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Conserved domains on  [gi|1088191048|gb|OHA50413|]
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hypothetical protein A3B75_02655 [Candidatus Terrybacteria bacterium RIFCSPHIGHO2_02_FULL_43_14]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 11440933)

MBL fold metallo-hydrolase similar to Methanopyrus kandleri ribonuclease Z

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-252 1.64e-55

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


:

Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 178.46  E-value: 1.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   1 MKLTVLGSGTMMLKKDKFPSSFLLEEGDIKLLLDCGFGAIARLSEMDMDLRQINAVFISHFHADHFGDAFNLVHARFVAD 80
Cdd:COG1234     1 MKLTFLGTGGAVPTPGRATSSYLLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  81 LYEnkphsKLIFICPETTKDRFMKWREVYWPEPkeDYPLEFKE--GSLEMDLGQLHIETFPVSH-VPwfkSVGIRVSFKD 157
Cdd:COG1234    81 REK-----PLTIYGPPGTKEFLEALLKASGTDL--DFPLEFHEiePGEVFEIGGFTVTAFPLDHpVP---AYGYRFEEPG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048 158 KLLVYTGDIGSShdfEDLVKRTQNADLLMIEA------AAQKPTPNHFTLEQIQELTERAAVKKALIVHTRPQKEWQERI 231
Cdd:COG1234   151 RSLVYSGDTRPC---EALVELAKGADLLIHEAtfldeeAELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDDPEEL 227

                         250       260
                  ....*....|....*....|...
gi 1088191048 232 RNFIKD--KPTLILAEDKMTFEI 252
Cdd:COG1234   228 LAEARAvfPGPVELAEDGMVIEL 250
 
Name Accession Description Interval E-value
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-252 1.64e-55

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 178.46  E-value: 1.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   1 MKLTVLGSGTMMLKKDKFPSSFLLEEGDIKLLLDCGFGAIARLSEMDMDLRQINAVFISHFHADHFGDAFNLVHARFVAD 80
Cdd:COG1234     1 MKLTFLGTGGAVPTPGRATSSYLLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  81 LYEnkphsKLIFICPETTKDRFMKWREVYWPEPkeDYPLEFKE--GSLEMDLGQLHIETFPVSH-VPwfkSVGIRVSFKD 157
Cdd:COG1234    81 REK-----PLTIYGPPGTKEFLEALLKASGTDL--DFPLEFHEiePGEVFEIGGFTVTAFPLDHpVP---AYGYRFEEPG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048 158 KLLVYTGDIGSShdfEDLVKRTQNADLLMIEA------AAQKPTPNHFTLEQIQELTERAAVKKALIVHTRPQKEWQERI 231
Cdd:COG1234   151 RSLVYSGDTRPC---EALVELAKGADLLIHEAtfldeeAELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDDPEEL 227

                         250       260
                  ....*....|....*....|...
gi 1088191048 232 RNFIKD--KPTLILAEDKMTFEI 252
Cdd:COG1234   228 LAEARAvfPGPVELAEDGMVIEL 250
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 3-189 5.27e-40

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: 136.24  E-value: 5.27e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   3 LTVLGSGTMMLKKDKFPSSFLLEEGDIKLLLDCGFGAIARLSEMDMDLRQINAVFISHFHADHFGDAFNLVHARFVADly 82
Cdd:cd16272     1 LTFLGTGGAVPSLTRNTSSYLLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGG-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  83 ENKPhskLIFICPETTKDRFMKWREVYWPEPKEDYPLEFKE---GSLEMDLGQLHIETFPVSHVPwfKSVGIRVSFKDKL 159
Cdd:cd16272    79 RKKP---LTIYGPKGIKEFLEKLLNFPVEILPLGFPLEIEEleeGGEVLELGDLKVEAFPVKHSV--ESLGYRIEAEGKS 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 1088191048 160 LVYTGDIGSShdfEDLVKRTQNADLLMIEA 189
Cdd:cd16272   154 IVYSGDTGPC---ENLVELAKGADLLIHEC 180
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 2-252 1.22e-17

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: 80.34  E-value: 1.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   2 KLTVLGSGTMMLKKDKFPSSFLLEEGDIKLLLDCGFGAIARLSEMDMDLRQINAVFISHFHADHFGDAFNLVHARfvaDL 81
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLNGELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTM---SF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  82 YENKphSKLIFICPETTKDRFMKWREVYwpEPKEDYPL---EFKEGSLEMDLGQLHIETFPVSH-VPwfkSVGIRVSFKD 157
Cdd:TIGR02651  78 QGRK--EPLTIYGPPGIKEFIETSLRVS--YTYLNYPIkihEIEEGGLVFEDDGFKVEAFPLDHsIP---SLGYRFEEKD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048 158 KL--------------------------------------------------LVYTGDIGSshdFEDLVKRTQNADLLMI 187
Cdd:TIGR02651 151 RPgkfdrekakelgippgplygklkrgetvtlidgriidpedvlgpprkgrkIAYTGDTRP---CEEVIEFAKNADLLIH 227

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1088191048 188 EA---------AAQKptpNHFTLEQIQELTERAAVKKALIVH-----TRPQKEWQERIRNFikdkPTLILAEDKMTFEI 252
Cdd:TIGR02651 228 EAtfldedkklAKEY---GHSTAAQAAEIAKEANVKRLILTHisprySDEEELLEEAKKIF----PNTYIAEDFMEIEI 299
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-252 1.77e-16

