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Conserved domains on  [gi|1706422444|ref|WP_142805320|]
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phosphonate metabolism protein PhnP [Tepidiphilus sp. J10]

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; ...
 11-249 2.60e-145

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: 406.03  E-value: 2.60e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  11 AGGVPLYGCDCSACTRARAVADFRRRPCTALVEAGDTRILLDAGLTDLTERFPPGSLSAIVLTHFHPDHVQGLFHLRWGI 90
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  91 GPSIPVFAPPDTEGCADLYKNHGLLEFRR-LSKFEPVMIGNLVLTPLPLNHSKATFGYAIeETDGQRFAYLTDTAGLPPP 169
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKpLEAFEPFDLGGLRVTPLPLVHSKLTFGYLL-ETDGQRVAYLTDTAGLPPD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444 170 TEAFLKKWRPASFALDCSYPPQSDLPRNHNDLTLALAIAETLAPARVWLTHVSHELDAWLLKNIGnLPPHMAVAYDSQVV 249
Cdd:TIGR03307 160 TEAFLKNHPLDVLILDCSHPPQSDAPRNHNDLTRALAINEQLRPKQVILTHISHQLDAWLMENPD-LPSGVAVGYDGQTL 238
 
Name Accession Description Interval E-value
PhnP TIGR03307
phosphonate metabolism protein PhnP; This family of proteins found in operons encoding ...
 11-249 2.60e-145

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: 406.03  E-value: 2.60e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  11 AGGVPLYGCDCSACTRARAVADFRRRPCTALVEAGDTRILLDAGLTDLTERFPPGSLSAIVLTHFHPDHVQGLFHLRWGI 90
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  91 GPSIPVFAPPDTEGCADLYKNHGLLEFRR-LSKFEPVMIGNLVLTPLPLNHSKATFGYAIeETDGQRFAYLTDTAGLPPP 169
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKpLEAFEPFDLGGLRVTPLPLVHSKLTFGYLL-ETDGQRVAYLTDTAGLPPD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444 170 TEAFLKKWRPASFALDCSYPPQSDLPRNHNDLTLALAIAETLAPARVWLTHVSHELDAWLLKNIGnLPPHMAVAYDSQVV 249
Cdd:TIGR03307 160 TEAFLKNHPLDVLILDCSHPPQSDAPRNHNDLTRALAINEQLRPKQVILTHISHQLDAWLMENPD-LPSGVAVGYDGQTL 238
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 1-186 1.25e-108

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: 311.09  E-value: 1.25e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   1 MRITFLGTGDAGGVPLYGCDCSACTRARAVADFRRRPCTALVEAGDTRILLDAGLTDLTERFPPGSLSAIVLTHFHPDHV 80
Cdd:cd07736     1 MKLTFLGTGDAGGVPVYGCDCSACQRARQDPSYRRRPCSALIEVDGERILLDAGLTDLAERFPPGSIDAILLTHFHMDHV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  81 QGLFHLRWGIGPSIPVFAPPDTEGCADLYKNHGLLEFRRLSK-FEPVMIGNLVLTPLPLNHSKATFGYAIeETDGQRFAY 159
Cdd:cd07736    81 QGLFHLRWGVGDPIPVYGPPDPQGCADLFKHPGILDFQPLVApFQSFELGGLKITPLPLNHSKPTFGYLL-ESGGKRLAY 159

                         170       180
                  ....*....|....*....|....*..
gi 1706422444 160 LTDTAGLPPPTEAFLKKWRPASFALDC 186
Cdd:cd07736   160 LTDTLGLPEETLEFLKQQQPDVLVLDC 186
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-250 7.71e-67

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 207.83  E-value: 7.71e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   1 MRITFLGTGDAGGVPLYGCDCSACtrARAVADFRRRPCTALVEAGDTRILLDAGlTDLTERF-----PPGSLSAIVLTHF 75
Cdd:COG1235     1 MKVTFLGSGSSGGVPQIGCDCPVC--ASTDPRYGRTRSSILVEADGTRLLIDAG-PDLREQLlrlglDPSKIDAILLTHE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  76 HPDHVQGLFHLRWGIGPS-IPVFAPPDTegCADLYKN--------HGLLEFRRLSKFEPVMIGNLVLTPLPLNHSKA-TF 145
Cdd:COG1235    78 HADHIAGLDDLRPRYGPNpIPVYATPGT--LEALERRfpylfapyPGKLEFHEIEPGEPFEIGGLTVTPFPVPHDAGdPV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444 146 GYAIeETDGQRFAYLTDTAGLPPPTEAFLKKwrPASFALDCSYppqsDLPR-NHNDLTLALAIAETLAPARVWLTHVS-- 222
Cdd:COG1235   156 GYRI-EDGGKKLAYATDTGYIPEEVLELLRG--ADLLILDATY----DDPEpGHLSNEEALELLARLGPKRLVLTHLSpd 228

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1706422444 223 ---HELDAWLLKNIgNLPPHMAVAYDSQVVS 250
Cdd:COG1235   229 nndHELDYDELEAA-LLPAGVEVAYDGMEIE 258
PRK02113 PRK02113
MBL fold metallo-hydrolase;
1-245 3.63e-24

