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Conserved domains on  [gi|490290950|ref|WP_004186555|]
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MULTISPECIES: phosphonate metabolism protein PhnP [Klebsiella]

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; ...
 13-249 6.62e-134

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 TIGR03307:

Pssm-ID: 451500  Cd Length: 238  Bit Score: 377.14  E-value: 6.62e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950   13 AQLVPVFGCDCAACRRARREENHRRRPCSGVVTFNSAVTLLDAGRPDLMEHHPAGSFQQVLLTHYHLDHVQGLFPLRWGV 92
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950   93 GASIPVYGPPDDAGCDDLLKHPGLLDFSHTVTPFVMFNLQGLRVTPLPLNHSKLTFGYLLESAHSRLAWLSDTAGLPDKS 172
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLLETDGQRVAYLTDTAGLPPDT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490290950  173 LKFLLNNRPQAMIIDCSHEPRAQTPRNHNDLNTVRSLNQVIGCPRVILTHISHQFDVWMMDNP-LPTGFEAGYDGMEI 249
Cdd:TIGR03307 161 EAFLKNHPLDVLILDCSHPPQSDAPRNHNDLTRALAINEQLRPKQVILTHISHQLDAWLMENPdLPSGVAVGYDGQTL 238
 
Name Accession Description Interval E-value
PhnP TIGR03307
phosphonate metabolism protein PhnP; This family of proteins found in operons encoding ...
 13-249 6.62e-134

phosphonate metabolism protein PhnP; This family of proteins found in operons encoding phosphonate C-P lyase systems as is observed in E. coli and is a member of the metallo-beta-lactamase superfamily (pfam00753). As defined by this model, all instances of this protein are associated with the C-P lyase, but not all genomes containing the C-P lyase system contain phnP.


Pssm-ID: 163212  Cd Length: 238  Bit Score: 377.14  E-value: 6.62e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950   13 AQLVPVFGCDCAACRRARREENHRRRPCSGVVTFNSAVTLLDAGRPDLMEHHPAGSFQQVLLTHYHLDHVQGLFPLRWGV 92
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950   93 GASIPVYGPPDDAGCDDLLKHPGLLDFSHTVTPFVMFNLQGLRVTPLPLNHSKLTFGYLLESAHSRLAWLSDTAGLPDKS 172
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLLETDGQRVAYLTDTAGLPPDT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490290950  173 LKFLLNNRPQAMIIDCSHEPRAQTPRNHNDLNTVRSLNQVIGCPRVILTHISHQFDVWMMDNP-LPTGFEAGYDGMEI 249
Cdd:TIGR03307 161 EAFLKNHPLDVLILDCSHPPQSDAPRNHNDLTRALAINEQLRPKQVILTHISHQLDAWLMENPdLPSGVAVGYDGQTL 238
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 3-188 1.12e-104

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. 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: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 301.08  E-value: 1.12e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950   3 LTLRLTGTGGAQLVPVFGCDCAACRRARREENHRRRPCSGVVTFNSAVTLLDAGRPDLMEHHPAGSFQQVLLTHYHLDHV 82
Cdd:cd07736    1 MKLTFLGTGDAGGVPVYGCDCSACQRARQDPSYRRRPCSALIEVDGERILLDAGLTDLAERFPPGSIDAILLTHFHMDHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  83 QGLFPLRWGVGASIPVYGPPDDAGCDDLLKHPGLLDFSHTVTPFVMFNLQGLRVTPLPLNHSKLTFGYLLESAHSRLAWL 162
Cdd:cd07736   81 QGLFHLRWGVGDPIPVYGPPDPQGCADLFKHPGILDFQPLVAPFQSFELGGLKITPLPLNHSKPTFGYLLESGGKRLAYL 160

                        170       180
                 ....*....|....*....|....*.
gi 490290950 163 SDTAGLPDKSLKFLLNNRPQAMIIDC 188
Cdd:cd07736  161 TDTLGLPEETLEFLKQQQPDVLVLDC 186
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 3-251 4.27e-52

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 169.69  E-value: 4.27e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950   3 LTLRLTGTGGAQLVPVFGCDCAACRRARREenHRRRPCSGVVTFNSAVTLLDAGrPDLME-----HHPAGSFQQVLLTHY 77
Cdd:COG1235    1 MKVTFLGSGSSGGVPQIGCDCPVCASTDPR--YGRTRSSILVEADGTRLLIDAG-PDLREqllrlGLDPSKIDAILLTHE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  78 HLDHVQGLFPLRWG-VGASIPVYGPPDDagCDDLLK--------HPGLLDFsHTVTPFVMFNLQGLRVTPLPLNHSKL-T 147
Cdd:COG1235   78 HADHIAGLDDLRPRyGPNPIPVYATPGT--LEALERrfpylfapYPGKLEF-HEIEPGEPFEIGGLTVTPFPVPHDAGdP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950 148 FGYLLESAHSRLAWLSDTAGLPDKSLKFLLNnrPQAMIIDCSHEPRAQtprNHNDLNTVRSLNQVIGCPRVILTHIS--- 224
Cdd:COG1235  155 VGYRIEDGGKKLAYATDTGYIPEEVLELLRG--ADLLILDATYDDPEP---GHLSNEEALELLARLGPKRLVLTHLSpdn 229

                        250       260       270
                 ....*....|....*....|....*....|
gi 490290950 225 --HQFDVWMMDN-PLPTGFEAGYDGMEIAL 251
Cdd:COG1235  230 ndHELDYDELEAaLLPAGVEVAYDGMEIEL 259
PRK02113 PRK02113
MBL fold metallo-hydrolase;
3-251 3.37e-22

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 91.77  E-value: 3.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950   3 LTLRLTGTGGAQLVPVFGCDCAACRRARREENHRRrpCSGVVTFNSAVTLLDAGrPDL---MEHHPAGSFQQVLLTHYHL 79
Cdd:PRK02113   1 MKIRILGSGTSTGVPEIGCTCPVCTSKDPRDNRLR--TSALVETEGARILIDCG-PDFreqMLRLPFGKIDAVLITHEHY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  80 DHVQGLFPLR-WGVGASIPVYGPPDDAG--------CDDLLKHPGLLDFS-HTVTPFVMFNLQGLRVTPLPLNHSKLT-F 148
Cdd:PRK02113  78 DHVGGLDDLRpFCRFGEVPIYAEQYVAErlrsrmpyCFVEHSYPGVPNIPlREIEPDRPFLVNHTEVTPLRVMHGKLPiL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950 149 GYLLesahSRLAWLSDTAGLPDKSLKFLLNNRpqAMIIDCShepRAQTPRNHNDLNTVRSLNQVIGCPRVILTHISHQFD 228
Cdd:PRK02113 158 GYRI----GKMAYITDMLTMPEEEYEQLQGID--VLVMNAL---RIAPHPTHQSLEEALENIKRIGAKETYLIHMSHHIG 228

                        250       260
                 ....*....|....*....|....
gi 490290950 229 VWM-MDNPLPTGFEAGYDGMEIAL 251
Cdd:PRK02113 229 LHAdVEKELPPHVHFAYDGLEIIF 252
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 52-223 2.72e-10

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: 58.09  E-value: 2.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950   52 LLDAGrPDLME-----HHPAGSFQQ----VLLTHYHLDHVQGLFPLRWGVGAsiPVYGPPddaGCDDLLKHPGLLDFS-- 120
Cdd:pfam12706   4 LIDPG-PDLRQqalpaLQPGRLRDDpidaVLLTHDHYDHLAGLLDLREGRPR--PLYAPL---GVLAHLRRNFPYLFLle 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  121 ------HTVTPF--VMFNLQGLRVTPLPLNHSK---------LTFGYLLESAHSRLAWLSDTAGLPDKSLKFLlnNRPQA 183
Cdd:pfam12706  78 hygvrvHEIDWGesFTVGDGGLTVTATPARHGSprgldpnpgDTLGFRIEGPGKRVYYAGDTGYFPDEIGERL--GGADL 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 490290950  184 MIID-CSHEPRAQTPRNHNDLN-TVRSLNQvIGCPRVILTHI 223
Cdd:pfam12706 156 LLLDgGAWRDDEMIHMGHMTPEeAVEAAAD-LGARRKVLIHI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 41-117 1.48e-03