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 76.37  E-value: 1.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   1 MKLTVLGSGTMMLKKDKFPSSFLLEEGDIKLLLDCGFGAIARLSEMDMDLRQINAVFISHFHADHFGDAFNLVhARFVAD 80
Cdd:PRK00055    2 MELTFLGTGSGVPTPTRNVSSILLRLGGELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLL-STRSLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  81 lyeNKPHsKLIFICPETTKDRFMKWREVYwpePKEDYPLEFKEGSLEMDLGQLhiETFPVSHVPWFK------------- 147
Cdd:PRK00055   81 ---GRTE-PLTIYGPKGIKEFVETLLRAS---GSLGYRIAEKDKPGKLDAEKL--KALGVPPGPLFGklkrgedvtledg 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048 148 -----SVGIRVSFKDKLLVYTGDIGSSHDFEDLVKrtqNADLLMIEAA-----AQKPTPN-HFTLEQIQELTERAAVKKA 216
Cdd:PRK00055  152 riinpADVLGPPRKGRKVAYCGDTRPCEALVELAK---GADLLVHEATfgdedEELAKEYgHSTARQAAEIAKEAGVKRL 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1088191048 217 LIVHTRPQ-----KEWQERIRN-FikdkPTLILAEDKMTFEI 252
Cdd:PRK00055  229 ILTHFSPRytgdpEELLKEAREiF----PNTELAEDLMRVEV 266
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
18-175 1.26e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 70.09  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  18 FPSSFLLEEGDIKLLLDCGFGA----IARLSEMDMDLRQINAVFISHFHADHFGDAFNLVHARFVAdLYENKPHSKLIFI 93
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTGGSAeaalLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVP-VIVVAEEARELLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  94 CPETTKDRFMKWREVYWPEPKEDYPLEFKEGSLEMDLGQLHIETFPVSHvpwfksVGIRVSFKDKLLVYTGDIGSSHDFE 173
Cdd:pfam00753  84 EELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGP------GHVVVYYGGGKVLFTGDLLFAGEIG 157


                  ..
gi 1088191048 174 DL 175
Cdd:pfam00753 158 RL 159
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 20-193 1.12e-11

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: 61.80  E-value: 1.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   20 SSFLLEEGDIKLLLDCGFG-AIARLSEM-DMDLRQINAVFISHFHADHFGDAfNLVHARFVADLYENKPHSKLIficpeT 97
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGeAEDLLAELkKLGPKKIDAIILTHGHPDHIGGL-PELLEAPGAPVYAPEGTAELL-----K 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   98 TKDRFMKWREVYWPEPKEDYPLEFKEgslEMDLGQLHIETFPV-SHVPwfKSVGIRvsFKDKLLVYTGDIGSSHDFEDLV 176
Cdd:smart00849  75 DLLALLGELGAEAEPAPPDRTLKDGD---ELDLGGGELEVIHTpGHTP--GSIVLY--LPEGKILFTGDLLFAGGDGRTL 147

                          170
                   ....*....|....*..
gi 1088191048  177 KRTQNADLLMIEAAAQK 193
Cdd:smart00849 148 VDGGDAAASDALESLLK 164
 
Name Accession Description Interval E-value
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-252 1.64e-55

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 178.46  E-value: 1.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   1 MKLTVLGSGTMMLKKDKFPSSFLLEEGDIKLLLDCGFGAIARLSEMDMDLRQINAVFISHFHADHFGDAFNLVHARFVAD 80
Cdd:COG1234     1 MKLTFLGTGGAVPTPGRATSSYLLEAGGERLLIDCGEGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  81 LYEnkphsKLIFICPETTKDRFMKWREVYWPEPkeDYPLEFKE--GSLEMDLGQLHIETFPVSH-VPwfkSVGIRVSFKD 157
Cdd:COG1234    81 REK-----PLTIYGPPGTKEFLEALLKASGTDL--DFPLEFHEiePGEVFEIGGFTVTAFPLDHpVP---AYGYRFEEPG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048 158 KLLVYTGDIGSShdfEDLVKRTQNADLLMIEA------AAQKPTPNHFTLEQIQELTERAAVKKALIVHTRPQKEWQERI 231
Cdd:COG1234   151 RSLVYSGDTRPC---EALVELAKGADLLIHEAtfldeeAELAKETGHSTAKEAAELAAEAGVKRLVLTHFSPRYDDPEEL 227

                         250       260
                  ....*....|....*....|...
gi 1088191048 232 RNFIKD--KPTLILAEDKMTFEI 252
Cdd:COG1234   228 LAEARAvfPGPVELAEDGMVIEL 250
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 3-189 5.27e-40

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: 136.24  E-value: 5.27e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   3 LTVLGSGTMMLKKDKFPSSFLLEEGDIKLLLDCGFGAIARLSEMDMDLRQINAVFISHFHADHFGDAFNLVHARFVADly 82
Cdd:cd16272     1 LTFLGTGGAVPSLTRNTSSYLLETGGTRILLDCGEGTVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGG-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  83 ENKPhskLIFICPETTKDRFMKWREVYWPEPKEDYPLEFKE---GSLEMDLGQLHIETFPVSHVPwfKSVGIRVSFKDKL 159
Cdd:cd16272    79 RKKP---LTIYGPKGIKEFLEKLLNFPVEILPLGFPLEIEEleeGGEVLELGDLKVEAFPVKHSV--ESLGYRIEAEGKS 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 1088191048 160 LVYTGDIGSShdfEDLVKRTQNADLLMIEA 189
Cdd:cd16272   154 IVYSGDTGPC---ENLVELAKGADLLIHEC 180
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 2-189 4.26e-38

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: 131.03  E-value: 4.26e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   2 KLTVLG-SGTmmlkkdkFP------SSFLLEEGDIKLLLDCGFGAIARLSEMdMDLRQINAVFISHFHADHFGDAFNLVH 74
Cdd:cd07716     1 KLTVLGcSGS-------YPgpggacSGYLLEADGFRILLDCGSGVLSRLQRY-IDPEDLDAVVLSHLHPDHCADLGVLQY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  75 ARFVADlyENKPHSKLIFICPETTKDRFmkwREVYWPEPKEDyPLEFKEGSlEMDLGQLHIETFPVSH-VPwfkSVGIRV 153
Cdd:cd07716    73 ARRYHP--RGARKPPLPLYGPAGPAERL---AALYGLEDVFD-FHPIEPGE-PLEIGPFTITFFRTVHpVP---CYAMRI 142

