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Conserved domains on  [gi|447052364|ref|WP_001129620|]
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MULTISPECIES: MBL fold metallo-hydrolase [Bacillus]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 581040)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme

Graphical summary

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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; ...
 60-236 5.62e-101

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 cd16283:

Pssm-ID: 451500  Cd Length: 181  Bit Score: 294.19  E-value: 5.62e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364  60 WIGHSTFLIQTNGLNILTDPVWANKLKLVP-----RLTEPGLSINELPKIDIVLLSHGHYDHLDFSTLRQLNDDILYLVP 134
Cdd:cd16283    1 WIGHATFLIQIEGLNILTDPVFSERASPVSfggpkRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPPYLVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364 135 IGLKKLFTRKKFNNVEEYKWWESTTIDDVSFHFVPAQHWTRRSLFDMNTSHWGGWIIKNDnmEETIYFCGDSGYFQGFKE 214
Cdd:cd16283   81 LGLKKWFLKKGITNVVELDWWQSTEIGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGE--GFRIYFAGDTGYFPGFRE 158

                        170       180
                 ....*....|....*....|...
gi 447052364 215 IGKRFS-IDVALMPIGAYEPEWF 236
Cdd:cd16283  159 IGRRFGpIDLALLPIGAYEPRWF 181
 
Name Accession Description Interval E-value
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 60-236 5.62e-101

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: 294.19  E-value: 5.62e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364  60 WIGHSTFLIQTNGLNILTDPVWANKLKLVP-----RLTEPGLSINELPKIDIVLLSHGHYDHLDFSTLRQLNDDILYLVP 134
Cdd:cd16283    1 WIGHATFLIQIEGLNILTDPVFSERASPVSfggpkRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPPYLVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364 135 IGLKKLFTRKKFNNVEEYKWWESTTIDDVSFHFVPAQHWTRRSLFDMNTSHWGGWIIKNDnmEETIYFCGDSGYFQGFKE 214
Cdd:cd16283   81 LGLKKWFLKKGITNVVELDWWQSTEIGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGE--GFRIYFAGDTGYFPGFRE 158

                        170       180
                 ....*....|....*....|...
gi 447052364 215 IGKRFS-IDVALMPIGAYEPEWF 236
Cdd:cd16283  159 IGRRFGpIDLALLPIGAYEPRWF 181
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 57-281 3.23e-86

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 258.31  E-value: 3.23e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364  57 TVTWIGHSTFLIQTNGLNILTDPVWANKLKLVPrltEPGLSINELPKIDIVLLSHGHYDHLDFSTLRQL-NDDILYLVPI 135
Cdd:COG2220    5 KITWLGHATFLIETGGKRILIDPVFSGRASPVN---PLPLDPEDLPKIDAVLVTHDHYDHLDDATLRALkRTGATVVAPL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364 136 GLKKLFTRKKFNNVEEYKWWESTTIDDVSFHFVPAQHWTRRslFDMNTSHWGGWIIKNDnmEETIYFCGDSGYFQGFKEI 215
Cdd:COG2220   82 GVAAWLRAWGFPRVTELDWGESVELGGLTVTAVPARHSSGR--PDRNGGLWVGFVIETD--GKTIYHAGDTGYFPEMKEI 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447052364 216 GKRFSIDVALMPIGAYEpewfmkiSHVSPEEAVQAYLDLNATHFIPMHYGAFALADETPREAITRL 281
Cdd:COG2220  158 GERFPIDVALLPIGAYP-------FTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDEDPLERFAAA 216
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 74-264 1.08e-41

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: 143.60  E-value: 1.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364   74 NILTDPVWaNKLKLVPRLTEPGLSINElpKIDIVLLSHGHYDHL-DFSTLRQLNDDILYL---VPIGLKKLF-----TRK 144
Cdd:pfam12706   2 RILIDPGP-DLRQQALPALQPGRLRDD--PIDAVLLTHDHYDHLaGLLDLREGRPRPLYAplgVLAHLRRNFpylflLEH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364  145 KFNNVEEYKWWESTTIDD--VSFHFVPAQHWTRRsLFDMNTSHWGGWIIKNDnmEETIYFCGDSGYFQGfkEIGKRFS-I 221
Cdd:pfam12706  79 YGVRVHEIDWGESFTVGDggLTVTATPARHGSPR-GLDPNPGDTLGFRIEGP--GKRVYYAGDTGYFPD--EIGERLGgA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 447052364  222 DVALMPIGAYEPEWFMKISHVSPEEAVQAYLDLNATHFIPMHY 264
Cdd:pfam12706 154 DLLLLDGGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 58-276 3.60e-27

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 106.05  E-value: 3.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364  58 VTWIGHSTFLIQTNGLNILTDPVwanklklvprltepgLSINEL-------PKIDIVLLSHGHYDHL-DFSTLRQLND-- 127
Cdd:PRK00685   3 ITWLGHSAFLIETGGKKILIDPF---------------ITGNPLadlkpedVKVDYILLTHGHGDHLgDTVEIAKRTGat 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364 128 -----DI-LYLVpiglkklftRKKFNNVEEYKWWESTTIDDVSFHFVPAQHWTrrSLFDMNTSHWG----GWIIKNDnmE 197
Cdd:PRK00685  68 vianaELaNYLS---------EKGVEKTHPMNIGGTVEFDGGKVKLTPALHSS--SFIDEDGITYLgnptGFVITFE--G 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364 198 ETIYFCGDSGYFQGFKEIGKRFSIDVALMPIGayepEWF-MkishvSPEEAVQAYLDLNATHFIPMHYGAFALADETPRE 276
Cdd:PRK00685 135 KTIYHAGDTGLFSDMKLIGELHKPDVALLPIG----DNFtM-----GPEDAALAVELIKPKIVIPMHYNTFPLIEQDPEK 205
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 64-244 6.90e-07

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: 48.70  E-value: 6.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364    64 STFLIQTNGLNILTDPVWANKLKLVPRLTEPGLSinelpKIDIVLLSHGHYDHldFSTLRqlnddilylvpiGLKKLFTR 143
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPK-----KIDAIILTHGHPDH--IGGLP------------ELLEAPGA 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364   144 KKFNNVEEYKWWESTTIDDVSFHFVPAQHWTRRSLFDMNTSHWGGWIIK--------NDNM-----EETIYFCGDSGYFQ 210
Cdd:smart00849  62 PVYAPEGTAELLKDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEvihtpghtPGSIvlylpEGKILFTGDLLFAG 141

                          170       180       190
                   ....*....|....*....|....*....|....
gi 447052364   211 GFKEIGKRFSIDVALMPIGAYEPEWFMKISHVSP 244
Cdd:smart00849 142 GDGRTLVDGGDAAASDALESLLKLLKLLPKLVVP 175
 
Name Accession Description Interval E-value
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 60-236 5.62e-101

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: 294.19  E-value: 5.62e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364  60 WIGHSTFLIQTNGLNILTDPVWANKLKLVP-----RLTEPGLSINELPKIDIVLLSHGHYDHLDFSTLRQLNDDILYLVP 134
Cdd:cd16283    1 WIGHATFLIQIEGLNILTDPVFSERASPVSfggpkRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPPYLVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364 135 IGLKKLFTRKKFNNVEEYKWWESTTIDDVSFHFVPAQHWTRRSLFDMNTSHWGGWIIKNDnmEETIYFCGDSGYFQGFKE 214
Cdd:cd16283   81 LGLKKWFLKKGITNVVELDWWQSTEIGGVRITFVPAQHWSRRTLFDTNESLWGGWVIEGE--GFRIYFAGDTGYFPGFRE 158

                        170       180
                 ....*....|....*....|...
gi 447052364 215 IGKRFS-IDVALMPIGAYEPEWF 236
Cdd:cd16283  159 IGRRFGpIDLALLPIGAYEPRWF 181
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 57-281 3.23e-86

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 258.31  E-value: 3.23e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364  57 TVTWIGHSTFLIQTNGLNILTDPVWANKLKLVPrltEPGLSINELPKIDIVLLSHGHYDHLDFSTLRQL-NDDILYLVPI 135
Cdd:COG2220    5 KITWLGHATFLIETGGKRILIDPVFSGRASPVN---PLPLDPEDLPKIDAVLVTHDHYDHLDDATLRALkRTGATVVAPL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364 136 GLKKLFTRKKFNNVEEYKWWESTTIDDVSFHFVPAQHWTRRslFDMNTSHWGGWIIKNDnmEETIYFCGDSGYFQGFKEI 215
Cdd:COG2220   82 GVAAWLRAWGFPRVTELDWGESVELGGLTVTAVPARHSSGR--PDRNGGLWVGFVIETD--GKTIYHAGDTGYFPEMKEI 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447052364 216 GKRFSIDVALMPIGAYEpewfmkiSHVSPEEAVQAYLDLNATHFIPMHYGAFALADETPREAITRL 281
Cdd:COG2220  158 GERFPIDVALLPIGAYP-------FTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDEDPLERFAAA 216
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 74-264 1.08e-41

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: 143.60  E-value: 1.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364   74 NILTDPVWaNKLKLVPRLTEPGLSINElpKIDIVLLSHGHYDHL-DFSTLRQLNDDILYL---VPIGLKKLF-----TRK 144
Cdd:pfam12706   2 RILIDPGP-DLRQQALPALQPGRLRDD--PIDAVLLTHDHYDHLaGLLDLREGRPRPLYAplgVLAHLRRNFpylflLEH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364  145 KFNNVEEYKWWESTTIDD--VSFHFVPAQHWTRRsLFDMNTSHWGGWIIKNDnmEETIYFCGDSGYFQGfkEIGKRFS-I 221
Cdd:pfam12706  79 YGVRVHEIDWGESFTVGDggLTVTATPARHGSPR-GLDPNPGDTLGFRIEGP--GKRVYYAGDTGYFPD--EIGERLGgA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 447052364  222 DVALMPIGAYEPEWFMKISHVSPEEAVQAYLDLNATHFIPMHY 264
Cdd:pfam12706 154 DLLLLDGGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 58-276 3.60e-27

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 106.05  E-value: 3.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364  58 VTWIGHSTFLIQTNGLNILTDPVwanklklvprltepgLSINEL-------PKIDIVLLSHGHYDHL-DFSTLRQLND-- 127
Cdd:PRK00685   3 ITWLGHSAFLIETGGKKILIDPF---------------ITGNPLadlkpedVKVDYILLTHGHGDHLgDTVEIAKRTGat 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364 128 -----DI-LYLVpiglkklftRKKFNNVEEYKWWESTTIDDVSFHFVPAQHWTrrSLFDMNTSHWG----GWIIKNDnmE 197
Cdd:PRK00685  68 vianaELaNYLS---------EKGVEKTHPMNIGGTVEFDGGKVKLTPALHSS--SFIDEDGITYLgnptGFVITFE--G 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364 198 ETIYFCGDSGYFQGFKEIGKRFSIDVALMPIGayepEWF-MkishvSPEEAVQAYLDLNATHFIPMHYGAFALADETPRE 276
Cdd:PRK00685 135 KTIYHAGDTGLFSDMKLIGELHKPDVALLPIG----DNFtM-----GPEDAALAVELIKPKIVIPMHYNTFPLIEQDPEK 205
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 57-263 1.05e-20

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: 86.88  E-value: 1.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364   57 TVTWIGHSTFLIQTNGLNILTDPVWANKLKLVPRLTepglsinelpkIDIVLLSHGHYDHLDFSTLRQlndDILYLVPig 136
Cdd:pfam13483   1 EITWLGHSSFLIEGGGARILTDPFRATVGYRPPPVT-----------ADLVLISHGHDDHGHPETLPG---NPHVLDG-- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364  137 lkklftrkkfnnveeykwWESTTIDDVSFHFVPAQHWTRR-SLFDMNTshwgGWIIKNDNMeeTIYFCGDSGY---FQGF 212
Cdd:pfam13483  65 ------------------GGSYTVGGLEIRGVPTDHDRVGgRRRGGNS----IFLFEQDGL--TIYHLGHLGHplsDEQL 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 447052364  213 KEIGkrfSIDVALMPIGAyePEWfmkishVSPEEAVQAYLDLNATHFIPMH 263
Cdd:pfam13483 121 AELG---RVDVLLIPVGG--PLT------YGAEEALELAKRLRPRVVIPMH 160
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
58-116 4.30e-07

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 49.67  E-value: 4.30e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 447052364   58 VTWIGHSTFLIQTNGLNILTDPVWANKLKLVPRLTEPGLSINelpKIDIVLLSHGHYDH 116
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLGPK---DIDAVILTHGHFDH 56
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
62-272 5.17e-07

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 49.81  E-value: 5.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364  62 GHSTFLIQTNGLNILTDP---VwanklklVPRLTEPGLSINelpKIDIVLLSHGHYDH-LDFSTLRQL-----NDDILYL 132
Cdd:COG1234   18 ATSSYLLEAGGERLLIDCgegT-------QRQLLRAGLDPR---DIDAIFITHLHGDHiAGLPGLLSTrslagREKPLTI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364 133 V-PIGLKKLF--------TRKKFN-NVEEYKWWESTTIDDVSFHFVPAQHwTRRSLfdmntshwgGWIIKNDNMeeTIYF 202
Cdd:COG1234   88 YgPPGTKEFLeallkasgTDLDFPlEFHEIEPGEVFEIGGFTVTAFPLDH-PVPAY---------GYRFEEPGR--SLVY 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447052364 203 CGDSGYFQGFKEIGKrfsiDVALMPIGAY----EPEWFMKISHVSPEEAVQAYLDLNA-----THFIPMHYGAFALADE 272
Cdd:COG1234  156 SGDTRPCEALVELAK----GADLLIHEATfldeEAELAKETGHSTAKEAAELAAEAGVkrlvlTHFSPRYDDPEELLAE 230
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 64-244 6.90e-07

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: 48.70  E-value: 6.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364    64 STFLIQTNGLNILTDPVWANKLKLVPRLTEPGLSinelpKIDIVLLSHGHYDHldFSTLRqlnddilylvpiGLKKLFTR 143
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPK-----KIDAIILTHGHPDH--IGGLP------------ELLEAPGA 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364   144 KKFNNVEEYKWWESTTIDDVSFHFVPAQHWTRRSLFDMNTSHWGGWIIK--------NDNM-----EETIYFCGDSGYFQ 210
Cdd:smart00849  62 PVYAPEGTAELLKDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEvihtpghtPGSIvlylpEGKILFTGDLLFAG 141

                          170       180       190
                   ....*....|....*....|....*....|....
gi 447052364   211 GFKEIGKRFSIDVALMPIGAYEPEWFMKISHVSP 244
Cdd:smart00849 142 GDGRTLVDGGDAAASDALESLLKLLKLLPKLVVP 175
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 64-116 9.95e-07

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


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 48.35  E-value: 9.95e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 447052364  64 STFLIQTNGLNILTDP--VWaNKLKLVPRLTEPGLSINElpkIDIVLLSHGHYDH 116
Cdd:cd07711   23 TVTLIKDGGKNILVDTgtPW-DRDLLLKALAEHGLSPED---IDYVVLTHGHPDH 73
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 66-168 4.10e-06

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: 47.62  E-value: 4.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364  66 FLIQTNGLNILTD----PVWANKLKLvprltepgLSINeLPKIDIVLLSHGHYDHLD-FSTLRQLNDDI-LYLVPIGLKK 139
Cdd:cd07713   23 LLIETEGKKILFDtgqsGVLLHNAKK--------LGID-LSDIDAVVLSHGHYDHTGgLKALLELNPKApVYAHPDAFEP 93

                         90       100
                 ....*....|....*....|....*....
gi 447052364 140 LFTRKKFNNVEEYKWWESTTIDDVSFHFV 168
Cdd:cd07713   94 RYSKRGGGKKGIGIGREELEKAGARLVLV 122
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 103-263 5.09e-06

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 47.20  E-value: 5.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364 103 KIDIVLLSHGHYDH---LDF----------------STLRQLNDDILYLVPIGLKKLftrkKFNNVEEYkwwESTTIDDV 163
Cdd:COG1235   68 KIDAILLTHEHADHiagLDDlrprygpnpipvyatpGTLEALERRFPYLFAPYPGKL----EFHEIEPG---EPFEIGGL 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364 164 SFHFVPAQHWTRRSLfdmntshwgGWIIKNDNmeETIYFCGDSGYFqgFKEIGKRFS-IDVALmpIGA--YEPEWfmkiS 240
Cdd:COG1235  141 TVTPFPVPHDAGDPV---------GYRIEDGG--KKLAYATDTGYI--PEEVLELLRgADLLI--LDAtyDDPEP----G 201

                        170       180
                 ....*....|....*....|...
gi 447052364 241 HVSPEEAVQAYLDLNATHFIPMH 263
Cdd:COG1235  202 HLSNEEALELLARLGPKRLVLTH 224
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 66-116 5.15e-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: 43.72  E-value: 5.15e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 447052364  66 FLIQTNGLNILTDP-----VWANKLKLVPRltepglsinelpKIDIVLLSHGHYDH 116
Cdd:cd07741   23 IWIELNGKNIHIDPgpgalVRMCRPKLDPT------------KLDAIILSHRHLDH 66
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 62-217 7.79e-05

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: 42.64  E-value: 7.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364  62 GHSTFLIQTNGLNILTD---PVwanklklVPRLTEPGLSINelpKIDIVLLSHGHYDH-LDFSTL-----RQLNDDILYL 132
Cdd:cd16272   16 NTSSYLLETGGTRILLDcgeGT-------VYRLLKAGVDPD---KLDAIFLSHFHLDHiGGLPTLlfarrYGGRKKPLTI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364 133 -VPIGLKKLFTR-KKFNNVEEYKWW-----------ESTTIDDVSFHFVPAQHWTRRSlfdmntshwgGWIIKNDNmeET 199
Cdd:cd16272   86 yGPKGIKEFLEKlLNFPVEILPLGFpleieeleeggEVLELGDLKVEAFPVKHSVESL----------GYRIEAEG--KS 153

                        170
                 ....*....|....*...
gi 447052364 200 IYFCGDSGYFQGFKEIGK 217
Cdd:cd16272  154 IVYSGDTGPCENLVELAK 171
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 67-116 1.98e-04

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: 41.35  E-value: 1.98e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 447052364  67 LIQTNGLNILTD--PVWAN-KLKLVPRLTEPGLSinelpKIDIVLLSHGHYDH 116
Cdd:cd07731   14 LIQTPGKTILIDtgPRDSFgEDVVVPYLKARGIK-----KLDYLILTHPDADH 61
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
66-116 3.28e-04

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 41.79  E-value: 3.28e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 447052364  66 FLIQTNGLNILTD----PVWANKLKLvprltepgLSINeLPKIDIVLLSHGHYDH 116
Cdd:COG1237   25 ALIETEGKRILFDtgqsDVLLKNAEK--------LGID-LSDIDAVVLSHGHYDH 70
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 56-116 1.61e-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: 39.29  E-value: 1.61e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447052364  56 TTVTWIGHSTFLIQTNGLNILTDPVWANKL--KLVPRLTEPGLsinelpKIDIVLLSHGHYDH 116
Cdd:COG0491    8 TPGAGLGVNSYLIVGGDGAVLIDTGLGPADaeALLAALAALGL------DIKAVLLTHLHPDH 64
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 64-123 3.31e-03

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: 37.81  E-value: 3.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447052364  64 STFLIQTNGLNILTDP---VWANKLKLVPrltepglsineLPKIDIVLLSHGHYDH-LDFSTLR 123
Cdd:cd07716   19 SGYLLEADGFRILLDCgsgVLSRLQRYID-----------PEDLDAVVLSHLHPDHcADLGVLQ 71
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 67-172 4.73e-03

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: 37.45  E-value: 4.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447052364  67 LIQTNGLNILTDpvwanklklvprlTEPGLSI----NELPKIDIVLLSHGHYDHL----DfstLRQLNDDILYLVPI--- 135
Cdd:cd16279   39 LIETGGKNILID-------------TGPDFRQqalrAGIRKLDAVLLTHAHADHIhgldD---LRPFNRLQQRPIPVyas 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 447052364 136 -----GLKKLFTRKKFNNVEEYKWW---------ESTTIDDVSFHFVPAQH 172
Cdd:cd16279  103 eetldDLKRRFPYFFAATGGGGVPKldlhiiepdEPFTIGGLEITPLPVLH 153
 
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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