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 97.16  E-value: 3.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   1 MRITFLGTGDAGGVPLYGCDCSACTRARAvADFRRRpCTALVEAGDTRILLDAGlTDLTE---RFPPGSLSAIVLTHFHP 77
Cdd:PRK02113    1 MKIRILGSGTSTGVPEIGCTCPVCTSKDP-RDNRLR-TSALVETEGARILIDCG-PDFREqmlRLPFGKIDAVLITHEHY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  78 DHVQGLFHLR-WGIGPSIPVFAPPDT-EGCAD---------LYKNHGLLEFRRLSKFEPVMIGNLVLTPLPLNHSK-ATF 145
Cdd:PRK02113   78 DHVGGLDDLRpFCRFGEVPIYAEQYVaERLRSrmpycfvehSYPGVPNIPLREIEPDRPFLVNHTEVTPLRVMHGKlPIL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444 146 GYAIeetdgQRFAYLTDTAGLPPPTEAFLKKWRPASFALDCSYPPQSdlprnHNDLTLALAIAETLAPARVWLTHVSHE- 224
Cdd:PRK02113  158 GYRI-----GKMAYITDMLTMPEEEYEQLQGIDVLVMNALRIAPHPT-----HQSLEEALENIKRIGAKETYLIHMSHHi 227

                         250       260
                  ....*....|....*....|..
gi 1706422444 225 -LDAWLLKnigNLPPHMAVAYD 245
Cdd:PRK02113  228 gLHADVEK---ELPPHVHFAYD 246
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 47-220 7.75e-17

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: 76.19  E-value: 7.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  47 TRILLDAGLtDLTERFPP---------GSLSAIVLTHFHPDHVQGLFHLRwgIGPSIPVFAPPDT------EGCADLYKN 111
Cdd:pfam12706   1 RRILIDPGP-DLRQQALPalqpgrlrdDPIDAVLLTHDHYDHLAGLLDLR--EGRPRPLYAPLGVlahlrrNFPYLFLLE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444 112 HGLLEFRRLSKFEPVMIG--NLVLTPLPLNHSKA---------TFGYAIeETDGQRFAYLTDTAGLPPPTEAFLkkwRPA 180
Cdd:pfam12706  78 HYGVRVHEIDWGESFTVGdgGLTVTATPARHGSPrgldpnpgdTLGFRI-EGPGKRVYYAGDTGYFPDEIGERL---GGA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1706422444 181 SFALD--CSYPPQSDLPRNHNDLTLALAIAETLAPARVWLTH 220
Cdd:pfam12706 154 DLLLLdgGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIH 195
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 41-151 2.63e-09

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: 55.25  E-value: 2.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   41 LVEAGDTRILLDAGLTDLT------ERFPPGSLSAIVLTHFHPDHVQGLFHLRWgiGPSIPVFAPPDT---------EGC 105
Cdd:smart00849   4 LVRDDGGAILIDTGPGEAEdllaelKKLGPKKIDAIILTHGHPDHIGGLPELLE--APGAPVYAPEGTaellkdllaLLG 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1706422444  106 ADLYKNHGLLEFRRLSKFEPVMIGNLVLTPLPL-NHSKATFGYAIEE 151
Cdd:smart00849  82 ELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTpGHTPGSIVLYLPE 128
 
Name Accession Description Interval E-value
PhnP TIGR03307
phosphonate metabolism protein PhnP; This family of proteins found in operons encoding ...
 11-249 2.60e-145

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: 406.03  E-value: 2.60e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  11 AGGVPLYGCDCSACTRARAVADFRRRPCTALVEAGDTRILLDAGLTDLTERFPPGSLSAIVLTHFHPDHVQGLFHLRWGI 90
Cdd:TIGR03307   1 AQQVPVYGCDCVACQRARRNPDYRRQPCSAVIEFNGARTLIDAGLTDLAERFPPGSLQAILLTHYHMDHVQGLFPLRWGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  91 GPSIPVFAPPDTEGCADLYKNHGLLEFRR-LSKFEPVMIGNLVLTPLPLNHSKATFGYAIeETDGQRFAYLTDTAGLPPP 169
Cdd:TIGR03307  81 GEPIPVYGPPDEEGCDDLFKHPGILDFSKpLEAFEPFDLGGLRVTPLPLVHSKLTFGYLL-ETDGQRVAYLTDTAGLPPD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444 170 TEAFLKKWRPASFALDCSYPPQSDLPRNHNDLTLALAIAETLAPARVWLTHVSHELDAWLLKNIGnLPPHMAVAYDSQVV 249
Cdd:TIGR03307 160 TEAFLKNHPLDVLILDCSHPPQSDAPRNHNDLTRALAINEQLRPKQVILTHISHQLDAWLMENPD-LPSGVAVGYDGQTL 238
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 1-186 1.25e-108

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: 311.09  E-value: 1.25e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   1 MRITFLGTGDAGGVPLYGCDCSACTRARAVADFRRRPCTALVEAGDTRILLDAGLTDLTERFPPGSLSAIVLTHFHPDHV 80
Cdd:cd07736     1 MKLTFLGTGDAGGVPVYGCDCSACQRARQDPSYRRRPCSALIEVDGERILLDAGLTDLAERFPPGSIDAILLTHFHMDHV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  81 QGLFHLRWGIGPSIPVFAPPDTEGCADLYKNHGLLEFRRLSK-FEPVMIGNLVLTPLPLNHSKATFGYAIeETDGQRFAY 159
Cdd:cd07736    81 QGLFHLRWGVGDPIPVYGPPDPQGCADLFKHPGILDFQPLVApFQSFELGGLKITPLPLNHSKPTFGYLL-ESGGKRLAY 159

                         170       180
                  ....*....|....*....|....*..
gi 1706422444 160 LTDTAGLPPPTEAFLKKWRPASFALDC 186
Cdd:cd07736   160 LTDTLGLPEETLEFLKQQQPDVLVLDC 186
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-250 7.71e-67