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1088191048 154 SFKDKLLVYTGDIGSshdFEDLVKRTQNADLLMIEA 189
Cdd:cd07716   143 EDGGKVLVYTGDTGY---CDELVEFARGADLLLCEA 175
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 2-186 1.40e-35

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: 125.32  E-value: 1.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   2 KLTVLGSGTMMLKKDKFPSSFLLEEGDIKLLLDCGFGAIARLSEMDMDLRQINAVFISHFHADHFGDAFNLVHARFVADL 81
Cdd:cd07719     1 RVTLLGTGGPIPDPDRAGPSTLVVVGGRVYLVDAGSGVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPALLLTAWLAGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  82 yenkpHSKLIFICPETTK------------DRFMKWREVYWPEPKEDYPL---EFKEGSLEMDLGQLHIETFPVSHVPWF 146
Cdd:cd07719    81 -----KTPLPVYGPPGTRalvdgllaayalDIDYRARIGDEGRPDPGALVevhEIAAGGVVYEDDGVKVTAFLVDHGPVP 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1088191048 147 KSVGIRVSFKDKLLVYTGDIGSSHDFEDLVKrtqNADLLM 186
Cdd:cd07719   156 PALAYRFDTPGRSVVFSGDTGPSENLIELAK---GADLLV 192
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-252 1.18e-32

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 119.61  E-value: 1.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   1 MKLTVLGSGT----------------MMLKKDKFPSSFLLEEGDIKLLLDCGFGAIARLSEMDMDLRQINAVFISHFHAD 64
Cdd:COG1235     1 MKVTFLGSGSsggvpqigcdcpvcasTDPRYGRTRSSILVEADGTRLLIDAGPDLREQLLRLGLDPSKIDAILLTHEHAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  65 HFGDAFNLVHARFVADLYenkphsklIFICPETTKDRFMKWREVYWPEPKEDYPLEFKEGSlEMDLGQLHIETFPVSHvP 144
Cdd:COG1235    81 HIAGLDDLRPRYGPNPIP--------VYATPGTLEALERRFPYLFAPYPGKLEFHEIEPGE-PFEIGGLTVTPFPVPH-D 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048 145 WFKSVGIRVSFKDKLLVYTGDIGssHDFEDLVKRTQNADLLMIEAAAQKPTPNHFTLEQIQELTERAAVKKALIVH---T 221
Cdd:COG1235   151 AGDPVGYRIEDGGKKLAYATDTG--YIPEEVLELLRGADLLILDATYDDPEPGHLSNEEALELLARLGPKRLVLTHlspD 228

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1088191048 222 RPQKEWQERIRNFIKDKPTLILAEDKMTFEI 252
Cdd:COG1235   229 NNDHELDYDELEAALLPAGVEVAYDGMEIEL 259
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 4-198 3.60e-31

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: 113.89  E-value: 3.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   4 TVLGSGtmmlkkDKFPS------SFLLEEGDIKLLLDCGFGAIARLSEMDMDLRQINAVFISHFHADHFGD-AFNLVHAR 76
Cdd:cd07740     1 TFLGSG------DAFGSggrlntCFHVASEAGRFLIDCGASSLIALKRAGIDPNAIDAIFITHLHGDHFGGlPFFLLDAQ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  77 FVAdlyenKPHSKLIFICPETTKDRFMKWREVYWP---EPKEDYPLEFKE--GSLEMDLGQLHIETFPVSHVPWFKSVGI 151
Cdd:cd07740    75 FVA-----KRTRPLTIAGPPGLRERLRRAMEALFPgssKVPRRFDLEVIElePGEPTTLGGVTVTAFPVVHPSGALPLAL 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1088191048 152 RVSFKDKLLVYTGDIgSSHDfeDLVKRTQNADLLMIEA-AAQKPTPNH 198
Cdd:cd07740   150 RLEAAGRVLAYSGDT-EWTD--ALVPLARGADLFICECyFFEKKVPGH 194
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 3-251 6.51e-20

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: 85.58  E-value: 6.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   3 LTVLGSGTMMLKKDKFPSSFLLEEGDIKLLLDCGFGAIARLSEMDMDLRQINAVFISHFHADHF----GdafnlvharFV 78
Cdd:cd07717     1 LTFLGTGSAVPTPERNLSSIALRLEGELWLFDCGEGTQRQLLRAGLSPSKIDRIFITHLHGDHIlglpG---------LL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  79 ADLYENKPHSKLIFICPETTKDRFMKWREVYWPEPkeDYPLEFKE----GSLEMDLGQLHIETFPVSH-VPwfkSVGIRV 153
Cdd:cd07717    72 STMSLLGRTEPLTIYGPKGLKEFLETLLRLSASRL--PYPIEVHElepdPGLVFEDDGFTVTAFPLDHrVP---CFGYRF 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048 154 SFKDKlLVYTGDigsSHDFEDLVKRTQNADLLMIEA---------AAQKPtpnHFTLEQIQELTERAAVKKALIVHTRPQ 224
Cdd:cd07717   147 EEGRK-IAYLGD---TRPCEGLVELAKGADLLIHEAtfldddaekAKETG---HSTAKQAAEIAKKAGVKKLVLTHFSAR 219

                         250       260
                  ....*....|....*....|....*...
gi 1088191048 225 -KEWQERIRNFIKDKPTLILAEDKMTFE 251
Cdd:cd07717   220 yKDPEELLKEARAVFPNTILAEDFMTIE 247
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 20-189 4.00e-18

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: 79.90  E-value: 4.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  20 SSFLLEEGDIK-LLLDCG---FGAIARL---SEMDMDLRQINAVFISHFHADHFGDAFNLVHARFVADLYENKPhskLIF 92
Cdd:cd07718    18 SGILLRIPGDGsILLDCGegtLGQLRRHygpEEADEVLRNLKCIFISHLHADHHLGLIRLLAERKKLFKPPSPP---LYV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  93 ICP--------------ETTKDRFMKWREVYWPEPKEDYPLEFKEGSLEM--DLGQLHIETFPVSHVPWfkSVGIRVSFK 156
Cdd:cd07718    95 VAPrqlrrwlreyssleDLGLHDISFISNRVSQSLPESDDPLSRDLLSNLleELGLKSIETVPVIHCPD--AYGIVLTHE 172

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1088191048 157 DKL-LVYTGDIGSShdfEDLVKRTQNADLLMIEA 189
Cdd:cd07718   173 DGWkIVYSGDTRPC---EALVEAGKGADLLIHEA 203
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 2-252 1.22e-17

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: 80.34  E-value: 1.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   2 KLTVLGSGTMMLKKDKFPSSFLLEEGDIKLLLDCGFGAIARLSEMDMDLRQINAVFISHFHADHFGDAFNLVHARfvaDL 81
Cdd:TIGR02651   1 EITFLGTGGGVPTKERNLPSIALKLNGELWLFDCGEGTQRQMLRSGISPMKIDRIFITHLHGDHILGLPGLLSTM---SF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  82 YENKphSKLIFICPETTKDRFMKWREVYwpEPKEDYPL---EFKEGSLEMDLGQLHIETFPVSH-VPwfkSVGIRVSFKD 157
Cdd:TIGR02651  78 QGRK--EPLTIYGPPGIKEFIETSLRVS--YTYLNYPIkihEIEEGGLVFEDDGFKVEAFPLDHsIP---SLGYRFEEKD 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048 158 KL--------------------------------------------------LVYTGDIGSshdFEDLVKRTQNADLLMI 187
Cdd:TIGR02651 151 RPgkfdrekakelgippgplygklkrgetvtlidgriidpedvlgpprkgrkIAYTGDTRP---CEEVIEFAKNADLLIH 227

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1088191048 188 EA---------AAQKptpNHFTLEQIQELTERAAVKKALIVH-----TRPQKEWQERIRNFikdkPTLILAEDKMTFEI 252
Cdd:TIGR02651 228 EAtfldedkklAKEY---GHSTAAQAAEIAKEANVKRLILTHisprySDEEELLEEAKKIF----PNTYIAEDFMEIEI 299
PRK00055 PRK00055
ribonuclease Z; Reviewed
 1-252 1.77e-16

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 76.37  E-value: 1.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   1 MKLTVLGSGTMMLKKDKFPSSFLLEEGDIKLLLDCGFGAIARLSEMDMDLRQINAVFISHFHADHFGDAFNLVhARFVAD 80
Cdd:PRK00055    2 MELTFLGTGSGVPTPTRNVSSILLRLGGELFLFDCGEGTQRQLLKTGIKPRKIDKIFITHLHGDHIFGLPGLL-STRSLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  81 lyeNKPHsKLIFICPETTKDRFMKWREVYwpePKEDYPLEFKEGSLEMDLGQLhiETFPVSHVPWFK------------- 147
Cdd:PRK00055   81 ---GRTE-PLTIYGPKGIKEFVETLLRAS---GSLGYRIAEKDKPGKLDAEKL--KALGVPPGPLFGklkrgedvtledg 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048 148 -----SVGIRVSFKDKLLVYTGDIGSSHDFEDLVKrtqNADLLMIEAA-----AQKPTPN-HFTLEQIQELTERAAVKKA 216
Cdd:PRK00055  152 riinpADVLGPPRKGRKVAYCGDTRPCEALVELAK---GADLLVHEATfgdedEELAKEYgHSTARQAAEIAKEAGVKRL 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1088191048 217 LIVHTRPQ-----KEWQERIRN-FikdkPTLILAEDKMTFEI 252
Cdd:PRK00055  229 ILTHFSPRytgdpEELLKEAREiF----PNTELAEDLMRVEV 266
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
18-175 1.26e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 70.09  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  18 FPSSFLLEEGDIKLLLDCGFGA----IARLSEMDMDLRQINAVFISHFHADHFGDAFNLVHARFVAdLYENKPHSKLIFI 93
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTGGSAeaalLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVP-VIVVAEEARELLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  94 CPETTKDRFMKWREVYWPEPKEDYPLEFKEGSLEMDLGQLHIETFPVSHvpwfksVGIRVSFKDKLLVYTGDIGSSHDFE 173
Cdd:pfam00753  84 EELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGP------GHVVVYYGGGKVLFTGDLLFAGEIG 157


                  ..
gi 1088191048 174 DL 175
Cdd:pfam00753 158 RL 159
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-220 2.20e-14

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: 69.91  E-value: 2.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  22 FLLEEGDIKLLLDCGFGAIARLSEMDMDLRQINAVFISHFHADHFGDAFNLVHArfVADLYENKphsKLIFICPETT--- 98
Cdd:cd07741    23 IWIELNGKNIHIDPGPGALVRMCRPKLDPTKLDAIILSHRHLDHSNDANVLIEA--MTEGGFKK---RGTLLAPEDAlng 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  99 KDRFmkwrEVYWPEPKEDYPLEFKEGSlEMDLGQLHIETFPVSH-VPwfKSVGIRVSFKDKLLVYTGDigsSHDFEDLVK 177
Cdd:cd07741    98 EPVV----LLYYHRRKLEEIEILEEGD-EYELGGIKIEATRHKHsDP--TTYGFIFRTSDKKIGYISD---TRYFEELIE 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1088191048 178 RTQNADLLMIEAAAQKPTPN--HFTLEQIQELTERAAVKKALIVH 220
Cdd:cd07741   168 YYSNCDVLIINVTRPRPRKGvdHLSVEDVEKILKEIKPKLAILTH 212
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 1-197 4.97e-14