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: 38.30  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950    41 SGVVTFNSAVTLLDAGRPDLMEHHPA------GSFQQVLLTHYHLDHVQGLFPLRWGVGAsiPVYGPPDDAgcdDLLKHP 114
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDLLAElkklgpKKIDAIILTHGHPDHIGGLPELLEAPGA--PVYAPEGTA---ELLKDL 76


                   ...
gi 490290950   115 GLL 117
Cdd:smart00849  77 LAL 79
 
Name Accession Description Interval E-value
PhnP TIGR03307
phosphonate metabolism protein PhnP; This family of proteins found in operons encoding ...
 13-249 6.62e-134

phosphonate metabolism protein PhnP; This family of proteins found in operons encoding phosphonate C-P lyase systems as is observed in E. coli and is a member of the metallo-beta-lactamase superfamily (pfam00753). As defined by this model, all instances of this protein are associated with the C-P lyase, but not all genomes containing the C-P lyase system contain phnP.


Pssm-ID: 163212  Cd Length: 238  Bit Score: 377.14  E-value: 6.62e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950   13 AQLVPVFGCDCAACRRARREENHRRRPCSGVVTFNSAVTLLDAGRPDLMEHHPAGSFQQVLLTHYHLDHVQGLFPLRWGV 92
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950   93 GASIPVYGPPDDAGCDDLLKHPGLLDFSHTVTPFVMFNLQGLRVTPLPLNHSKLTFGYLLESAHSRLAWLSDTAGLPDKS 172
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLLETDGQRVAYLTDTAGLPPDT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490290950  173 LKFLLNNRPQAMIIDCSHEPRAQTPRNHNDLNTVRSLNQVIGCPRVILTHISHQFDVWMMDNP-LPTGFEAGYDGMEI 249
Cdd:TIGR03307 161 EAFLKNHPLDVLILDCSHPPQSDAPRNHNDLTRALAINEQLRPKQVILTHISHQLDAWLMENPdLPSGVAVGYDGQTL 238
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 3-188 1.12e-104

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. 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: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 301.08  E-value: 1.12e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950   3 LTLRLTGTGGAQLVPVFGCDCAACRRARREENHRRRPCSGVVTFNSAVTLLDAGRPDLMEHHPAGSFQQVLLTHYHLDHV 82
Cdd:cd07736    1 MKLTFLGTGDAGGVPVYGCDCSACQRARQDPSYRRRPCSALIEVDGERILLDAGLTDLAERFPPGSIDAILLTHFHMDHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  83 QGLFPLRWGVGASIPVYGPPDDAGCDDLLKHPGLLDFSHTVTPFVMFNLQGLRVTPLPLNHSKLTFGYLLESAHSRLAWL 162
Cdd:cd07736   81 QGLFHLRWGVGDPIPVYGPPDPQGCADLFKHPGILDFQPLVAPFQSFELGGLKITPLPLNHSKPTFGYLLESGGKRLAYL 160

                        170       180
                 ....*....|....*....|....*.
gi 490290950 163 SDTAGLPDKSLKFLLNNRPQAMIIDC 188
Cdd:cd07736  161 TDTLGLPEETLEFLKQQQPDVLVLDC 186
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 3-251 4.27e-52

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 169.69  E-value: 4.27e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950   3 LTLRLTGTGGAQLVPVFGCDCAACRRARREenHRRRPCSGVVTFNSAVTLLDAGrPDLME-----HHPAGSFQQVLLTHY 77
Cdd:COG1235    1 MKVTFLGSGSSGGVPQIGCDCPVCASTDPR--YGRTRSSILVEADGTRLLIDAG-PDLREqllrlGLDPSKIDAILLTHE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  78 HLDHVQGLFPLRWG-VGASIPVYGPPDDagCDDLLK--------HPGLLDFsHTVTPFVMFNLQGLRVTPLPLNHSKL-T 147
Cdd:COG1235   78 HADHIAGLDDLRPRyGPNPIPVYATPGT--LEALERrfpylfapYPGKLEF-HEIEPGEPFEIGGLTVTPFPVPHDAGdP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950 148 FGYLLESAHSRLAWLSDTAGLPDKSLKFLLNnrPQAMIIDCSHEPRAQtprNHNDLNTVRSLNQVIGCPRVILTHIS--- 224
Cdd:COG1235  155 VGYRIEDGGKKLAYATDTGYIPEEVLELLRG--ADLLILDATYDDPEP---GHLSNEEALELLARLGPKRLVLTHLSpdn 229

