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Conserved domains on  [gi|488217646|ref|WP_002288854|]
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MULTISPECIES: MBL fold metallo-hydrolase [Enterococcus]

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 ...
 11-198 2.01e-80

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: 239.09  E-value: 2.01e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  11 SILASGSSGNSLYIESEKKRLLVDAGLSGKKITSLMAQIDRTPDQLDGILVTHEHRDHIHGVGVLARKYHLDVFANQQTW 90
Cdd:cd07733    1 SVLASGSKGNCTYLETEDGKLLIDAGLSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  91 EAMEPLIGNVPVEQKHLFEMGKVRTFGDIDIESFGVSHDAAAPQFYRFHKENRSFVMLTDtgycsdymrgvienadgylm 170
Cdd:cd07733   81 RAMERKVGLIDVDQKQIFEPGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTD-------------------- 140

                        170       180
                 ....*....|....*....|....*...
gi 488217646 171 esnhdlemlrmgpypwnLKQRILGDRGH 198
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 ...
 11-198 2.01e-80

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: 239.09  E-value: 2.01e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  11 SILASGSSGNSLYIESEKKRLLVDAGLSGKKITSLMAQIDRTPDQLDGILVTHEHRDHIHGVGVLARKYHLDVFANQQTW 90
Cdd:cd07733    1 SVLASGSKGNCTYLETEDGKLLIDAGLSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  91 EAMEPLIGNVPVEQKHLFEMGKVRTFGDIDIESFGVSHDAAAPQFYRFHKENRSFVMLTDtgycsdymrgvienadgylm 170
Cdd:cd07733   81 RAMERKVGLIDVDQKQIFEPGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTD-------------------- 140

                        170       180
                 ....*....|....*....|....*...
gi 488217646 171 esnhdlemlrmgpypwnLKQRILGDRGH 198
Cdd:cd07733  141 -----------------LKQRILSDRGH 151
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 8-257 9.73e-65

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 202.82  E-value: 9.73e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646   8 FKISILASGSSG-----------------------NSLYIESEKKRLLVDAGLSGKKitsLMAQIDRTPDQLDGILVTHE 64
Cdd:COG1235    1 MKVTFLGSGSSGgvpqigcdcpvcastdprygrtrSSILVEADGTRLLIDAGPDLRE---QLLRLGLDPSKIDAILLTHE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  65 HRDHIHGVGVLARKY---HLDVFANQQTWEAMEPLIGNVPVE-----QKHLFEMGKVRTFGDIDIESFGVSHDAAAPQFY 136
Cdd:COG1235   78 HADHIAGLDDLRPRYgpnPIPVYATPGTLEALERRFPYLFAPypgklEFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646 137 RFHKENRSFVMLTDTGYCSDYMRGVIENADGYLMESNHDLemlrmgPYPwnlkqrilgdrGHLSNEDGALVMTDVignRT 216
Cdd:COG1235  158 RIEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATYDD------PEP-----------GHLSNEEALELLARL---GP 217

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 488217646 217 KRIYLGHLSKENNMKELAHLTMENVLKEKDFGVGHDFEIYD 257
Cdd:COG1235  218 KRLVLTHLSPDNNDHELDYDELEAALLPAGVEVAYDGMEIE 258
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 20-180 1.09e-15

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: 72.97  E-value: 1.09e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646    20 NSLYIESEKKRLLVDAGLSGkkITSLMAQIDR-TPDQLDGILVTHEHRDHIHGVGVLARKYHLDVFANQQTWEAME---- 94
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGE--AEDLLAELKKlGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKdlla 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646    95 ----PLIGNVPVEQKHLFEMGKVRTFGDIDIESFGVSHDAAAPQFYRFHKENrsfVMLT-DTGYCSDYMRGVIENADGYL 169
Cdd:smart00849  79 llgeLGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGK---ILFTgDLLFAGGDGRTLVDGGDAAA 155

                          170
                   ....*....|.
gi 488217646   170 MESNHDLEMLR 180
Cdd:smart00849 156 SDALESLLKLL 166
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 30-223 3.24e-13

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: 66.56  E-value: 3.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646   30 RLLVDAGLSgkkitsLMAQIDRTP-------DQLDGILVTHEHRDHIHGVGVLARKYHLDVFANQQTWEAMEPL-----I 97
Cdd:pfam12706   2 RILIDPGPD------LRQQALPALqpgrlrdDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLRRNfpylfL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646   98 GNVPVEQKHLFEMGKVRTFGD--IDIESFGVSHDAAAPQF--------YRFHKENRSFVMLTDTGYCSDYMRGVIENADG 167
Cdd:pfam12706  76 LEHYGVRVHEIDWGESFTVGDggLTVTATPARHGSPRGLDpnpgdtlgFRIEGPGKRVYYAGDTGYFPDEIGERLGGADL 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 488217646  168 YLMESN--HDLEMLRMgpypwnlkqrilgdrGHLSNEDGALVMTDVignRTKRIYLGH 223
Cdd:pfam12706 156 LLLDGGawRDDEMIHM---------------GHMTPEEAVEAAADL---GARRKVLIH 195
PRK02113 PRK02113
MBL fold metallo-hydrolase;
21-225 3.67e-07

