NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1052486764|gb|AOC97101|]
View 

metal-dependent hydrolase [Flavobacterium anhuiense]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 581040)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 1-226 7.83e-75

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.


The actual alignment was detected with superfamily member PRK00685:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 228  Bit Score: 225.85  E-value: 7.83e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764   1 MKITYYGHSCFSVYANEKHILFDPFITPNELAKeVDVDAIKADYIFISHAHYDHILDVERIAKNTGAKVLGNFEIYNWLL 80
Cdd:PRK00685    1 MKITWLGHSAFLIETGGKKILIDPFITGNPLAD-LKPEDVKVDYILLTHGHGDHLGDTVEIAKRTGATVIANAELANYLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  81 KNGIENAHPINPGGKFDFDFGTVKCVVAQHPSSFMDGS---YGGIACGFVLTTSDGNFYYSGDTALTLDMQLIPKFTKLD 157
Cdd:PRK00685   80 EKGVEKTHPMNIGGTVEFDGGKVKLTPALHSSSFIDEDgitYLGNPTGFVITFEGKTIYHAGDTGLFSDMKLIGELHKPD 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1052486764 158 FAVFPIGDGLTMGIEEAIEASKLVGVKKILGVHYDTFGFIVMDHQKALDAFKDASLQLFLPKINSTIEI 226
Cdd:PRK00685  160 VALLPIGDNFTMGPEDAALAVELIKPKIVIPMHYNTFPLIEQDPEKFKALVEGLGTKVVILKPGESIEL 228
 
Name Accession Description Interval E-value
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 1-226 7.83e-75

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 225.85  E-value: 7.83e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764   1 MKITYYGHSCFSVYANEKHILFDPFITPNELAKeVDVDAIKADYIFISHAHYDHILDVERIAKNTGAKVLGNFEIYNWLL 80
Cdd:PRK00685    1 MKITWLGHSAFLIETGGKKILIDPFITGNPLAD-LKPEDVKVDYILLTHGHGDHLGDTVEIAKRTGATVIANAELANYLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  81 KNGIENAHPINPGGKFDFDFGTVKCVVAQHPSSFMDGS---YGGIACGFVLTTSDGNFYYSGDTALTLDMQLIPKFTKLD 157
Cdd:PRK00685   80 EKGVEKTHPMNIGGTVEFDGGKVKLTPALHSSSFIDEDgitYLGNPTGFVITFEGKTIYHAGDTGLFSDMKLIGELHKPD 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1052486764 158 FAVFPIGDGLTMGIEEAIEASKLVGVKKILGVHYDTFGFIVMDHQKALDAFKDASLQLFLPKINSTIEI 226
Cdd:PRK00685  160 VALLPIGDNFTMGPEDAALAVELIKPKIVIPMHYNTFPLIEQDPEKFKALVEGLGTKVVILKPGESIEL 228
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 1-211 3.14e-65

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 201.30  E-value: 3.14e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764   1 MKITYYGHSCFSVYANEKHILFDPFITPNELA---KEVDVDAI-KADYIFISHAHYDHiLDVERIA--KNTGAKVLGNFE 74
Cdd:COG2220     4 MKITWLGHATFLIETGGKRILIDPVFSGRASPvnpLPLDPEDLpKIDAVLVTHDHYDH-LDDATLRalKRTGATVVAPLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  75 IYNWLLKNGIENAHPINPGGKFDFDFGTVKCVVAQHPSSFMDGSYGGiACGFVLTTSDGNFYYSGDTALTLDMQLIPKFT 154
Cdd:COG2220    83 VAAWLRAWGFPRVTELDWGESVELGGLTVTAVPARHSSGRPDRNGGL-WVGFVIETDGKTIYHAGDTGYFPEMKEIGERF 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1052486764 155 KLDFAVFPIGDG-LTMGIEEAIEASKLVGVKKILGVHYDTFGFIVMDhqkALDAFKDA 211
Cdd:COG2220   162 PIDVALLPIGAYpFTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDED---PLERFAAA 216
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 20-191 3.11e-28

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 105.47  E-value: 3.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  20 ILFDPF------ITPNELAKEVDVDAIkaDYIFISHAHYDHILDVERIAKNTGAKVLG---------NFEIYNWLLKNGI 84
Cdd:pfam12706   3 ILIDPGpdlrqqALPALQPGRLRDDPI--DAVLLTHDHYDHLAGLLDLREGRPRPLYAplgvlahlrRNFPYLFLLEHYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  85 ENAHPINPGGKFDFDFG--TVKCVVAQHPSSFMDGSYGGIACGFVLTTSDGNFYYSGDTALTlDMQLIPKFTKLDFAVFP 162
Cdd:pfam12706  81 VRVHEIDWGESFTVGDGglTVTATPARHGSPRGLDPNPGDTLGFRIEGPGKRVYYAGDTGYF-PDEIGERLGGADLLLLD 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1052486764 163 IG--------DGLTMGIEEAIEASKLVGVKKILGVHY 191
Cdd:pfam12706 160 GGawrddemiHMGHMTPEEAVEAAADLGARRKVLIHI 196
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 7-164 7.40e-18

Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. 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: 293841  Cd Length: 181  Bit Score: 77.70  E-value: 7.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764   7 GHSCFSVYANEKHILFDP----------FITPNELAKE-VDVDAI-KADYIFISHAHYDHiLDVERIaKNTGAKVLGNFE 74
Cdd:cd16283     3 GHATFLIQIEGLNILTDPvfseraspvsFGGPKRLTPPgLPLEELpPIDAVLISHNHYDH-LDLPTV-KRLGGRPPYLVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  75 IYN--WLLKNGIENAHPINPGGKFDFDFGTVKCVVAQHPS--SFMDGsYGGIACGFVLTTSDGNFYYSGDTALTLDMQLI 150
Cdd:cd16283    81 LGLkkWFLKKGITNVVELDWWQSTEIGGVRITFVPAQHWSrrTLFDT-NESLWGGWVIEGEGFRIYFAGDTGYFPGFREI 159

                         170
                  ....*....|....*
gi 1052486764 151 -PKFTKLDFAVFPIG 164
Cdd:cd16283   160 gRRFGPIDLALLPIG 174
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 9-190 2.68e-10

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: 57.56  E-value: 2.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764    9 SCFSVYANEKHILFDPFITPNE--LAKEVDVDAIKADYIFISHAHYDHILDVERIAKNTGAKVLGNFEIYNWL------- 79
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEdlLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLkdllall 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764   80 -----LKNGIENAHPINPGGKFDFDFGTVKCVVAQhpssfmdgsyGGIACGFVLTTSDGNFYYSGDTALTLDMQLIpkft 154
Cdd:smart00849  81 gelgaEAEPAPPDRTLKDGDELDLGGGELEVIHTP----------GHTPGSIVLYLPEGKILFTGDLLFAGGDGRT---- 146

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1052486764  155 kldfaVFPIGDGLTMGIEEAIEASKLVGVKKILGVH 190
Cdd:smart00849 147 -----LVDGGDAAASDALESLLKLLKLLPKLVVPGH 177
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 38-140 8.36e-03

beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and RNase J2, involved in mRNA degradation in a wide range of organism. [Transcription, Degradation of RNA]


Pssm-ID: 273195 [Multi-domain]  Cd Length: 422  Bit Score: 36.56  E-value: 8.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  38 DAIKAdyIFISHAHYDHILDVERIAKNtgakvLGNFEIY----------NWLLKNGIENAHP---INPGGKFDFDFG-TV 103
Cdd:TIGR00649  57 DKVKG--IFITHGHEDHIGAVPYLLHQ-----VGFFPIYgtpltialikSKIKEHGLNVRTDlleIHEGEPVEFGENtAI 129

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1052486764 104 KCVVAQH--PSSFmdgsyggiacGFVLTTSDGNFYYSGD 140
Cdd:TIGR00649 130 EFFRITHsiPDSV----------GFALHTPLGYIVYTGD 158
 
Name Accession Description Interval E-value
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 1-226 7.83e-75

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 225.85  E-value: 7.83e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764   1 MKITYYGHSCFSVYANEKHILFDPFITPNELAKeVDVDAIKADYIFISHAHYDHILDVERIAKNTGAKVLGNFEIYNWLL 80
Cdd:PRK00685    1 MKITWLGHSAFLIETGGKKILIDPFITGNPLAD-LKPEDVKVDYILLTHGHGDHLGDTVEIAKRTGATVIANAELANYLS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  81 KNGIENAHPINPGGKFDFDFGTVKCVVAQHPSSFMDGS---YGGIACGFVLTTSDGNFYYSGDTALTLDMQLIPKFTKLD 157
Cdd:PRK00685   80 EKGVEKTHPMNIGGTVEFDGGKVKLTPALHSSSFIDEDgitYLGNPTGFVITFEGKTIYHAGDTGLFSDMKLIGELHKPD 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1052486764 158 FAVFPIGDGLTMGIEEAIEASKLVGVKKILGVHYDTFGFIVMDHQKALDAFKDASLQLFLPKINSTIEI 226
Cdd:PRK00685  160 VALLPIGDNFTMGPEDAALAVELIKPKIVIPMHYNTFPLIEQDPEKFKALVEGLGTKVVILKPGESIEL 228
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 1-211 3.14e-65

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 201.30  E-value: 3.14e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764   1 MKITYYGHSCFSVYANEKHILFDPFITPNELA---KEVDVDAI-KADYIFISHAHYDHiLDVERIA--KNTGAKVLGNFE 74
Cdd:COG2220     4 MKITWLGHATFLIETGGKRILIDPVFSGRASPvnpLPLDPEDLpKIDAVLVTHDHYDH-LDDATLRalKRTGATVVAPLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  75 IYNWLLKNGIENAHPINPGGKFDFDFGTVKCVVAQHPSSFMDGSYGGiACGFVLTTSDGNFYYSGDTALTLDMQLIPKFT 154
Cdd:COG2220    83 VAAWLRAWGFPRVTELDWGESVELGGLTVTAVPARHSSGRPDRNGGL-WVGFVIETDGKTIYHAGDTGYFPEMKEIGERF 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1052486764 155 KLDFAVFPIGDG-LTMGIEEAIEASKLVGVKKILGVHYDTFGFIVMDhqkALDAFKDA 211
Cdd:COG2220   162 PIDVALLPIGAYpFTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDED---PLERFAAA 216
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 20-191 3.11e-28

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 105.47  E-value: 3.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  20 ILFDPF------ITPNELAKEVDVDAIkaDYIFISHAHYDHILDVERIAKNTGAKVLG---------NFEIYNWLLKNGI 84
Cdd:pfam12706   3 ILIDPGpdlrqqALPALQPGRLRDDPI--DAVLLTHDHYDHLAGLLDLREGRPRPLYAplgvlahlrRNFPYLFLLEHYG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  85 ENAHPINPGGKFDFDFG--TVKCVVAQHPSSFMDGSYGGIACGFVLTTSDGNFYYSGDTALTlDMQLIPKFTKLDFAVFP 162
Cdd:pfam12706  81 VRVHEIDWGESFTVGDGglTVTATPARHGSPRGLDPNPGDTLGFRIEGPGKRVYYAGDTGYF-PDEIGERLGGADLLLLD 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1052486764 163 IG--------DGLTMGIEEAIEASKLVGVKKILGVHY 191
Cdd:pfam12706 160 GGawrddemiHMGHMTPEEAVEAAADLGARRKVLIHI 196
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 7-164 7.40e-18

Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. 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: 293841  Cd Length: 181  Bit Score: 77.70  E-value: 7.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764   7 GHSCFSVYANEKHILFDP----------FITPNELAKE-VDVDAI-KADYIFISHAHYDHiLDVERIaKNTGAKVLGNFE 74
Cdd:cd16283     3 GHATFLIQIEGLNILTDPvfseraspvsFGGPKRLTPPgLPLEELpPIDAVLISHNHYDH-LDLPTV-KRLGGRPPYLVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  75 IYN--WLLKNGIENAHPINPGGKFDFDFGTVKCVVAQHPS--SFMDGsYGGIACGFVLTTSDGNFYYSGDTALTLDMQLI 150
Cdd:cd16283    81 LGLkkWFLKKGITNVVELDWWQSTEIGGVRITFVPAQHWSrrTLFDT-NESLWGGWVIEGEGFRIYFAGDTGYFPGFREI 159

                         170
                  ....*....|....*
gi 1052486764 151 -PKFTKLDFAVFPIG 164
Cdd:cd16283   160 gRRFGPIDLALLPIG 174
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 2-190 3.86e-15

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: 69.93  E-value: 3.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764   2 KITYYGHSCFSVYANEKHILFDPF-ITPNELAKEVDVDAikadyIFISHAHYDHildveriakntgakvlgnfeiynWLL 80
Cdd:pfam13483   1 EITWLGHSSFLIEGGGARILTDPFrATVGYRPPPVTADL-----VLISHGHDDH-----------------------GHP 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  81 KNGIENAHPINPGGKFDFDFGTVKCVVAQHPSSFmdGSYGGIACGFVLTTSDGNFYYSGDTALTLDMQLIPKFTKLDFAV 160
Cdd:pfam13483  53 ETLPGNPHVLDGGGSYTVGGLEIRGVPTDHDRVG--GRRRGGNSIFLFEQDGLTIYHLGHLGHPLSDEQLAELGRVDVLL 130

                         170       180       190
                  ....*....|....*....|....*....|
gi 1052486764 161 FPIGDGLTMGIEEAIEASKLVGVKKILGVH 190
Cdd:pfam13483 131 IPVGGPLTYGAEEALELAKRLRPRVVIPMH 160
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 9-214 1.36e-13

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 67.61  E-value: 1.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764   9 SCFSVYANEKHILFD--PFITPNELAKEVDVDAIKAdyIFISHAHYDHILDVERIA-------------KNTGAKVLGNF 73
Cdd:COG1235    36 SSILVEADGTRLLIDagPDLREQLLRLGLDPSKIDA--ILLTHEHADHIAGLDDLRprygpnpipvyatPGTLEALERRF 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  74 EIYNWLLKNGIEnAHPINPGGKFDFDFGTVKCVVAQHPSsfmdgsygGIACGFVLTTSDGNFYYSGDTAlTLDMQLIPKF 153
Cdd:COG1235   114 PYLFAPYPGKLE-FHEIEPGEPFEIGGLTVTPFPVPHDA--------GDPVGYRIEDGGKKLAYATDTG-YIPEEVLELL 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1052486764 154 TKLDFAVFpigDGLT-------MGIEEAIEASKLVGVKKILGVHYDTfgfIVMDHQKALDAFKDASLQ 214
Cdd:COG1235   184 RGADLLIL---DATYddpepghLSNEEALELLARLGPKRLVLTHLSP---DNNDHELDYDELEAALLP 245
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 9-190 2.68e-10

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: 57.56  E-value: 2.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764    9 SCFSVYANEKHILFDPFITPNE--LAKEVDVDAIKADYIFISHAHYDHILDVERIAKNTGAKVLGNFEIYNWL------- 79
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEdlLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLkdllall 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764   80 -----LKNGIENAHPINPGGKFDFDFGTVKCVVAQhpssfmdgsyGGIACGFVLTTSDGNFYYSGDTALTLDMQLIpkft 154
Cdd:smart00849  81 gelgaEAEPAPPDRTLKDGDELDLGGGELEVIHTP----------GHTPGSIVLYLPEGKILFTGDLLFAGGDGRT---- 146

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1052486764  155 kldfaVFPIGDGLTMGIEEAIEASKLVGVKKILGVH 190
Cdd:smart00849 147 -----LVDGGDAAASDALESLLKLLKLLPKLVVPGH 177
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-144 3.42e-10

