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Conserved domains on  [gi|695842754|ref|WP_032756052|]
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MULTISPECIES: MBL fold metallo-hydrolase [Klebsiella]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 11454817)

MBL fold metallo-hydrolase similar to as Sus scrofa cytidine monophosphate-N-acetylneuraminic acid hydroxylase and Bacillus subtilis UPF0173 protein YddR; may be inactive as a hydrolase such as human inactive cytidine monophosphate-N-acetylneuraminic CMAHP

CATH:  3.60.15.30
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  11471246|17597585
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 1-227 2.93e-40

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


:

Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 138.51  E-value: 2.93e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754   1 MNITHIRNATQRIDYAGKRFLIDPMLADKGAwpgfpgtarselrnPLVELPFSRDKIIDVDAVIVTHTHDDHWDAAAIAA 80
Cdd:COG2220    4 MKITWLGHATFLIETGGKRILIDPVFSGRAS--------------PVNPLPLDPEDLPKIDAVLVTHDHYDHLDDATLRA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754  81 IPKTLPVFVQHEADAALLRSQGFQDLRLLSADS--EFAGVRLqKTTSGQHGSDRTyavpamAERLGEACGVVFRHPqEKT 158
Cdd:COG2220   70 LKRTGATVVAPLGVAAWLRAWGFPRVTELDWGEsvELGGLTV-TAVPARHSSGRP------DRNGGLWVGFVIETD-GKT 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695842754 159 LWLMGDTIWRDDIAADLLKLRPDVVVLNAGYAHvigfgpIIMGKEDLLNVHFALPEAKIMAIHLEAVNH 227
Cdd:COG2220  142 IYHAGDTGYFPEMKEIGERFPIDVALLPIGAYP------FTMGPEEAAEAARDLKPKVVIPIHYGTFPL 204
 
Name Accession Description Interval E-value
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 1-227 2.93e-40

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 138.51  E-value: 2.93e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754   1 MNITHIRNATQRIDYAGKRFLIDPMLADKGAwpgfpgtarselrnPLVELPFSRDKIIDVDAVIVTHTHDDHWDAAAIAA 80
Cdd:COG2220    4 MKITWLGHATFLIETGGKRILIDPVFSGRAS--------------PVNPLPLDPEDLPKIDAVLVTHDHYDHLDDATLRA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754  81 IPKTLPVFVQHEADAALLRSQGFQDLRLLSADS--EFAGVRLqKTTSGQHGSDRTyavpamAERLGEACGVVFRHPqEKT 158
Cdd:COG2220   70 LKRTGATVVAPLGVAAWLRAWGFPRVTELDWGEsvELGGLTV-TAVPARHSSGRP------DRNGGLWVGFVIETD-GKT 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695842754 159 LWLMGDTIWRDDIAADLLKLRPDVVVLNAGYAHvigfgpIIMGKEDLLNVHFALPEAKIMAIHLEAVNH 227
Cdd:COG2220  142 IYHAGDTGYFPEMKEIGERFPIDVALLPIGAYP------FTMGPEEAAEAARDLKPKVVIPIHYGTFPL 204
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 6-167 2.38e-09

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: 55.36  E-value: 2.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754   6 IRNATQRIDYAGKRFLIDPMLADKgAWP-GFPGTARselrnpLVELPFSRDKIIDVDAVIVTHTHDDHWDAAAIAAIPKT 84
Cdd:cd16283    2 IGHATFLIQIEGLNILTDPVFSER-ASPvSFGGPKR------LTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754  85 LPVFVQHeADAALLRSQGFQDLRLLS--ADSEFAGVRLQKTTSgQHGSDRTyaVPAMAERLGeaCGVVFRHPQEKtLWLM 162
Cdd:cd16283   75 PPYLVPL-GLKKWFLKKGITNVVELDwwQSTEIGGVRITFVPA-QHWSRRT--LFDTNESLW--GGWVIEGEGFR-IYFA 147


                 ....*
gi 695842754 163 GDTIW 167
Cdd:cd16283  148 GDTGY 152
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 1-165 9.85e-09

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 54.05  E-value: 9.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754   1 MNITHIRNATQRIDYAGKRFLIDPMLADKGAWPGFPGTarselrnplvelpfsrdkiIDVDAVIVTHTHDDHW-DAAAIA 79
Cdd:PRK00685   1 MKITWLGHSAFLIETGGKKILIDPFITGNPLADLKPED-------------------VKVDYILLTHGHGDHLgDTVEIA 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754  80 AIPKTlPVFVQHEAdAALLRSQGFQDLRLLS--ADSEFAGVRLqKTTSGQHGSDRTYAVPAMAerLGEACGVVFrHPQEK 157
Cdd:PRK00685  62 KRTGA-TVIANAEL-ANYLSEKGVEKTHPMNigGTVEFDGGKV-KLTPALHSSSFIDEDGITY--LGNPTGFVI-TFEGK 135


