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Conserved domains on  [gi|2535869693|ref|WP_292643024|]
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MBL fold metallo-hydrolase [Nitrososphaera sp.]

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; ...
 33-195 1.10e-08

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 pfam12706:

Pssm-ID: 451500 [Multi-domain]  Cd Length: 196  Bit Score: 54.62  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869693  33 LLVDAGNGVAASLKSGAGEHGYKETP-DAVLITSARKEHVAELASVIGSARG--YCTAECLGQLTAMPQLA----DKRSN 105
Cdd:pfam12706   3 ILIDPGPDLRQQALPALQPGRLRDDPiDAVLLTHDHYDHLAGLLDLREGRPRplYAPLGVLAHLRRNFPYLflleHYGVR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869693 106 FTTVQPGQAFSAGPF--SITPIAAN-----NAGDAPGLAGSaiYIIEGGGKKVIAGWDFLTLPGADEKLMWKPDLLVLGT 178
Cdd:pfam12706  83 VHEIDWGESFTVGDGglTVTATPARhgsprGLDPNPGDTLG--FRIEGPGKRVYYAGDTGYFPDEIGERLGGADLLLLDG 160

                         170
                  ....*....|....*....
gi 2535869693 179 ETYNEHPSTGMI--SVSEA 195
Cdd:pfam12706 161 GAWRDDEMIHMGhmTPEEA 179
 
Name Accession Description Interval E-value
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 33-195 1.10e-08

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: 54.62  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869693  33 LLVDAGNGVAASLKSGAGEHGYKETP-DAVLITSARKEHVAELASVIGSARG--YCTAECLGQLTAMPQLA----DKRSN 105
Cdd:pfam12706   3 ILIDPGPDLRQQALPALQPGRLRDDPiDAVLLTHDHYDHLAGLLDLREGRPRplYAPLGVLAHLRRNFPYLflleHYGVR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869693 106 FTTVQPGQAFSAGPF--SITPIAAN-----NAGDAPGLAGSaiYIIEGGGKKVIAGWDFLTLPGADEKLMWKPDLLVLGT 178
Cdd:pfam12706  83 VHEIDWGESFTVGDGglTVTATPARhgsprGLDPNPGDTLG--FRIEGPGKRVYYAGDTGYFPDEIGERLGGADLLLLDG 160

                         170
                  ....*....|....*....
gi 2535869693 179 ETYNEHPSTGMI--SVSEA 195
Cdd:pfam12706 161 GAWRDDEMIHMGhmTPEEA 179
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 59-151 1.23e-03

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


Pssm-ID: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 39.90  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869693  59 DAVLITSARKEHVAELASVIGSARGYCTAECLGQLTAMPQLADK----RSNFTTVQPGQAFSAGPFSITPIAANNagDAP 134
Cdd:cd07732    77 DAVLLSHAHLDHYGLLNYLRPDIPVYMGEATKRILKALLPFFGEgdpvPRNIRVFESGKSFTIGDFTVTPYLVDH--SAP 154

                          90
                  ....*....|....*..
gi 2535869693 135 GLAGsaiYIIEGGGKKV 151
Cdd:cd07732   155 GAYA---FLIEAPGKRI 168
 
Name Accession Description Interval E-value
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 33-195 1.10e-08

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: 54.62  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869693  33 LLVDAGNGVAASLKSGAGEHGYKETP-DAVLITSARKEHVAELASVIGSARG--YCTAECLGQLTAMPQLA----DKRSN 105
Cdd:pfam12706   3 ILIDPGPDLRQQALPALQPGRLRDDPiDAVLLTHDHYDHLAGLLDLREGRPRplYAPLGVLAHLRRNFPYLflleHYGVR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869693 106 FTTVQPGQAFSAGPF--SITPIAAN-----NAGDAPGLAGSaiYIIEGGGKKVIAGWDFLTLPGADEKLMWKPDLLVLGT 178
Cdd:pfam12706  83 VHEIDWGESFTVGDGglTVTATPARhgsprGLDPNPGDTLG--FRIEGPGKRVYYAGDTGYFPDEIGERLGGADLLLLDG 160

                         170
                  ....*....|....*....
gi 2535869693 179 ETYNEHPSTGMI--SVSEA 195
Cdd:pfam12706 161 GAWRDDEMIHMGhmTPEEA 179
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 59-151 1.23e-03

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


Pssm-ID: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 39.90  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535869693  59 DAVLITSARKEHVAELASVIGSARGYCTAECLGQLTAMPQLADK----RSNFTTVQPGQAFSAGPFSITPIAANNagDAP 134
Cdd:cd07732    77 DAVLLSHAHLDHYGLLNYLRPDIPVYMGEATKRILKALLPFFGEgdpvPRNIRVFESGKSFTIGDFTVTPYLVDH--SAP 154

                          90
                  ....*....|....*..
gi 2535869693 135 GLAGsaiYIIEGGGKKV 151
Cdd:cd07732   155 GAYA---FLIEAPGKRI 168
 
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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