                        250       260       270
                 ....*....|....*....|....*....|
gi 490290950 225 --HQFDVWMMDN-PLPTGFEAGYDGMEIAL 251
Cdd:COG1235  230 ndHELDYDELEAaLLPAGVEVAYDGMEIEL 259
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 3-188 2.41e-28

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: 106.40  E-value: 2.41e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950   3 LTLRLTGTGGAQLVPVFGCDCAACRRArREENHRRRpCSGVVTFNSAVTLLDAGrPDL---MEHHPAGSFQQVLLTHYHL 79
Cdd:cd16279    1 MKLTFLGTGTSSGVPVIGCDCGVCDSS-DPKNRRLR-SSILIETGGKNILIDTG-PDFrqqALRAGIRKLDAVLLTHAHA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  80 DHVQG---LFPLRWGVGASIPVYGPP----------DDAGCDDLLKHPGLLDFsHTVTPFVMFNLQGLRVTPLPLNHSKL 146
Cdd:cd16279   78 DHIHGlddLRPFNRLQQRPIPVYASEetlddlkrrfPYFFAATGGGGVPKLDL-HIIEPDEPFTIGGLEITPLPVLHGKL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 490290950 147 -TFGYLLEsahsRLAWLSDTAGLPDKSLKFLLNnrPQAMIIDC 188
Cdd:cd16279  157 pSLGFRFG----DFAYLTDVSEIPEESLEKLRG--LDVLILDA 193
PRK02113 PRK02113
MBL fold metallo-hydrolase;
3-251 3.37e-22

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 91.77  E-value: 3.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950   3 LTLRLTGTGGAQLVPVFGCDCAACRRARREENHRRrpCSGVVTFNSAVTLLDAGrPDL---MEHHPAGSFQQVLLTHYHL 79
Cdd:PRK02113   1 MKIRILGSGTSTGVPEIGCTCPVCTSKDPRDNRLR--TSALVETEGARILIDCG-PDFreqMLRLPFGKIDAVLITHEHY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  80 DHVQGLFPLR-WGVGASIPVYGPPDDAG--------CDDLLKHPGLLDFS-HTVTPFVMFNLQGLRVTPLPLNHSKLT-F 148
Cdd:PRK02113  78 DHVGGLDDLRpFCRFGEVPIYAEQYVAErlrsrmpyCFVEHSYPGVPNIPlREIEPDRPFLVNHTEVTPLRVMHGKLPiL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950 149 GYLLesahSRLAWLSDTAGLPDKSLKFLLNNRpqAMIIDCShepRAQTPRNHNDLNTVRSLNQVIGCPRVILTHISHQFD 228
Cdd:PRK02113 158 GYRI----GKMAYITDMLTMPEEEYEQLQGID--VLVMNAL---RIAPHPTHQSLEEALENIKRIGAKETYLIHMSHHIG 228

                        250       260
                 ....*....|....*....|....
gi 490290950 229 VWM-MDNPLPTGFEAGYDGMEIAL 251
Cdd:PRK02113 229 LHAdVEKELPPHVHFAYDGLEIIF 252
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
36-228 3.56e-18

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 81.01  E-value: 3.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  36 RRRPCSGV-VTFNSAVTLLDAGR--PDLMEHHPAgSFQQ---VLLTHYHLDHVQGLFPL---RW--GVGASIPVYGPPdd 104
Cdd:COG1234   15 PGRATSSYlLEAGGERLLIDCGEgtQRQLLRAGL-DPRDidaIFITHLHGDHIAGLPGLlstRSlaGREKPLTIYGPP-- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950 105 aGCDDLLKH-----PGLLDFS---HTVTPFVMFNLQGLRVTPLPLNHSKLTFGYLLESAHSRLAWLSDTAglPDKSLKFL 176
Cdd:COG1234   92 -GTKEFLEAllkasGTDLDFPlefHEIEPGEVFEIGGFTVTAFPLDHPVPAYGYRFEEPGRSLVYSGDTR--PCEALVEL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490290950 177 LNNrPQAMIIDCSH-EPRAQTPRNHNDLnTVRSLNQVI---GCPRVILTHISHQFD 228
Cdd:COG1234  169 AKG-ADLLIHEATFlDEEAELAKETGHS-TAKEAAELAaeaGVKRLVLTHFSPRYD 222
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 34-166 9.28e-12

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: 61.90  E-value: 9.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  34 NHRRRPCSGVVTFNSAVTLLDAGR---PDLMEHH-PAGSFQQVLLTHYHLDHVQGLFPLRW-----GVGASIPVYGPPDD 104
Cdd:cd16272   12 SLTRNTSSYLLETGGTRILLDCGEgtvYRLLKAGvDPDKLDAIFLSHFHLDHIGGLPTLLFarrygGRKKPLTIYGPKGI 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950 105 A-------GCDDLLKHPGL-LDFSHTVTPFVMFNLQGLRVTPLPLNHSKLTFGYLLESAHSRLAWLSDTA 166
Cdd:cd16272   92 KeflekllNFPVEILPLGFpLEIEELEEGGEVLELGDLKVEAFPVKHSVESLGYRIEAEGKSIVYSGDTG 161
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 52-188 1.26e-11

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: 62.13  E-value: 1.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  52 LLDAG---RP---DLMEHHPAGSFQqVLLTHYHLDHVQGL--F-PLrWGVGASIPVYGPPDDAGC-----DDLLKHP--- 114
Cdd:cd07715   36 ILDAGtgiRElgnELMKEGPPGEAH-LLLSHTHWDHIQGFpfFaPA-YDPGNRIHIYGPHKDGGSleevlRRQMSPPyfp 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950 115 -GLLDFS-----HTVTPFVMFNLQGLRVTPLPLNHSKLTFGYLLESAHSRLAWLSDT-----AGLPDKSLKFLLNNrpqA 183
Cdd:cd07715  114 vPLEELLaaiefHDLEPGEPFSIGGVTVTTIPLNHPGGALGYRIEEDGKSVVYATDTehypdDGESDEALLEFARG---A 190


                 ....*..
gi 490290950 184 --MIIDC 188
Cdd:cd07715  191 dlLIHDA 197
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 52-223 2.72e-10

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: 58.09  E-value: 2.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950   52 LLDAGrPDLME-----HHPAGSFQQ----VLLTHYHLDHVQGLFPLRWGVGAsiPVYGPPddaGCDDLLKHPGLLDFS-- 120
Cdd:pfam12706   4 LIDPG-PDLRQqalpaLQPGRLRDDpidaVLLTHDHYDHLAGLLDLREGRPR--PLYAPL---GVLAHLRRNFPYLFLle 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  121 ------HTVTPF--VMFNLQGLRVTPLPLNHSK---------LTFGYLLESAHSRLAWLSDTAGLPDKSLKFLlnNRPQA 183
Cdd:pfam12706  78 hygvrvHEIDWGesFTVGDGGLTVTATPARHGSprgldpnpgDTLGFRIEGPGKRVYYAGDTGYFPDEIGERL--GGADL 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 490290950  184 MIID-CSHEPRAQTPRNHNDLN-TVRSLNQvIGCPRVILTHI 223
Cdd:pfam12706 156 LLLDgGAWRDDEMIHMGHMTPEeAVEAAAD-LGARRKVLIHI 196
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 36-166 8.61e-10

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


Pssm-ID: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 57.46  E-value: 8.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  36 RRRPCSG-VVTFNSAVTLLDAG----RPdLMEHHpaGSFQQV---LLTHYHLDHVQGLFPL-----RWGVGASIPVYGPP 102
Cdd:cd07717   13 PERNLSSiALRLEGELWLFDCGegtqRQ-LLRAG--LSPSKIdriFITHLHGDHILGLPGLlstmsLLGRTEPLTIYGPK 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490290950 103 ddaGCDDLLKHpgLLDFSHTVTPF------------VMFNLQGLRVTPLPLNHSKLTFGYLLESAHSrLAWLSDTA 166
Cdd:cd07717   90 ---GLKEFLET--LLRLSASRLPYpievhelepdpgLVFEDDGFTVTAFPLDHRVPCFGYRFEEGRK-IAYLGDTR 159
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 38-166 8.76e-10

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: 56.30  E-value: 8.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  38 RPCSG-VVTFNSAVTLLDAG-----RpdLMEHHPAGSFQQVLLTHYHLDHVQGLFPLR--------WGVGASIPVYGPPD 103
Cdd:cd07716   16 GACSGyLLEADGFRILLDCGsgvlsR--LQRYIDPEDLDAVVLSHLHPDHCADLGVLQyarryhprGARKPPLPLYGPAG 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490290950 104 DAGCDDLLK-HPGLLDFsHTVTPFVMFNLQGLRVTPLPLNHSKLTFGYLLESAHSRLAWLSDTA 166
Cdd:cd07716   94 PAERLAALYgLEDVFDF-HPIEPGEPLEIGPFTITFFRTVHPVPCYAMRIEDGGKVLVYTGDTG 156
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 4-156 4.46e-09

Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 54.44  E-value: 4.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950   4 TLRLTGTGGAQLVPvfgcdcaacrrarreenHRRRPCSGVVTfNSAVTLLDAGRpdlmehhpaGSFQQ------------ 71
Cdd:cd07719    1 RVTLLGTGGPIPDP-----------------DRAGPSTLVVV-GGRVYLVDAGS---------GVVRRlaqaglplgdld 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  72 -VLLTHYHLDHVQGLFPL---RWGVGAS--IPVYGPP--------------DDAGCDDLLKHPGLLDFSHTVT------P 125
Cdd:cd07719   54 aVFLTHLHSDHVADLPALlltAWLAGRKtpLPVYGPPgtralvdgllaayaLDIDYRARIGDEGRPDPGALVEvheiaaG 133

                        170       180       190
                 ....*....|....*....|....*....|...
gi 490290950 126 FVMFNLQGLRVTPLPLNHS--KLTFGYLLESAH 156
Cdd:cd07719  134 GVVYEDDGVKVTAFLVDHGpvPPALAYRFDTPG 166
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 72-222 7.06e-09

class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. 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: 293821  Cd Length: 259  Bit Score: 54.91  E-value: 7.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  72 VLLTHYHLDHVQGLfPL-----RWGVGASIPVYGPPDDagCDDLLKH--PGLL--DFSHTVTPFVMFN------------ 130
Cdd:cd07735   69 YLITHAHLDHIAGL-PLlspndGGQRGSPKTIYGLPET--IDALKKHifNWVIwpDFTSIPSGKYPYLrlepiepeypia 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950 131 LQGLRVTPLPLNHSKL-TFGYLLESAHSRLAWLSDT------------------AGLPDKSLKfllnnrpqAMIIDCS-- 189
Cdd:cd07735  146 LTGLSVTAFPVSHGVPvSTAFLIRDGGDSFLFFGDTgpdsvsksprldalwralAPLIPKKLK--------AIIIECSfp 217

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 490290950 190 -HEPRAQ-----TPRN-HNDLNtvrSLNQVIGC-----PRVILTH 222
Cdd:cd07735  218 nSRPDALlyghlTPKLlAEELA---KLAKEVLKgalkgLNVIITH 259
PQQB-like_MBL-fold cd16274
Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold ...
 5-141 2.56e-06

Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold metallo hydrolase domainhydrolase domain; PQQB is essential for the synthesis of the cofactor pyrroloquinoline quinone (PQQ) in Klebsiella pneumonia. PqqB is not directly involved in the PQQ biosynthesis but may serve as a carrier for PQQ when PQQ is released from PqqC. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293832 [Multi-domain]  Cd Length: 220  Bit Score: 46.84  E-value: 2.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950   5 LRLTGT---GGaqlVPVFGCDCAACRRARRE-ENHRRRPCSGVvtfnsAVT-------LLDAGrPDL---MEHHPAGSFQ 70
Cdd:cd16274    3 IKVLGSaagGG---FPQWNCNCPNCALARAGdGRATARTQSSI-----AVSadgenwvLINAS-PDIrqqIEATPELQPR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  71 Q---------VLLTHYHLDHVQGLFPLRwgVGASIPVYGPP-------DDAGCDDLLKHPGLLDFsHTVTPFVMFNLQ-- 132
Cdd:cd16274   74 PglrdtpiaaVLLTDAEIDHTTGLLSLR--EGQPLTVYATApvledltTNFPFFVLLHAYGGVRR-HRILPGEPFTLAgc 150