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 50.17  E-value: 3.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  21 SLYIESEKKRLLVDAGlsgkkiTSLMAQIDRTP-DQLDGILVTHEHRDHIHGVGVL---ARKYHLDVFANQQTWEAMEPL 96
Cdd:PRK02113  37 SALVETEGARILIDCG------PDFREQMLRLPfGKIDAVLITHEHYDHVGGLDDLrpfCRFGEVPIYAEQYVAERLRSR 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  97 IGNVPVEQKH-------LFEMGKVRTF--GDIDIESFGVSHDAAAPQFYRFHKenrsFVMLTDTGYCSDYMRGVIENADG 167
Cdd:PRK02113 111 MPYCFVEHSYpgvpnipLREIEPDRPFlvNHTEVTPLRVMHGKLPILGYRIGK----MAYITDMLTMPEEEYEQLQGIDV 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488217646 168 YLMESnhdlemLRMGPYPwnlkqrilgdrGHLSNEDgALVMTDVIGNrtKRIYLGHLS 225
Cdd:PRK02113 187 LVMNA------LRIAPHP-----------THQSLEE-ALENIKRIGA--KETYLIHMS 224
 
Name Accession Description Interval E-value
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 11-198 2.01e-80

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: 239.09  E-value: 2.01e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  11 SILASGSSGNSLYIESEKKRLLVDAGLSGKKITSLMAQIDRTPDQLDGILVTHEHRDHIHGVGVLARKYHLDVFANQQTW 90
Cdd:cd07733    1 SVLASGSKGNCTYLETEDGKLLIDAGLSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  91 EAMEPLIGNVPVEQKHLFEMGKVRTFGDIDIESFGVSHDAAAPQFYRFHKENRSFVMLTDtgycsdymrgvienadgylm 170
Cdd:cd07733   81 RAMERKVGLIDVDQKQIFEPGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTD-------------------- 140

                        170       180
                 ....*....|....*....|....*...
gi 488217646 171 esnhdlemlrmgpypwnLKQRILGDRGH 198
Cdd:cd07733  141 -----------------LKQRILSDRGH 151
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 8-257 9.73e-65

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 202.82  E-value: 9.73e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646   8 FKISILASGSSG-----------------------NSLYIESEKKRLLVDAGLSGKKitsLMAQIDRTPDQLDGILVTHE 64
Cdd:COG1235    1 MKVTFLGSGSSGgvpqigcdcpvcastdprygrtrSSILVEADGTRLLIDAGPDLRE---QLLRLGLDPSKIDAILLTHE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  65 HRDHIHGVGVLARKY---HLDVFANQQTWEAMEPLIGNVPVE-----QKHLFEMGKVRTFGDIDIESFGVSHDAAAPQFY 136
Cdd:COG1235   78 HADHIAGLDDLRPRYgpnPIPVYATPGTLEALERRFPYLFAPypgklEFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646 137 RFHKENRSFVMLTDTGYCSDYMRGVIENADGYLMESNHDLemlrmgPYPwnlkqrilgdrGHLSNEDGALVMTDVignRT 216
Cdd:COG1235  158 RIEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATYDD------PEP-----------GHLSNEEALELLARL---GP 217

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 488217646 217 KRIYLGHLSKENNMKELAHLTMENVLKEKDFGVGHDFEIYD 257
Cdd:COG1235  218 KRLVLTHLSPDNNDHELDYDELEAALLPAGVEVAYDGMEIE 258
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
8-225 7.23e-22

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 91.41  E-value: 7.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646   8 FKISILASGSS-------GNSLYIESEKKRLLVDAGlSGkkITSLMAQIDRTPDQLDGILVTHEHRDHIHGVGVLA---- 76
Cdd:COG1234    1 MKLTFLGTGGAvptpgraTSSYLLEAGGERLLIDCG-EG--TQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLstrs 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  77 ---RKYHLDVFANQQTWEAMEPLIGNVPVEQK-----HLFEMGKVRTFGDIDIESFGVSHdaAAPQF-YRFHKENRSFVM 147
Cdd:COG1234   78 lagREKPLTIYGPPGTKEFLEALLKASGTDLDfplefHEIEPGEVFEIGGFTVTAFPLDH--PVPAYgYRFEEPGRSLVY 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488217646 148 LTDTGYCSDYMRgVIENADGYLMESNHDLEMLRMGPypwnlkqrilgDRGHLSNEDGALVMTDVignRTKRIYLGHLS 225
Cdd:COG1234  156 SGDTRPCEALVE-LAKGADLLIHEATFLDEEAELAK-----------ETGHSTAKEAAELAAEA---GVKRLVLTHFS 218
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 21-128 1.22e-16

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: 75.97  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  21 SLYIESEKKRLLVDAGlsgkkiTSLMAQIDRTP-DQLDGILVTHEHRDHIHGVG-----VLARKYHLDVFANQQTWEAM- 93
Cdd:cd16279   37 SILIETGGKNILIDTG------PDFRQQALRAGiRKLDAVLLTHAHADHIHGLDdlrpfNRLQQRPIPVYASEETLDDLk 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488217646  94 --------EPLIGNVPVEQKHLFEMGKVRTFGDIDIESFGVSH 128
Cdd:cd16279  111 rrfpyffaATGGGGVPKLDLHIIEPDEPFTIGGLEITPLPVLH 153
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 20-180 1.09e-15

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: 72.97  E-value: 1.09e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646    20 NSLYIESEKKRLLVDAGLSGkkITSLMAQIDR-TPDQLDGILVTHEHRDHIHGVGVLARKYHLDVFANQQTWEAME---- 94
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGE--AEDLLAELKKlGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKdlla 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646    95 ----PLIGNVPVEQKHLFEMGKVRTFGDIDIESFGVSHDAAAPQFYRFHKENrsfVMLT-DTGYCSDYMRGVIENADGYL 169
Cdd:smart00849  79 llgeLGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGK---ILFTgDLLFAGGDGRTLVDGGDAAA 155

                          170
                   ....*....|.
gi 488217646   170 MESNHDLEMLR 180
Cdd:smart00849 156 SDALESLLKLL 166
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 20-122 2.33e-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: 72.80  E-value: 2.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  20 NSLYIESEKKRLLVDAGLSGKKITSLMAQIDRTPDQLDGILVTHEHRDHIHGVGVLARKYHLDVFANQQTWEAME----- 94
Cdd:COG0491   16 NSYLIVGGDGAVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEapaag 95

                         90       100
                 ....*....|....*....|....*...
gi 488217646  95 PLIGNVPVEQKHLFEMGKVRTFGDIDIE 122
Cdd:COG0491   96 ALFGREPVPPDRTLEDGDTLELGGPGLE 123
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 15-156 1.13e-14

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: 70.16  E-value: 1.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  15 SGSSGnslY-IESEKKRLLVDAGlSGKkITSLMAQIDrtPDQLDGILVTHEHRDHIHGVGVL--ARKYH--------LDV 83
Cdd:cd07716   16 GACSG---YlLEADGFRILLDCG-SGV-LSRLQRYID--PEDLDAVVLSHLHPDHCADLGVLqyARRYHprgarkppLPL 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488217646  84 FANQQTWEAMEPLIGNVPVEQKHLFEMGKVRTFGDIDIESFGVSH--DAAApqfYRFHKENRSFVMLTDTGYCSD 156
Cdd:cd07716   89 YGPAGPAERLAALYGLEDVFDFHPIEPGEPLEIGPFTITFFRTVHpvPCYA---MRIEDGGKVLVYTGDTGYCDE 160
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 30-223 3.24e-13

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: 66.56  E-value: 3.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646   30 RLLVDAGLSgkkitsLMAQIDRTP-------DQLDGILVTHEHRDHIHGVGVLARKYHLDVFANQQTWEAMEPL-----I 97
Cdd:pfam12706   2 RILIDPGPD------LRQQALPALqpgrlrdDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLRRNfpylfL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646   98 GNVPVEQKHLFEMGKVRTFGD--IDIESFGVSHDAAAPQF--------YRFHKENRSFVMLTDTGYCSDYMRGVIENADG 167
Cdd:pfam12706  76 LEHYGVRVHEIDWGESFTVGDggLTVTATPARHGSPRGLDpnpgdtlgFRIEGPGKRVYYAGDTGYFPDEIGERLGGADL 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 488217646  168 YLMESN--HDLEMLRMgpypwnlkqrilgdrGHLSNEDGALVMTDVignRTKRIYLGH 223
Cdd:pfam12706 156 LLLDGGawRDDEMIHM---------------GHMTPEEAVEAAADL---GARRKVLIH 195
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 10-166 1.43e-12

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: 64.21  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  10 ISILASGSSGNSL-------YIESEKKRLLVDAGlSGkkITSLMAQIDRTPDQLDGILVTHEHRDHIHGVG--VLARKYH 80
Cdd:cd16272    1 LTFLGTGGAVPSLtrntssyLLETGGTRILLDCG-EG--TVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPtlLFARRYG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  81 -----LDVFANQQTWEAMEPLIGNV--------PVEQKHLFEMGKVRTFGDIDIESFGVSHdaAAPQF-YRFHKENRSFV 146
Cdd:cd16272   78 grkkpLTIYGPKGIKEFLEKLLNFPveilplgfPLEIEELEEGGEVLELGDLKVEAFPVKH--SVESLgYRIEAEGKSIV 155

                        170       180
                 ....*....|....*....|
gi 488217646 147 MLTDTGYCSDYMRgVIENAD 166
Cdd:cd16272  156 YSGDTGPCENLVE-LAKGAD 174
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 20-122 6.20e-12

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 62.69  E-value: 6.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  20 NSLYIESEKKR-LLVDAGLSGKKitSLMAQIDRTPDQLDGILVTHEHRDHIHGVGVLARKYHLDVFANQQTWEAMEPLIG 98
Cdd:cd06262   11 NCYLVSDEEGEaILIDPGAGALE--KILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAELLEDPEL 88

                         90       100       110
                 ....*....|....*....|....*....|...
gi 488217646  99 N---------VPVEQKHLFEMGKVRTFGDIDIE 122
Cdd:cd06262   89 NlaffgggplPPPEPDILLEDGDTIELGGLELE 121
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
18-122 1.77e-11

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 61.62  E-value: 1.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646   18 SGNSLYIESEKKRLLVDAGLSGKKIT-SLMAQIDRTPDQLDGILVTHEHRDHIHGVGVLARKYHLDVFANQQTWEAMEPL 96
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTGGSAEAALlLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDE 84

                          90       100
                  ....*....|....*....|....*.
gi 488217646   97 IGNVPVEQKHLFEMGKVRTFGDIDIE 122
Cdd:pfam00753  85 ELGLAASRLGLPGPPVVPLPPDVVLE 110
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 9-85 1.12e-10

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: 59.54  E-value: 1.12e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488217646   9 KISILASGSSGNSLYIESEKKRLLVDAGL--SGKKITSLMAQIDRTPDQLDGILVTHEHRDHIHGVGVLARKYHLDVFA 85
Cdd:cd07721    1 GVYQLPLLPPVNAYLIEDDDGLTLIDTGLpgSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYA 79
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 9-167 1.22e-09

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: 56.37  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646   9 KISILASGS-------SGNSLYIESEKKRLLVDAGlSGkkiTSL-MAQIDRTPDQLDGILVTHEHRDHIHGVGVLA---- 76
Cdd:cd07719    1 RVTLLGTGGpipdpdrAGPSTLVVVGGRVYLVDAG-SG---VVRrLAQAGLPLGDLDAVFLTHLHSDHVADLPALLltaw 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  77 ---RKYHLDVF----------ANQQTWEAMEPLIGNVPVEQK---------HLFEMGKVR-TFGDIDIESFGVSHDAAAP 133
Cdd:cd07719   77 lagRKTPLPVYgppgtralvdGLLAAYALDIDYRARIGDEGRpdpgalvevHEIAAGGVVyEDDGVKVTAFLVDHGPVPP 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 488217646 134 QF-YRFHKENRSFVMLTDTGYCSdymrGVIENADG 167
Cdd:cd07719  157 ALaYRFDTPGRSVVFSGDTGPSE----NLIELAKG 187
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 20-257 2.49e-09

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: 56.30  E-value: 2.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  20 NSLYIESEKKRLLVDAG------LsgKKITSLMAQIDRtpdqldgILVTHEHRDHIHG-VGVLA------RKYHLDVFAN 86
Cdd:cd07717   18 SSIALRLEGELWLFDCGegtqrqL--LRAGLSPSKIDR-------IFITHLHGDHILGlPGLLStmsllgRTEPLTIYGP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  87 QQTWEAMEPLIG------NVPVEQKHL-FEMGKVRTFGDIDIESFGVSHDAAApQFYRFhKENRSFVMLTDTGYCSDyMR 159
Cdd:cd07717   89 KGLKEFLETLLRlsasrlPYPIEVHELePDPGLVFEDDGFTVTAFPLDHRVPC-FGYRF-EEGRKIAYLGDTRPCEG-LV 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646 160 GVIENADGYLMESNHDLEMLRMGpypwnlkqrilGDRGHLSNEDGALVMTDVignRTKRIYLGHLSKennmkelAHLTME 239
Cdd:cd07717  166 ELAKGADLLIHEATFLDDDAEKA-----------KETGHSTAKQAAEIAKKA---GVKKLVLTHFSA-------RYKDPE 224

                        250       260
                 ....*....|....*....|...
gi 488217646 240 NVLKE--KDFG---VGHDFEIYD 257
Cdd:cd07717  225 ELLKEarAVFPntiLAEDFMTIE 247
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 20-122 3.84e-09

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: 54.47  E-value: 3.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  20 NSLYI---ESEKKRLLVDAGlsgKKITSLMAQIDRTPDQLDGILVTHEHRDHIHGVGVLARKYHLDVFANQQTWEAMEPL 96
Cdd:cd16275   12 NYSYIiidKATREAAVVDPA---WDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDYYGFR 88

                         90       100
                 ....*....|....*....|....*.
gi 488217646  97 IGNVpveqkHLFEMGKVRTFGDIDIE 122
Cdd:cd16275   89 CPNL-----IPLEDGDTIKIGDTEIT 109
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-173 6.63e-09

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 54.19  E-value: 6.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  14 ASGSSG---NSLYIESEKKRLLVDAGLSgkkitSLMA----QIDrtPDQLDGILVTHEHRDHIHGVG--------VLARK 78
Cdd:cd07740    8 AFGSGGrlnTCFHVASEAGRFLIDCGAS-----SLIAlkraGID--PNAIDAIFITHLHGDHFGGLPfflldaqfVAKRT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  79 YHLDVFANQ--QTW--EAMEPLI-GNVPVEQKhlFEM-------GKVRTFGDIDIESFGVSHDAAAPQFY-RFHKENRSF 145
Cdd:cd07740   81 RPLTIAGPPglRERlrRAMEALFpGSSKVPRR--FDLevielepGEPTTLGGVTVTAFPVVHPSGALPLAlRLEAAGRVL 158

                        170       180
                 ....*....|....*....|....*...
gi 488217646 146 VMLTDTGYCsDYMRGVIENADGYLMESN 173
Cdd:cd07740  159 AYSGDTEWT-DALVPLARGADLFICECY 185
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 11-151 2.30e-08

MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain; Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 52.88  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  11 SILASGSS-----GNS--LYIESEKKRLLVDAGlSGkkITSLMAQIDRTPDQLDG-ILVTHEHRDHIHG----VGVLARK 78
Cdd:cd07715    8 SIPVPGPDtvrygGNTscVEVRAGGELLILDAG-TG--IRELGNELMKEGPPGEAhLLLSHTHWDHIQGfpffAPAYDPG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  79 YHLDVFANQQTWEAMEPLIGN--------VPVEQ------KHLFEMGKVRTFGDIDIESFGVSH--DAAApqfYRFHKEN 142
Cdd:cd07715   85 NRIHIYGPHKDGGSLEEVLRRqmsppyfpVPLEEllaaieFHDLEPGEPFSIGGVTVTTIPLNHpgGALG---YRIEEDG 161


                 ....*....
gi 488217646 143 RSFVMLTDT 151
Cdd:cd07715  162 KSVVYATDT 170
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 20-163 2.94e-08

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 53.00  E-value: 2.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  20 NSLYIESEKKRLLVDAGLSGKKITSLMAQIDRT-PDQLDGILVTHEHRDHIHGVGVLA-RKYHLDVFANqqtwEAMEPLI 97
Cdd:COG2220   12 ATFLIETGGKRILIDPVFSGRASPVNPLPLDPEdLPKIDAVLVTHDHYDHLDDATLRAlKRTGATVVAP----LGVAAWL 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488217646  98 GNVPVEQKHLFEMGKVRTFGDIDIESFGVSHDAAAPQF-------YRFHKENRSFVMLTDTGYCSDyMRGVIE 163
Cdd:COG2220   88 RAWGFPRVTELDWGESVELGGLTVTAVPARHSSGRPDRngglwvgFVIETDGKTIYHAGDTGYFPE-MKEIGE 159
PRK02113 PRK02113
MBL fold metallo-hydrolase;
21-225 3.67e-07

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 50.17  E-value: 3.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  21 SLYIESEKKRLLVDAGlsgkkiTSLMAQIDRTP-DQLDGILVTHEHRDHIHGVGVL---ARKYHLDVFANQQTWEAMEPL 96
Cdd:PRK02113  37 SALVETEGARILIDCG------PDFREQMLRLPfGKIDAVLITHEHYDHVGGLDDLrpfCRFGEVPIYAEQYVAERLRSR 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  97 IGNVPVEQKH-------LFEMGKVRTF--GDIDIESFGVSHDAAAPQFYRFHKenrsFVMLTDTGYCSDYMRGVIENADG 167
Cdd:PRK02113 111 MPYCFVEHSYpgvpnipLREIEPDRPFlvNHTEVTPLRVMHGKLPILGYRIGK----MAYITDMLTMPEEEYEQLQGIDV 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488217646 168 YLMESnhdlemLRMGPYPwnlkqrilgdrGHLSNEDgALVMTDVIGNrtKRIYLGHLS 225
Cdd:PRK02113 187 LVMNA------LRIAPHP-----------THQSLEE-ALENIKRIGA--KETYLIHMS 224
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 21-176 4.94e-07

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


Pssm-ID: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 48.77  E-value: 4.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  21 SLYIESEKKRLLVDAGLsgkkiTSLmAQIdRTPDQLDGILVTHEHRDHIHGVgvlarkYHLdvfanqqTWEAMEPLignv 100
Cdd:cd07736   39 SALIEVDGERILLDAGL-----TDL-AER-FPPGSIDAILLTHFHMDHVQGL------FHL-------RWGVGDPI---- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646 101 PV-----EQ--------------KHLFEMGKVRTFGDIDIESFGVSHdaAAPQF-YRFHKENRSFVMLTDTgycsdymRG 160
Cdd:cd07736   95 PVygppdPQgcadlfkhpgildfQPLVAPFQSFELGGLKITPLPLNH--SKPTFgYLLESGGKRLAYLTDT-------LG 165

