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Conserved domains on  [gi|490311672|ref|WP_004206367|]
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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 1.52e-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: 378.68  E-value: 1.52e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672   13 AQLVPAFGCDCAACRRARREESHRRRPCSGVVTFNSAVTLLDAGRPDLMEHHPAGSFQQVLLTHYHLDHVQGLFPLRWGV 92
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672   93 GAPIPVYGPPDDAGCDDLLKHPGLLDFSHTVTPFVVFELQGLRVTPLPLNHSKLTFGYLLESAHSRVAWLSDTAGLPDKT 172
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLLETDGQRVAYLTDTAGLPPDT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490311672  173 LKFLLSNRPQAMIIDCSHEPRAQTPRNHNDFNTVRALNQAIGCPRVILTHISHQFDVWMMDNP-LPEGFEAGYDGMEI 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 1.52e-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: 378.68  E-value: 1.52e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672   13 AQLVPAFGCDCAACRRARREESHRRRPCSGVVTFNSAVTLLDAGRPDLMEHHPAGSFQQVLLTHYHLDHVQGLFPLRWGV 92
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672   93 GAPIPVYGPPDDAGCDDLLKHPGLLDFSHTVTPFVVFELQGLRVTPLPLNHSKLTFGYLLESAHSRVAWLSDTAGLPDKT 172
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLLETDGQRVAYLTDTAGLPPDT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490311672  173 LKFLLSNRPQAMIIDCSHEPRAQTPRNHNDFNTVRALNQAIGCPRVILTHISHQFDVWMMDNP-LPEGFEAGYDGMEI 249
Cdd:TIGR03307 161 EAFLKNHPLDVLILDCSHPPQSDAPRNHNDLTRALAINEQLRPKQVILTHISHQLDAWLMENPdLPSGVAVGYDGQTL 238
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 3-188 2.63e-106

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: 305.32  E-value: 2.63e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672   3 LTLRLTGTGGAQLVPAFGCDCAACRRARREESHRRRPCSGVVTFNSAVTLLDAGRPDLMEHHPAGSFQQVLLTHYHLDHV 82
Cdd:cd07736    1 MKLTFLGTGDAGGVPVYGCDCSACQRARQDPSYRRRPCSALIEVDGERILLDAGLTDLAERFPPGSIDAILLTHFHMDHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  83 QGLFPLRWGVGAPIPVYGPPDDAGCDDLLKHPGLLDFSHTVTPFVVFELQGLRVTPLPLNHSKLTFGYLLESAHSRVAWL 162
Cdd:cd07736   81 QGLFHLRWGVGDPIPVYGPPDPQGCADLFKHPGILDFQPLVAPFQSFELGGLKITPLPLNHSKPTFGYLLESGGKRLAYL 160

                        170       180
                 ....*....|....*....|....*.
gi 490311672 163 SDTAGLPDKTLKFLLSNRPQAMIIDC 188
Cdd:cd07736  161 TDTLGLPEETLEFLKQQQPDVLVLDC 186
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 3-251 1.91e-54

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 175.85  E-value: 1.91e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672   3 LTLRLTGTGGAQLVPAFGCDCAACRRARREesHRRRPCSGVVTFNSAVTLLDAGrPDLME-----HHPAGSFQQVLLTHY 77
Cdd:COG1235    1 MKVTFLGSGSSGGVPQIGCDCPVCASTDPR--YGRTRSSILVEADGTRLLIDAG-PDLREqllrlGLDPSKIDAILLTHE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  78 HLDHVQGLFPLRWG-VGAPIPVYGPPDDagCDDLLK--------HPGLLDFsHTVTPFVVFELQGLRVTPLPLNHSKL-T 147
Cdd:COG1235   78 HADHIAGLDDLRPRyGPNPIPVYATPGT--LEALERrfpylfapYPGKLEF-HEIEPGEPFEIGGLTVTPFPVPHDAGdP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672 148 FGYLLESAHSRVAWLSDTAGLPDKTLKFLlsNRPQAMIIDCSHEPRAQtprNHNDFNTVRALNQAIGCPRVILTHIS--- 224
Cdd:COG1235  155 VGYRIEDGGKKLAYATDTGYIPEEVLELL--RGADLLILDATYDDPEP---GHLSNEEALELLARLGPKRLVLTHLSpdn 229