                 ....*...
gi 695842754 158 TLWLMGDT 165
Cdd:PRK00685 136 TIYHAGDT 143
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 3-208 3.16e-06

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: 46.04  E-value: 3.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754    3 ITHIRNATQRIDYAGKRFLIDPmladkgaWPGFPGTARSElrnplvelpfsrdkiIDVDAVIVTHTHDDHWDAAAIAAIP 82
Cdd:pfam13483   2 ITWLGHSSFLIEGGGARILTDP-------FRATVGYRPPP---------------VTADLVLISHGHDDHGHPETLPGNP 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754   83 KTLpvfvqHEADAAllrsqgfqdlrllsadsEFAGVRLQKTtsgqhgsdRTYAVPAMAERLGEACGVVFRHPQEKTLWLm 162
Cdd:pfam13483  60 HVL-----DGGGSY-----------------TVGGLEIRGV--------PTDHDRVGGRRRGGNSIFLFEQDGLTIYHL- 108

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 695842754  163 GDTIWRDDIAADLLKLRPDVVVLNAGyahvigfGPIIMGKEDLLNV 208
Cdd:pfam13483 109 GHLGHPLSDEQLAELGRVDVLLIPVG-------GPLTYGAEEALEL 147
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-100 1.65e-04

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: 41.39  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754    13 IDYAGKRFLIDPmladkgaWPGFPGTARSELRnplvelpfsRDKIIDVDAVIVTHTHDDH-WDAAAIAAIPKTlPVFVqH 91
Cdd:smart00849   5 VRDDGGAILIDT-------GPGEAEDLLAELK---------KLGPKKIDAIILTHGHPDHiGGLPELLEAPGA-PVYA-P 66


                   ....*....
gi 695842754    92 EADAALLRS 100
Cdd:smart00849  67 EGTAELLKD 75
 
Name Accession Description Interval E-value
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 1-227 2.93e-40

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 138.51  E-value: 2.93e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754   1 MNITHIRNATQRIDYAGKRFLIDPMLADKGAwpgfpgtarselrnPLVELPFSRDKIIDVDAVIVTHTHDDHWDAAAIAA 80
Cdd:COG2220    4 MKITWLGHATFLIETGGKRILIDPVFSGRAS--------------PVNPLPLDPEDLPKIDAVLVTHDHYDHLDDATLRA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754  81 IPKTLPVFVQHEADAALLRSQGFQDLRLLSADS--EFAGVRLqKTTSGQHGSDRTyavpamAERLGEACGVVFRHPqEKT 158
Cdd:COG2220   70 LKRTGATVVAPLGVAAWLRAWGFPRVTELDWGEsvELGGLTV-TAVPARHSSGRP------DRNGGLWVGFVIETD-GKT 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 695842754 159 LWLMGDTIWRDDIAADLLKLRPDVVVLNAGYAHvigfgpIIMGKEDLLNVHFALPEAKIMAIHLEAVNH 227
Cdd:COG2220  142 IYHAGDTGYFPEMKEIGERFPIDVALLPIGAYP------FTMGPEEAAEAARDLKPKVVIPIHYGTFPL 204
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 6-167 2.38e-09

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: 55.36  E-value: 2.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754   6 IRNATQRIDYAGKRFLIDPMLADKgAWP-GFPGTARselrnpLVELPFSRDKIIDVDAVIVTHTHDDHWDAAAIAAIPKT 84
Cdd:cd16283    2 IGHATFLIQIEGLNILTDPVFSER-ASPvSFGGPKR------LTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754  85 LPVFVQHeADAALLRSQGFQDLRLLS--ADSEFAGVRLQKTTSgQHGSDRTyaVPAMAERLGeaCGVVFRHPQEKtLWLM 162
Cdd:cd16283   75 PPYLVPL-GLKKWFLKKGITNVVELDwwQSTEIGGVRITFVPA-QHWSRRT--LFDTNESLW--GGWVIEGEGFR-IYFA 147


                 ....*
gi 695842754 163 GDTIW 167
Cdd:cd16283  148 GDTGY 152
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 1-165 9.85e-09

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 54.05  E-value: 9.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754   1 MNITHIRNATQRIDYAGKRFLIDPMLADKGAWPGFPGTarselrnplvelpfsrdkiIDVDAVIVTHTHDDHW-DAAAIA 79
Cdd:PRK00685   1 MKITWLGHSAFLIETGGKKILIDPFITGNPLADLKPED-------------------VKVDYILLTHGHGDHLgDTVEIA 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754  80 AIPKTlPVFVQHEAdAALLRSQGFQDLRLLS--ADSEFAGVRLqKTTSGQHGSDRTYAVPAMAerLGEACGVVFrHPQEK 157
Cdd:PRK00685  62 KRTGA-TVIANAEL-ANYLSEKGVEKTHPMNigGTVEFDGGKV-KLTPALHSSSFIDEDGITY--LGNPTGFVI-TFEGK 135


                 ....*...
gi 695842754 158 TLWLMGDT 165
Cdd:PRK00685 136 TIYHAGDT 143
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 3-208 3.16e-06

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: 46.04  E-value: 3.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754    3 ITHIRNATQRIDYAGKRFLIDPmladkgaWPGFPGTARSElrnplvelpfsrdkiIDVDAVIVTHTHDDHWDAAAIAAIP 82
Cdd:pfam13483   2 ITWLGHSSFLIEGGGARILTDP-------FRATVGYRPPP---------------VTADLVLISHGHDDHGHPETLPGNP 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754   83 KTLpvfvqHEADAAllrsqgfqdlrllsadsEFAGVRLQKTtsgqhgsdRTYAVPAMAERLGEACGVVFRHPQEKTLWLm 162
Cdd:pfam13483  60 HVL-----DGGGSY-----------------TVGGLEIRGV--------PTDHDRVGGRRRGGNSIFLFEQDGLTIYHL- 108

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 695842754  163 GDTIWRDDIAADLLKLRPDVVVLNAGyahvigfGPIIMGKEDLLNV 208
Cdd:pfam13483 109 GHLGHPLSDEQLAELGRVDVLLIPVG-------GPLTYGAEEALEL 147
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
13-180 3.02e-05

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 43.51  E-value: 3.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754   13 IDYAGKRFLIDPmladkgawpGFPGTARSELRNPLVELpfsrdKIIDVDAVIVTHTHDDH-WDAAAIAAIPKTlPVFVQH 91
Cdd:pfam00753  11 IEGGGGAVLIDT---------GGSAEAALLLLLAALGL-----GPKDIDAVILTHGHFDHiGGLGELAEATDV-PVIVVA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754   92 EADAALLRSQGFQDLRLLSA----DSEFAGVRLQKTTSGQHGSDRTYAVpaMAERLGEACGVVFRHPQEKTLwLMGDTIW 167
Cdd:pfam00753  76 EEARELLDEELGLAASRLGLpgppVVPLPPDVVLEEGDGILGGGLGLLV--THGPGHGPGHVVVYYGGGKVL-FTGDLLF 152

                         170
                  ....*....|...
gi 695842754  168 RDDIAADLLKLRP 180
Cdd:pfam00753 153 AGEIGRLDLPLGG 165
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 13-100 3.34e-05

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: 43.43  E-value: 3.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754  13 IDYAGKRFLIDPmladkgawpgfPGTARSELRNPLVELPfsrdkiIDVDAVIVTHTHDDH-WDAAAIAAIPKtLPVFVqH 91
Cdd:cd06262   16 SDEEGEAILIDP-----------GAGALEKILEAIEELG------LKIKAILLTHGHFDHiGGLAELKEAPG-APVYI-H 76


                 ....*....
gi 695842754  92 EADAALLRS 100
Cdd:cd06262   77 EADAELLED 85
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 13-83 4.36e-05

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: 43.22  E-value: 4.36e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695842754  13 IDYAGKRFLIDpmladKGAwpgFPGTARSELRNPLvELPFsrdKIIDVDAVIVTHTHDDHwdaaaIAAIPK 83
Cdd:cd16295   17 LETGGKRILLD-----CGL---FQGGKELEELNNE-PFPF---DPKEIDAVILTHAHLDH-----SGRLPL 70
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-100 1.65e-04

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: 41.39  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754    13 IDYAGKRFLIDPmladkgaWPGFPGTARSELRnplvelpfsRDKIIDVDAVIVTHTHDDH-WDAAAIAAIPKTlPVFVqH 91
Cdd:smart00849   5 VRDDGGAILIDT-------GPGEAEDLLAELK---------KLGPKKIDAIILTHGHPDHiGGLPELLEAPGA-PVYA-P 66


                   ....*....
gi 695842754    92 EADAALLRS 100
Cdd:smart00849  67 EGTAELLKD 75
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 50-99 2.88e-04

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 40.67  E-value: 2.88e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 695842754  50 LPFSRDKII-----------DVDAVIVTHTHDDHwdAAAIAAIPKT--LPVFVqHEADAALLR 99
Cdd:cd07721   29 LPGSAKRILkalrelglspkDIRRILLTHGHIDH--IGSLAALKEApgAPVYA-HEREAPYLE 88
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 60-184 2.97e-04