                        170
                 ....*....|....*.
gi 488217646 161 VIENADGYLMESNHDL 176
Cdd:cd07736  166 LPEETLEFLKQQQPDV 181
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-166 8.71e-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: 48.34  E-value: 8.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  22 LYIESEKKRLLVDAGlSGKKITSLMAQIDrtPDQLDGILVTHEHRDHIHGVGVLAR------KYHLDVFANQQT----WE 91
Cdd:cd07741   23 IWIELNGKNIHIDPG-PGALVRMCRPKLD--PTKLDAIILSHRHLDHSNDANVLIEamteggFKKRGTLLAPEDalngEP 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488217646  92 AMEPLIGNVPVEQKHLFEMGKVRTFGDIDIESFGVSHDAAAPQFYRFHKENRSFVMLTDTGYcSDYMRGVIENAD 166
Cdd:cd07741  100 VVLLYYHRRKLEEIEILEEGDEYELGGIKIEATRHKHSDPTTYGFIFRTSDKKIGYISDTRY-FEELIEYYSNCD 173
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-126 1.02e-06

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 47.91  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  22 LYIESEKKRLLVDAGLSGKKITSLMAQIDRTPDQLDGILVTHEHRDHIHGVGVLARKYHLDVFANQQtwEA-------ME 94
Cdd:cd07743   12 VYVFGDKEALLIDSGLDEDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKI--EKafienplLE 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 488217646  95 PLI---GNVPVEQKHLFEMGK------VRTFGDIDIESFGV 126
Cdd:cd07743   90 PSYlggAYPPKELRNKFLMAKpskvddIIEEGELELGGVGL 130
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 24-79 1.42e-06

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: 47.87  E-value: 1.42e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488217646  24 IESEKKRLLVDAG--LSGKKITSLMAQIDRTPDQLDGILVTHEHRDHIHGVGVLARKY 79
Cdd:cd07726   21 LDGEGRPALIDTGpsSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLAEAL 78
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 19-96 3.09e-06

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


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 46.68  E-value: 3.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  19 GNSLYIESEKKRLLVDAGLS-GKKITSL--MAQIDRTPDQLDGILVTHEHRDHIHGVGVLARK-YHLDVFANQQTWEAME 94
Cdd:cd16295   12 GSCYLLETGGKRILLDCGLFqGGKELEElnNEPFPFDPKEIDAVILTHAHLDHSGRLPLLVKEgFRGPIYATPATKDLAE 91


                 ..
gi 488217646  95 PL 96
Cdd:cd16295   92 LL 93
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 54-128 3.59e-06

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: 47.02  E-value: 3.59e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488217646  54 DQLDGILVTHEHRDHIHGVGVLARKYHLDVFANQQTWEAMEPLIGNVPVEQK---HLFEMGKVRTFGDIDIESFGVSH 128
Cdd:cd07714   54 DKIKGIFITHGHEDHIGALPYLLPELNVPIYATPLTLALIKKKLEEFKLIKKvklNEIKPGERIKLGDFEVEFFRVTH 131
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 21-85 1.27e-05

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: 45.31  E-value: 1.27e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488217646  21 SLYIESEKKRLLVDAGLSGkkitSL---MAQIDRTPDQLDGILVTHEHRDHIHGV-GVLARKYHLDVFA 85
Cdd:cd07713   22 SLLIETEGKKILFDTGQSG----VLlhnAKKLGIDLSDIDAVVLSHGHYDHTGGLkALLELNPKAPVYA 86
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 22-85 1.46e-05

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 44.37  E-value: 1.46e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488217646  22 LYIESEKKRLLVDAGLSGKkitsLMAQIDRTPDQLDGILVTHEHRDHIHGVGVLARKY-HLDVFA 85
Cdd:cd07723   14 IVDEATGEAAVVDPGEAEP----VLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFpDAPVYG 74
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 19-130 2.88e-05

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: 43.75  E-value: 2.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  19 GNSLYIESEKKRLLVDAGLS-------------------------GKKITSLMAQIDRTPDQ-LDGILVTHEHRDHIHGV 72
Cdd:cd07732   13 GNCIEVETGGTRILLDFGLPldpeskyfdevldflelgllpdivgLYRDPLLLGGLRSEEDPsVDAVLLSHAHLDHYGLL 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488217646  73 GVLARKyhLDVFANQQTWEAMEPLIGNVPVEQKHL-----FEMGKVRTFGDIDIESFGVSHDA 130
Cdd:cd07732   93 NYLRPD--IPVYMGEATKRILKALLPFFGEGDPVPrnirvFESGKSFTIGDFTVTPYLVDHSA 153
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 18-73 2.97e-05

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: 43.73  E-value: 2.97e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488217646  18 SGNSLYIESEKKRLLVDAGL--SGKKITSLMAQIDRTPDQLDGILVTHEHRDHIHGVG 73
Cdd:cd07711   21 SSTVTLIKDGGKNILVDTGTpwDRDLLLKALAEHGLSPEDIDYVVLTHGHPDHIGNLN 78
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
21-85 4.20e-05

