIAlAKEK---GLPVPQHGfsdslTLKLGGKK----IVCRYFGEGH 135
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 22-117 2.29e-03

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 38.30  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  22 DEKKLLVDAG--LSGKATEALFKQA--ELNINDVSGILVTHEHSDHIKGLGVLARKYDL------PVYANEKTWNAMEHL 91
Cdd:COG2333   20 DGKTILIDTGprPSFDAGERVVLPYlrALGIRRLDLLVLTHPDADHIGGLAAVLEAFPVgrvlvsGPPDTSETYERLLEA 99

                         90       100
                 ....*....|....*....|....*...
gi 446444982  92 IG--NIPTEQkfiFSVGDVKTFGDIEVE 117
Cdd:COG2333  100 LKekGIPVRP---CRAGDTWQLGGVRFE 124
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 14-72 2.85e-03

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


Pssm-ID: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 38.31  E-value: 2.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446444982  14 GNMLYVGT----------DEKKLLVDAGLSGKATE--ALFKQAELNINDVSGILVTHEHSDHIKGLGVLAR 72
Cdd:cd16313   12 GNTYYVGTggisavlitsPQGHILIDGGFPKSPEQiaASIRQLGFKLEDVKYILSSHDHWDHAGGIAALQK 82
PRK11709 PRK11709
putative L-ascorbate 6-phosphate lactonase; Provisional
 48-119 2.95e-03

putative L-ascorbate 6-phosphate lactonase; Provisional


Pssm-ID: 236958  Cd Length: 355  Bit Score: 38.44  E-value: 2.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  48 INDVSGILVTHEHSDHIkglgvlarkyDLPVYA---NektwNAMEH--LIG-----------NIPTEQKFIFSVGDVKTF 111
Cdd:PRK11709 107 IREIDAVLATHDHSDHI----------DVNVAAavlQ----NCADHvkFIGpqacvdlwigwGVPKERCIVVKPGDVVKV 172

                         90
                 ....*....|.
gi 446444982 112 GDIEV---ESF 119
Cdd:PRK11709 173 KDIKIhalDSF 183
PRK11539 PRK11539
ComEC family competence protein; Provisional
 50-91 3.41e-03

ComEC family competence protein; Provisional


Pssm-ID: 236924 [Multi-domain]  Cd Length: 755  Bit Score: 38.44  E-value: 3.41e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 446444982  50 DVSGILVTHEHSDHIKGLGVLARKY-DLPVYAnekTWNAMEHL 91
Cdd:PRK11539 551 TPEGIILSHEHLDHRGGLASLLHAWpMAWIRS---PLNWANHL 590
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 16-75 5.97e-03

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: 36.73  E-value: 5.97e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446444982  16 MLYVG--------TDEKKLLVDAG---LSGKATEALFKQAeLNINDVSGILVTHEHSDHIKGLGVLARKYD 75
Cdd:cd07731    4 FLDVGqgdailiqTPGKTILIDTGprdSFGEDVVVPYLKA-RGIKKLDYLILTHPDADHIGGLDAVLKNFP 73
NorV COG0426
Flavorubredoxin [Energy production and conversion];
22-93 6.66e-03

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 37.50  E-value: 6.66e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446444982  22 DEKKLLVDAGlSGKATEALFK--QAELNINDVSGILVTHEHSDHIKGLGVLARKY-DLPVYANEKTWNAMEHLIG 93
Cdd:COG0426   41 DEKTALIDTV-GESFFEEFLEnlSKVIDPKKIDYIIVNHQEPDHSGSLPELLELApNAKIVCSKKAARFLPHFYG 114
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 14-90 8.62e-03

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


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 36.92  E-value: 8.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446444982  14 GNMLYVGTD----------EKKLLVDAGL--SGKATEALFKQAELNINDVSGILVTHEHSDHIKGLGVLARKYDLPVYAN 81
Cdd:cd16288   12 GNVYYVGTSglasylittpQGLILIDTGLesSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAALKKLTGAKLMAS 91


                 ....*....
gi 446444982  82 EKTWNAMEH 90
Cdd:cd16288   92 AEDAALLAS 100
 
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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