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 41.01  E-value: 2.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754  60 VDAVIVTHTHDDHWDAAaiAAIPKTLPVFVQHEADAALLRSQGFQDLRLLSADSE--FAGVRLQKTtsgqhgsDRTYAvP 137
Cdd:cd16282   53 VRYVVNTHYHGDHTLGN--AAFADAGAPIIAHENTREELAARGEAYLELMRRLGGdaMAGTELVLP-------DRTFD-D 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 695842754 138 AMAERLGeacGVVFR-------H---------PQEKTLWlMGDTIWRDDIAAD--------------LLKLRPDVVV 184
Cdd:cd16282  123 GLTLDLG---GRTVElihlgpaHtpgdlvvwlPEEGVLF-AGDLVFNGRIPFLpdgslagwiaaldrLLALDATVVV 195
PRK11709 PRK11709
putative L-ascorbate 6-phosphate lactonase; Provisional
 43-78 8.57e-04

putative L-ascorbate 6-phosphate lactonase; Provisional


Pssm-ID: 236958  Cd Length: 355  Bit Score: 39.98  E-value: 8.57e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 695842754  43 LRN-PLVELPFSrdkIIDVDAVIVTHTHDDHWD---AAAI 78
Cdd:PRK11709  95 LRTqPFVLDPFA---IREIDAVLATHDHSDHIDvnvAAAV 131
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 13-189 1.99e-03

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 38.72  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754  13 IDYAGKRFLIDPmladkgawpGfPGTARSELRNPLvelpfsrdKIIDVDAVIVTHTHDDHW---DAAAIAAIPKTLPVFV 89
Cdd:COG1235   40 VEADGTRLLIDA---------G-PDLREQLLRLGL--------DPSKIDAILLTHEHADHIaglDDLRPRYGPNPIPVYA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754  90 QHEADAALLRSQGFQ--------DLRLLSADSEF--AGVRLQkTTSGQHGSdrtyavpamaerlGEACGVVFRHpQEKTL 159
Cdd:COG1235  102 TPGTLEALERRFPYLfapypgklEFHEIEPGEPFeiGGLTVT-PFPVPHDA-------------GDPVGYRIED-GGKKL 166

                        170       180       190
                 ....*....|....*....|....*....|
gi 695842754 160 WLMGDTIWRDDIAADLLKlRPDVVVLNAGY 189
Cdd:COG1235  167 AYATDTGYIPEEVLELLR-GADLLILDATY 195
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 13-72 2.11e-03

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 39.01  E-value: 2.11e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754  13 IDYAGKRFLIDPMLadkgawpgFPGtarSELRNPLvELPFsrdKIIDVDAVIVTHTHDDH 72
Cdd:COG1236   19 LETGGTRILIDCGL--------FQG---GKERNWP-PFPF---RPSDVDAVVLTHAHLDH 63
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 44-102 6.88e-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: 36.82  E-value: 6.88e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 695842754  44 RNPLVELPFSRDKIIDVDAVIVTHTHDDHWdaAAIAAIPKTLPVFVqHEADAALLRSQG 102
Cdd:cd07732   60 RDPLLLGGLRSEEDPSVDAVLLSHAHLDHY--GLLNYLRPDIPVYM-GEATKRILKALL 115
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 13-72 8.03e-03

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293814  Cd Length: 249  Bit Score: 36.85  E-value: 8.03e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 695842754  13 IDYAGKRFLIDP-----MLADKGAwPGFPGTARSELRNPLVELPFSRDkiiDVDAVIVTHTHDDH 72
Cdd:cd07728   48 IQYQGKNYLIDAgigngKLTEKQK-RNFGVTEESSIEESLAELGLTPE---DIDYVLMTHLHFDH 108
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 19-221 9.49e-03

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: 36.13  E-value: 9.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754   19 RFLIDPmladkgaWPGFPGTArselrNPLVELPFSRDKiiDVDAVIVTHTHDDH---------WDAAAIAAIPKTLPVFV 89
Cdd:pfam12706   2 RILIDP-------GPDLRQQA-----LPALQPGRLRDD--PIDAVLLTHDHYDHlaglldlreGRPRPLYAPLGVLAHLR 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695842754   90 QHEADAALLRSQGFQdLRLLSADSEFA----GVRLqKTTSGQHGSDRtyavpAMAERLGEACGVVFRHPqEKTLWLMGDT 165
Cdd:pfam12706  68 RNFPYLFLLEHYGVR-VHEIDWGESFTvgdgGLTV-TATPARHGSPR-----GLDPNPGDTLGFRIEGP-GKRVYYAGDT 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 695842754  166 -IWRDDIAAdllKLRP-DVVVLNAGYAHVIGFGPII-MGKEDLLNVHFALPEAKIMAIH 221
Cdd:pfam12706 140 gYFPDEIGE---RLGGaDLLLLDGGAWRDDEMIHMGhMTPEEAVEAAADLGARRKVLIH 195
 
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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