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 43.72  E-value: 4.20e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488217646  21 SLYIESEKKRLLVDAGlSGKKITSLMAQIDRTPDQLDGILVTHEHRDHIHGV-GVLARKYHLDVFA 85
Cdd:COG1237   24 SALIETEGKRILFDTG-QSDVLLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLpALLELNPKAPVYA 88
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 19-122 4.64e-05

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: 43.69  E-value: 4.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  19 GNSLYIES-EKKRLLVDAG------LSGKKITSLMAQIDRtpDQLDGILVTHEHRDHIHGVGVLARKYHLDVF------A 85
Cdd:COG2333   11 GDAILIRTpDGKTILIDTGprpsfdAGERVVLPYLRALGI--RRLDLLVLTHPDADHIGGLAAVLEAFPVGRVlvsgppD 88

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488217646  86 NQQTWEAMEPLIGNVPVEQKHLFEmGKVRTFGDIDIE 122
Cdd:COG2333   89 TSETYERLLEALKEKGIPVRPCRA-GDTWQLGGVRFE 124
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 22-118 5.22e-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: 43.40  E-value: 5.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  22 LYIESEKKRLLVDAGLSGKKIT-----------------SLmAQIDRTPDQLDGILVTHEHRDHIHGVGVLARKYHLDVF 84
Cdd:cd07728   46 ILIQYQGKNYLIDAGIGNGKLTekqkrnfgvteessieeSL-AELGLTPEDIDYVLMTHLHFDHASGLTKVKGEQLVSVF 124

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488217646  85 AN------QQTWEAM-EPLI--GNVPVEQKHLFEMGKVRTFGD 118
Cdd:cd07728  125 PNatiyvsEIEWEEMrNPNIrsKNTYWKENWEPIEDQVKTFSD 167
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 9-99 7.15e-05

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 43.64  E-value: 7.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646   9 KISIL--ASGSSGNSLYIESEKKRLLVDAGLSGKKITSLMAQIDRTPDQLDGILVTHEHRDHIHGVGVLARK-YHLDVFA 85
Cdd:COG1236    2 KLTFLgaAGEVTGSCYLLETGGTRILIDCGLFQGGKERNWPPFPFRPSDVDAVVLTHAHLDHSGALPLLVKEgFRGPIYA 81

                         90
                 ....*....|....
gi 488217646  86 NQQTWEAMEPLIGN 99
Cdd:COG1236   82 TPATADLARILLGD 95
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 19-79 7.63e-05

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 42.51  E-value: 7.63e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488217646  19 GNSLYIESEKKRLLVDAG----LSGKKITS-LMAQIDRtpdQLDGILVTHEHRDHIHGVGVLARKY 79
Cdd:cd07731   10 GDAILIQTPGKTILIDTGprdsFGEDVVVPyLKARGIK---KLDYLILTHPDADHIGGLDAVLKNF 72
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 20-71 1.22e-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: 42.54  E-value: 1.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  20 NSLYIESEKKRLLVDAGL-------SGKKITSL-MAQIDrtPDQLDGILVTHEHRDHIHG 71
Cdd:cd07720   50 NAFLVRTGGRLILVDTGAgglfgptAGKLLANLaAAGID--PEDIDDVLLTHLHPDHIGG 107
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 23-86 1.60e-04

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 41.72  E-value: 1.60e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488217646  23 YIESEKKRLLVDAGLSGKKITSLMAQiDRTPDQldgILVTHEHRDHIHGVGVLARKYHLDVFAN 86
Cdd:PRK00685  12 LIETGGKKILIDPFITGNPLADLKPE-DVKVDY---ILLTHGHGDHLGDTVEIAKRTGATVIAN 71
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 21-105 6.01e-04

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


Pssm-ID: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 39.84  E-value: 6.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  21 SLYIESEKKR-LLVDAGLSGKKItslMAQIDRTPDQLDGILVTHEHRDHIHGVGVLARKYHLDVFANQQtweAMEPLIGN 99
Cdd:cd07737   14 SLIWCEETKEaAVIDPGGDADKI---LQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHK---EDKFLLEN 87


                 ....*.
gi 488217646 100 VPVEQK 105
Cdd:cd07737   88 LPEQSQ 93
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-94 2.20e-03

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 38.32  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  14 ASGSSGNSLYIESEKKRLLVDAGLSGKKITSLMAQIDRTPDQ-LDGILVTHEHRDHIHGVGVLARKyHLDVFANQQTWEA 92
Cdd:cd16282   10 GGGFISNIGFIVGDDGVVVIDTGASPRLARALLAAIRKVTDKpVRYVVNTHYHGDHTLGNAAFADA-GAPIIAHENTREE 88


                 ..
gi 488217646  93 ME 94
Cdd:cd16282   89 LA 90
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 24-94 2.27e-03

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


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 38.25  E-value: 2.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488217646  24 IESEKKRLLVDAGLSGKKITSLMAQIDRTPDQLDGILVTHEHRDHIHGVGVLarkyhLDVF------ANQQTWEAME 94
Cdd:cd07739   21 IYGETEAVLVDAQFTRADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVL-----LEAFpdakvvATPAVVAHIK 92
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 20-133 2.28e-03

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


Pssm-ID: 433247 [Multi-domain]  Cd Length: 160  Bit Score: 37.57  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646   20 NSLYIESEKKRLLVDAGLSGKKITslmaqidRTPDQLDGILVTHEHRDHihgvgvlarkYHLDvfanqqtweamePLIGN 99
Cdd:pfam13483   8 SSFLIEGGGARILTDPFRATVGYR-------PPPVTADLVLISHGHDDH----------GHPE------------TLPGN 58

                          90       100       110
                  ....*....|....*....|....*....|....
gi 488217646  100 VPVeqkhLFEMGKVrTFGDIDIESFGVSHDAAAP 133
Cdd:pfam13483  59 PHV----LDGGGSY-TVGGLEIRGVPTDHDRVGG 87
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
24-128 2.34e-03

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 38.89  E-value: 2.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  24 IESEKKRLLVDAGLS-------G-----KKITSLMAQIDRtpdqLDGILVTHEHRDHIHGVGVLARKYHLDVFANQQTWE 91
Cdd:COG0595   24 YEYDDDIIIVDCGLKfpedempGvdlviPDISYLEENKDK----IKGIVLTHGHEDHIGALPYLLKELNVPVYGTPLTLA 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488217646  92 AME------PLIGNVPVeqkHLFEMGKVRTFGDIDIESFGVSH 128
Cdd:COG0595  100 LLEaklkehGLLKKVKL---HVVKPGDRIKFGPFKVEFFRVTH 139
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 28-122 2.35e-03

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


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 38.10  E-value: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  28 KKRLLVDaglSGKKITSLMAQIDRTPDQLDGILVTHEHRDHIHGVGVLARKYHLDVFANQQT---WEA-----------M 93
Cdd:cd16322   22 GEAVLVD---PGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDlplYEAadlgakafglgI 98

                         90       100
                 ....*....|....*....|....*....
gi 488217646  94 EPLIgnvPVEqkHLFEMGKVRTFGDIDIE 122
Cdd:cd16322   99 EPLP---PPD--RLLEDGQTLTLGGLEFK 122
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 59-94 2.73e-03

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 38.33  E-value: 2.73e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 488217646  59 ILVTHEHRDHIHGVGVLARKYHLDVFANQQTWEAME 94
Cdd:cd16280   65 ILITHGHGDHYGGAAYLKDLYGAKVVMSEADWDMME 100
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 8-119 3.38e-03

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: 38.20  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646   8 FKI--SILASGSSGNSLY-IESEKKRLLVDAGLsgkkiTSLMAQIDRTPDQLDG-------ILVTHEHRDHIHGVGVLAR 77
Cdd:cd16310    8 FRIvdNIYYVGTKGIGSYlITSNHGAILLDGGL-----EENAALIEQNIKALGFklsdikiIINTHAHYDHAGGLAQLKA 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488217646  78 KYHLDVFANQQTWEAME---PLIGNV-------PVEQKHLFEMGKVRTFGDI 119
Cdd:cd16310   83 DTGAKLWASRGDRPALEagkHIGDNItqpapfpAVKVDRILGDGEKIKLGDI 134
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 20-85 4.52e-03

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: 37.28  E-value: 4.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  20 NSLYIESEKKRLLVDAGL----SGKKITSLMAQIDRTPDQLDGILVTHEHRDHIHGVGVLARKYHLDVFA 85
Cdd:cd07725   16 NVYLLRDGDETTLIDTGLateeDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGATVYI 85
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 18-124 5.85e-03

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


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 36.88  E-value: 5.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217646  18 SGNSLYIESEKKRLLVDAGLSGKKITSLMAQI-DRTPDQLDGILVTHEHRDHIHGVGVLARKyHLDVFANQQTWE--AME 94
Cdd:cd16285   25 PSNGLIVIDGKGLVLIDTPWTEAQTATLLDWIeKKLGKPVTAAISTHSHDDRTGGIKALNAR-GIPTYATALTNElaKKE 103

                         90       100       110
                 ....*....|....*....|....*....|
gi 488217646  95 PlignvPVEQKHLFEMGKvrTFGDIDIESF 124
Cdd:cd16285  104 G-----KPVPTHSLKGAL--TLGFGPLEVF 126
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 26-72 7.71e-03

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: 36.36  E-value: 7.71e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 488217646  26 SEKKRLLVDAGlSGKK--ITSLMAQIDRTPD-QLDGILVTHEHRDHIHGV 72
Cdd:cd07722   25 TGKRRILIDTG-EGRPsyIPLLKSVLDSEGNaTISDILLTHWHHDHVGGL 73
 
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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