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 207.83  E-value: 7.71e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   1 MRITFLGTGDAGGVPLYGCDCSACtrARAVADFRRRPCTALVEAGDTRILLDAGlTDLTERF-----PPGSLSAIVLTHF 75
Cdd:COG1235     1 MKVTFLGSGSSGGVPQIGCDCPVC--ASTDPRYGRTRSSILVEADGTRLLIDAG-PDLREQLlrlglDPSKIDAILLTHE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  76 HPDHVQGLFHLRWGIGPS-IPVFAPPDTegCADLYKN--------HGLLEFRRLSKFEPVMIGNLVLTPLPLNHSKA-TF 145
Cdd:COG1235    78 HADHIAGLDDLRPRYGPNpIPVYATPGT--LEALERRfpylfapyPGKLEFHEIEPGEPFEIGGLTVTPFPVPHDAGdPV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444 146 GYAIeETDGQRFAYLTDTAGLPPPTEAFLKKwrPASFALDCSYppqsDLPR-NHNDLTLALAIAETLAPARVWLTHVS-- 222
Cdd:COG1235   156 GYRI-EDGGKKLAYATDTGYIPEEVLELLRG--ADLLILDATY----DDPEpGHLSNEEALELLARLGPKRLVLTHLSpd 228

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1706422444 223 ---HELDAWLLKNIgNLPPHMAVAYDSQVVS 250
Cdd:COG1235   229 nndHELDYDELEAA-LLPAGVEVAYDGMEIE 258
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 1-175 9.47e-40

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: 136.06  E-value: 9.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   1 MRITFLGTGDAGGVPLYGCDCSACTRArAVADFRRRpCTALVEAGDTRILLDAGlTDLTE---RFPPGSLSAIVLTHFHP 77
Cdd:cd16279     1 MKLTFLGTGTSSGVPVIGCDCGVCDSS-DPKNRRLR-SSILIETGGKNILIDTG-PDFRQqalRAGIRKLDAVLLTHAHA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  78 DHVQGLFHLR---WGIGPSIPVFAPPDTEG----------CADLYKNHGLLEFRRLSKFEPVMIGNLVLTPLPLNHSK-A 143
Cdd:cd16279    78 DHIHGLDDLRpfnRLQQRPIPVYASEETLDdlkrrfpyffAATGGGGVPKLDLHIIEPDEPFTIGGLEITPLPVLHGKlP 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1706422444 144 TFGYAIEetdgqRFAYLTDTAGLPPPTEAFLK 175
Cdd:cd16279   158 SLGFRFG-----DFAYLTDVSEIPEESLEKLR 184
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-226 5.48e-34

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 123.00  E-value: 5.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   1 MRITFLGTGdaGGVPLygcdcsactraravadfRRRPCTA-LVEAGDTRILLDAG------LTDLteRFPPGSLSAIVLT 73
Cdd:COG1234     1 MKLTFLGTG--GAVPT-----------------PGRATSSyLLEAGGERLLIDCGegtqrqLLRA--GLDPRDIDAIFIT 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  74 HFHPDHVQGLFHL---RW--GIGPSIPVFAPPDT----EGCADLYKNHGL--LEFRRLSKFEPVMIGNLVLTPLPLNHSK 142
Cdd:COG1234    60 HLHGDHIAGLPGLlstRSlaGREKPLTIYGPPGTkeflEALLKASGTDLDfpLEFHEIEPGEVFEIGGFTVTAFPLDHPV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444 143 ATFGYAIEEtDGQRFAYLTDTAglppPTEAFLKKWRPASFAL-DCSYPPQSD---LPRNHNDLTLALAIAETLAPARVWL 218
Cdd:COG1234   140 PAYGYRFEE-PGRSLVYSGDTR----PCEALVELAKGADLLIhEATFLDEEAelaKETGHSTAKEAAELAAEAGVKRLVL 214


                  ....*...
gi 1706422444 219 THVSHELD 226
Cdd:COG1234   215 THFSPRYD 222
PRK02113 PRK02113
MBL fold metallo-hydrolase;
1-245 3.63e-24

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 97.16  E-value: 3.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   1 MRITFLGTGDAGGVPLYGCDCSACTRARAvADFRRRpCTALVEAGDTRILLDAGlTDLTE---RFPPGSLSAIVLTHFHP 77
Cdd:PRK02113    1 MKIRILGSGTSTGVPEIGCTCPVCTSKDP-RDNRLR-TSALVETEGARILIDCG-PDFREqmlRLPFGKIDAVLITHEHY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  78 DHVQGLFHLR-WGIGPSIPVFAPPDT-EGCAD---------LYKNHGLLEFRRLSKFEPVMIGNLVLTPLPLNHSK-ATF 145
Cdd:PRK02113   78 DHVGGLDDLRpFCRFGEVPIYAEQYVaERLRSrmpycfvehSYPGVPNIPLREIEPDRPFLVNHTEVTPLRVMHGKlPIL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444 146 GYAIeetdgQRFAYLTDTAGLPPPTEAFLKKWRPASFALDCSYPPQSdlprnHNDLTLALAIAETLAPARVWLTHVSHE- 224
Cdd:PRK02113  158 GYRI-----GKMAYITDMLTMPEEEYEQLQGIDVLVMNALRIAPHPT-----HQSLEEALENIKRIGAKETYLIHMSHHi 227

                         250       260
                  ....*....|....*....|..
gi 1706422444 225 -LDAWLLKnigNLPPHMAVAYD 245
Cdd:PRK02113  228 gLHADVEK---ELPPHVHFAYD 246
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 3-164 8.35e-23

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: 91.94  E-value: 8.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   3 ITFLGTGdaGGVPlygcdcsactraravaDFRRRPCTALVEAGDTRILLDAG------LtdLTERFPPGSLSAIVLTHFH 76
Cdd:cd16272     1 LTFLGTG--GAVP----------------SLTRNTSSYLLETGGTRILLDCGegtvyrL--LKAGVDPDKLDAIFLSHFH 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  77 PDHVQGLFHLRW-----GIGPSIPVFAPPDTEGCADLYKNHGL--------LEFRRLSKFEPV-MIGNLVLTPLPLNHSK 142
Cdd:cd16272    61 LDHIGGLPTLLFarrygGRKKPLTIYGPKGIKEFLEKLLNFPVeilplgfpLEIEELEEGGEVlELGDLKVEAFPVKHSV 140

