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Conserved domains on  [gi|1998278153|ref|WP_206547570|]
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MULTISPECIES: MBL fold metallo-hydrolase [Alphaproteobacteria]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10888664)

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

Gene Ontology:  GO:0016787
PubMed:  17597585

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 5-207 2.40e-92

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: 271.27  E-value: 2.40e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153   5 LRLTILGCGSSPGTPRITGDWGACDPANPKNRRRRCAAMVERvsasgGITRVVIDTGPDFREQMISAGVDRLDAAVYTHP 84
Cdd:cd16279     1 MKLTFLGTGTSSGVPVIGCDCGVCDSSDPKNRRLRSSILIET-----GGKNILIDTGPDFRQQALRAGIRKLDAVLLTHA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  85 HADHIHGIDDLRGFVMNQRHLMDVYADKPTLQRLIEAFGYCFEtPPGSNYPPILKAHPISHEAPFSINGaggpLTFQPLP 164
Cdd:cd16279    76 HADHIHGLDDLRPFNRLQQRPIPVYASEETLDDLKRRFPYFFA-ATGGGGVPKLDLHIIEPDEPFTIGG----LEITPLP 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1998278153 165 QIHGDILSLGYRIGGLAYCPDVSQFPEETPALIAGADVLVIDA 207
Cdd:cd16279   151 VLHGKLPSLGFRFGDFAYLTDVSEIPEESLEKLRGLDVLILDA 193
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 5-207 2.40e-92

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: 271.27  E-value: 2.40e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153   5 LRLTILGCGSSPGTPRITGDWGACDPANPKNRRRRCAAMVERvsasgGITRVVIDTGPDFREQMISAGVDRLDAAVYTHP 84
Cdd:cd16279     1 MKLTFLGTGTSSGVPVIGCDCGVCDSSDPKNRRLRSSILIET-----GGKNILIDTGPDFRQQALRAGIRKLDAVLLTHA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  85 HADHIHGIDDLRGFVMNQRHLMDVYADKPTLQRLIEAFGYCFEtPPGSNYPPILKAHPISHEAPFSINGaggpLTFQPLP 164
Cdd:cd16279    76 HADHIHGLDDLRPFNRLQQRPIPVYASEETLDDLKRRFPYFFA-ATGGGGVPKLDLHIIEPDEPFTIGG----LEITPLP 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1998278153 165 QIHGDILSLGYRIGGLAYCPDVSQFPEETPALIAGADVLVIDA 207
Cdd:cd16279   151 VLHGKLPSLGFRFGDFAYLTDVSEIPEESLEKLRGLDVLILDA 193
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 5-267 4.00e-88

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 263.29  E-value: 4.00e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153   5 LRLTILGCGSSPGTPRITGDWGACDPANPKNRRRRCAAMVErvsaSGGiTRVVIDTGPDFREQMISAGVD--RLDAAVYT 82
Cdd:COG1235     1 MKVTFLGSGSSGGVPQIGCDCPVCASTDPRYGRTRSSILVE----ADG-TRLLIDAGPDLREQLLRLGLDpsKIDAILLT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  83 HPHADHIHGIDDLRGFVMNQRhlMDVYADKPTLQRLIEAFGYCFETppgsnYPPILKAHPISHEAPFSIngagGPLTFQP 162
Cdd:COG1235    76 HEHADHIAGLDDLRPRYGPNP--IPVYATPGTLEALERRFPYLFAP-----YPGKLEFHEIEPGEPFEI----GGLTVTP 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153 163 LPQIHGDILSLGYRI----GGLAYCPDVSQFPEETPALIAGADVLVIDALQYRPHPSHFSLEEALGWIERLSPRRAVLTH 238
Cdd:COG1235   145 FPVPHDAGDPVGYRIedggKKLAYATDTGYIPEEVLELLRGADLLILDATYDDPEPGHLSNEEALELLARLGPKRLVLTH 224

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1998278153 239 MHIP-----LDYETVLRE-TPDHVEPGFDGMVIEI 267
Cdd:COG1235   225 LSPDnndheLDYDELEAAlLPAGVEVAYDGMEIEL 259
MBL_Geo_Pelo NF038231
GPMC system MBL fold metallohydrolase; Members of this family, distantly related to ...
 7-266 3.03e-81

GPMC system MBL fold metallohydrolase; Members of this family, distantly related to metallo-beta-lactamases, are MBL fold hydrolases of the GPMC (Geobacter/Pelobacter Mystery Cassette) system, in which the most distinctive signature is the TIGR04442 protein family.


Pssm-ID: 439532  Cd Length: 250  Bit Score: 245.28  E-value: 3.03e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153   7 LTILGCGSSPGTPRITGDWGACDPANPKNRRRRCAAMVErvsaSGGiTRVVIDTGPDFREQMISAGVDRLDAAVYTHPHA 86
Cdd:NF038231    2 ITILGSGTSTGVPMIGCHCPVCRSTDPRNKRTRCSALLS----WGG-KNILIDTSTDLRQQALREGIPHIDAVLYTHAHA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  87 DHIHGIDDLRGFVMNQRHLMDVYADKPTLQRLIEAFGYCFETPPGSNYPPILKAHPIshEAPFSINGaggpLTFQPLPQI 166
Cdd:NF038231   77 DHVHGIDDLRGFNFLHRRVIPCYGSAATMAQLRRNFSYIFRGEEGAGYRPLLEPHPI--SGPFDLFG----LRVVPVPLR 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153 167 HGDILSLGYRIGGLAYCPDVSQFPEETPALIAGADVLVIDALQYRPHPSHFSLEEALGWIERLSPRRAVLTHMHIPLDYE 246
Cdd:NF038231  151 HGAMEATGYRIGPLAYLTDCSAIPEASLELLQGLELLVIDGLRFRPHPTHFNIEQAIEVAQRLGARRTILTHLSHEVDHA 230

                         250       260
                  ....*....|....*....|
gi 1998278153 247 TVLRETPDHVEPGFDGMVIE 266
Cdd:NF038231  231 RDGAELPAGVEFAYDGMQLS 250
PRK02113 PRK02113
MBL fold metallo-hydrolase;
5-267 3.68e-63

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 199.24  E-value: 3.68e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153   5 LRLTILGCGSSPGTPRITGDWGACDPANPKNRRRRCAAMVERVSAsggitRVVIDTGPDFREQMISAGVDRLDAAVYTHP 84
Cdd:PRK02113    1 MKIRILGSGTSTGVPEIGCTCPVCTSKDPRDNRLRTSALVETEGA-----RILIDCGPDFREQMLRLPFGKIDAVLITHE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  85 HADHIHGIDDLRGFVmnqRHL-MDVYADKPTLQRLIEAFGYCFETPPgsnYP--PILKAHPISHEAPFSINGaggpLTFQ 161
Cdd:PRK02113   76 HYDHVGGLDDLRPFC---RFGeVPIYAEQYVAERLRSRMPYCFVEHS---YPgvPNIPLREIEPDRPFLVNH----TEVT 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153 162 PLPQIHGDILSLGYRIGGLAYCPDVSQFPEETPALIAGADVLVIDALQYRPHPSHFSLEEALGWIERLSPRRAVLTHM-- 239
Cdd:PRK02113  146 PLRVMHGKLPILGYRIGKMAYITDMLTMPEEEYEQLQGIDVLVMNALRIAPHPTHQSLEEALENIKRIGAKETYLIHMsh 225

                         250       260
                  ....*....|....*....|....*...
gi 1998278153 240 HIPLdYETVLRETPDHVEPGFDGMVIEI 267
Cdd:PRK02113  226 HIGL-HADVEKELPPHVHFAYDGLEIIF 252
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 54-239 4.54e-40

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: 138.21  E-value: 4.54e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  54 TRVVIDTGPDFREQMISAGV------DRLDAAVYTHPHADHIHGIDDLRgfvmnQRHLMDVYADKPTLQRLIEAFGYCFe 127
Cdd:pfam12706   1 RRILIDPGPDLRQQALPALQpgrlrdDPIDAVLLTHDHYDHLAGLLDLR-----EGRPRPLYAPLGVLAHLRRNFPYLF- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153 128 tppgSNYPPILKAHPISHEAPFSINGAGgpLTFQPLPQIHGDI--------LSLGYRIGG----LAYCPDVSQFPEETPA 195
Cdd:pfam12706  75 ----LLEHYGVRVHEIDWGESFTVGDGG--LTVTATPARHGSPrgldpnpgDTLGFRIEGpgkrVYYAGDTGYFPDEIGE 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1998278153 196 LIAGADVLVIDALQYRP----HPSHFSLEEALGWIERLSPRRAVLTHM 239
Cdd:pfam12706 149 RLGGADLLLLDGGAWRDdemiHMGHMTPEEAVEAAADLGARRKVLIHI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 55-208 1.10e-08

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: 53.71  E-value: 1.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153   55 RVVIDTGPDFREQMI----SAGVDRLDAAVYTHPHADHIHGIDDLRgfvmnQRHLMDVYADKPTLQRLIEAFGYCfeTPP 130
Cdd:smart00849  11 AILIDTGPGEAEDLLaelkKLGPKKIDAIILTHGHPDHIGGLPELL-----EAPGAPVYAPEGTAELLKDLLALL--GEL 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998278153  131 GSNYPPILKAHPISHEAPFSIngAGGPLTFQPLP-QIHGDIlSLGYRIGGLAYCPDVSQFPEETPALIAGADVLVIDAL 208
Cdd:smart00849  84 GAEAEPAPPDRTLKDGDELDL--GGGELEVIHTPgHTPGSI-VLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAASDAL 159
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 5-207 2.40e-92

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: 271.27  E-value: 2.40e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153   5 LRLTILGCGSSPGTPRITGDWGACDPANPKNRRRRCAAMVERvsasgGITRVVIDTGPDFREQMISAGVDRLDAAVYTHP 84
Cdd:cd16279     1 MKLTFLGTGTSSGVPVIGCDCGVCDSSDPKNRRLRSSILIET-----GGKNILIDTGPDFRQQALRAGIRKLDAVLLTHA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  85 HADHIHGIDDLRGFVMNQRHLMDVYADKPTLQRLIEAFGYCFEtPPGSNYPPILKAHPISHEAPFSINGaggpLTFQPLP 164
Cdd:cd16279    76 HADHIHGLDDLRPFNRLQQRPIPVYASEETLDDLKRRFPYFFA-ATGGGGVPKLDLHIIEPDEPFTIGG----LEITPLP 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1998278153 165 QIHGDILSLGYRIGGLAYCPDVSQFPEETPALIAGADVLVIDA 207
Cdd:cd16279   151 VLHGKLPSLGFRFGDFAYLTDVSEIPEESLEKLRGLDVLILDA 193
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 5-267 4.00e-88

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 263.29  E-value: 4.00e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153   5 LRLTILGCGSSPGTPRITGDWGACDPANPKNRRRRCAAMVErvsaSGGiTRVVIDTGPDFREQMISAGVD--RLDAAVYT 82
Cdd:COG1235     1 MKVTFLGSGSSGGVPQIGCDCPVCASTDPRYGRTRSSILVE----ADG-TRLLIDAGPDLREQLLRLGLDpsKIDAILLT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  83 HPHADHIHGIDDLRGFVMNQRhlMDVYADKPTLQRLIEAFGYCFETppgsnYPPILKAHPISHEAPFSIngagGPLTFQP 162
Cdd:COG1235    76 HEHADHIAGLDDLRPRYGPNP--IPVYATPGTLEALERRFPYLFAP-----YPGKLEFHEIEPGEPFEI----GGLTVTP 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153 163 LPQIHGDILSLGYRI----GGLAYCPDVSQFPEETPALIAGADVLVIDALQYRPHPSHFSLEEALGWIERLSPRRAVLTH 238
Cdd:COG1235   145 FPVPHDAGDPVGYRIedggKKLAYATDTGYIPEEVLELLRGADLLILDATYDDPEPGHLSNEEALELLARLGPKRLVLTH 224

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1998278153 239 MHIP-----LDYETVLRE-TPDHVEPGFDGMVIEI 267
Cdd:COG1235   225 LSPDnndheLDYDELEAAlLPAGVEVAYDGMEIEL 259
MBL_Geo_Pelo NF038231
GPMC system MBL fold metallohydrolase; Members of this family, distantly related to ...
 7-266 3.03e-81

GPMC system MBL fold metallohydrolase; Members of this family, distantly related to metallo-beta-lactamases, are MBL fold hydrolases of the GPMC (Geobacter/Pelobacter Mystery Cassette) system, in which the most distinctive signature is the TIGR04442 protein family.


Pssm-ID: 439532  Cd Length: 250  Bit Score: 245.28  E-value: 3.03e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153   7 LTILGCGSSPGTPRITGDWGACDPANPKNRRRRCAAMVErvsaSGGiTRVVIDTGPDFREQMISAGVDRLDAAVYTHPHA 86
Cdd:NF038231    2 ITILGSGTSTGVPMIGCHCPVCRSTDPRNKRTRCSALLS----WGG-KNILIDTSTDLRQQALREGIPHIDAVLYTHAHA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  87 DHIHGIDDLRGFVMNQRHLMDVYADKPTLQRLIEAFGYCFETPPGSNYPPILKAHPIshEAPFSINGaggpLTFQPLPQI 166
Cdd:NF038231   77 DHVHGIDDLRGFNFLHRRVIPCYGSAATMAQLRRNFSYIFRGEEGAGYRPLLEPHPI--SGPFDLFG----LRVVPVPLR 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153 167 HGDILSLGYRIGGLAYCPDVSQFPEETPALIAGADVLVIDALQYRPHPSHFSLEEALGWIERLSPRRAVLTHMHIPLDYE 246
Cdd:NF038231  151 HGAMEATGYRIGPLAYLTDCSAIPEASLELLQGLELLVIDGLRFRPHPTHFNIEQAIEVAQRLGARRTILTHLSHEVDHA 230

                         250       260
                  ....*....|....*....|
gi 1998278153 247 TVLRETPDHVEPGFDGMVIE 266
Cdd:NF038231  231 RDGAELPAGVEFAYDGMQLS 250
PRK02113 PRK02113
MBL fold metallo-hydrolase;
5-267 3.68e-63

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 199.24  E-value: 3.68e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153   5 LRLTILGCGSSPGTPRITGDWGACDPANPKNRRRRCAAMVERVSAsggitRVVIDTGPDFREQMISAGVDRLDAAVYTHP 84
Cdd:PRK02113    1 MKIRILGSGTSTGVPEIGCTCPVCTSKDPRDNRLRTSALVETEGA-----RILIDCGPDFREQMLRLPFGKIDAVLITHE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  85 HADHIHGIDDLRGFVmnqRHL-MDVYADKPTLQRLIEAFGYCFETPPgsnYP--PILKAHPISHEAPFSINGaggpLTFQ 161
Cdd:PRK02113   76 HYDHVGGLDDLRPFC---RFGeVPIYAEQYVAERLRSRMPYCFVEHS---YPgvPNIPLREIEPDRPFLVNH----TEVT 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153 162 PLPQIHGDILSLGYRIGGLAYCPDVSQFPEETPALIAGADVLVIDALQYRPHPSHFSLEEALGWIERLSPRRAVLTHM-- 239
Cdd:PRK02113  146 PLRVMHGKLPILGYRIGKMAYITDMLTMPEEEYEQLQGIDVLVMNALRIAPHPTHQSLEEALENIKRIGAKETYLIHMsh 225

                         250       260
                  ....*....|....*....|....*...
gi 1998278153 240 HIPLdYETVLRETPDHVEPGFDGMVIEI 267
Cdd:PRK02113  226 HIGL-HADVEKELPPHVHFAYDGLEIIF 252
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 54-239 4.54e-40

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: 138.21  E-value: 4.54e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  54 TRVVIDTGPDFREQMISAGV------DRLDAAVYTHPHADHIHGIDDLRgfvmnQRHLMDVYADKPTLQRLIEAFGYCFe 127
Cdd:pfam12706   1 RRILIDPGPDLRQQALPALQpgrlrdDPIDAVLLTHDHYDHLAGLLDLR-----EGRPRPLYAPLGVLAHLRRNFPYLF- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153 128 tppgSNYPPILKAHPISHEAPFSINGAGgpLTFQPLPQIHGDI--------LSLGYRIGG----LAYCPDVSQFPEETPA 195
Cdd:pfam12706  75 ----LLEHYGVRVHEIDWGESFTVGDGG--LTVTATPARHGSPrgldpnpgDTLGFRIEGpgkrVYYAGDTGYFPDEIGE 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1998278153 196 LIAGADVLVIDALQYRP----HPSHFSLEEALGWIERLSPRRAVLTHM 239
Cdd:pfam12706 149 RLGGADLLLLDGGAWRDdemiHMGHMTPEEAVEAAADLGARRKVLIHI 196
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 7-207 4.27e-10

Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 57.66  E-value: 4.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153   7 LTILGcgsspgtpriTGDWGacdpanPKNRRRRCAAMVErvsasGGITRVVIDTGPDFREQMISAGVD--RLDAAVYTHP 84
Cdd:cd16272     1 LTFLG----------TGGAV------PSLTRNTSSYLLE-----TGGTRILLDCGEGTVYRLLKAGVDpdKLDAIFLSHF 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  85 HADHIHGiddLRGFVM-----NQRHLMDVYADKPtLQRLIEAFGYCFETPPGSNYPpiLKAHPISHEAPFSIngaGGPLT 159
Cdd:cd16272    60 HLDHIGG---LPTLLFarrygGRKKPLTIYGPKG-IKEFLEKLLNFPVEILPLGFP--LEIEELEEGGEVLE---LGDLK 130

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1998278153 160 FQPLPQIHGdILSLGYRI--GG--LAYCPDVSqFPEETPALIAGADVLVIDA 207
Cdd:cd16272   131 VEAFPVKHS-VESLGYRIeaEGksIVYSGDTG-PCENLVELAKGADLLIHEC 180
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 6-207 9.82e-09

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


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 53.60  E-value: 9.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153   6 RLTILGC-GSSPGtpritgdwgacdPANPknrrrrcaamvervsASG-----GITRVVIDTGPdfreqmisaGV------ 73
Cdd:cd07716     1 KLTVLGCsGSYPG------------PGGA---------------CSGylleaDGFRILLDCGS---------GVlsrlqr 44

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  74 ----DRLDAAVYTHPHADHI-------HGIDDLRGFVMNQRhlMDVYADKPTLQRLIEAFGycfetppgsnYPPILKAHP 142
Cdd:cd07716    45 yidpEDLDAVVLSHLHPDHCadlgvlqYARRYHPRGARKPP--LPLYGPAGPAERLAALYG----------LEDVFDFHP 112

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1998278153 143 ISHEAPFSIngagGPLTFQPLPQIHgDILSLGYRI----------GGLAYCPDVSQFpeetpalIAGADVLVIDA 207
Cdd:cd07716   113 IEPGEPLEI----GPFTITFFRTVH-PVPCYAMRIedggkvlvytGDTGYCDELVEF-------ARGADLLLCEA 175
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 49-238 1.08e-08

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: 54.12  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  49 ASGGI------TRVVIDTGPDFREQMISAGVD--RLDAAVYTHPHADH-----------IHGIDDLRGFVMNQRHLMDVY 109
Cdd:cd07741    19 ASGGIwielngKNIHIDPGPGALVRMCRPKLDptKLDAIILSHRHLDHsndanvlieamTEGGFKKRGTLLAPEDALNGE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153 110 AD--KPTLQRLIEafgycfetppgsnyppilKAHPISHEAPFSINGaggpLTFQPLPQIHGDILSLGYRIGG----LAYC 183
Cdd:cd07741    99 PVvlLYYHRRKLE------------------EIEILEEGDEYELGG----IKIEATRHKHSDPTTYGFIFRTsdkkIGYI 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1998278153 184 PDvSQFPEETPALIAGADVLVIDALQYRPHPS--HFSLEEALGWIERLSPRRAVLTH 238
Cdd:cd07741   157 SD-TRYFEELIEYYSNCDVLIINVTRPRPRKGvdHLSVEDVEKILKEIKPKLAILTH 212
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 55-208 1.10e-08

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: 53.71  E-value: 1.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153   55 RVVIDTGPDFREQMI----SAGVDRLDAAVYTHPHADHIHGIDDLRgfvmnQRHLMDVYADKPTLQRLIEAFGYCfeTPP 130
Cdd:smart00849  11 AILIDTGPGEAEDLLaelkKLGPKKIDAIILTHGHPDHIGGLPELL-----EAPGAPVYAPEGTAELLKDLLALL--GEL 83

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1998278153  131 GSNYPPILKAHPISHEAPFSIngAGGPLTFQPLP-QIHGDIlSLGYRIGGLAYCPDVSQFPEETPALIAGADVLVIDAL 208
Cdd:smart00849  84 GAEAEPAPPDRTLKDGDELDL--GGGELEVIHTPgHTPGSI-VLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAASDAL 159
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 54-225 2.72e-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: 2.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  54 TRVVIDTGPDFRE--QMISAGVDRLDAAV-YTHPHADHIHGIDDLRGFVMNQRHLmDVYADKPTLQRLIEAFGYCFETP- 129
Cdd:cd07715    33 ELLILDAGTGIRElgNELMKEGPPGEAHLlLSHTHWDHIQGFPFFAPAYDPGNRI-HIYGPHKDGGSLEEVLRRQMSPPy 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153 130 ---PGSNYPPILKAHPISHEAPFSINGaggpLTFQPLPQIHGDiLSLGYRI--GG--LAYCPDVSQFP------EETPAL 196
Cdd:cd07715   112 fpvPLEELLAAIEFHDLEPGEPFSIGG----VTVTTIPLNHPG-GALGYRIeeDGksVVYATDTEHYPddgesdEALLEF 186

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1998278153 197 IAGADVLVIDAlqyrphpsHFSLEEAL---GW 225
Cdd:cd07715   187 ARGADLLIHDA--------QYTDEEYPskrGW 210
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 56-95 9.82e-08

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: 51.78  E-value: 9.82e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1998278153  56 VVIDTGPDFREQMISA---------GVDRLDAAVYTHPHADHIHGIDDL 95
Cdd:COG2333    24 ILIDTGPRPSFDAGERvvlpylralGIRRLDLLVLTHPDADHIGGLAAV 72
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
56-238 1.09e-07

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 51.22  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  56 VVIDTGPD------FREQMISAGVDRLDAAVYTHPHADHIHGIDDLRgfvmnQRHLMDVYADKPTLQRLIEAFGYCFETP 129
Cdd:pfam00753  18 VLIDTGGSaeaallLLLAALGLGPKDIDAVILTHGHFDHIGGLGELA-----EATDVPVIVVAEEARELLDEELGLAASR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153 130 PGSNYPPILKAHPIsheaPFSINGAGGPLTFQPLPQIHG-----DILSLGYRIGGLAYCPDVSqFPEETPALIagadvLV 204
Cdd:pfam00753  93 LGLPGPPVVPLPPD----VVLEEGDGILGGGLGLLVTHGpghgpGHVVVYYGGGKVLFTGDLL-FAGEIGRLD-----LP 162

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1998278153 205 IDALQYRPHPSHFSLEEALGWIERLSPRRAVLTH 238
Cdd:pfam00753 163 LGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 45-204 2.71e-07

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: 49.82  E-value: 2.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  45 ERVSAS-----GGiTRVVIDTGPDFREQMISAGVD--RLDAAVYTHPHADHIHGIDDL--RGFVMNQRHLMDVYADKPTl 115
Cdd:cd07719    15 DRAGPStlvvvGG-RVYLVDAGSGVVRRLAQAGLPlgDLDAVFLTHLHSDHVADLPALllTAWLAGRKTPLPVYGPPGT- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153 116 QRLIEAFGYCFETP-------PGSNYPPI---LKAHPISHEAP-FSINGaggpLTFQPLPQIHGDIL-SLGYRI------ 177
Cdd:cd07719    93 RALVDGLLAAYALDidyrariGDEGRPDPgalVEVHEIAAGGVvYEDDG----VKVTAFLVDHGPVPpALAYRFdtpgrs 168

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1998278153 178 ----GGLAYCPDVSQFpeetpAliAGADVLV 204
Cdd:cd07719   169 vvfsGDTGPSENLIEL-----A--KGADLLV 192
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 56-95 6.59e-07

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: 48.67  E-value: 6.59e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1998278153  56 VVIDTGP--DFREQMI-----SAGVDRLDAAVYTHPHADHIHGIDDL 95
Cdd:cd07731    22 ILIDTGPrdSFGEDVVvpylkARGIKKLDYLILTHPDADHIGGLDAV 68
PQQB-like_MBL-fold cd16274
Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold ...
 47-206 3.40e-06

Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold metallo hydrolase domainhydrolase domain; PQQB is essential for the synthesis of the cofactor pyrroloquinoline quinone (PQQ) in Klebsiella pneumonia. PqqB is not directly involved in the PQQ biosynthesis but may serve as a carrier for PQQ when PQQ is released from PqqC. 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: 293832 [Multi-domain]  Cd Length: 220  Bit Score: 46.84  E-value: 3.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  47 VSASGgITRVVIDTGPDFREQMIS---------------AGVDRLDAAVythphaDHIHGIDDLRgfvmnQRHLMDVYAD 111
Cdd:cd16274    44 VSADG-ENWVLINASPDIRQQIEAtpelqprpglrdtpiAAVLLTDAEI------DHTTGLLSLR-----EGQPLTVYAT 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153 112 KPTLQRLIEAFGycFETPPGSNYPpiLKAHPISHEAPFSINGAGGpLTFQPLP--------------QIHGDilSLGYRI 177
Cdd:cd16274   112 APVLEDLTTNFP--FFVLLHAYGG--VRRHRILPGEPFTLAGCPG-LTVTPFPvpgkaplysehrdaPEPGD--TIGLRI 184

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1998278153 178 ------GGLAYCPDVSQFPEETPALIAGADVLVID 206
Cdd:cd16274   185 edgrtgGRLFYAPGCAAVTDELRARLAGADCLLFD 219
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 67-207 3.96e-06

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: 47.06  E-value: 3.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  67 QMISAGVD--RLDAAVYTHPHADHIHGiddLRGFV----MNQR-HLMDVYADKPtLQRLIEAFGYCFETPPgsNYPPILk 139
Cdd:cd07717    40 QLLRAGLSpsKIDRIFITHLHGDHILG---LPGLLstmsLLGRtEPLTIYGPKG-LKEFLETLLRLSASRL--PYPIEV- 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1998278153 140 aHPISHEAPFSINGAGgpLTFQPLPQIHGdILSLGYRI-GG--LAYCPDvSQFPEETPALIAGADVLVIDA 207
Cdd:cd07717   113 -HELEPDPGLVFEDDG--FTVTAFPLDHR-VPCFGYRFeEGrkIAYLGD-TRPCEGLVELAKGADLLIHEA 178
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 8-216 4.14e-06

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 46.48  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153   8 TILGCGSSPGTPritgdwgacdpanpkNRRRRCAAMVervsasGGITRVVIDTGPDFREQMISAGVDR--LDAAVYTHPH 85
Cdd:cd07740     1 TFLGSGDAFGSG---------------GRLNTCFHVA------SEAGRFLIDCGASSLIALKRAGIDPnaIDAIFITHLH 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  86 ADHIHGID----DLRgFVMNQRHLMDVYADKPTLQRLIEAFGYCFetpPGSN---------YPPILKAHPISHeapfsin 152
Cdd:cd07740    60 GDHFGGLPffllDAQ-FVAKRTRPLTIAGPPGLRERLRRAMEALF---PGSSkvprrfdleVIELEPGEPTTL------- 128

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1998278153 153 gagGPLTFQPLPQIHGD-ILSLGYRI--GG--LAYCPDVsqfpEETPALI---AGADVLVIDALQY-RPHPSH 216
Cdd:cd07740   129 ---GGVTVTAFPVVHPSgALPLALRLeaAGrvLAYSGDT----EWTDALVplaRGADLFICECYFFeKKVPGH 194
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 50-116 5.97e-06

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: 45.33  E-value: 5.97e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1998278153  50 SGGITRVVIDTGPDFRE---QMISAGVD--RLDAAVYTHPHADHIHGIDdlrgfVMNQRHLMDVYADKPTLQ 116
Cdd:cd07733    15 ETEDGKLLIDAGLSGRKitgRLAEIGRDpeDIDAILVTHEHADHIKGLG-----VLARKYNVPIYATAGTLR 81
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 56-96 7.17e-06

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: 45.74  E-value: 7.17e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1998278153  56 VVIDTGPDFREQMISAGVD---RLDAAVYTHPHADHIHGIDDLR 96
Cdd:cd06262    23 ILIDPGAGALEKILEAIEElglKIKAILLTHGHFDHIGGLAELK 66
PRK05184 PRK05184
pyrroloquinoline quinone biosynthesis protein PqqB; Provisional
 47-267 1.95e-05

pyrroloquinoline quinone biosynthesis protein PqqB; Provisional


Pssm-ID: 235361 [Multi-domain]  Cd Length: 302  Bit Score: 45.19  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  47 VSAsGGITRVVIDTGPDFREQMIS------AGVDR---LDAAVYTHPHADHIHGIDDLRgfvmnQRHLMDVYADKPTLQR 117
Cdd:PRK05184   44 VSA-DGEDWVLLNASPDIRQQIQAtpalqpARGLRdtpIAAVVLTDGQIDHTTGLLTLR-----EGQPFPVYATPAVLED 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153 118 LIEAF-------GYCfetppgsnyppILKAHPISHEAPFSINGAGGpLTFQPLP--------------QIHGDilSLGYR 176
Cdd:PRK05184  118 LSTGFpifnvldHYG-----------GVQRRPIALDGPFAVPGLPG-LRFTAFPvpskappysphrsdPEPGD--NIGLR 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153 177 I------GGLAYCPDVSQFPEETPALIAGADVLVIDALQYRP---------HPS-----HFSLEEALGWIERLSP---RR 233
Cdd:PRK05184  184 IedratgKRLFYAPGLAEVTDALRARLAGADCVLFDGTLWTDdemiragvgTKTgrrmgHLPQSGPGGMIAALARlpiAR 263

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1998278153 234 AVLTHMHipldyET--VLRE-TPDH-------VEPGFDGMVIEI 267
Cdd:PRK05184  264 KILIHIN-----NTnpILDEdSPERaeleaagIEVAHDGMEIEL 302
PRK00055 PRK00055
ribonuclease Z; Reviewed
 5-268 3.86e-05

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 44.02  E-value: 3.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153   5 LRLTILGCGSspGTPRitgdwgacdpanpknRRRRCAAMVerVSASGGItrVVIDTGPDFREQMISAGV--DRLDAAVYT 82
Cdd:PRK00055    2 MELTFLGTGS--GVPT---------------PTRNVSSIL--LRLGGEL--FLFDCGEGTQRQLLKTGIkpRKIDKIFIT 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  83 HPHADHIHGiddLRGFVMnQRHL------MDVYADKPT---LQRLIEAF---GYCFETPPGSNYPPI--LKAHPISHEAP 148
Cdd:PRK00055   61 HLHGDHIFG---LPGLLS-TRSLsgrtepLTIYGPKGIkefVETLLRASgslGYRIAEKDKPGKLDAekLKALGVPPGPL 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153 149 FSINGAGGPLTFQPLPQIHG-DILSLGYRIGGLAYCPDvSQFPEETPALIAGADVLVIDAL-------QYRPHpSHFSLE 220
Cdd:PRK00055  137 FGKLKRGEDVTLEDGRIINPaDVLGPPRKGRKVAYCGD-TRPCEALVELAKGADLLVHEATfgdedeeLAKEY-GHSTAR 214

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1998278153 221 EALGWIERLSPRRAVLTHM--HIPLDYETVLRETP---DHVEPGFDGMVIEIP 268
Cdd:PRK00055  215 QAAEIAKEAGVKRLILTHFspRYTGDPEELLKEAReifPNTELAEDLMRVEVP 267
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 56-193 2.18e-04

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 41.36  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  56 VVIDTGPD-----FREQMISAGVDRLDAAVYTHPHADHIHGIDDLRgfvmNQRHLmDVYA---DKPTLQR-LIEAFGYCF 126
Cdd:cd07743    21 LLIDSGLDedagrKIRKILEELGWKLKAIINTHSHADHIGGNAYLQ----KKTGC-KVYApkiEKAFIENpLLEPSYLGG 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1998278153 127 ETPPGSNYPPILKAHPISHEAPFS---INGAGGPLTFQPLP-----QIhgdilslGYRIG-GLAYCPDvSQFPEET 193
Cdd:cd07743    96 AYPPKELRNKFLMAKPSKVDDIIEegeLELGGVGLEIIPLPghsfgQI-------GILTPdGVLFAGD-ALFGEEV 163
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 70-164 8.64e-04

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: 39.52  E-value: 8.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1998278153  70 SAGVDRLDAAVYTHPHADHIHGIDDLrgfvmnqRHLMDVYADKPTLqRLIEAFGYCFetppGSNYPPILKAHPISHEAPF 149
Cdd:cd07732    70 SEEDPSVDAVLLSHAHLDHYGLLNYL-------RPDIPVYMGEATK-RILKALLPFF----GEGDPVPRNIRVFESGKSF 137

                          90
                  ....*....|....*
gi 1998278153 150 SIngagGPLTFQPLP 164
Cdd:cd07732   138 TI----GDFTVTPYL 148
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 52-96 1.78e-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: 38.67  E-value: 1.78e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1998278153  52 GITRVVIDTG-------PDFREQMISAGVDRLDAAVYTHPHADHIHGIDDLR 96
Cdd:cd07722    26 GKRRILIDTGegrpsyiPLLKSVLDSEGNATISDILLTHWHHDHVGGLPDVL 77
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 56-96 4.95e-03

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: 37.36  E-value: 4.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1998278153  56 VVIDTGPDFRE-----QMISAGVDRLDAAVYTHPHADHIHGIDDLR 96
Cdd:COG0491    27 VLIDTGLGPADaeallAALAALGLDIKAVLLTHLHPDHVGGLAALA 72
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 54-95 9.71e-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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 36.86  E-value: 9.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1998278153  54 TRVVIDTGPDFREQMISAGVD--RLDAAVYTHPHADHIHGIDDL 95
Cdd:cd07730    60 TPVPLEVEEDVAEQLAAGGIDpeDIDAVILSHLHWDHIGGLSDF 103
 
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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