                        250       260       270
                 ....*....|....*....|....*....|
gi 490311672 225 --HQFDVWMMDN-PLPEGFEAGYDGMEIVL 251
Cdd:COG1235  230 ndHELDYDELEAaLLPAGVEVAYDGMEIEL 259
PRK02113 PRK02113
MBL fold metallo-hydrolase;
3-251 1.09e-21

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 90.61  E-value: 1.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672   3 LTLRLTGTGGAQLVPAFGCDCAACRRARREESHRRrpCSGVVTFNSAVTLLDAGrPDL---MEHHPAGSFQQVLLTHYHL 79
Cdd:PRK02113   1 MKIRILGSGTSTGVPEIGCTCPVCTSKDPRDNRLR--TSALVETEGARILIDCG-PDFreqMLRLPFGKIDAVLITHEHY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  80 DHVQGLFPLR-WGVGAPIPVYGPPDDAG--------CDDLLKHPGLLDFS-HTVTPFVVFELQGLRVTPLPLNHSKLT-F 148
Cdd:PRK02113  78 DHVGGLDDLRpFCRFGEVPIYAEQYVAErlrsrmpyCFVEHSYPGVPNIPlREIEPDRPFLVNHTEVTPLRVMHGKLPiL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672 149 GYLLesahSRVAWLSDTAGLPDKTLKFLLSNRpqAMIIDcsheprAQTPRNHNDFNTVR-ALNQA--IGCPRVILTHISH 225
Cdd:PRK02113 158 GYRI----GKMAYITDMLTMPEEEYEQLQGID--VLVMN------ALRIAPHPTHQSLEeALENIkrIGAKETYLIHMSH 225

                        250       260
                 ....*....|....*....|....*..
gi 490311672 226 QFDVWM-MDNPLPEGFEAGYDGMEIVL 251
Cdd:PRK02113 226 HIGLHAdVEKELPPHVHFAYDGLEIIF 252
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 52-223 4.31e-12

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: 63.10  E-value: 4.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672   52 LLDAGrPDLME-----HHPAGSFQQ----VLLTHYHLDHVQGLFPLRwgVGAPIPVYGPPddaGCDDLLKHPGLLDFS-- 120
Cdd:pfam12706   4 LIDPG-PDLRQqalpaLQPGRLRDDpidaVLLTHDHYDHLAGLLDLR--EGRPRPLYAPL---GVLAHLRRNFPYLFLle 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  121 ------HTVTPFVVFEL--QGLRVTPLPLNHSK---------LTFGYLLESAHSRVAWLSDTAGLPDKTLKFLlsNRPQA 183
Cdd:pfam12706  78 hygvrvHEIDWGESFTVgdGGLTVTATPARHGSprgldpnpgDTLGFRIEGPGKRVYYAGDTGYFPDEIGERL--GGADL 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 490311672  184 MIID-CSHEPRAQTPRNHNDFN-TVRALnQAIGCPRVILTHI 223
Cdd:pfam12706 156 LLLDgGAWRDDEMIHMGHMTPEeAVEAA-ADLGARRKVLIHI 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 41-130 1.07e-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: 38.69  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672    41 SGVVTFNSAVTLLDAGRPDLMEHHPA------GSFQQVLLTHYHLDHVQGLFPLRWGVGAPIpvYGPPDDAG--CDDLLK 112
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDLLAElkklgpKKIDAIILTHGHPDHIGGLPELLEAPGAPV--YAPEGTAEllKDLLAL 79

                           90
                   ....*....|....*...
gi 490311672   113 HPGLLDFSHTVTPFVVFE 130
Cdd:smart00849  80 LGELGAEAEPAPPDRTLK 97
 
Name Accession Description Interval E-value
PhnP TIGR03307
phosphonate metabolism protein PhnP; This family of proteins found in operons encoding ...
 13-249 1.52e-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: 378.68  E-value: 1.52e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672   13 AQLVPAFGCDCAACRRARREESHRRRPCSGVVTFNSAVTLLDAGRPDLMEHHPAGSFQQVLLTHYHLDHVQGLFPLRWGV 92
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672   93 GAPIPVYGPPDDAGCDDLLKHPGLLDFSHTVTPFVVFELQGLRVTPLPLNHSKLTFGYLLESAHSRVAWLSDTAGLPDKT 172
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKPLEAFEPFDLGGLRVTPLPLVHSKLTFGYLLETDGQRVAYLTDTAGLPPDT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490311672  173 LKFLLSNRPQAMIIDCSHEPRAQTPRNHNDFNTVRALNQAIGCPRVILTHISHQFDVWMMDNP-LPEGFEAGYDGMEI 249
Cdd:TIGR03307 161 EAFLKNHPLDVLILDCSHPPQSDAPRNHNDLTRALAINEQLRPKQVILTHISHQLDAWLMENPdLPSGVAVGYDGQTL 238
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 3-188 2.63e-106