                         170       180
                  ....*....|....*....|..
gi 1706422444 143 ATFGYAIEEtDGQRFAYLTDTA 164
Cdd:cd16272   141 ESLGYRIEA-EGKSIVYSGDTG 161
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 36-164 5.03e-22

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: 89.42  E-value: 5.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  36 RPCTA-LVEAGDTRILLDAG---LTDLTERFPPGSLSAIVLTHFHPDHVQGLFHLR--WGIGPS------IPVFAPPDTE 103
Cdd:cd07716    16 GACSGyLLEADGFRILLDCGsgvLSRLQRYIDPEDLDAVVLSHLHPDHCADLGVLQyaRRYHPRgarkppLPLYGPAGPA 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1706422444 104 GC-ADLYKNHGLLEFRRLSKFEPVMIGNLVLTPLPLNHSKATFGYAIEEtDGQRFAYLTDTA 164
Cdd:cd07716    96 ERlAALYGLEDVFDFHPIEPGEPLEIGPFTITFFRTVHPVPCYAMRIED-GGKVLVYTGDTG 156
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 47-220 7.75e-17

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: 76.19  E-value: 7.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  47 TRILLDAGLtDLTERFPP---------GSLSAIVLTHFHPDHVQGLFHLRwgIGPSIPVFAPPDT------EGCADLYKN 111
Cdd:pfam12706   1 RRILIDPGP-DLRQQALPalqpgrlrdDPIDAVLLTHDHYDHLAGLLDLR--EGRPRPLYAPLGVlahlrrNFPYLFLLE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444 112 HGLLEFRRLSKFEPVMIG--NLVLTPLPLNHSKA---------TFGYAIeETDGQRFAYLTDTAGLPPPTEAFLkkwRPA 180
Cdd:pfam12706  78 HYGVRVHEIDWGESFTVGdgGLTVTATPARHGSPrgldpnpgdTLGFRI-EGPGKRVYYAGDTGYFPDEIGERL---GGA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1706422444 181 SFALD--CSYPPQSDLPRNHNDLTLALAIAETLAPARVWLTH 220
Cdd:pfam12706 154 DLLLLdgGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIH 195
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 3-180 1.38e-16

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: 76.72  E-value: 1.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   3 ITFLGTGdaGGVPlygcdcsacTRARAVadfrrrPCTALvEAGDTRILLDAGltdltE---------RFPPGSLSAIVLT 73
Cdd:cd07717     1 LTFLGTG--SAVP---------TPERNL------SSIAL-RLEGELWLFDCG-----EgtqrqllraGLSPSKIDRIFIT 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  74 HFHPDHVQGLFHL-----RWGIGPSIPVFAPPDTE---------GCADL-YKnhglLEFRRLSKFEPVMI--GNLVLTPL 136
Cdd:cd07717    58 HLHGDHILGLPGLlstmsLLGRTEPLTIYGPKGLKefletllrlSASRLpYP----IEVHELEPDPGLVFedDGFTVTAF 133

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1706422444 137 PLNHSKATFGYAIEEtdGQRFAYLTDTAglppPTEAFLKKWRPA 180
Cdd:cd07717   134 PLDHRVPCFGYRFEE--GRKIAYLGDTR----PCEGLVELAKGA 171
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 40-163 4.31e-16

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: 73.07  E-value: 4.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  40 ALVEAGDTRILLDAGLT--DLTERFP-----PGSLSAIVLTHFHPDHVQGLFHL--RWGigpsIPVFAPPDT-EGCADLY 109
Cdd:cd07733    12 TYLETEDGKLLIDAGLSgrKITGRLAeigrdPEDIDAILVTHEHADHIKGLGVLarKYN----VPIYATAGTlRAMERKV 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1706422444 110 KNHGLLEFRRLSKFEPVMIGNLVLTPLPLNHSKA-TFGYAIEEtDGQRFAYLTDT 163
Cdd:cd07733    88 GLIDVDQKQIFEPGETFSIGDFDVESFGVSHDAAdPVGYRFEE-GGRRFGMLTDL 141
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 42-186 6.42e-15

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: 71.37  E-value: 6.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  42 VEAGDTRILLDAGlT-------DLTERFPPGSLSaIVLTHFHPDHVQGL----------FHLRwgigpsipVFAPPDTEG 104
Cdd:cd07715    28 VRAGGELLILDAG-TgirelgnELMKEGPPGEAH-LLLSHTHWDHIQGFpffapaydpgNRIH--------IYGPHKDGG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444 105 CA---------------DLYKNHGLLEFRRLSKFEPVMIGNLVLTPLPLNHSKATFGYAIEEtDGQRFAYLTDTAgLPPP 169
Cdd:cd07715    98 SLeevlrrqmsppyfpvPLEELLAAIEFHDLEPGEPFSIGGVTVTTIPLNHPGGALGYRIEE-DGKSVVYATDTE-HYPD 175

                         170
                  ....*....|....*..
gi 1706422444 170 TEAFLKKWrpASFALDC 186
Cdd:cd07715   176 DGESDEAL--LEFARGA 190
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 39-220 6.47e-12

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 63.40  E-value: 6.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  39 TALVEAGDTRILLDAGLTDLTERFPPGSLS--------AIVLTHFHPDHV--QGLFHLRwgiGPSIPVFAPPdteGCADL 108
Cdd:COG2220    13 TFLIETGGKRILIDPVFSGRASPVNPLPLDpedlpkidAVLVTHDHYDHLddATLRALK---RTGATVVAPL---GVAAW 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444 109 YKNHGLLEFRRLSKFEPVMIGNLVLTPLPLNHSKATF--------GYAIeETDGQRFAYLTDTaGLPPPTEAFLKKWRPA 180
Cdd:COG2220    87 LRAWGFPRVTELDWGESVELGGLTVTAVPARHSSGRPdrngglwvGFVI-ETDGKTIYHAGDT-GYFPEMKEIGERFPID 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1706422444 181 SFALDCSYPPQsdlprnHNDLTLALAIAETLAPARVWLTH 220
Cdd:COG2220   165 VALLPIGAYPF------TMGPEEAAEAARDLKPKVVIPIH 198
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 2-103 1.19e-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: 61.76  E-value: 1.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   2 RITFLGTGdaGGVPLYGcdcsactraravadfRRRPCTaLVEAGDTRILLDAG---LTDLTE-RFPPGSLSAIVLTHFHP 77
Cdd:cd07719     1 RVTLLGTG--GPIPDPD---------------RAGPST-LVVVGGRVYLVDAGsgvVRRLAQaGLPLGDLDAVFLTHLHS 62

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1706422444  78 DHVQGL---FHLRWGIGPS--IPVFAPPDTE 103
Cdd:cd07719    63 DHVADLpalLLTAWLAGRKtpLPVYGPPGTR 93
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-172 2.42e-11

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 62.12  E-value: 2.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   1 MRITFLGTGdaGGVPlygcdcsacTRARAVadfrrrPCTALvEAGDTRILLDAGltdltE---------RFPPGSLSAIV 71
Cdd:PRK00055    2 MELTFLGTG--SGVP---------TPTRNV------SSILL-RLGGELFLFDCG-----EgtqrqllktGIKPRKIDKIF 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  72 LTHFHPDHVQGLFHL-----RWGIGPSIPVFAPPDT----EGCADLYKNHG--LLEFRRLSKFEPVMIGNLVLTPLPLNh 140
Cdd:PRK00055   59 ITHLHGDHIFGLPGLlstrsLSGRTEPLTIYGPKGIkefvETLLRASGSLGyrIAEKDKPGKLDAEKLKALGVPPGPLF- 137

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1706422444 141 SKATFGYAIEETD---------------GQRFAYLTDTAglppPTEA 172
Cdd:PRK00055  138 GKLKRGEDVTLEDgriinpadvlgpprkGRKVAYCGDTR----PCEA 180
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 41-159 5.45e-11

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


Pssm-ID: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 60.32  E-value: 5.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  41 LVEAGDTRILLDAGL--------------TDLTERFPP-------------------GSLSAIVLTHFHPDHVQGLFHLR 87
Cdd:cd07732    17 EVETGGTRILLDFGLpldpeskyfdevldFLELGLLPDivglyrdplllgglrseedPSVDAVLLSHAHLDHYGLLNYLR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  88 wgigPSIPVFAppdTEGCADLYK------NHGLLEFRRLSKFE---PVMIGNLVLTPLPLNHSkaTFG-YAIE-ETDGQR 156
Cdd:cd07732    97 ----PDIPVYM---GEATKRILKallpffGEGDPVPRNIRVFEsgkSFTIGDFTVTPYLVDHS--APGaYAFLiEAPGKR 167


                  ...
gi 1706422444 157 FAY 159
Cdd:cd07732   168 IFY 170
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 40-101 1.58e-10

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. 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: 293799  Cd Length: 269  Bit Score: 59.94  E-value: 1.58e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1706422444  40 ALVEAGDTRILLDAGLTDLTER------FPPGSLSAIVLTHFHPDHVQGLFHLRWgIGPSIPVFAPPD 101
Cdd:cd07713    23 LLIETEGKKILFDTGQSGVLLHnakklgIDLSDIDAVVLSHGHYDHTGGLKALLE-LNPKAPVYAHPD 89
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 3-173 3.39e-10

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: 57.97  E-value: 3.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   3 ITFLGTGdaGGvplygcdcsactRaRAVADFRRRPCTALVEAGDTRILLDAG----LTDLTERFPPGSLSAIVLTHFHPD 78
Cdd:cd07741     1 IIFLGTG--GG------------R-FVVITQLRASGGIWIELNGKNIHIDPGpgalVRMCRPKLDPTKLDAIILSHRHLD 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  79 H-----------VQGLFHLRwGIgpsipVFAPPDT---EGCADLYKNHGLLEfrRLSKFEP---VMIGNLVLTPLPLNHS 141
Cdd:cd07741    66 HsndanvlieamTEGGFKKR-GT-----LLAPEDAlngEPVVLLYYHRRKLE--EIEILEEgdeYELGGIKIEATRHKHS 137

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1706422444 142 KA-TFGYAIeETDGQRFAYLTDTAGLPPPTEAF 173
Cdd:cd07741   138 DPtTYGFIF-RTSDKKIGYISDTRYFEELIEYY 169
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 4-174 3.64e-10

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: 57.65  E-value: 3.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   4 TFLGTGDA---GGvplygcdcsactraravadfRRRPCTaLVEAGDTRILLDAGLTDLT--ERF--PPGSLSAIVLTHFH 76
Cdd:cd07740     1 TFLGSGDAfgsGG--------------------RLNTCF-HVASEAGRFLIDCGASSLIalKRAgiDPNAIDAIFITHLH 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  77 PDHVQGL----FHLRWGIGPS--IPVFAPPDTEG----CADLYKNHGL-------LEFRRLSKFEPVMIGNLVLTPLPLN 139
Cdd:cd07740    60 GDHFGGLpfflLDAQFVAKRTrpLTIAGPPGLRErlrrAMEALFPGSSkvprrfdLEVIELEPGEPTTLGGVTVTAFPVV 139

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1706422444 140 HSKATFGYAIE-ETDGQRFAYLTDTAglppPTEAFL 174
Cdd:cd07740   140 HPSGALPLALRlEAAGRVLAYSGDTE----WTDALV 171
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 2-156 8.55e-10

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: 58.00  E-value: 8.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   2 RITFLGTGdaGGVPlygcdcsacTRARAVadfrrrpcTA-LVEAGDTRILLDAG--------LTDLTerfpPGSLSAIVL 72
Cdd:TIGR02651   1 EITFLGTG--GGVP---------TKERNL--------PSiALKLNGELWLFDCGegtqrqmlRSGIS----PMKIDRIFI 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  73 THFHPDHVQGLFHL-----RWGIGPSIPVFAPPdtegcadlyknhGLLEF----RRLSKFE---PVMI------------ 128
Cdd:TIGR02651  58 THLHGDHILGLPGLlstmsFQGRKEPLTIYGPP------------GIKEFietsLRVSYTYlnyPIKIheieegglvfed 125

                         170       180
                  ....*....|....*....|....*...
gi 1706422444 129 GNLVLTPLPLNHSKATFGYAIEETDGQR 156
Cdd:TIGR02651 126 DGFKVEAFPLDHSIPSLGYRFEEKDRPG 153
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-102 1.79e-09

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 57.50  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   1 MRITFLGtgDAGGVplygcdcsacTRARAvadfrrrpctaLVEAGDTRILLDAGL-----TDLTERFP--PGSLSAIVLT 73
Cdd:COG1236     1 MKLTFLG--AAGEV----------TGSCY-----------LLETGGTRILIDCGLfqggkERNWPPFPfrPSDVDAVVLT 57

                          90       100
                  ....*....|....*....|....*....
gi 1706422444  74 HFHPDHVqGLFHLRWGIGPSIPVFAPPDT 102
Cdd:COG1236    58 HAHLDHS-GALPLLVKEGFRGPIYATPAT 85
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 41-151 2.63e-09

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: 55.25  E-value: 2.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   41 LVEAGDTRILLDAGLTDLT------ERFPPGSLSAIVLTHFHPDHVQGLFHLRWgiGPSIPVFAPPDT---------EGC 105
Cdd:smart00849   4 LVRDDGGAILIDTGPGEAEdllaelKKLGPKKIDAIILTHGHPDHIGGLPELLE--APGAPVYAPEGTaellkdllaLLG 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1706422444  106 ADLYKNHGLLEFRRLSKFEPVMIGNLVLTPLPL-NHSKATFGYAIEE 151
Cdd:smart00849  82 ELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTpGHTPGSIVLYLPE 128
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 39-118 5.65e-09

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: 54.46  E-value: 5.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  39 TALVEAGDTRILLDAG---------LTDLTERFPPGSLSAIVLTHFHPDHVQGLFHLR-WGIGPSIPVF-APPDTEGCAD 107
Cdd:cd07722    20 TYLVGTGKRRILIDTGegrpsyiplLKSVLDSEGNATISDILLTHWHHDHVGGLPDVLdLLRGPSPRVYkFPRPEEDEDP 99

                          90
                  ....*....|.
gi 1706422444 108 LYKNHGLLEFR 118
Cdd:cd07722   100 DEDGGDIHDLQ 110
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 1-220 2.24e-08

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: 53.37  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   1 MRITFLGTGdaGGVPlyGCDCSActraravadFRRRPCTAlveagDTRILLDAG--LTDLTER------FPPGSLSA--- 69
Cdd:cd07735     1 FELVVLGCS--GGPD--EGNTSS---------FLLDPAGS-----DGDILLDAGtgVGALSLEemfndiLFPSQKAAyel 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  70 ------IVLTHFHPDHVQGL------FHLRwgIGPSIPVFAPPDTegCADLyKNH------------GLLEFRRLSKFEP 125
Cdd:cd07735    63 yqrirhYLITHAHLDHIAGLpllspnDGGQ--RGSPKTIYGLPET--IDAL-KKHifnwviwpdftsIPSGKYPYLRLEP 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444 126 ------VMIGNLVLTPLPLNHSK-ATFGYAIEEtDGQRFAYLTDT----AGLPPPTEAFlkkWRPAS----------FaL 184
Cdd:cd07735   138 iepeypIALTGLSVTAFPVSHGVpVSTAFLIRD-GGDSFLFFGDTgpdsVSKSPRLDAL---WRALAplipkklkaiI-I 212

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1706422444 185 DCSYP---PQSDL-----PRN-HNDLT-LA-LAIAETLAPARVWLTH 220
Cdd:cd07735   213 ECSFPnsrPDALLyghltPKLlAEELAkLAkEVLKGALKGLNVIITH 259
PQQB-like_MBL-fold cd16274
Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold ...
 1-174 2.81e-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: 52.62  E-value: 2.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   1 MRITFLGTGDAGGVPLYGCDCSACTRARAVAD---FRRRPCTALVEAGDTRILLDAGlTDL---TERFP---PGS----- 66
Cdd:cd16274     1 MRIKVLGSAAGGGFPQWNCNCPNCALARAGDGratARTQSSIAVSADGENWVLINAS-PDIrqqIEATPelqPRPglrdt 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  67 -LSAIVLTHFHPDHVQGLFHLRWGiGPsIPVFAPP-------DTEGCADLYKNHGLLEFRRLSKFEPVMIG---NLVLTP 135
Cdd:cd16274    80 pIAAVLLTDAEIDHTTGLLSLREG-QP-LTVYATApvledltTNFPFFVLLHAYGGVRRHRILPGEPFTLAgcpGLTVTP 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1706422444 136 LPL-------------NHSKATFGYAIEETD-GQRFAYLTDTAGLPPPTEAFL 174
Cdd:cd16274   158 FPVpgkaplysehrdaPEPGDTIGLRIEDGRtGGRLFYAPGCAAVTDELRARL 210
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 41-108 4.39e-08