                        170
                 ....*....|
gi 490290950 133 -GLRVTPLPL 141
Cdd:cd16274  151 pGLTVTPFPV 160
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 52-165 1.20e-05

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


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 44.18  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  52 LLDAGRP--------DLMEHHPAgSFQQVLLTHYHLDHVQGLfplrwGVGA---SIPVYGPPDDAgcDDLLKHPGLLDfS 120
Cdd:cd07733   22 LIDAGLSgrkitgrlAEIGRDPE-DIDAILVTHEHADHIKGL-----GVLArkyNVPIYATAGTL--RAMERKVGLID-V 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 490290950 121 HTVTPFVM---FNLQGLRVTPLPLNHSKL-TFGYLLESAHSRLAWLSDT 165
Cdd:cd07733   93 DQKQIFEPgetFSIGDFDVESFGVSHDAAdPVGYRFEEGGRRFGMLTDL 141
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 72-127 1.90e-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: 44.20  E-value: 1.90e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490290950  72 VLLTHYHLDHVQGLFPLRWGVGAsiPVYGPPDDAgcdDLLKHPGLLDFSHTVTPFV 127
Cdd:cd06262   49 ILLTHGHFDHIGGLAELKEAPGA--PVYIHEADA---ELLEDPELNLAFFGGGPLP 99
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 72-170 3.61e-05

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 43.75  E-value: 3.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  72 VLLTHYHLDHV--QGLFPLRwgvGASIPVYGPPDDAgcdDLLKHPGLLDFsHTVTPFVMFNLQGLRVTPLPLNHS----- 144
Cdd:COG2220   52 VLVTHDHYDHLddATLRALK---RTGATVVAPLGVA---AWLRAWGFPRV-TELDWGESVELGGLTVTAVPARHSsgrpd 124

                         90       100
                 ....*....|....*....|....*....
gi 490290950 145 ---KLTFGYLLESAHSRLAWLSDTAGLPD 170
Cdd:COG2220  125 rngGLWVGFVIETDGKTIYHAGDTGYFPE 153
PRK05184 PRK05184
pyrroloquinoline quinone biosynthesis protein PqqB; Provisional
 11-141 3.78e-05

pyrroloquinoline quinone biosynthesis protein PqqB; Provisional


Pssm-ID: 235361 [Multi-domain]  Cd Length: 302  Bit Score: 44.04  E-value: 3.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  11 GGaqlVPVFGCDCAACRRARREE-NHRRRPCSGVvtfnsAVT-------LLDAGrPDLM-------EHHPAGSF-----Q 70
Cdd:PRK05184  12 GG---FPQWNCNCPNCRGARAGTiRAKPRTQSSI-----AVSadgedwvLLNAS-PDIRqqiqatpALQPARGLrdtpiA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  71 QVLLTHYHLDHVQGLFPLRWGVGasIPVYGPPD--DAGCD-----DLLKHPGLLDFsHTVT---PFVMFNLQGLRVTPLP 140
Cdd:PRK05184  83 AVVLTDGQIDHTTGLLTLREGQP--FPVYATPAvlEDLSTgfpifNVLDHYGGVQR-RPIAldgPFAVPGLPGLRFTAFP 159


                 .
gi 490290950 141 L 141
Cdd:PRK05184 160 V 160
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 41-105 4.31e-05

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: 43.14  E-value: 4.31e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490290950  41 SGVVTFNSAVTLLDAGRPDLMEHHPAGSFQQ-------VLLTHYHLDHVQGLFPLRWGVGAsiPVYGPPDDA 105
Cdd:COG0491   17 SYLIVGGDGAVLIDTGLGPADAEALLAALAAlgldikaVLLTHLHPDHVGGLAALAEAFGA--PVYAHAAEA 86
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 72-113 2.84e-04

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 40.14  E-value: 2.84e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 490290950  72 VLLTHYHLDHVQGLFPL--RWGvgaSIPVYGPPDD--AGCDDLLKH 113
Cdd:cd07723   47 ILTTHHHWDHTGGNAELkaLFP---DAPVYGPAEDriPGLDHPVKD 89
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 72-222 4.04e-04

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


Pssm-ID: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 40.25  E-value: 4.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  72 VLLTHYHLDH-----------VQGLFPLRwGVgasipVYGpPDDA--GCDDLLK--HPGLLDFSHTVTPFVMFNLQGLRV 136
Cdd:cd07741   57 IILSHRHLDHsndanvlieamTEGGFKKR-GT-----LLA-PEDAlnGEPVVLLyyHRRKLEEIEILEEGDEYELGGIKI 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950 137 TPLPLNHS-KLTFGYLLESAHSRLAWLSDTAGLPDKSLKFllnNRPQAMIIDCSHePRAQTPRNHNDLNTVRSLNQVIGC 215
Cdd:cd07741  130 EATRHKHSdPTTYGFIFRTSDKKIGYISDTRYFEELIEYY---SNCDVLIINVTR-PRPRKGVDHLSVEDVEKILKEIKP 205


                 ....*..
gi 490290950 216 PRVILTH 222
Cdd:cd07741  206 KLAILTH 212
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 52-121 4.75e-04

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 39.82  E-value: 4.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950  52 LLDAGRP---------DLMEHHPAGSFQQVLLTHYHLDHVQGLFPLR-WGVGASIPVYG-PPDDAGCDDLLKHPGLLDFS 120
Cdd:cd07722   31 LIDTGEGrpsyipllkSVLDSEGNATISDILLTHWHHDHVGGLPDVLdLLRGPSPRVYKfPRPEEDEDPDEDGGDIHDLQ 110


                 .
gi 490290950 121 H 121
Cdd:cd07722  111 D 111
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 41-117 1.48e-03

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: 38.30  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950    41 SGVVTFNSAVTLLDAGRPDLMEHHPA------GSFQQVLLTHYHLDHVQGLFPLRWGVGAsiPVYGPPDDAgcdDLLKHP 114
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDLLAElkklgpKKIDAIILTHGHPDHIGGLPELLEAPGA--PVYAPEGTA---ELLKDL 76


                   ...
gi 490290950   115 GLL 117
Cdd:smart00849  77 LAL 79
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 9-153 2.50e-03

ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of endonuclease or exonuclease activity, and differs in different species. Member of this family are ribonuclease Z, a tRNA 3-prime endonuclease that processes tRNAs to prepare for addition of CCA. In species where all tRNA sequences already have the CCA tail, such as E. coli, the need for such an enzyme is unclear. Protein similar to the E. coli enzyme, matched by TIGRFAMs model TIGR02649, are designated ribonuclease BN. [Transcription, RNA processing]


Pssm-ID: 274246 [Multi-domain]  Cd Length: 299  Bit Score: 38.35  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950    9 GTGGAqlVPvfgcdcaacrrarreeNHRRRPCSGVVTFNSAVTLLDAG----RPdlMEHHPAgSFQQV---LLTHYHLDH 81
Cdd:TIGR02651   6 GTGGG--VP----------------TKERNLPSIALKLNGELWLFDCGegtqRQ--MLRSGI-SPMKIdriFITHLHGDH 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490290950   82 VQGLFPL-----RWGVGASIPVYGPPddaGCDDLLKHpgLLDFS----------HTVTPF-VMFNLQGLRVTPLPLNHSK 145
Cdd:TIGR02651  65 ILGLPGLlstmsFQGRKEPLTIYGPP---GIKEFIET--SLRVSytylnypikiHEIEEGgLVFEDDGFKVEAFPLDHSI 139


                  ....*...
gi 490290950  146 LTFGYLLE 153
Cdd:TIGR02651 140 PSLGYRFE 147
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 50-105 6.02e-03

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: 36.82  E-value: 6.02e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490290950  50 VTLLDAGRPDLMEH-----HPAG-SFQQ---VLLTHYHLDHVQGLFPLR--WGVgasiPVYGPPDDA 105
Cdd:cd07721   22 LTLIDTGLPGSAKRilkalRELGlSPKDirrILLTHGHIDHIGSLAALKeaPGA----PVYAHEREA 84
 
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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