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: 305.32  E-value: 2.63e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672   3 LTLRLTGTGGAQLVPAFGCDCAACRRARREESHRRRPCSGVVTFNSAVTLLDAGRPDLMEHHPAGSFQQVLLTHYHLDHV 82
Cdd:cd07736    1 MKLTFLGTGDAGGVPVYGCDCSACQRARQDPSYRRRPCSALIEVDGERILLDAGLTDLAERFPPGSIDAILLTHFHMDHV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  83 QGLFPLRWGVGAPIPVYGPPDDAGCDDLLKHPGLLDFSHTVTPFVVFELQGLRVTPLPLNHSKLTFGYLLESAHSRVAWL 162
Cdd:cd07736   81 QGLFHLRWGVGDPIPVYGPPDPQGCADLFKHPGILDFQPLVAPFQSFELGGLKITPLPLNHSKPTFGYLLESGGKRLAYL 160

                        170       180
                 ....*....|....*....|....*.
gi 490311672 163 SDTAGLPDKTLKFLLSNRPQAMIIDC 188
Cdd:cd07736  161 TDTLGLPEETLEFLKQQQPDVLVLDC 186
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 3-251 1.91e-54

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 175.85  E-value: 1.91e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672   3 LTLRLTGTGGAQLVPAFGCDCAACRRARREesHRRRPCSGVVTFNSAVTLLDAGrPDLME-----HHPAGSFQQVLLTHY 77
Cdd:COG1235    1 MKVTFLGSGSSGGVPQIGCDCPVCASTDPR--YGRTRSSILVEADGTRLLIDAG-PDLREqllrlGLDPSKIDAILLTHE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  78 HLDHVQGLFPLRWG-VGAPIPVYGPPDDagCDDLLK--------HPGLLDFsHTVTPFVVFELQGLRVTPLPLNHSKL-T 147
Cdd:COG1235   78 HADHIAGLDDLRPRyGPNPIPVYATPGT--LEALERrfpylfapYPGKLEF-HEIEPGEPFEIGGLTVTPFPVPHDAGdP 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672 148 FGYLLESAHSRVAWLSDTAGLPDKTLKFLlsNRPQAMIIDCSHEPRAQtprNHNDFNTVRALNQAIGCPRVILTHIS--- 224
Cdd:COG1235  155 VGYRIEDGGKKLAYATDTGYIPEEVLELL--RGADLLILDATYDDPEP---GHLSNEEALELLARLGPKRLVLTHLSpdn 229

                        250       260       270
                 ....*....|....*....|....*....|
gi 490311672 225 --HQFDVWMMDN-PLPEGFEAGYDGMEIVL 251
Cdd:COG1235  230 ndHELDYDELEAaLLPAGVEVAYDGMEIEL 259
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 3-176 2.83e-27

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: 103.71  E-value: 2.83e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672   3 LTLRLTGTGGAQLVPAFGCDCAACRRArrEESHRRRPCSGVVTFNSAVTLLDAGrPDL---MEHHPAGSFQQVLLTHYHL 79
Cdd:cd16279    1 MKLTFLGTGTSSGVPVIGCDCGVCDSS--DPKNRRLRSSILIETGGKNILIDTG-PDFrqqALRAGIRKLDAVLLTHAHA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  80 DHVQG---LFPLRWGVGAPIPVYGPP----------DDAGCDDLLKHPGLLDFsHTVTPFVVFELQGLRVTPLPLNHSKL 146
Cdd:cd16279   78 DHIHGlddLRPFNRLQQRPIPVYASEetlddlkrrfPYFFAATGGGGVPKLDL-HIIEPDEPFTIGGLEITPLPVLHGKL 156

                        170       180       190
                 ....*....|....*....|....*....|.
gi 490311672 147 -TFGYLLEsahsRVAWLSDTAGLPDKTLKFL 176
Cdd:cd16279  157 pSLGFRFG----DFAYLTDVSEIPEESLEKL 183
PRK02113 PRK02113
MBL fold metallo-hydrolase;
3-251 1.09e-21

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 90.61  E-value: 1.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672   3 LTLRLTGTGGAQLVPAFGCDCAACRRARREESHRRrpCSGVVTFNSAVTLLDAGrPDL---MEHHPAGSFQQVLLTHYHL 79
Cdd:PRK02113   1 MKIRILGSGTSTGVPEIGCTCPVCTSKDPRDNRLR--TSALVETEGARILIDCG-PDFreqMLRLPFGKIDAVLITHEHY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  80 DHVQGLFPLR-WGVGAPIPVYGPPDDAG--------CDDLLKHPGLLDFS-HTVTPFVVFELQGLRVTPLPLNHSKLT-F 148
Cdd:PRK02113  78 DHVGGLDDLRpFCRFGEVPIYAEQYVAErlrsrmpyCFVEHSYPGVPNIPlREIEPDRPFLVNHTEVTPLRVMHGKLPiL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672 149 GYLLesahSRVAWLSDTAGLPDKTLKFLLSNRpqAMIIDcsheprAQTPRNHNDFNTVR-ALNQA--IGCPRVILTHISH 225
Cdd:PRK02113 158 GYRI----GKMAYITDMLTMPEEEYEQLQGID--VLVMN------ALRIAPHPTHQSLEeALENIkrIGAKETYLIHMSH 225

                        250       260
                 ....*....|....*....|....*..
gi 490311672 226 QFDVWM-MDNPLPEGFEAGYDGMEIVL 251
Cdd:PRK02113 226 HIGLHAdVEKELPPHVHFAYDGLEIIF 252
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
5-228 2.43e-21

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 89.48  E-value: 2.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672   5 LRLT--GTGGAqlVPAfgcdcaacrrarreeshRRRPCSGV-VTFNSAVTLLDAGR--PDLMEHHPAgSFQQ---VLLTH 76
Cdd:COG1234    1 MKLTflGTGGA--VPT-----------------PGRATSSYlLEAGGERLLIDCGEgtQRQLLRAGL-DPRDidaIFITH 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  77 YHLDHVQGLFPL---RW--GVGAPIPVYGPPddaGCDDLLKH-----PGLLDFS---HTVTPFVVFELQGLRVTPLPLNH 143
Cdd:COG1234   61 LHGDHIAGLPGLlstRSlaGREKPLTIYGPP---GTKEFLEAllkasGTDLDFPlefHEIEPGEVFEIGGFTVTAFPLDH 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672 144 SKLTFGYLLESAHSRVAWLSDTAglPDKTLKFLLSNrPQAMIIDCSH-EPRAQTPRNHNDFNTVRALN--QAIGCPRVIL 220
Cdd:COG1234  138 PVPAYGYRFEEPGRSLVYSGDTR--PCEALVELAKG-ADLLIHEATFlDEEAELAKETGHSTAKEAAElaAEAGVKRLVL 214


                 ....*...
gi 490311672 221 THISHQFD 228
Cdd:COG1234  215 THFSPRYD 222
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 9-249 1.73e-14

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: 70.56  E-value: 1.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672   9 GTGGAqlVPafgcdcaacrrarreeSHRRRPCSGVVTFNSAVTLLDAG----RPdLMEHHpaGSFQQV---LLTHYHLDH 81
Cdd:cd07717    5 GTGSA--VP----------------TPERNLSSIALRLEGELWLFDCGegtqRQ-LLRAG--LSPSKIdriFITHLHGDH 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  82 VQGLFPL-----RWGVGAPIPVYGPPddaGCDDLLKHpgLLDFSHTVTPF------------VVFELQGLRVTPLPLNHS 144
Cdd:cd07717   64 ILGLPGLlstmsLLGRTEPLTIYGPK---GLKEFLET--LLRLSASRLPYpievhelepdpgLVFEDDGFTVTAFPLDHR 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672 145 KLTFGYLLESAHSrVAWLSDTAglPDKTLKFLLSNrPQAMIIDC----SHEPRAQtPRNHNDFNTVRALNQAIGCPRVIL 220
Cdd:cd07717  139 VPCFGYRFEEGRK-IAYLGDTR--PCEGLVELAKG-ADLLIHEAtfldDDAEKAK-ETGHSTAKQAAEIAKKAGVKKLVL 213

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 490311672 221 THISHqfdvwMMDNPLP------EGF---EAGYDGMEI 249
Cdd:cd07717  214 THFSA-----RYKDPEEllkearAVFpntILAEDFMTI 246
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 34-166 1.17e-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: 67.29  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  34 SHRRRPCSGVVTFNSAVTLLDAGR---PDLMEHH-PAGSFQQVLLTHYHLDHVQGLFPLRW-----GVGAPIPVYGPPDD 104
Cdd:cd16272   12 SLTRNTSSYLLETGGTRILLDCGEgtvYRLLKAGvDPDKLDAIFLSHFHLDHIGGLPTLLFarrygGRKKPLTIYGPKGI 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672 105 A-------GCDDLLKHPGL-LDFSHTVTPFVVFELQGLRVTPLPLNHSKLTFGYLLESAHSRVAWLSDTA 166
Cdd:cd16272   92 KeflekllNFPVEILPLGFpLEIEELEEGGEVLELGDLKVEAFPVKHSVESLGYRIEAEGKSIVYSGDTG 161
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 52-223 4.31e-12

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: 63.10  E-value: 4.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672   52 LLDAGrPDLME-----HHPAGSFQQ----VLLTHYHLDHVQGLFPLRwgVGAPIPVYGPPddaGCDDLLKHPGLLDFS-- 120
Cdd:pfam12706   4 LIDPG-PDLRQqalpaLQPGRLRDDpidaVLLTHDHYDHLAGLLDLR--EGRPRPLYAPL---GVLAHLRRNFPYLFLle 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  121 ------HTVTPFVVFEL--QGLRVTPLPLNHSK---------LTFGYLLESAHSRVAWLSDTAGLPDKTLKFLlsNRPQA 183
Cdd:pfam12706  78 hygvrvHEIDWGESFTVgdGGLTVTATPARHGSprgldpnpgDTLGFRIEGPGKRVYYAGDTGYFPDEIGERL--GGADL 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 490311672  184 MIID-CSHEPRAQTPRNHNDFN-TVRALnQAIGCPRVILTHI 223
Cdd:pfam12706 156 LLLDgGAWRDDEMIHMGHMTPEeAVEAA-ADLGARRKVLIHI 196
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 38-166 8.87e-12

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: 61.69  E-value: 8.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  38 RPCSG-VVTFNSAVTLLDAG-----RpdLMEHHPAGSFQQVLLTHYHLDHVQGLFPLR--------WGVGAPIPVYGPPD 103
Cdd:cd07716   16 GACSGyLLEADGFRILLDCGsgvlsR--LQRYIDPEDLDAVVLSHLHPDHCADLGVLQyarryhprGARKPPLPLYGPAG 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490311672 104 DAGCDDLLK-HPGLLDFsHTVTPFVVFELQGLRVTPLPLNHSKLTFGYLLESAHSRVAWLSDTA 166
Cdd:cd07716   94 PAERLAALYgLEDVFDF-HPIEPGEPLEIGPFTITFFRTVHPVPCYAMRIEDGGKVLVYTGDTG 156
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 4-166 2.18e-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: 60.99  E-value: 2.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672   4 TLRLTGTGGAQLVPafgcdcaacrrarreesHRRRPCSGVVTfNSAVTLLDAGRpdlmehhpaGSFQQ------------ 71
Cdd:cd07719    1 RVTLLGTGGPIPDP-----------------DRAGPSTLVVV-GGRVYLVDAGS---------GVVRRlaqaglplgdld 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  72 -VLLTHYHLDHVQGLFPL---RWGVGA--PIPVYGPP--------------DDAGCDDLLKHPGLLDFSHTVT------P 125
Cdd:cd07719   54 aVFLTHLHSDHVADLPALlltAWLAGRktPLPVYGPPgtralvdgllaayaLDIDYRARIGDEGRPDPGALVEvheiaaG 133

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 490311672 126 FVVFELQGLRVTPLPLNHS--KLTFGYLLESAHSRVAWLSDTA 166
Cdd:cd07719  134 GVVYEDDGVKVTAFLVDHGpvPPALAYRFDTPGRSVVFSGDTG 176
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 52-165 2.37e-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: 61.36  E-value: 2.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  52 LLDAG---RP---DLMEHHPAGSFQqVLLTHYHLDHVQGL--FplrwgvgAP--IP-----VYGPPDDAGC-----DDLL 111
Cdd:cd07715   36 ILDAGtgiRElgnELMKEGPPGEAH-LLLSHTHWDHIQGFpfF-------APayDPgnrihIYGPHKDGGSleevlRRQM 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490311672 112 KHP----GLLDFS-----HTVTPFVVFELQGLRVTPLPLNHSKLTFGYLLESAHSRVAWLSDT 165
Cdd:cd07715  108 SPPyfpvPLEELLaaiefHDLEPGEPFSIGGVTVTTIPLNHPGGALGYRIEEDGKSVVYATDT 170
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 72-189 7.81e-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: 7.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  72 VLLTHYHLDHVQGLfPL-----RWGVGAPIPVYGPPDDagCDDLLKH-------PGLLDFSHTVTPFVVFE--------- 130
Cdd:cd07735   69 YLITHAHLDHIAGL-PLlspndGGQRGSPKTIYGLPET--IDALKKHifnwviwPDFTSIPSGKYPYLRLEpiepeypia 145

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490311672 131 LQGLRVTPLPLNHSKL-TFGYLLESAHSRVAWLSDT------------------AGLPDKTLKfllsnrpqAMIIDCS 189
Cdd:cd07735  146 LTGLSVTAFPVSHGVPvSTAFLIRDGGDSFLFFGDTgpdsvsksprldalwralAPLIPKKLK--------AIIIECS 215
PQQB-like_MBL-fold cd16274
Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold ...
 5-141 5.26e-08

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: 51.85  E-value: 5.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672   5 LRLTGT---GGaqlVPAFGCDCAACRRARREES--HRRRPCSGVVTFNSAVTLLDAGRPDL---MEHHPAGSFQQ----- 71
Cdd:cd16274    3 IKVLGSaagGG---FPQWNCNCPNCALARAGDGraTARTQSSIAVSADGENWVLINASPDIrqqIEATPELQPRPglrdt 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  72 ----VLLTHYHLDHVQGLFPLRwgVGAPIPVYGPP-------DDAGCDDLLKHPGLLDFsHTVTPFVVFELQ---GLRVT 137
Cdd:cd16274   80 piaaVLLTDAEIDHTTGLLSLR--EGQPLTVYATApvledltTNFPFFVLLHAYGGVRR-HRILPGEPFTLAgcpGLTVT 156


                 ....
gi 490311672 138 PLPL 141
Cdd:cd16274  157 PFPV 160
PRK05184 PRK05184
pyrroloquinoline quinone biosynthesis protein PqqB; Provisional
 11-251 7.42e-08

pyrroloquinoline quinone biosynthesis protein PqqB; Provisional


Pssm-ID: 235361 [Multi-domain]  Cd Length: 302  Bit Score: 52.13  E-value: 7.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  11 GGaqlVPAFGCDCAACRRARREESH-RRRPCSGVvtfnsAVT-------LLDAGrPDLM-------EHHPAGSF-----Q 70
Cdd:PRK05184  12 GG---FPQWNCNCPNCRGARAGTIRaKPRTQSSI-----AVSadgedwvLLNAS-PDIRqqiqatpALQPARGLrdtpiA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  71 QVLLTHYHLDHVQGLFPLRwgVGAPIPVYGPPD--DAGCD-----DLLKHPGLLDFsHTVT---PFVVFELQGLRVTPLP 140
Cdd:PRK05184  83 AVVLTDGQIDHTTGLLTLR--EGQPFPVYATPAvlEDLSTgfpifNVLDHYGGVQR-RPIAldgPFAVPGLPGLRFTAFP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672 141 L-------------NHSKLTFGYLLESAHSR----------------VAWLSD-----------------TAGLPDKTlk 174
Cdd:PRK05184 160 VpskappysphrsdPEPGDNIGLRIEDRATGkrlfyapglaevtdalRARLAGadcvlfdgtlwtddemiRAGVGTKT-- 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672 175 fllsnrPQAMiidcSHEPRAqtprnhNDFNTVRALNQaIGCPRVILTHISHQFDVWMMDNP-----LPEGFEAGYDGMEI 249
Cdd:PRK05184 238 ------GRRM----GHLPQS------GPGGMIAALAR-LPIARKILIHINNTNPILDEDSPeraelEAAGIEVAHDGMEI 300


                 ..
gi 490311672 250 VL 251
Cdd:PRK05184 301 EL 302
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 9-153 2.71e-06

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: 47.60  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672    9 GTGGAqlVPafgcdcaacrrarreeSHRRRPCSGVVTFNSAVTLLDAG----RPdlMEHHPAgSFQQV---LLTHYHLDH 81
Cdd:TIGR02651   6 GTGGG--VP----------------TKERNLPSIALKLNGELWLFDCGegtqRQ--MLRSGI-SPMKIdriFITHLHGDH 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672   82 VQGLFPL-----RWGVGAPIPVYGPPddaGCDDLLKHpgLLDFS----------HTVTPF-VVFELQGLRVTPLPLNHSK 145
Cdd:TIGR02651  65 ILGLPGLlstmsFQGRKEPLTIYGPP---GIKEFIET--SLRVSytylnypikiHEIEEGgLVFEDDGFKVEAFPLDHSI 139


                  ....*...
gi 490311672  146 LTFGYLLE 153
Cdd:TIGR02651 140 PSLGYRFE 147
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 72-170 5.36e-06

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 46.06  E-value: 5.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  72 VLLTHYHLDHV--QGLFPLRwgvGAPIPVYGPPDDAgcdDLLKHPGLLDFsHTVTPFVVFELQGLRVTPLPLNHS----- 144
Cdd:COG2220   52 VLVTHDHYDHLddATLRALK---RTGATVVAPLGVA---AWLRAWGFPRV-TELDWGESVELGGLTVTAVPARHSsgrpd 124

                         90       100
                 ....*....|....*....|....*....
gi 490311672 145 ---KLTFGYLLESAHSRVAWLSDTAGLPD 170
Cdd:COG2220  125 rngGLWVGFVIETDGKTIYHAGDTGYFPE 153
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 72-130 1.08e-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: 44.97  E-value: 1.08e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490311672  72 VLLTHYHLDHVQGLFPLRWGVGApiPVYGPPDDAgcdDLLKHPGLLDFSHTVTPFVVFE 130
Cdd:cd06262   49 ILLTHGHFDHIGGLAELKEAPGA--PVYIHEADA---ELLEDPELNLAFFGGGPLPPPE 102
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 52-165 1.32e-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: 43.79  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  52 LLDAGRP--------DLMEHHPAgSFQQVLLTHYHLDHVQGLFPL--RWGVgapiPVYGPPDDAGCDDLLKHPGLLDFSH 121
Cdd:cd07733   22 LIDAGLSgrkitgrlAEIGRDPE-DIDAILVTHEHADHIKGLGVLarKYNV----PIYATAGTLRAMERKVGLIDVDQKQ 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 490311672 122 TVTPFVVFELQGLRVTPLPLNHSKL-TFGYLLESAHSRVAWLSDT 165
Cdd:cd07733   97 IFEPGETFSIGDFDVESFGVSHDAAdPVGYRFEEGGRRFGMLTDL 141
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 41-144 1.75e-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: 44.30  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  41 SGVVTFNSAVTLLDAGRPDLMEHHPAGSFQQ-------VLLTHYHLDHVQGLFPLRWGVGAPIpvYGPPDDAgcdDLLKH 113
Cdd:COG0491   17 SYLIVGGDGAVLIDTGLGPADAEALLAALAAlgldikaVLLTHLHPDHVGGLAALAEAFGAPV--YAHAAEA---EALEA 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 490311672 114 PGLLDF--------SHTVTPFVVFELQGLRVTPLPLN-HS 144
Cdd:COG0491   92 PAAGALfgrepvppDRTLEDGDTLELGGPGLEVIHTPgHT 131
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 72-175 9.28e-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: 42.18  E-value: 9.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  72 VLLTHYHLDH-----------VQGLFPLRwGVgapipVYGpPDDA--GCDDLLK--HPGLLDFSHTVTPFVVFELQGLRV 136
Cdd:cd07741   57 IILSHRHLDHsndanvlieamTEGGFKKR-GT-----LLA-PEDAlnGEPVVLLyyHRRKLEEIEILEEGDEYELGGIKI 129

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 490311672 137 TPLPLNHS-KLTFGYLLESAHSRVAWLSDTAGLPDKTLKF 175
Cdd:cd07741  130 EATRHKHSdPTTYGFIFRTSDKKIGYISDTRYFEELIEYY 169
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 52-121 3.36e-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: 40.21  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  52 LLDAGRP---------DLMEHHPAGSFQQVLLTHYHLDHVQGLFPLR-WGVGAPIPVYG-PPDDAGCDDLLKHPGLLDFS 120
Cdd:cd07722   31 LIDTGEGrpsyipllkSVLDSEGNATISDILLTHWHHDHVGGLPDVLdLLRGPSPRVYKfPRPEEDEDPDEDGGDIHDLQ 110


                 .
gi 490311672 121 H 121
Cdd:cd07722  111 D 111
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 72-113 4.40e-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: 39.75  E-value: 4.40e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 490311672  72 VLLTHYHLDHVQGLFPL--RWGvgaPIPVYGPPDD--AGCDDLLKH 113
Cdd:cd07723   47 ILTTHHHWDHTGGNAELkaLFP---DAPVYGPAEDriPGLDHPVKD 89
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-166 6.97e-04

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 39.55  E-value: 6.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  35 HRRRPCSGVVTfNSAVTLLDAGRPDLMEHHPAG----SFQQVLLTHYHLDHVQGLfP-------LRWGVGAPIPVYGPPd 103
Cdd:cd07740   13 GRLNTCFHVAS-EAGRFLIDCGASSLIALKRAGidpnAIDAIFITHLHGDHFGGL-PfflldaqFVAKRTRPLTIAGPP- 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490311672 104 daGCDDLLKH------PG----LLDFSHTVT---PFVVFELQGLRVTPLPLNHSKLTFGYLLESAHSR--VAWLSDTA 166
Cdd:cd07740   90 --GLRERLRRamealfPGsskvPRRFDLEVIelePGEPTTLGGVTVTAFPVVHPSGALPLALRLEAAGrvLAYSGDTE 165
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 43-108 7.21e-04

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 39.40  E-value: 7.21e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490311672  43 VVTFNSAVTLLDAGrPDLMEHH-------PAGSFQQVLLTHYHLDHVQGLFPLRWGVGAPIPVYGPPDDAGCD 108
Cdd:cd16278   22 LLGAPDGVVVIDPG-PDDPAHLdallaalGGGRVSAILVTHTHRDHSPGAARLAERTGAPVRAFGPHRAGGQD 93
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 41-130 1.07e-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: 38.69  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672    41 SGVVTFNSAVTLLDAGRPDLMEHHPA------GSFQQVLLTHYHLDHVQGLFPLRWGVGAPIpvYGPPDDAG--CDDLLK 112
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDLLAElkklgpKKIDAIILTHGHPDHIGGLPELLEAPGAPV--YAPEGTAEllKDLLAL 79

                           90
                   ....*....|....*...
gi 490311672   113 HPGLLDFSHTVTPFVVFE 130
Cdd:smart00849  80 LGELGAEAEPAPPDRTLK 97
PRK00055 PRK00055
ribonuclease Z; Reviewed
 72-102 2.26e-03

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 38.62  E-value: 2.26e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 490311672  72 VLLTHYHLDHVQGLFPL-----RWGVGAPIPVYGPP 102
Cdd:PRK00055  57 IFITHLHGDHIFGLPGLlstrsLSGRTEPLTIYGPK 92
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 72-144 7.22e-03

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. 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: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 37.00  E-value: 7.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490311672  72 VLLTHYHLDHvqglfplrwgVGA--------PIPVYGPPDDAGC--DDLLKHPGLLDFS-HTVTPFVVFELQGLRVTPLP 140
Cdd:cd07714   59 IFITHGHEDH----------IGAlpyllpelNVPIYATPLTLALikKKLEEFKLIKKVKlNEIKPGERIKLGDFEVEFFR 128


                 ....
gi 490311672 141 LNHS 144
Cdd:cd07714  129 VTHS 132
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 72-105 7.44e-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: 36.43  E-value: 7.44e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 490311672  72 VLLTHYHLDHVQGLFPLR--WGVgapiPVYGPPDDA 105
Cdd:cd07721   53 ILLTHGHIDHIGSLAALKeaPGA----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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