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 51.69  E-value: 4.39e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1706422444  41 LVEAGDTRILLDAGL----TDLTER------FPPGSLSAIVLTHFHPDHVQGLFHLRWgIGPSIPVFAppdTEGCADL 108
Cdd:cd16295    16 LLETGGKRILLDCGLfqggKELEELnnepfpFDPKEIDAVILTHAHLDHSGRLPLLVK-EGFRGPIYA---TPATKDL 89
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
41-220 6.82e-08

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 51.22  E-value: 6.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  41 LVEAGDTRILLDAGLTDLTER--------FPPGSLSAIVLTHFHPDHVQGLFHLR------WGIGPSIPVFAPPDTEGCA 106
Cdd:pfam00753  10 LIEGGGGAVLIDTGGSAEAALllllaalgLGPKDIDAVILTHGHFDHIGGLGELAeatdvpVIVVAEEARELLDEELGLA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444 107 DLYKNHGLLEFRRLSK--------FEPVMIGNLVLTPLPLNHSkatfGYAIEETDGQRFAYLTDTagLPPPTEAFLKKWR 178
Cdd:pfam00753  90 ASRLGLPGPPVVPLPPdvvleegdGILGGGLGLLVTHGPGHGP----GHVVVYYGGGKVLFTGDL--LFAGEIGRLDLPL 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1706422444 179 PASFALDcsyppqsdlPRNHNDLTLALAIAETLAPARVWLTH 220
Cdd:pfam00753 164 GGLLVLH---------PSSAESSLESLLKLAKLKAAVIVPGH 196
PRK05184 PRK05184
pyrroloquinoline quinone biosynthesis protein PqqB; Provisional
 1-174 1.84e-07

pyrroloquinoline quinone biosynthesis protein PqqB; Provisional


Pssm-ID: 235361 [Multi-domain]  Cd Length: 302  Bit Score: 50.97  E-value: 1.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   1 MRITFLGTGDAGGVPLYGCDCSACTRARAvADFRRRPCT----ALVEAGDTRILLDAG------LTDLTERFPPGSL--- 67
Cdd:PRK05184    1 MRIIVLGSAAGGGFPQWNCNCPNCRGARA-GTIRAKPRTqssiAVSADGEDWVLLNASpdirqqIQATPALQPARGLrdt 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  68 --SAIVLTHFHPDHVQGLFHLRWGIGpsIPVFAPPD-----TEGCA--DLYKNHGLLEFRRLSKFEPVMIG---NLVLTP 135
Cdd:PRK05184   80 piAAVVLTDGQIDHTTGLLTLREGQP--FPVYATPAvledlSTGFPifNVLDHYGGVQRRPIALDGPFAVPglpGLRFTA 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1706422444 136 LPLNhSKA--------------TFGYAIEETD-GQRFAYLTDTAGLPPPTEAFL 174
Cdd:PRK05184  158 FPVP-SKAppysphrsdpepgdNIGLRIEDRAtGKRLFYAPGLAEVTDALRARL 210
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 41-101 9.68e-07

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: 47.99  E-value: 9.68e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  41 LVEAGDTRILLDAGLTDLTER---------FPPGSLSAIVLTHFHPDHVQGLFHLRwgIGPSIPVFAPPD 101
Cdd:cd07721    15 LIEDDDGLTLIDTGLPGSAKRilkalrelgLSPKDIRRILLTHGHIDHIGSLAALK--EAPGAPVYAHER 82
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 38-150 1.03e-06

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: 48.56  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  38 CTAlVEAGDTRILLDAGLTdlterFP----PG----------------SLSAIVLTHFHPDHVQGLFHL--RWGigpsIP 95
Cdd:cd07714    13 MYV-VEYDDDIIIIDCGLK-----FPdedmPGvdyiipdfsyleenkdKIKGIFITHGHEDHIGALPYLlpELN----VP 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  96 VFAPPDTEGCA-DLYKNHGLL---EFRRLSKFEPVMIGNLVLTPLPLNHSKA-TFGYAIE 150
Cdd:cd07714    83 IYATPLTLALIkKKLEEFKLIkkvKLNEIKPGERIKLGDFEVEFFRVTHSIPdSVGLAIK 142
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 41-83 2.30e-06

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. 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: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 47.54  E-value: 2.30e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1706422444  41 LVEAGDTRILLDAGLTDL----TERFP---------PGSLSAIVLTHFHPDHVQGL 83
Cdd:cd07720    53 LVRTGGRLILVDTGAGGLfgptAGKLLanlaaagidPEDIDDVLLTHLHPDHIGGL 108
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
39-150 8.51e-06

mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 46.59  E-value: 8.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  39 TALVEAGDTRILLDAGLTdlterFP----PG----------------SLSAIVLTHFHPDHVQGLFHL--RWGigpsIPV 96
Cdd:COG0595    21 MYVYEYDDDIIIVDCGLK-----FPedemPGvdlvipdisyleenkdKIKGIVLTHGHEDHIGALPYLlkELN----VPV 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1706422444  97 FAPPDTEGCADLY-KNHGLL---EFRRLSKFEPVMIGNLVLTPLPLNHSKA-TFGYAIE 150
Cdd:COG0595    92 YGTPLTLALLEAKlKEHGLLkkvKLHVVKPGDRIKFGPFKVEFFRVTHSIPdSLGLAIR 150
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 38-153 1.20e-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: 44.58  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  38 CTALVEAGDTRILLDAG------LTDLTERFPpGSLSAIVLTHFHPDHVQGLFHLRWGIGpsIPVFAPPDTEGCA-DLYK 110
Cdd:cd06262    12 CYLVSDEEGEAILIDPGagalekILEAIEELG-LKIKAILLTHGHFDHIGGLAELKEAPG--APVYIHEADAELLeDPEL 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1706422444 111 NHGLLEFRRLSKFEP---------VMIGNLVLTPLPL-NHSKATFGYAIEETD 153
Cdd:cd06262    89 NLAFFGGGPLPPPEPdilledgdtIELGGLELEVIHTpGHTPGSVCFYIEEEG 141
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 41-151 1.40e-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: 44.68  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  41 LVEAGDTRILLDAGLTD---------LTERFPPgsLSAIVLTHFHPDHVQGLFHLRWGIGpsIPVFAPPDT------EGC 105
Cdd:COG0491    19 LIVGGDGAVLIDTGLGPadaeallaaLAALGLD--IKAVLLTHLHPDHVGGLAALAEAFG--APVYAHAAEaealeaPAA 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1706422444 106 ADLYKNHGLLEFRRLSKFEPVMIGNLVLTPLPLN-HSKATFGYAIEE 151
Cdd:COG0491    95 GALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPgHTPGHVSFYVPD 141
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 36-102 4.51e-05

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: 43.09  E-value: 4.51e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1706422444  36 RPCTaLVEAGDTRILLDAGL---TDLTERFPP------GSLSAIVLTHFHPDHVQGLFHLRWGIGPSIPVFAPPDT 102
Cdd:cd07734    11 RSCF-LVEFKGRTVLLDCGMnpgKEDPEACLPqfellpPEIDAILISHFHLDHCGALPYLFRGFIFRGPIYATHPT 85
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 36-98 5.60e-04

cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; MBL-fold metallo-hydrolase domain; CPSF2, also known as cleavage and polyadenylation specificity factor 100 kDa subunit (CPSF-100), is a component 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. This subgroup includes Ydh1p, the yeast homolog of CPSF2. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain. 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: 293851  Cd Length: 199  Bit Score: 39.81  E-value: 5.60e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1706422444  36 RPCTALVEAGDTRILLDAGLTDLT--------ERFPPgSLSAIVLTHFHPDHVQGLFHLRWGIGPSIPVFA 98
Cdd:cd16293    11 SPLCYLLEIDDVTILLDCGWDESFdmeyleslKRIAP-TIDAVLLSHPDLEHLGALPYLVGKLGLTCPVYA 80
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 39-107 6.33e-04

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. 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: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 39.59  E-value: 6.33e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1706422444  39 TALVEAG----DTRILLDAGLTDLTERfpPGSLSAIVLTHFHPDHVqGLfhLRWGIGPSIPVFAPPDTEGCAD 107
Cdd:cd07725    26 TTLIDTGlateEDAEALWEGLKELGLK--PSDIDRVLLTHHHPDHI-GL--AGKLQEKSGATVYILDVTPVKD 93
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 47-136 9.67e-04

Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; Bacillus amyloliquefaciens BaeB may play a role in the synthesis of the antibiotic polyketide bacillaene. 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: 293833 [Multi-domain]  Cd Length: 174  Bit Score: 39.06  E-value: 9.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444  47 TRILLDAGLTDLTerfppgsLSAIVLTHFHPDHVQG---LFHLrwgigPSIPVFAPPdTEgcADLYKNHgLLEFRRLSKF 123
Cdd:cd16275    35 EKILAKLNELGLT-------LTGILLTHSHFDHVNLvepLLAK-----YDAPVYMSK-EE--IDYYGFR-CPNLIPLEDG 98

                          90
                  ....*....|...
gi 1706422444 124 EPVMIGNLVLTPL 136
Cdd:cd16275    99 DTIKIGDTEITCL 111
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 3-86 4.73e-03

Ribonuclease Z ELAC1, C-terminus of ELAC2, 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. 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 eukaryotic subgroup includes short forms (ELAC1) and the C-terminus of long forms including human ELAC2. 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: 293804 [Multi-domain]  Cd Length: 204  Bit Score: 37.14  E-value: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1706422444   3 ITFLGTGdaggvplygcdCSACTRARAVAdfrrrpCTALVEAGDTRILLDAG---LTDLTERFPPG-------SLSAIVL 72
Cdd:cd07718     1 VVFLGTG-----------SAIPSKYRNVS------GILLRIPGDGSILLDCGegtLGQLRRHYGPEeadevlrNLKCIFI 63

                          90
                  ....*....|....
gi 1706422444  73 THFHPDHVQGLFHL 86
Cdd:cd07718    64 SHLHADHHLGLIRL 77
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 41-109 4.96e-03

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 433247 [Multi-domain]  Cd Length: 160  Bit Score: 36.80  E-value: 4.96e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1706422444  41 LVEAGDTRILLDAGLTDLTERFPPGSLSAIVLTHFHPDHvqglFHLRwGIGPSIPVFAPPDTEGCADLY 109
Cdd:pfam13483  11 LIEGGGARILTDPFRATVGYRPPPVTADLVLISHGHDDH----GHPE-TLPGNPHVLDGGGSYTVGGLE 74
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 41-97 7.58e-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) 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: 293839  Cd Length: 252  Bit Score: 36.70  E-value: 7.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1706422444  41 LVEAGDTRILLDAGLTDL------------TERFPPGSLSA----------IVLTHFHPDHVQGLFhLRWGIGPSIPVF 97
Cdd:cd16281    47 LIETGGRNILIDTGIGDKqdpkfrsiyvqhSEHSLLKSLARlglspeditdVILTHLHFDHCGGAT-RADDDGLVELLF 124
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 41-80 8.47e-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) 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: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 36.73  E-value: 8.47e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1706422444  41 LVEAGDTRILLDAGL----------------TDLTER-----FPPGSLSAIVLTHFHPDHV 80
Cdd:cd16277    17 LVRTPGRTILVDTGIgndkprpgppafhnlnTPYLERlaaagVRPEDVDYVLCTHLHVDHV 77
 
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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