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: 69.55  E-value: 4.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   1 MKLTVLG-SGTMMlkkDKFPSSFLLEEGDIK--LLLDCGFGaIARLSEMDMD--------------LRQINAVFISHFHA 63
Cdd:cd07735     1 FELVVLGcSGGPD---EGNTSSFLLDPAGSDgdILLDAGTG-VGALSLEEMFndilfpsqkaayelYQRIRHYLITHAHL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  64 DHFGD-AFNlvharfVADLYENKPHSKLIFICPETT---KDRFMKWRevYWP----EPKEDYP---LEFKEGSLEMDLGQ 132
Cdd:cd07735    77 DHIAGlPLL------SPNDGGQRGSPKTIYGLPETIdalKKHIFNWV--IWPdftsIPSGKYPylrLEPIEPEYPIALTG 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1088191048 133 LHIETFPVSH-VPwfKSVGIRVSFKDKLLVYTGDIGSSHdfedLVKRTQNADLlmIEAAAQKPTPN 197
Cdd:cd07735   149 LSVTAFPVSHgVP--VSTAFLIRDGGDSFLFFGDTGPDS----VSKSPRLDAL--WRALAPLIPKK 206
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 1-189 9.21e-14

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 69.83  E-value: 9.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   1 MKLTVLGSGTMMLKkdkfpSSFLLEEGDIKLLLDCG--FGAIAR-LSEMDMDLRQINAVFISHFHADHFGDAFNLVHARF 77
Cdd:COG1236     1 MKLTFLGAAGEVTG-----SCYLLETGGTRILIDCGlfQGGKERnWPPFPFRPSDVDAVVLTHAHLDHSGALPLLVKEGF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  78 VADLYenkphsklifiCPETTKD--RFM---------KWREVYWPEPKED--------YPLEFKEgslEMDLGQLHIETF 138
Cdd:COG1236    76 RGPIY-----------ATPATADlaRILlgdsakiqeEEAEAEPLYTEEDaeralelfQTVDYGE---PFEIGGVRVTFH 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1088191048 139 PVSHVPwfKSVGIRVSFKDKLLVYTGDIGSSHD-----FEdLVKRtqnADLLMIEA 189
Cdd:COG1236   142 PAGHIL--GSAQVELEVGGKRIVFSGDYGREDDpllapPE-PVPP---ADVLITES 191
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 1-189 1.90e-13

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: 66.73  E-value: 1.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   1 MKLTVLGSGTMM---------------LKKDK-FPSSFLLEEGDIKLLLDCG--FgaiaRLSEMDMDLRQINAVFISHFH 62
Cdd:cd16279     1 MKLTFLGTGTSSgvpvigcdcgvcdssDPKNRrLRSSILIETGGKNILIDTGpdF----RQQALRAGIRKLDAVLLTHAH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  63 ADHFG-----DAFNLVHARFVaDLYenkphsklifiCPETTKDRFMKWREVYWPEPKEDYPLEFKEGSLEMD----LGQL 133
Cdd:cd16279    77 ADHIHglddlRPFNRLQQRPI-PVY-----------ASEETLDDLKRRFPYFFAATGGGGVPKLDLHIIEPDepftIGGL 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1088191048 134 HIETFPVSHvPWFKSVGIRvsFKDklLVYTGDIgsSHDFEDLVKRTQNADLLMIEA 189
Cdd:cd16279   145 EITPLPVLH-GKLPSLGFR--FGD--FAYLTDV--SEIPEESLEKLRGLDVLILDA 193
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 1-240 3.39e-12

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 63.78  E-value: 3.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   1 MKLTVLGSgtmmlkkdkfpSSFLLEEGDIKLLLDCGFGAIARLSEMDM----DLRQINAVFISHFHADHFGDAfnlvhar 76
Cdd:COG2220     4 MKITWLGH-----------ATFLIETGGKRILIDPVFSGRASPVNPLPldpeDLPKIDAVLVTHDHYDHLDDA------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  77 FVADLYENKPHskliFICPETTKDRFMKW-----REVYWPEpkedyplefkegslEMDLGQLHIETFPVSHVPWFKS--- 148
Cdd:COG2220    66 TLRALKRTGAT----VVAPLGVAAWLRAWgfprvTELDWGE--------------SVELGGLTVTAVPARHSSGRPDrng 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048 149 ---VGIRVSFKDKLLVYTGDIGSSHDFEDLVKRtQNADLLMIEAAAqkpTPNHFTLEQIQELTERAAVKKALIVH----T 221
Cdd:COG2220   128 glwVGFVIETDGKTIYHAGDTGYFPEMKEIGER-FPIDVALLPIGA---YPFTMGPEEAAEAARDLKPKVVIPIHygtfP 203

                         250
                  ....*....|....*....
gi 1088191048 222 RPQKEWQERIRNFIKDKPT 240
Cdd:COG2220   204 LLDEDPLERFAAALAAAGV 222
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 20-193 1.12e-11

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: 61.80  E-value: 1.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   20 SSFLLEEGDIKLLLDCGFG-AIARLSEM-DMDLRQINAVFISHFHADHFGDAfNLVHARFVADLYENKPHSKLIficpeT 97
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGeAEDLLAELkKLGPKKIDAIILTHGHPDHIGGL-PELLEAPGAPVYAPEGTAELL-----K 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   98 TKDRFMKWREVYWPEPKEDYPLEFKEgslEMDLGQLHIETFPV-SHVPwfKSVGIRvsFKDKLLVYTGDIGSSHDFEDLV 176
Cdd:smart00849  75 DLLALLGELGAEAEPAPPDRTLKDGD---ELDLGGGELEVIHTpGHTP--GSIVLY--LPEGKILFTGDLLFAGGDGRTL 147

                          170
                   ....*....|....*..
gi 1088191048  177 KRTQNADLLMIEAAAQK 193
Cdd:smart00849 148 VDGGDAAASDALESLLK 164
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 31-220 7.76e-11

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 59.63  E-value: 7.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  31 LLLDCGFGAIA----RLSEMDMDLRQINAVFISHFHADHFGDAFNL---------VHARFVADLYENKPhskLIFICPEt 97
Cdd:pfam12706   3 ILIDPGPDLRQqalpALQPGRLRDDPIDAVLLTHDHYDHLAGLLDLregrprplyAPLGVLAHLRRNFP---YLFLLEH- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  98 tkdRFMKWREVYWpepkedyplefkEGSLEMDLGQLHIETFPVSH-VPWFKS------VGIRVSFKDKLLVYTGDIGssh 170
Cdd:pfam12706  79 ---YGVRVHEIDW------------GESFTVGDGGLTVTATPARHgSPRGLDpnpgdtLGFRIEGPGKRVYYAGDTG--- 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1088191048 171 DFEDLV-KRTQNADLLMIEAAAQKPTPN----HFTLEQIQELTERAAVKKALIVH 220
Cdd:pfam12706 141 YFPDEIgERLGGADLLLLDGGAWRDDEMihmgHMTPEEAVEAAADLGARRKVLIH 195
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 4-142 7.86e-11

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: 58.81  E-value: 7.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   4 TVLGSGTMmlkkdkfPSSFLLEEGDIKLLLDCGFGA---IARLSEMDMDLRQINAVFISHFHADH------FGDAFNL-- 72
Cdd:cd07733     1 SVLASGSK-------GNCTYLETEDGKLLIDAGLSGrkiTGRLAEIGRDPEDIDAILVTHEHADHikglgvLARKYNVpi 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1088191048  73 -----VHARFVADLYENKPHSKLIFICPETtkdrfmkwrevywpepkedyplefkegsleMDLGQLHIETFPVSH 142
Cdd:cd07733    74 yatagTLRAMERKVGLIDVDQKQIFEPGET------------------------------FSIGDFDVESFGVSH 118
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 20-203 1.01e-10

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: 59.43  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  20 SSFLLEEGDIKLLLDCGFGaIARLSEM---DMDLRQINaVFISHFHADH------FGDAFNlvharfvadlyenkPHSKL 90
Cdd:cd07715    24 SCVEVRAGGELLILDAGTG-IRELGNElmkEGPPGEAH-LLLSHTHWDHiqgfpfFAPAYD--------------PGNRI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  91 IFICPETTK-------DRFMkwREVYWPEPKEDYP-----LEFKEGSlEMDLGQLHIETFPVSHvPWfKSVGIRVSFKDK 158
Cdd:cd07715    88 HIYGPHKDGgsleevlRRQM--SPPYFPVPLEELLaaiefHDLEPGE-PFSIGGVTVTTIPLNH-PG-GALGYRIEEDGK 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1088191048 159 LLVYTGDI----GSSHDFEDLVKRTQNADLLMIEAaaqkptpnHFTLEQ 203
Cdd:cd07715   163 SVVYATDTehypDDGESDEALLEFARGADLLIHDA--------QYTDEE 203
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 20-189 4.07e-10

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: 57.47  E-value: 4.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  20 SSFLLEEGDIKLLLDCG------FGAIARLSEMDMDLRQINAVFISHFHADHFGdafnlvharFVADLYENKPHSKlIFi 93
Cdd:cd16295    13 SCYLLETGGKRILLDCGlfqggkELEELNNEPFPFDPKEIDAVILTHAHLDHSG---------RLPLLVKEGFRGP-IY- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  94 CPETTKDrFMkwrEVYWP----------EPKEDYPLeFKEGSLEMDLGQLHI----ETFPVSHvpwfksvGIRVSFKD-- 157
Cdd:cd16295    82 ATPATKD-LA---ELLLLdsakiqeeeaEHPPAEPL-YTEEDVEKALKHFRPveygEPFEIGP-------GVKVTFYDag 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1088191048 158 ---------------KLLVYTGDIGSSHDFedLVKRTQ---NADLLMIEA 189
Cdd:cd16295   150 hilgsasveleigggKRILFSGDLGRKNTP--LLRDPApppEADYLIMES 197
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 21-174 1.51e-09

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: 56.86  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  21 SFLLEEGDIKLLLDCGFGAIAR--LSEMDMDLRQINAVFISHFHADHFGDafnlvharfVADLYENKPHSKLIficpeTT 98
Cdd:cd07713    22 SLLIETEGKKILFDTGQSGVLLhnAKKLGIDLSDIDAVVLSHGHYDHTGG---------LKALLELNPKAPVY-----AH 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1088191048  99 KDRFmkwREVYWPEPKEDYPLEFKEGSLEMDLGQLHIETFPVSHVPwfksvGIRVsfkdkllvyTGDIGSSHDFED 174
Cdd:cd07713    88 PDAF---EPRYSKRGGGKKGIGIGREELEKAGARLVLVEEPTEIAP-----GVYL---------TGEIPRVTDFEK 146
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
21-67 4.44e-08

Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440850  Cd Length: 273  Bit Score: 52.58  E-value: 4.44e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1088191048  21 SFLLEEGDIKLLLDCGFGAI----ARLseMDMDLRQINAVFISHFHADHFG 67
Cdd:COG1237    24 SALIETEGKRILFDTGQSDVllknAEK--LGIDLSDIDAVVLSHGHYDHTG 72
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 20-82 1.20e-07

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: 50.37  E-value: 1.20e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  20 SSFLLEEGDIKLLLDCGFG-------AIARLSEMDMDLRQINAVFISHFHADHFGDAfNLVHARFVADLY 82
Cdd:cd07725    16 NVYLLRDGDETTLIDTGLAteedaeaLWEGLKELGLKPSDIDRVLLTHHHPDHIGLA-GKLQEKSGATVY 84
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 53-188 3.70e-07

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: 49.15  E-value: 3.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  53 INAVFISHFHADHFGdafnlvharfvadlYENKPHSKLIFICPETTKDRFMKWREVYWPEPKEDYPLEFKEGSLEMDLGQ 132
Cdd:cd07732    76 VDAVLLSHAHLDHYG--------------LLNYLRPDIPVYMGEATKRILKALLPFFGEGDPVPRNIRVFESGKSFTIGD 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1088191048 133 LHIETFPVSH-VPwfKSVGIRVSFKDKLLVYTGDI---GS-SHDFEDLVKR-TQNADLLMIE 188
Cdd:cd07732   142 FTVTPYLVDHsAP--GAYAFLIEAPGKRIFYTGDFrfhGRkPELTEAFVEKaPKNIDVLLME 201
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 47-187 1.48e-05

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 44.85  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  47 DMDLRQINAVFISHFHADHFGDAfnlvharfvADLYENKPHSKLIFICPETTKDRFMKWREVYWPEPKEDYPLefKEGSl 126
Cdd:COG2333    47 ALGIRRLDLLVLTHPDADHIGGL---------AAVLEAFPVGRVLVSGPPDTSETYERLLEALKEKGIPVRPC--RAGD- 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1088191048 127 EMDLGQLHIETF-PVSHVPWFK-----SVGIRVSFKDKLLVYTGDIGSShDFEDLVKRTQN--ADLLMI 187
Cdd:COG2333   115 TWQLGGVRFEVLwPPEDLLEGSdennnSLVLRLTYGGFSFLLTGDAEAE-AEAALLARGPDlkADVLKV 182
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 13-67 1.68e-05

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: 44.85  E-value: 1.68e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1088191048  13 LKKDKFPSS---FLLEEGDIKLLLDCGFGA---------IARLSEMDMDLRQINAVFISHFHADHFG 67
Cdd:cd07720    40 LPPDPVETSvnaFLVRTGGRLILVDTGAGGlfgptagklLANLAAAGIDPEDIDDVLLTHLHPDHIG 106
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 31-179 3.62e-05

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 43.43  E-value: 3.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  31 LLLDCGFGAIARLSEMDMDL-RQINAVFISHFHADHFGDAfNLVHARFVADLYENKPHSKLIficpETTKDRFMKWREVY 109
Cdd:cd06262    23 ILIDPGAGALEKILEAIEELgLKIKAILLTHGHFDHIGGL-AELKEAPGAPVYIHEADAELL----EDPELNLAFFGGGP 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1088191048 110 WPEPKEDYPLEFKEgslEMDLGQLHIETFPV-SHVPWfkSVGIRvsFKDKLLVYTGDIGsshdFEDLVKRT 179
Cdd:cd06262    98 LPPPEPDILLEDGD---TIELGGLELEVIHTpGHTPG--SVCFY--IEEEGVLFTGDTL----FAGSIGRT 157
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 13-79 4.00e-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) 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 annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 43.80  E-value: 4.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  13 LKKDKFPS-SFLLE-EGDIKLLLDCGFG--------------------------AIARLSEMDMDLRQINAVFISHFHAD 64
Cdd:cd07730    16 LKRVTFPAlAFLIEhPTGGKILFDLGYRkdfeeytprvperlyrtpvpleveedVAEQLAAGGIDPEDIDAVILSHLHWD 95

                          90
                  ....*....|....*
gi 1088191048  65 HFGDAFNLVHARFVA 79
Cdd:cd07730    96 HIGGLSDFPNARLIV 110
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 21-82 4.77e-05

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 43.14  E-value: 4.77e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1088191048  21 SFLLEEGDIKLLLDCGFGA------IARLSEMDMDLRqinAVFISHFHADHFGDAFNLvHARFVADLY 82
Cdd:COG0491    17 SYLIVGGDGAVLIDTGLGPadaealLAALAALGLDIK---AVLLTHLHPDHVGGLAAL-AEAFGAPVY 80
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 20-67 7.67e-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: 42.32  E-value: 7.67e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1088191048  20 SSFLLEEGDIKLLLDCGF-----GAIARLSEMDMDLRQINAVFISHFHADHFG 67
Cdd:cd07734    12 SCFLVEFKGRTVLLDCGMnpgkeDPEACLPQFELLPPEIDAILISHFHLDHCG 64
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 2-78 3.38e-04

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes 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: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 40.66  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   2 KLTVLGSGTMMLKKD-------------KFP-SSFLLEEGDIKLLLDCGFGA-----------------------IARLS 44
Cdd:cd07729     1 KLYALDYGTVTVDKSslfyygrgpgepiDLPvYAYLIEHPEGTILVDTGFHPdaaddpgglelafppgvteeqtlEEQLA 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1088191048  45 EMDMDLRQINAVFISHFHADHFGDAFNLVHARFV 78
Cdd:cd07729    81 RLGLDPEDIDYVILSHLHFDHAGGLDLFPNATII 114
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 19-65 3.67e-04

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: 40.30  E-value: 3.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1088191048  19 PSSFLLEEGDIKLLLDCGfgaiarlsEMDMDLR----QINAVFISHFHADH 65
Cdd:cd07736    37 PCSALIEVDGERILLDAG--------LTDLAERfppgSIDAILLTHFHMDH 79
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 20-67 5.97e-04

cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; MBL-fold metallo-hydrolase domain; CPSF3 (also known as cleavage and polyadenylation specificity factor 73 kDa subunit/CPSF-73) functions as a 3' endonuclease in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and in 3' end processing of metazoan histone pre-mRNAs. This subgroup also contains the yeast homolog of CPSF-73, Ysh1/Brr5 which has roles in mRNA and snoRNA synthesis. 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, and a RMMBL domain (RNA-metabolizing metallo-beta-lactamase). 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: 293850  Cd Length: 194  Bit Score: 39.88  E-value: 5.97e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1088191048  20 SSFLLEEGDIKLLLDCG----FGAIARLSEMD-MDLRQINAVFISHFHADHFG 67
Cdd:cd16292    15 SCVILEFKGKTIMLDCGihpgYSGLASLPFFDeIDLSEIDLLLITHFHLDHCG 67
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 22-67 6.18e-04

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 39.90  E-value: 6.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1088191048  22 FLLEEGDIKLLLDCGF-----GAIARLSEMDMDLRQINAVFISHFHADHFG 67
Cdd:cd07721    14 YLIEDDDGLTLIDTGLpgsakRILKALRELGLSPKDIRRILLTHGHIDHIG 64
PRK02113 PRK02113
MBL fold metallo-hydrolase;
1-220 7.22e-04

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 39.77  E-value: 7.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048   1 MKLTVLGSGT------------MMLKKD----KFPSSFLLEEGDIKLLLDCG--FgaiaRLSEMDMDLRQINAVFISHFH 62
Cdd:PRK02113    1 MKIRILGSGTstgvpeigctcpVCTSKDprdnRLRTSALVETEGARILIDCGpdF----REQMLRLPFGKIDAVLITHEH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  63 ADHFGDAFNLvharfvadlyenKPhsklificpettkdrFMKWREVywPEPKEDYPLE---------FKE----GSLEMD 129
Cdd:PRK02113   77 YDHVGGLDDL------------RP---------------FCRFGEV--PIYAEQYVAErlrsrmpycFVEhsypGVPNIP 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048 130 LGQLHIET-FPVSHVpwfKSVGIRVSF-KDKLLVY-TGDIGSSHDFEDL----VKRTQNADLLMIEAAAQKPTPNHFTLE 202
Cdd:PRK02113  128 LREIEPDRpFLVNHT---EVTPLRVMHgKLPILGYrIGKMAYITDMLTMpeeeYEQLQGIDVLVMNALRIAPHPTHQSLE 204

                         250
                  ....*....|....*...
gi 1088191048 203 QIQELTERAAVKKALIVH 220
Cdd:PRK02113  205 EALENIKRIGAKETYLIH 222
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 19-67 1.44e-03

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: 38.66  E-value: 1.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1088191048  19 PSSFLLEEGDIKLLLDCG----FgAIARLSEMDMDLRQINAVFISHFHADHFG 67
Cdd:cd16293    12 PLCYLLEIDDVTILLDCGwdesF-DMEYLESLKRIAPTIDAVLLSHPDLEHLG 63
PRK02126 PRK02126
ribonuclease Z; Provisional
 31-76 2.78e-03

ribonuclease Z; Provisional


Pssm-ID: 235006 [Multi-domain]  Cd Length: 334  Bit Score: 38.36  E-value: 2.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1088191048  31 LLLDCGfgAIARLSEMDmdLRQINAVFISHFHADHFG---DAFNLVHAR 76
Cdd:PRK02126   30 LLFDLG--DLHHLPPRE--LLRISHIFVSHTHMDHFIgfdRLLRHCLGR 74
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 18-67 4.73e-03

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 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: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 37.18  E-value: 4.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1088191048  18 FPSSFLLEEGDIKLLLDCGFGA-----IARLSEMDMDLRQINAVFISHFHADHFG 67
Cdd:cd07711    21 SSTVTLIKDGGKNILVDTGTPWdrdllLKALAEHGLSPEDIDYVVLTHGHPDHIG 75
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 3-67 5.54e-03

Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a metazoan-specific multisubunit, multifunctional protein complex composed of 14 subunits named Int1-Int14 (Integrator subunits). This subgroup includes Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)). Integrator complex 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: 293849  Cd Length: 199  Bit Score: 36.86  E-value: 5.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1088191048   3 LTVLGSGtmmlkKDKFPSSFLLEEGDIKLLLDCG----------FGAIARLSEMDMDLRQINAVFISHFHADHFG 67
Cdd:cd16291     1 VTPLGAG-----QDVGRSCILVTIGGKNIMFDCGmhmgynderrFPDFSYISQNGPFTEHIDCVIISHFHLDHCG 70
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 31-166 7.20e-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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 36.77  E-value: 7.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1088191048  31 LLLDCGFG---------AIARLSEmdmdlRQINAVFISHFHADHFG--DAFNLVHARFVAdlyenkpHS---KLIFICPE 96
Cdd:cd16282    27 VVIDTGASprlarallaAIRKVTD-----KPVRYVVNTHYHGDHTLgnAAFADAGAPIIA-------HEntrEELAARGE 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1088191048  97 TTKDRFMKWREVYWPEPKEDYPLEFKEGSLEMDLG--QLHIETFPVSHVP-----WFKSVGIrvsfkdkllVYTGDI 166
Cdd:cd16282    95 AYLELMRRLGGDAMAGTELVLPDRTFDDGLTLDLGgrTVELIHLGPAHTPgdlvvWLPEEGV---------LFAGDL 162
 
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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