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 58.28  E-value: 3.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764   1 MKITYYG-----------HSCFSVYANEKHILFDP-FITPNELAK-EVDVDAIkaDYIFISHAHYDHILDVERIA----- 62
Cdd:COG1234     1 MKLTFLGtggavptpgraTSSYLLEAGGERLLIDCgEGTQRQLLRaGLDPRDI--DAIFITHLHGDHIAGLPGLLstrsl 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  63 ------------KNTGAKVLGNFEIYNWLLKNGIEnAHPINPGGKFDFDFGTVKCVVAQHPssfmdgsygGIACGFVLTT 130
Cdd:COG1234    79 agrekpltiygpPGTKEFLEALLKASGTDLDFPLE-FHEIEPGEVFEIGGFTVTAFPLDHP---------VPAYGYRFEE 148

                         170
                  ....*....|....
gi 1052486764 131 SDGNFYYSGDTALT 144
Cdd:COG1234   149 PGRSLVYSGDTRPC 162
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
7-190 2.17e-09

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 55.07  E-value: 2.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764   7 GHSCFSVYANEKHILFDPFITPNE----LAKEVDVDAIKADYIFISHAHYDHILDVERIAKNTGAKV---------LGNF 73
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTGGSAEAalllLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVivvaeeareLLDE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  74 EIYNWLLKNGIENAHPINPGGKFDFDFGTVKcVVAQHPSSFMDGsYGGIACGFVLTTSDGNFYYSGDTALTLDmqlIPKF 153
Cdd:pfam00753  85 ELGLAASRLGLPGPPVVPLPPDVVLEEGDGI-LGGGLGLLVTHG-PGHGPGHVVVYYGGGKVLFTGDLLFAGE---IGRL 159

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1052486764 154 TKLDFAVFPIGDGLTMGIEEAIEASKLVGVKKILGVH 190
Cdd:pfam00753 160 DLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 10-106 1.24e-07

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: 49.98  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  10 CFSVYANEKH-ILFDP-FITPNELAKEVDVDAIKADYIFISHAHYDHILDVERIAKNTGAKVL-------------GNFE 74
Cdd:cd06262    12 CYLVSDEEGEaILIDPgAGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYiheadaelledpeLNLA 91

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1052486764  75 IYNWLLKNGIENAHPINPGGKFDFDFGTVKCV 106
Cdd:cd06262    92 FFGGGPLPPPEPDILLEDGDTIELGGLELEVI 123
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 3-69 4.48e-07

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: 48.99  E-value: 4.48e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1052486764   3 ITYYGHSCFSVY---ANEKHILFD-------PFITPNELAKEVDVDAIKadYIFISHAHYDHILDVERIAKNTGAKV 69
Cdd:cd16310    14 IYYVGTKGIGSYlitSNHGAILLDggleenaALIEQNIKALGFKLSDIK--IIINTHAHYDHAGGLAQLKADTGAKL 88
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 6-142 6.11e-07

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: 48.03  E-value: 6.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764   6 YGHSCFSVYANEKHILFD-PFITPNELAKEvDVDAIKADYIFISHAHYDHILDV---------ERIAKN---TGAKVLGN 72
Cdd:cd16272    15 RNTSSYLLETGGTRILLDcGEGTVYRLLKA-GVDPDKLDAIFLSHFHLDHIGGLptllfarryGGRKKPltiYGPKGIKE 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1052486764  73 F-----EIYNWLLKNGIE-NAHPINPGGK-FDFDFGTVKCVVAQHPSSfmdgsyggiACGFVLTTSDGNFYYSGDTA 142
Cdd:cd16272    94 FlekllNFPVEILPLGFPlEIEELEEGGEvLELGDLKVEAFPVKHSVE---------SLGYRIEAEGKSIVYSGDTG 161
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 4-141 3.35e-06

Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase domain; Includes Dictyostelium discoideum cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A (also known as cyclic GMP-binding protein A, phosphodiesterase 5, phosphodiesterase D, and PDE5) and cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B (also known as cyclic GMP-binding protein B, phosphodiesterase 6, phosphodiesterase E, and PDE6. 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: 293824  Cd Length: 189  Bit Score: 46.13  E-value: 3.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764   4 TYYGH-SCFSVYANEKHILFDPFITPNELAKEVDVDAIKADYIFISHAHYDH-------ILDVERIAKNTGAKVLGNF-- 73
Cdd:cd07738    10 DPKGHtSGFIIWINGRGIMVDPPVNSTSYLRQNGISPRLVDHVILTHCHADHdagtfqkILEEEKITLYTTRTINESFlr 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  74 --------------EIYNWLLkngIENAHPIN-PGGKFDFDFgtvkcvvaqhpssfmdgSYGGIAC-GFVLTTSDGNFYY 137
Cdd:cd07738    90 kyaaltglppdfleELFDFRP---VIIGEKTKiNGAEFEFDY-----------------SFHSIPTiRFKVSYGGKSIAY 149


                  ....
gi 1052486764 138 SGDT 141
Cdd:cd07738   150 SGDT 153
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 17-140 5.04e-06

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily.Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 45.68  E-value: 5.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  17 EKHILFDPFITPNELAKE-VDVDAIkadyiFISHAHYDHILDVERIAKN-------TGAKVLGNFEIYNWLLKNGIENAH 88
Cdd:cd07732    55 IVGLYRDPLLLGGLRSEEdPSVDAV-----LLSHAHLDHYGLLNYLRPDipvymgeATKRILKALLPFFGEGDPVPRNIR 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1052486764  89 PINPGGKFDF-DFgTVKCVvaqhpssFMDGS-YGgiACGFVLTTSDGNFYYSGD 140
Cdd:cd07732   130 VFESGKSFTIgDF-TVTPY-------LVDHSaPG--AYAFLIEAPGKRIFYTGD 173
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 38-140 5.77e-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: 45.86  E-value: 5.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  38 DAIKAdyIFISHAHYDHI---------LDVERIA-KNTGAKVLGNFEIYNWLLKNGIenaHPINPGGKFDFDFGTVKCVV 107
Cdd:cd07714    54 DKIKG--IFITHGHEDHIgalpyllpeLNVPIYAtPLTLALIKKKLEEFKLIKKVKL---NEIKPGERIKLGDFEVEFFR 128

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1052486764 108 AQHpsSFMDgsyggiACGFVLTTSDGNFYYSGD 140
Cdd:cd07714   129 VTH--SIPD------SVGLAIKTPEGTIVHTGD 153
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 13-106 8.54e-06

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: 45.07  E-value: 8.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  13 VYANEKHILFDPFITPNELAKevDVDAIKA-----DYIFISHAHYDHILDVERIAKNTGAKVLGNFEIYNWLLKNGIENA 87
Cdd:COG0491    20 IVGGDGAVLIDTGLGPADAEA--LLAALAAlgldiKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEAPAAGAL 97

                          90       100
                  ....*....|....*....|....*...
gi 1052486764  88 ---------HPINPGGKFDFDFGTVKCV 106
Cdd:COG0491    98 fgrepvppdRTLEDGDTLELGGPGLEVI 125
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 9-144 1.43e-05

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: 43.97  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764   9 SCFSVYANEKHILFDP----------FITPNELakevdvdaikaDYIFISHAHYDHILDVE------RIAKNTGAK---- 68
Cdd:cd07716    19 SGYLLEADGFRILLDCgsgvlsrlqrYIDPEDL-----------DAVVLSHLHPDHCADLGvlqyarRYHPRGARKpplp 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  69 VLGNFEIYNWLLK-NGIENA---HPINPGGKFDF-DFgTVKCVVAQHPSSfmdgsyggiACGFVLTTSDGNFYYSGDTAL 143
Cdd:cd07716    88 LYGPAGPAERLAAlYGLEDVfdfHPIEPGEPLEIgPF-TITFFRTVHPVP---------CYAMRIEDGGKVLVYTGDTGY 157


                  .
gi 1052486764 144 T 144
Cdd:cd07716   158 C 158
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
11-55 2.39e-05

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 44.10  E-value: 2.39e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1052486764  11 FSVY--ANEKHILFD-----PFItPNelAKEVDVDAIKADYIFISHAHYDHI 55
Cdd:COG1237    23 LSALieTEGKRILFDtgqsdVLL-KN--AEKLGIDLSDIDAVVLSHGHYDHT 71
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 11-55 3.13e-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: 43.76  E-value: 3.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1052486764  11 FSVY--ANEKHILFD-----PFItPNelAKEVDVDAIKADYIFISHAHYDHI 55
Cdd:cd07713    21 LSLLieTEGKKILFDtgqsgVLL-HN--AKKLGIDLSDIDAVVLSHGHYDHT 69
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 16-152 6.57e-05

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


Pssm-ID: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 42.56  E-value: 6.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  16 NEKHILFDPfiTPNEL--AKEVDVDAIKADYIFISHAHYDHILDVERI--AKNTGAK------------VLGNFEIYNWL 79
Cdd:cd07741    28 NGKNIHIDP--GPGALvrMCRPKLDPTKLDAIILSHRHLDHSNDANVLieAMTEGGFkkrgtllapedaLNGEPVVLLYY 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1052486764  80 LKNGIENAHPINPGGKFDFDFGTVKCVVAQHpssfmdgsyGGIAC-GFVLTTSDGNFYYSGDTALTLDMQLIPK 152
Cdd:cd07741   106 HRRKLEEIEILEEGDEYELGGIKIEATRHKH---------SDPTTyGFIFRTSDKKIGYISDTRYFEELIEYYS 170
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 4-101 6.80e-05

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. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B3 MBLs include Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Stenotrophomonas Maltophilia L1, and Bradyrhizobium diazoefficiens BJP-1, Serratia marcescens SMB-1, and Pseudomonas Aeruginosa AIM-1. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 42.53  E-value: 6.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764   4 TYY----GHSCFSVYANEKHILFD-------PFITPNELAKEVDVDAIKadYIFISHAHYDHILDVERIAKNTGAKVLGn 72
Cdd:cd07708    14 TYYvgtdDLAAYLIVTPQGNILIDgdmeqnaPMIKANIKKLGFKFSDTK--LILISHAHFDHAGGSAEIKKQTGAKVMA- 90

                          90       100
                  ....*....|....*....|....*....
gi 1052486764  73 feiynwllknGIENAHPINPGGKFDFDFG 101
Cdd:cd07708    91 ----------GAEDVSLLLSGGSSDFHYA 109
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-55 7.23e-05

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 42.87  E-value: 7.23e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1052486764   1 MKITYYG------HSCFSVYANEKHILFDPFITPNELAK---EVDVDAIKADYIFISHAHYDHI 55
Cdd:COG1236     1 MKLTFLGaagevtGSCYLLETGGTRILIDCGLFQGGKERnwpPFPFRPSDVDAVVLTHAHLDHS 64
COG2248 COG2248
Predicted hydrolase, metallo-beta-lactamase superfamily [General function prediction only];
29-70 2.62e-04

Predicted hydrolase, metallo-beta-lactamase superfamily [General function prediction only];


Pssm-ID: 441849  Cd Length: 300  Bit Score: 41.08  E-value: 2.62e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1052486764  29 NELAKEVDVDAIKADYIFISHAHYDHILDVERIAKN--TGAKVL 70
Cdd:COG2248    53 EELREEIQEYAKKADIIIITHYHYDHHDPGEEIPKEiyRGKVLL 96
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 20-70 2.84e-04

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: 40.41  E-value: 2.84e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1052486764  20 ILFDPFITPNELAKEVDVDAIKADYIFISHAHYDHILDVERIAKNTGAKVL 70
Cdd:cd16322    25 VLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVY 75
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 9-55 4.86e-04

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: 39.75  E-value: 4.86e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1052486764   9 SCFSVYANEKHILFD--------PFITPNELAKEVDVDAIkaDYIFISHAHYDHI 55
Cdd:cd16295    13 SCYLLETGGKRILLDcglfqggkELEELNNEPFPFDPKEI--DAVILTHAHLDHS 65
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 6-101 6.01e-04

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


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 40.00  E-value: 6.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764   6 YGHSCFSVYANEKHILFD-------PFITPNELAKEVDVDAIKadYIFISHAHYDHILDVERIAKNTGAKVLGnfeiynw 78
Cdd:cd16288    20 SGLASYLITTPQGLILIDtglessaPMIKANIRKLGFKPSDIK--ILLNSHAHLDHAGGLAALKKLTGAKLMA------- 90

                          90       100
                  ....*....|....*....|...
gi 1052486764  79 llknGIENAHPINPGGKFDFDFG 101
Cdd:cd16288    91 ----SAEDAALLASGGKSDFHYG 109
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 3-56 1.25e-03

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: 38.63  E-value: 1.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052486764   3 ITYYGH-SCFSVYANEKHILFD------PFitPNELAKEVDVDAIkadYIFISHAHYDHIL 56
Cdd:cd07715    17 VRYGGNtSCVEVRAGGELLILDagtgirEL--GNELMKEGPPGEA---HLLLSHTHWDHIQ 72
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 4-70 1.37e-03

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


Pssm-ID: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 38.72  E-value: 1.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1052486764   4 TYY----GHSCFSVYANEKHILFD-------PFITPNELAKEVDVDAIKadYIFISHAHYDHILDVERIAKNTGAKVL 70
Cdd:cd16314    14 TWYvgtcGISALLVTSDAGHILIDggtdkaaPLIEANIRALGFRPEDVR--YIVSSHEHFDHAGGIARLQRATGAPVV 89
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 5-91 1.94e-03

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


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 38.23  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764   5 YY----GHSCFSVYANEKHILFD-------PFITPNELAKEVDVDAIKadYIFISHAHYDHILDVERIAKNTGAKVLGNf 73
Cdd:cd16309    15 YYvgtaGLGVFLITTPEGHILIDgampqstPLIKDNIKKLGFDVKDVK--YLLNTHAHFDHAGGLAELKKATGAQLVAS- 91

                          90
                  ....*....|....*...
gi 1052486764  74 EIYNWLLKNGIENAHPIN 91
Cdd:cd16309    92 AADKPLLESGYVGSGDTK 109
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 4-70 2.22e-03

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


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 38.10  E-value: 2.22e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1052486764   4 TYY----GHSCFSVYANEKHILFD-------PFITPNELAKEVDVDAIKadYIFISHAHYDHILDVERIAKNTGAKVL 70
Cdd:cd16290    14 TYYvgtgGLSAVLITSPQGLILIDgalpqsaPQIEANIRALGFRLEDVK--LILNSHAHFDHAGGIAALQRDSGATVA 89
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 44-88 3.38e-03

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


Pssm-ID: 293847  Cd Length: 239  Bit Score: 37.49  E-value: 3.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1052486764  44 YIFISHAHYDHILDVERIAKNTGAKVLGNFEIYNWLLKNGIENAH 88
Cdd:cd16289    63 LILHSHAHADHAGPLAALKRATGARVAANAESAVLLARGGSDDIH 107
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 20-70 4.45e-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: 37.10  E-value: 4.45e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1052486764  20 ILFDPFITPNElAKEVdVDAIKA-----DYIFISHAHYDHILDVERIAKN-TGAKVL 70
Cdd:cd07739    28 VLVDAQFTRAD-AERL-ADWIKAsgktlTTIYITHGHPDHYFGLEVLLEAfPDAKVV 82
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 38-140 8.36e-03

beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and RNase J2, involved in mRNA degradation in a wide range of organism. [Transcription, Degradation of RNA]


Pssm-ID: 273195 [Multi-domain]  Cd Length: 422  Bit Score: 36.56  E-value: 8.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052486764  38 DAIKAdyIFISHAHYDHILDVERIAKNtgakvLGNFEIY----------NWLLKNGIENAHP---INPGGKFDFDFG-TV 103
Cdd:TIGR00649  57 DKVKG--IFITHGHEDHIGAVPYLLHQ-----VGFFPIYgtpltialikSKIKEHGLNVRTDlleIHEGEPVEFGENtAI 129

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1052486764 104 KCVVAQH--PSSFmdgsyggiacGFVLTTSDGNFYYSGD 140
Cdd:TIGR00649 130 EFFRITHsiPDSV----------GFALHTPLGYIVYTGD 158
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH