NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|521291914|ref|WP_020456182|]
View 

MULTISPECIES: phosphonate metabolism protein PhnP [Enterobacteriaceae]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 581040)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold super family cl23716
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 13-249 8.30e-139

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: 389.47  E-value: 8.30e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   13 AQLVPVFGCDCAACRRARQNETHRRKPCSAVVKFNDAVTLLDAGIPDLMDTFPAGHFQQFLLTHYHMDHVQGLFPLRWGV 92
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   93 GEKIPVYGPPDEQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLFESAHSRVAWLSDTAGLPDKT 172
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLLETDGQRVAYLTDTAGLPPDT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521291914  173 LKFLLNNHPQVVVIDCSYEPRAQTPKNHSDLNTVIALNEVIGCPRVILTHISHVFDQWMMKNP-LPTGVEAGYDGMRI 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 8.30e-139

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: 389.47  E-value: 8.30e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   13 AQLVPVFGCDCAACRRARQNETHRRKPCSAVVKFNDAVTLLDAGIPDLMDTFPAGHFQQFLLTHYHMDHVQGLFPLRWGV 92
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   93 GEKIPVYGPPDEQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLFESAHSRVAWLSDTAGLPDKT 172
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLLETDGQRVAYLTDTAGLPPDT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521291914  173 LKFLLNNHPQVVVIDCSYEPRAQTPKNHSDLNTVIALNEVIGCPRVILTHISHVFDQWMMKNP-LPTGVEAGYDGMRI 249
Cdd:TIGR03307 161 EAFLKNHPLDVLILDCSHPPQSDAPRNHNDLTRALAINEQLRPKQVILTHISHQLDAWLMENPdLPSGVAVGYDGQTL 238
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 3-188 9.88e-114

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: 323.81  E-value: 9.88e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   3 LTITLTGTGGAQLVPVFGCDCAACRRARQNETHRRKPCSAVVKFNDAVTLLDAGIPDLMDTFPAGHFQQFLLTHYHMDHV 82
Cdd:cd07736    1 MKLTFLGTGDAGGVPVYGCDCSACQRARQDPSYRRRPCSALIEVDGERILLDAGLTDLAERFPPGSIDAILLTHFHMDHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  83 QGLFPLRWGVGEKIPVYGPPDEQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLFESAHSRVAWL 162
Cdd:cd07736   81 QGLFHLRWGVGDPIPVYGPPDPQGCADLFKHPGILDFQPLVAPFQSFELGGLKITPLPLNHSKPTFGYLLESGGKRLAYL 160

                        170       180
                 ....*....|....*....|....*.
gi 521291914 163 SDTAGLPDKTLKFLLNNHPQVVVIDC 188
Cdd:cd07736  161 TDTLGLPEETLEFLKQQQPDVLVLDC 186
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 3-251 4.96e-60

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 190.11  E-value: 4.96e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   3 LTITLTGTGGAQLVPVFGCDCAACRRArqNETHRRKPCSAVVKFNDAVTLLDAGiPDLMDTFPA-----GHFQQFLLTHY 77
Cdd:COG1235    1 MKVTFLGSGSSGGVPQIGCDCPVCAST--DPRYGRTRSSILVEADGTRLLIDAG-PDLREQLLRlgldpSKIDAILLTHE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  78 HMDHVQGLFPLRWGVGEK-IPVYGPPD-----EQGCDDLFKH-PGLLDFsHTVEPFVVFDLQGLQVTPLPLNHSKL-TFG 149
Cdd:COG1235   78 HADHIAGLDDLRPRYGPNpIPVYATPGtlealERRFPYLFAPyPGKLEF-HEIEPGEPFEIGGLTVTPFPVPHDAGdPVG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914 150 YLFESAHSRVAWLSDTAGLPDKTLKFLLNnhPQVVVIDCSYEPRAQtpkNHSDLNTVIALNEVIGCPRVILTHIS----- 224
Cdd:COG1235  157 YRIEDGGKKLAYATDTGYIPEEVLELLRG--ADLLILDATYDDPEP---GHLSNEEALELLARLGPKRLVLTHLSpdnnd 231

                        250       260
                 ....*....|....*....|....*...
gi 521291914 225 HVFDQWMMKN-PLPTGVEAGYDGMRIVL 251
Cdd:COG1235  232 HELDYDELEAaLLPAGVEVAYDGMEIEL 259
PRK02113 PRK02113
MBL fold metallo-hydrolase;
3-251 5.01e-23

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 94.08  E-value: 5.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   3 LTITLTGTGGAQLVPVFGCDCAACRRARQNETHRRkpCSAVVKFNDAVTLLDAGiPDL---MDTFPAGHFQQFLLTHYHM 79
Cdd:PRK02113   1 MKIRILGSGTSTGVPEIGCTCPVCTSKDPRDNRLR--TSALVETEGARILIDCG-PDFreqMLRLPFGKIDAVLITHEHY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  80 DHVQGLFPLR-WGVGEKIPVYGppdEQGCDDLFK-----------HPGLLDFS-HTVEPFVVFDLQGLQVTPLPLNHSKL 146
Cdd:PRK02113  78 DHVGGLDDLRpFCRFGEVPIYA---EQYVAERLRsrmpycfvehsYPGVPNIPlREIEPDRPFLVNHTEVTPLRVMHGKL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914 147 T-FGYLFesahSRVAWLSDTAGLPDKTLKFLLNnhPQVVVIDCSyepRAQTPKNHSDLNTVIALNEVIGCPRVILTHISH 225
Cdd:PRK02113 155 PiLGYRI----GKMAYITDMLTMPEEEYEQLQG--IDVLVMNAL---RIAPHPTHQSLEEALENIKRIGAKETYLIHMSH 225

                        250       260
                 ....*....|....*....|....*..
gi 521291914 226 VFD-QWMMKNPLPTGVEAGYDGMRIVL 251
Cdd:PRK02113 226 HIGlHADVEKELPPHVHFAYDGLEIIF 252
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 73-223 2.04e-11

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: 61.17  E-value: 2.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   73 LLTHYHMDHVQGLFPLRWGVGEkiPVYGPPD-----EQGCDDLFKHPGLLDFSHTVEPFVVFDL--QGLQVTPLPLNHSK 145
Cdd:pfam12706  33 LLTHDHYDHLAGLLDLREGRPR--PLYAPLGvlahlRRNFPYLFLLEHYGVRVHEIDWGESFTVgdGGLTVTATPARHGS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  146 ---------LTFGYLFESAHSRVAWLSDTAGLPDKTLKFLLNnhPQVVVID-CSYEPRAQTPKNHSDLNTVIALNEVIGC 215
Cdd:pfam12706 111 prgldpnpgDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLGG--ADLLLLDgGAWRDDEMIHMGHMTPEEAVEAAADLGA 188


                  ....*...
gi 521291914  216 PRVILTHI 223
Cdd:pfam12706 189 RRKVLIHI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 41-130 3.41e-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: 37.53  E-value: 3.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914    41 SAVVKFNDAVTLLDAGIPDLMDtfPAGHFQQF--------LLTHYHMDHVQGLFPLRWGVGekIPVYGPPDEQG--CDDL 110
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAED--LLAELKKLgpkkidaiILTHGHPDHIGGLPELLEAPG--APVYAPEGTAEllKDLL 77

                           90       100
                   ....*....|....*....|
gi 521291914   111 FKHPGLLDFSHTVEPFVVFD 130
Cdd:smart00849  78 ALLGELGAEAEPAPPDRTLK 97
 
Name Accession Description Interval E-value
PhnP TIGR03307
phosphonate metabolism protein PhnP; This family of proteins found in operons encoding ...
 13-249 8.30e-139

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: 389.47  E-value: 8.30e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   13 AQLVPVFGCDCAACRRARQNETHRRKPCSAVVKFNDAVTLLDAGIPDLMDTFPAGHFQQFLLTHYHMDHVQGLFPLRWGV 92
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   93 GEKIPVYGPPDEQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLFESAHSRVAWLSDTAGLPDKT 172
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLLETDGQRVAYLTDTAGLPPDT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 521291914  173 LKFLLNNHPQVVVIDCSYEPRAQTPKNHSDLNTVIALNEVIGCPRVILTHISHVFDQWMMKNP-LPTGVEAGYDGMRI 249
Cdd:TIGR03307 161 EAFLKNHPLDVLILDCSHPPQSDAPRNHNDLTRALAINEQLRPKQVILTHISHQLDAWLMENPdLPSGVAVGYDGQTL 238
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 3-188 9.88e-114

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: 323.81  E-value: 9.88e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   3 LTITLTGTGGAQLVPVFGCDCAACRRARQNETHRRKPCSAVVKFNDAVTLLDAGIPDLMDTFPAGHFQQFLLTHYHMDHV 82
Cdd:cd07736    1 MKLTFLGTGDAGGVPVYGCDCSACQRARQDPSYRRRPCSALIEVDGERILLDAGLTDLAERFPPGSIDAILLTHFHMDHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  83 QGLFPLRWGVGEKIPVYGPPDEQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLFESAHSRVAWL 162
Cdd:cd07736   81 QGLFHLRWGVGDPIPVYGPPDPQGCADLFKHPGILDFQPLVAPFQSFELGGLKITPLPLNHSKPTFGYLLESGGKRLAYL 160

                        170       180
                 ....*....|....*....|....*.
gi 521291914 163 SDTAGLPDKTLKFLLNNHPQVVVIDC 188
Cdd:cd07736  161 TDTLGLPEETLEFLKQQQPDVLVLDC 186
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 3-251 4.96e-60

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 190.11  E-value: 4.96e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   3 LTITLTGTGGAQLVPVFGCDCAACRRArqNETHRRKPCSAVVKFNDAVTLLDAGiPDLMDTFPA-----GHFQQFLLTHY 77
Cdd:COG1235    1 MKVTFLGSGSSGGVPQIGCDCPVCAST--DPRYGRTRSSILVEADGTRLLIDAG-PDLREQLLRlgldpSKIDAILLTHE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  78 HMDHVQGLFPLRWGVGEK-IPVYGPPD-----EQGCDDLFKH-PGLLDFsHTVEPFVVFDLQGLQVTPLPLNHSKL-TFG 149
Cdd:COG1235   78 HADHIAGLDDLRPRYGPNpIPVYATPGtlealERRFPYLFAPyPGKLEF-HEIEPGEPFEIGGLTVTPFPVPHDAGdPVG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914 150 YLFESAHSRVAWLSDTAGLPDKTLKFLLNnhPQVVVIDCSYEPRAQtpkNHSDLNTVIALNEVIGCPRVILTHIS----- 224
Cdd:COG1235  157 YRIEDGGKKLAYATDTGYIPEEVLELLRG--ADLLILDATYDDPEP---GHLSNEEALELLARLGPKRLVLTHLSpdnnd 231

                        250       260
                 ....*....|....*....|....*...
gi 521291914 225 HVFDQWMMKN-PLPTGVEAGYDGMRIVL 251
Cdd:COG1235  232 HELDYDELEAaLLPAGVEVAYDGMEIEL 259
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 3-188 1.22e-31

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: 114.88  E-value: 1.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   3 LTITLTGTGGAQLVPVFGCDCAACRRArqNETHRRKPCSAVVKFNDAVTLLDAGiPDLMdtfpaghfQQFL--------- 73
Cdd:cd16279    1 MKLTFLGTGTSSGVPVIGCDCGVCDSS--DPKNRRLRSSILIETGGKNILIDTG-PDFR--------QQALragirklda 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  74 --LTHYHMDHVQG---LFPLRWGVGEKIPVYGPP----------DEQGCDDLFKHPGLLDFsHTVEPFVVFDLQGLQVTP 138
Cdd:cd16279   70 vlLTHAHADHIHGlddLRPFNRLQQRPIPVYASEetlddlkrrfPYFFAATGGGGVPKLDL-HIIEPDEPFTIGGLEITP 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 521291914 139 LPLNHSKL-TFGYLFEsahsRVAWLSDTAGLPDKTLKFLLNnhPQVVVIDC 188
Cdd:cd16279  149 LPVLHGKLpSLGFRFG----DFAYLTDVSEIPEESLEKLRG--LDVLILDA 193
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
5-251 3.71e-23

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 94.11  E-value: 3.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   5 ITLTGTGGAqlVPvfgcdcaacrrarqneTHRRKPCSAVVKFNDAVTLLDAG--IPDLMDTFPAGHFQ--QFLLTHYHMD 80
Cdd:COG1234    3 LTFLGTGGA--VP----------------TPGRATSSYLLEAGGERLLIDCGegTQRQLLRAGLDPRDidAIFITHLHGD 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  81 HVQGLFPL---RW--GVGEKIPVYGPPD-EQGCDDLFK-HPGLLDFS---HTVEPFVVFDLQGLQVTPLPLNHSKLTFGY 150
Cdd:COG1234   65 HIAGLPGLlstRSlaGREKPLTIYGPPGtKEFLEALLKaSGTDLDFPlefHEIEPGEVFEIGGFTVTAFPLDHPVPAYGY 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914 151 LFESAHSRVAWLSDTAglPDKTLKFLLNNhPQVVVIDCSYEPRAQ---TPKNHSDLNTVIALNEVIGCPRVILTHISHVF 227
Cdd:COG1234  145 RFEEPGRSLVYSGDTR--PCEALVELAKG-ADLLIHEATFLDEEAelaKETGHSTAKEAAELAAEAGVKRLVLTHFSPRY 221

                        250       260
                 ....*....|....*....|....*....
gi 521291914 228 D---QWM--MKNPLPTGVEAGYDGMRIVL 251
Cdd:COG1234  222 DdpeELLaeARAVFPGPVELAEDGMVIEL 250
PRK02113 PRK02113
MBL fold metallo-hydrolase;
3-251 5.01e-23

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 94.08  E-value: 5.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   3 LTITLTGTGGAQLVPVFGCDCAACRRARQNETHRRkpCSAVVKFNDAVTLLDAGiPDL---MDTFPAGHFQQFLLTHYHM 79
Cdd:PRK02113   1 MKIRILGSGTSTGVPEIGCTCPVCTSKDPRDNRLR--TSALVETEGARILIDCG-PDFreqMLRLPFGKIDAVLITHEHY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  80 DHVQGLFPLR-WGVGEKIPVYGppdEQGCDDLFK-----------HPGLLDFS-HTVEPFVVFDLQGLQVTPLPLNHSKL 146
Cdd:PRK02113  78 DHVGGLDDLRpFCRFGEVPIYA---EQYVAERLRsrmpycfvehsYPGVPNIPlREIEPDRPFLVNHTEVTPLRVMHGKL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914 147 T-FGYLFesahSRVAWLSDTAGLPDKTLKFLLNnhPQVVVIDCSyepRAQTPKNHSDLNTVIALNEVIGCPRVILTHISH 225
Cdd:PRK02113 155 PiLGYRI----GKMAYITDMLTMPEEEYEQLQG--IDVLVMNAL---RIAPHPTHQSLEEALENIKRIGAKETYLIHMSH 225

                        250       260
                 ....*....|....*....|....*..
gi 521291914 226 VFD-QWMMKNPLPTGVEAGYDGMRIVL 251
Cdd:PRK02113 226 HIGlHADVEKELPPHVHFAYDGLEIIF 252
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 5-249 3.83e-15

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: 72.48  E-value: 3.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   5 ITLTGTGGAqlVPvfgcdcaacrrarqneTHRRKPCSAVVKFNDAVTLLDAG-------------IPDLMDTFpaghfqq 71
Cdd:cd07717    1 LTFLGTGSA--VP----------------TPERNLSSIALRLEGELWLFDCGegtqrqllraglsPSKIDRIF------- 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  72 flLTHYHMDHVQGLFPL-----RWGVGEKIPVYGPPdeqGCDDLFKHpgLLDFSHTVEPF------------VVFDLQGL 134
Cdd:cd07717   56 --ITHLHGDHILGLPGLlstmsLLGRTEPLTIYGPK---GLKEFLET--LLRLSASRLPYpievhelepdpgLVFEDDGF 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914 135 QVTPLPLNHSKLTFGYLFESAHSrVAWLSDTAgLPDKTLKFLLNnhPQVVVIDCSY----EPRAQtPKNHSdlnTV---- 206
Cdd:cd07717  129 TVTAFPLDHRVPCFGYRFEEGRK-IAYLGDTR-PCEGLVELAKG--ADLLIHEATFldddAEKAK-ETGHS---TAkqaa 200

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 521291914 207 -IALNevIGCPRVILTHISHvfdqwMMKNPLP---------TGVEAGYDGMRI 249
Cdd:cd07717  201 eIAKK--AGVKKLVLTHFSA-----RYKDPEEllkearavfPNTILAEDFMTI 246
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 5-166 4.82e-13

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: 65.36  E-value: 4.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   5 ITLTGTGGAqlVPvfgcdcaacrrarqneTHRRKPCSAVVKFNDAVTLLDAG---IPDLMDTFPAGHFQQFL-LTHYHMD 80
Cdd:cd16272    1 LTFLGTGGA--VP----------------SLTRNTSSYLLETGGTRILLDCGegtVYRLLKAGVDPDKLDAIfLSHFHLD 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  81 HVQGLFPL----RWGVGEK-IPVYGPPD-EQGCDDLFKHPGL-------LDFSHTVEPFVVFDLQGLQVTPLPLNHSKLT 147
Cdd:cd16272   63 HIGGLPTLlfarRYGGRKKpLTIYGPKGiKEFLEKLLNFPVEilplgfpLEIEELEEGGEVLELGDLKVEAFPVKHSVES 142

                        170
                 ....*....|....*....
gi 521291914 148 FGYLFESAHSRVAWLSDTA 166
Cdd:cd16272  143 LGYRIEAEGKSIVYSGDTG 161
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 4-166 1.01e-11

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: 62.15  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   4 TITLTGTGGAQLVPvfgcdcaacrrarqnetHRRKPCSAVVkFNDAVTLLDAGipdlmdtfpAGHFQQF----------- 72
Cdd:cd07719    1 RVTLLGTGGPIPDP-----------------DRAGPSTLVV-VGGRVYLVDAG---------SGVVRRLaqaglplgdld 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  73 --LLTHYHMDHVQGLFPL---RWGVGEK--IPVYGPP--------------DEQGCDDLFKHPGLLDFSHTVE------P 125
Cdd:cd07719   54 avFLTHLHSDHVADLPALlltAWLAGRKtpLPVYGPPgtralvdgllaayaLDIDYRARIGDEGRPDPGALVEvheiaaG 133

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 521291914 126 FVVFDLQGLQVTPLPLNHS--KLTFGYLFESAHSRVAWLSDTA 166
Cdd:cd07719  134 GVVYEDDGVKVTAFLVDHGpvPPALAYRFDTPGRSVVFSGDTG 176
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 73-223 2.04e-11

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: 61.17  E-value: 2.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   73 LLTHYHMDHVQGLFPLRWGVGEkiPVYGPPD-----EQGCDDLFKHPGLLDFSHTVEPFVVFDL--QGLQVTPLPLNHSK 145
Cdd:pfam12706  33 LLTHDHYDHLAGLLDLREGRPR--PLYAPLGvlahlRRNFPYLFLLEHYGVRVHEIDWGESFTVgdGGLTVTATPARHGS 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  146 ---------LTFGYLFESAHSRVAWLSDTAGLPDKTLKFLLNnhPQVVVID-CSYEPRAQTPKNHSDLNTVIALNEVIGC 215
Cdd:pfam12706 111 prgldpnpgDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLGG--ADLLLLDgGAWRDDEMIHMGHMTPEEAVEAAADLGA 188


                  ....*...
gi 521291914  216 PRVILTHI 223
Cdd:pfam12706 189 RRKVLIHI 196
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 52-192 3.18e-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: 60.97  E-value: 3.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  52 LLDAG---IP---DLMDTFPAGHFQqFLLTHYHMDHVQGL--F-PLrWGVGEKIPVYGPPDEQGC-----DDLFKHP--- 114
Cdd:cd07715   36 ILDAGtgiRElgnELMKEGPPGEAH-LLLSHTHWDHIQGFpfFaPA-YDPGNRIHIYGPHKDGGSleevlRRQMSPPyfp 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914 115 -GLLDFS-----HTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLFESAHSRVAWLSDT-----AGLPDKTLKFLLNNhPQV 183
Cdd:cd07715  114 vPLEELLaaiefHDLEPGEPFSIGGVTVTTIPLNHPGGALGYRIEEDGKSVVYATDTehypdDGESDEALLEFARG-ADL 192


                 ....*....
gi 521291914 184 VVIDCSYEP 192
Cdd:cd07715  193 LIHDAQYTD 201
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 48-222 8.11e-10

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: 57.61  E-value: 8.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  48 DAVTLLDAG------------IPDLMDTFPAGHF-----QQFLLTHYHMDHVQGLfPL-----RWGVGEKIPVYGPPDEq 105
Cdd:cd07735   28 DGDILLDAGtgvgalsleemfNDILFPSQKAAYElyqriRHYLITHAHLDHIAGL-PLlspndGGQRGSPKTIYGLPET- 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914 106 gCDDLFKH-------PGLLDFSHTVEPFVVFD---------LQGLQVTPLPLNHSKL-TFGYLFESAHSRVAWLSDTAgl 168
Cdd:cd07735  106 -IDALKKHifnwviwPDFTSIPSGKYPYLRLEpiepeypiaLTGLSVTAFPVSHGVPvSTAFLIRDGGDSFLFFGDTG-- 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914 169 PDKTLKFLLNNH------PQV------VVIDCSY---EPRAQ-----TPKN-HSDLNtviALNEVIGC-----PRVILTH 222
Cdd:cd07735  183 PDSVSKSPRLDAlwralaPLIpkklkaIIIECSFpnsRPDALlyghlTPKLlAEELA---KLAKEVLKgalkgLNVIITH 259
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 73-166 6.05e-09

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: 53.99  E-value: 6.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  73 LLTHYHMDHVQGLFPLR--------WGVGEKIPVYGPPDEQGC-DDLFKHPGLLDFsHTVEPFVVFDLQGLQVTPLPLNH 143
Cdd:cd07716   55 VLSHLHPDHCADLGVLQyarryhprGARKPPLPLYGPAGPAERlAALYGLEDVFDF-HPIEPGEPLEIGPFTITFFRTVH 133

                         90       100
                 ....*....|....*....|...
gi 521291914 144 SKLTFGYLFESAHSRVAWLSDTA 166
Cdd:cd07716  134 PVPCYAMRIEDGGKVLVYTGDTG 156
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 5-153 1.22e-08

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: 54.53  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914    5 ITLTGTGGAqlVPvfgcdcaacrrarqneTHRRKPCSAVVKFNDAVTLLDAGipdlmdtfpAGHFQQFL----------- 73
Cdd:TIGR02651   2 ITFLGTGGG--VP----------------TKERNLPSIALKLNGELWLFDCG---------EGTQRQMLrsgispmkidr 54

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   74 --LTHYHMDHVQGLFPL-----RWGVGEKIPVYGPPdeqGCDDLFKHpgLLDFSHTVEPF-----------VVFDLQGLQ 135
Cdd:TIGR02651  55 ifITHLHGDHILGLPGLlstmsFQGRKEPLTIYGPP---GIKEFIET--SLRVSYTYLNYpikiheieeggLVFEDDGFK 129

                         170
                  ....*....|....*...
gi 521291914  136 VTPLPLNHSKLTFGYLFE 153
Cdd:TIGR02651 130 VEAFPLDHSIPSLGYRFE 147
PQQB-like_MBL-fold cd16274
Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold ...
 1-158 3.03e-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: 3.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   1 MSLTITLTGTGGAqlVPVFGCDCAACRRARqNETHRRKP----CSAVVKFNDAVTLLDAGiPDL---MDTFPAGHFQQF- 72
Cdd:cd16274    1 MRIKVLGSAAGGG--FPQWNCNCPNCALAR-AGDGRATArtqsSIAVSADGENWVLINAS-PDIrqqIEATPELQPRPGl 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  73 --------LLTHYHMDHVQGLFPLRwgVGEKIPVYGPP-------DEQGCDDLFKHPGLLDFSHTV--EPFVVFDLQGLQ 135
Cdd:cd16274   77 rdtpiaavLLTDAEIDHTTGLLSLR--EGQPLTVYATApvledltTNFPFFVLLHAYGGVRRHRILpgEPFTLAGCPGLT 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 521291914 136 VTPLPL-------------NHSKLTFGYLFESAHSR 158
Cdd:cd16274  155 VTPFPVpgkaplysehrdaPEPGDTIGLRIEDGRTG 190
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 72-222 1.87e-05

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


Pssm-ID: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 44.49  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  72 FLLTHYHMDH-----------VQGLFPLRwGVgekipVYGPPD---EQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVT 137
Cdd:cd07741   57 IILSHRHLDHsndanvlieamTEGGFKKR-GT-----LLAPEDalnGEPVVLLYYHRRKLEEIEILEEGDEYELGGIKIE 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914 138 PLPLNHS-KLTFGYLFESAHSRVAWLSDTAGLPDKTLKFllnNHPQVVVIDCSYePRAQTPKNHSDLNTVIALNEVIGCP 216
Cdd:cd07741  131 ATRHKHSdPTTYGFIFRTSDKKIGYISDTRYFEELIEYY---SNCDVLIINVTR-PRPRKGVDHLSVEDVEKILKEIKPK 206


                 ....*.
gi 521291914 217 RVILTH 222
Cdd:cd07741  207 LAILTH 212
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 52-165 4.08e-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: 42.64  E-value: 4.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  52 LLDAGIP--------DLMDTFPAgHFQQFLLTHYHMDHVQGLFPLrwgvGEK--IPVYGPPDEqgCDDLFKHPGLLDFS- 120
Cdd:cd07733   22 LIDAGLSgrkitgrlAEIGRDPE-DIDAILVTHEHADHIKGLGVL----ARKynVPIYATAGT--LRAMERKVGLIDVDq 94

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 521291914 121 -HTVEPFVVFDLQGLQVTPLPLNHSKL-TFGYLFESAHSRVAWLSDT 165
Cdd:cd07733   95 kQIFEPGETFSIGDFDVESFGVSHDAAdPVGYRFEEGGRRFGMLTDL 141
PRK00055 PRK00055
ribonuclease Z; Reviewed
 5-102 3.05e-04

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 40.93  E-value: 3.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914   5 ITLTGTGGAqlVPvfgcdcaacrrarqneTHRRKPCSAVVKFNDAVTLLDAGipdlmdtfpAGHFQQFL----------- 73
Cdd:PRK00055   4 LTFLGTGSG--VP----------------TPTRNVSSILLRLGGELFLFDCG---------EGTQRQLLktgikprkidk 56

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 521291914  74 --LTHYHMDHVQGLFPL-----RWGVGEKIPVYGPP 102
Cdd:PRK00055  57 ifITHLHGDHIFGLPGLlstrsLSGRTEPLTIYGPK 92
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 73-170 4.08e-04

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 40.29  E-value: 4.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  73 LLTHYHMDHV--QGLFPLRwgvGEKIPVYGPPdeqGCDDLFKHPGLLDFsHTVEPFVVFDLQGLQVTPLPLNHS------ 144
Cdd:COG2220   53 LVTHDHYDHLddATLRALK---RTGATVVAPL---GVAAWLRAWGFPRV-TELDWGESVELGGLTVTAVPARHSsgrpdr 125

                         90       100
                 ....*....|....*....|....*...
gi 521291914 145 --KLTFGYLFESAHSRVAWLSDTAGLPD 170
Cdd:COG2220  126 ngGLWVGFVIETDGKTIYHAGDTGYFPE 153
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 73-130 6.97e-04

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: 39.58  E-value: 6.97e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 521291914  73 LLTHYHMDHVQGLFPLRWGVGekIPVYGPPDEQgcdDLFKHPGLLDFSHTVEPFVVFD 130
Cdd:cd06262   50 LLTHGHFDHIGGLAELKEAPG--APVYIHEADA---ELLEDPELNLAFFGGGPLPPPE 102
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 38-99 1.01e-03

Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; CPSF3 (cleavage and polyadenylation specificity factor subunit 3; also known as cleavage and polyadenylation specificity factor 73 kDa subunit, CPSF-73) and CPSF2 (also known as cleavage and polyadenylation specificity factor 100 kDa subunit /CPSF-100) are components of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. CPSF3 functions as a 3' endonuclease. Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)), and Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74) are subunits of Integrator, a metazoan-specific multifunctional protein complex composed of 14 subunits. Integrator has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. 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: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 39.24  E-value: 1.01e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 521291914  38 KPCSAVVKFNDAVtLLDAGIPDLMDTFPAGHFQQ---------FLLTHYHMDHVQGLFPLRWGVGEKIPVY 99
Cdd:cd07734   11 RSCFLVEFKGRTV-LLDCGMNPGKEDPEACLPQFellppeidaILISHFHLDHCGALPYLFRGFIFRGPIY 80
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 52-121 1.05e-03

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: 39.05  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  52 LLDAG---------IPDLMDTFPAGHFQQFLLTHYHMDHVQGLFPLR-WGVGEKIPVYG-PPDEQGCDDLFKHPGLLDFS 120
Cdd:cd07722   31 LIDTGegrpsyiplLKSVLDSEGNATISDILLTHWHHDHVGGLPDVLdLLRGPSPRVYKfPRPEEDEDPDEDGGDIHDLQ 110


                 .
gi 521291914 121 H 121
Cdd:cd07722  111 D 111
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 73-166 2.93e-03

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 37.62  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  73 LLTHYHMDHVQGLfP-------LRWGVGEKIPVYGPPD-----EQGCDDLFKHPGLLD--FSHTV---EPFVVFDLQGLQ 135
Cdd:cd07740   54 FITHLHGDHFGGL-PfflldaqFVAKRTRPLTIAGPPGlrerlRRAMEALFPGSSKVPrrFDLEVielEPGEPTTLGGVT 132

                         90       100       110
                 ....*....|....*....|....*....|...
gi 521291914 136 VTPLPLNHSKLTFGYLFESAHSR--VAWLSDTA 166
Cdd:cd07740  133 VTAFPVVHPSGALPLALRLEAAGrvLAYSGDTE 165
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 41-130 3.41e-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: 37.53  E-value: 3.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914    41 SAVVKFNDAVTLLDAGIPDLMDtfPAGHFQQF--------LLTHYHMDHVQGLFPLRWGVGekIPVYGPPDEQG--CDDL 110
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAED--LLAELKKLgpkkidaiILTHGHPDHIGGLPELLEAPG--APVYAPEGTAEllKDLL 77

                           90       100
                   ....*....|....*....|
gi 521291914   111 FKHPGLLDFSHTVEPFVVFD 130
Cdd:smart00849  78 ALLGELGAEAEPAPPDRTLK 97
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 43-144 4.55e-03

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 37.36  E-value: 4.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 521291914  43 VVKFNDAVTLLDAGIPDLMDTFPAGHFQQF-------LLTHYHMDHVQGLFPLRWGVGekIPVYGPPDE------QGCDD 109
Cdd:COG0491   19 LIVGGDGAVLIDTGLGPADAEALLAALAALgldikavLLTHLHPDHVGGLAALAEAFG--APVYAHAAEaealeaPAAGA 96

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 521291914 110 LFKHPGlLDFSHTVEPFVVFDLQGLQVTPLPLN-HS 144
Cdd:COG0491   97 LFGREP-VPPDRTLEDGDTLELGGPGLEVIHTPgHT 131
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 43-104 6.07e-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: 6.07e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 521291914  43 VVKFNDAVTLLDAGIPDLMDTFPAG---HFQQF------LLTHYHMDHVQGLFPLR--WGVgekiPVYGPPDE 104
Cdd:cd07721   15 LIEDDDGLTLIDTGLPGSAKRILKAlreLGLSPkdirriLLTHGHIDHIGSLAALKeaPGA----PVYAHERE 83
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 73-113 7.52e-03

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: 36.28  E-value: 7.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 521291914  73 LLTHYHMDHVQGLFPL--RWGvgeKIPVYGPPDEQ--GCDDLFKH 113
Cdd:cd07723   48 LTTHHHWDHTGGNAELkaLFP---DAPVYGPAEDRipGLDHPVKD 89
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH