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Conserved domains on  [gi|2624589444|ref|WP_320132973|]
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MBL fold metallo-hydrolase [uncultured Holophaga sp.]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 11440937)

uncharacterized MBL fold metallo-hydrolase similar to uncharacterized Bacillus subtilis YycJ (WalJ) which affects the coordination of cell division with DNA replication, and may play a role in cell wall metabolism

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-244 2.76e-48

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


:

Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 160.83  E-value: 2.76e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444   1 MDYASLASGSKG-----------------------NCHALASQDSILLIDAGISflqIRKRLEYLGLDLGQVGAVAITHE 57
Cdd:COG1235     1 MKVTFLGSGSSGgvpqigcdcpvcastdprygrtrSSILVEADGTRLLIDAGPD---LREQLLRLGLDPSKIDAILLTHE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  58 HSDHIAALPMILKR---TRWTLMSTPATLEAILATQDMELPPER----FIPLHPGRALDWQGWSILPFSIPHDAADPVGF 130
Cdd:COG1235    78 HADHIAGLDDLRPRygpNPIPVYATPGTLEALERRFPYLFAPYPgkleFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444 131 RVERDGQAAGVVTDLGHPTALVADHCSGLDHLTLEANHDVRmlregsYPpqlksrilsrvGHLSNEAAAELLDRVWSPRl 210
Cdd:COG1235   158 RIEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATYDDP------EP-----------GHLSNEEALELLARLGPKR- 219

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2624589444 211 vsVVLAHLSEQNNLPDLARFAAGQVLRGRSTELA 244
Cdd:COG1235   220 --LVLTHLSPDNNDHELDYDELEAALLPAGVEVA 251
 
Name Accession Description Interval E-value
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-244 2.76e-48

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 160.83  E-value: 2.76e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444   1 MDYASLASGSKG-----------------------NCHALASQDSILLIDAGISflqIRKRLEYLGLDLGQVGAVAITHE 57
Cdd:COG1235     1 MKVTFLGSGSSGgvpqigcdcpvcastdprygrtrSSILVEADGTRLLIDAGPD---LREQLLRLGLDPSKIDAILLTHE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  58 HSDHIAALPMILKR---TRWTLMSTPATLEAILATQDMELPPER----FIPLHPGRALDWQGWSILPFSIPHDAADPVGF 130
Cdd:COG1235    78 HADHIAGLDDLRPRygpNPIPVYATPGTLEALERRFPYLFAPYPgkleFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444 131 RVERDGQAAGVVTDLGHPTALVADHCSGLDHLTLEANHDVRmlregsYPpqlksrilsrvGHLSNEAAAELLDRVWSPRl 210
Cdd:COG1235   158 RIEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATYDDP------EP-----------GHLSNEEALELLARLGPKR- 219

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2624589444 211 vsVVLAHLSEQNNLPDLARFAAGQVLRGRSTELA 244
Cdd:COG1235   220 --LVLTHLSPDNNDHELDYDELEAALLPAGVEVA 251
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 4-192 3.20e-37

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: 128.92  E-value: 3.20e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444   4 ASLASGSKGNCHALASQDSILLIDAGISFLQIRKRLEYLGLDLGQVGAVAITHEHSDHIAALPMILKRTRWTLMSTPATL 83
Cdd:cd07733     1 SVLASGSKGNCTYLETEDGKLLIDAGLSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  84 EAILATQDMeLPPERFIPLHPGRALDWQGWSILPFSIPHDAADPVGFRVERDGQAAGVVTDlghptalvadhcsgldhlt 163
Cdd:cd07733    81 RAMERKVGL-IDVDQKQIFEPGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTD------------------- 140

                         170       180
                  ....*....|....*....|....*....
gi 2624589444 164 leanhdvrmlregsyppqLKSRILSRVGH 192
Cdd:cd07733   141 ------------------LKQRILSDRGH 151
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 24-211 6.51e-15

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: 71.19  E-value: 6.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  24 LLIDAGISFLQIRKRLEYLGLDLGQ-VGAVAITHEHSDHIAALPMILKRTRWTLMSTPATLeAILATQ--DMELPPERFI 100
Cdd:pfam12706   3 ILIDPGPDLRQQALPALQPGRLRDDpIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVL-AHLRRNfpYLFLLEHYGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444 101 PLHPgraLDWQ--------GWSILPFSIPHDAA--------DPVGFRVERDGQAAGVVTDLGHPTALVADHCSGLDHLTL 164
Cdd:pfam12706  82 RVHE---IDWGesftvgdgGLTVTATPARHGSPrgldpnpgDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLGGADLLLL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2624589444 165 EAnhdvrmlreGSYPPQLKSRIlsrvGHLSNEAAAELLDRVWSPRLV 211
Cdd:pfam12706 159 DG---------GAWRDDEMIHM----GHMTPEEAVEAAADLGARRKV 192
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-136 3.47e-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: 60.65  E-value: 3.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444   13 NCHALASQDSILLIDAGISF-LQIRKRLEYLGLDlgQVGAVAITHEHSDHIAALPMILKRTRWTLMSTPATLEAILATQD 91
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEaEDLLAELKKLGPK--KIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2624589444   92 MEL-------PPERFIPLHPGRALDWQGWSILPFSIPHDAADPVGFRVERDG 136
Cdd:smart00849  79 LLGelgaeaePAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGK 130
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 12-130 1.83e-06

beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and RNase J2, involved in mRNA degradation in a wide range of organism. [Transcription, Degradation of RNA]


Pssm-ID: 273195 [Multi-domain]  Cd Length: 422  Bit Score: 48.50  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  12 GNCHALASQDSILLIDAGISFlqirKRLEYLGLDL------------GQVGAVAITHEHSDHIAALPMILKRTR-WTLMS 78
Cdd:TIGR00649  14 KNMYVVEIDDEIVIFDAGILF----PEDEMLGVDGvipdftylqeneDKVKGIFITHGHEDHIGAVPYLLHQVGfFPIYG 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2624589444  79 TPATLEAILATQDME--LPPERFIPLHPGRALDW-QGWSILPFSIPHDAADPVGF 130
Cdd:TIGR00649  90 TPLTIALIKSKIKEHglNVRTDLLEIHEGEPVEFgENTAIEFFRITHSIPDSVGF 144
PRK02113 PRK02113
MBL fold metallo-hydrolase;
19-217 1.67e-03

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 39.00  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  19 SQDSILLIDAGISFlqirkRLEYLGLDLGQVGAVAITHEHSDHIAALPMILKRTRWTLMSTPA---TLEAI-----LATQ 90
Cdd:PRK02113   42 TEGARILIDCGPDF-----REQMLRLPFGKIDAVLITHEHYDHVGGLDDLRPFCRFGEVPIYAeqyVAERLrsrmpYCFV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  91 DMELPPERFIPLH---PGRALDWQGWSILPFSIPHDAADPVGFRVERdgqaAGVVTDLGHPTALVADHCSGLDHLTLEAn 167
Cdd:PRK02113  117 EHSYPGVPNIPLReiePDRPFLVNHTEVTPLRVMHGKLPILGYRIGK----MAYITDMLTMPEEEYEQLQGIDVLVMNA- 191

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2624589444 168 hdvrmLREGSYPpqlksrilsrvGHLSNEAAAELLDRVWSPRLVSVVLAH 217
Cdd:PRK02113  192 -----LRIAPHP-----------THQSLEEALENIKRIGAKETYLIHMSH 225
 
Name Accession Description Interval E-value
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-244 2.76e-48

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 160.83  E-value: 2.76e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444   1 MDYASLASGSKG-----------------------NCHALASQDSILLIDAGISflqIRKRLEYLGLDLGQVGAVAITHE 57
Cdd:COG1235     1 MKVTFLGSGSSGgvpqigcdcpvcastdprygrtrSSILVEADGTRLLIDAGPD---LREQLLRLGLDPSKIDAILLTHE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  58 HSDHIAALPMILKR---TRWTLMSTPATLEAILATQDMELPPER----FIPLHPGRALDWQGWSILPFSIPHDAADPVGF 130
Cdd:COG1235    78 HADHIAGLDDLRPRygpNPIPVYATPGTLEALERRFPYLFAPYPgkleFHEIEPGEPFEIGGLTVTPFPVPHDAGDPVGY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444 131 RVERDGQAAGVVTDLGHPTALVADHCSGLDHLTLEANHDVRmlregsYPpqlksrilsrvGHLSNEAAAELLDRVWSPRl 210
Cdd:COG1235   158 RIEDGGKKLAYATDTGYIPEEVLELLRGADLLILDATYDDP------EP-----------GHLSNEEALELLARLGPKR- 219

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2624589444 211 vsVVLAHLSEQNNLPDLARFAAGQVLRGRSTELA 244
Cdd:COG1235   220 --LVLTHLSPDNNDHELDYDELEAALLPAGVEVA 251
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 4-192 3.20e-37

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: 128.92  E-value: 3.20e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444   4 ASLASGSKGNCHALASQDSILLIDAGISFLQIRKRLEYLGLDLGQVGAVAITHEHSDHIAALPMILKRTRWTLMSTPATL 83
Cdd:cd07733     1 SVLASGSKGNCTYLETEDGKLLIDAGLSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVLARKYNVPIYATAGTL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  84 EAILATQDMeLPPERFIPLHPGRALDWQGWSILPFSIPHDAADPVGFRVERDGQAAGVVTDlghptalvadhcsgldhlt 163
Cdd:cd07733    81 RAMERKVGL-IDVDQKQIFEPGETFSIGDFDVESFGVSHDAADPVGYRFEEGGRRFGMLTD------------------- 140

                         170       180
                  ....*....|....*....|....*....
gi 2624589444 164 leanhdvrmlregsyppqLKSRILSRVGH 192
Cdd:cd07733   141 ------------------LKQRILSDRGH 151
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
14-244 7.55e-18

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 80.24  E-value: 7.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  14 CHALASQDSILLIDAGISFLQirkRLEYLGLDLGQVGAVAITHEHSDHIAALPMILKRTRWTLMSTPAT----------L 83
Cdd:COG1234    21 SYLLEAGGERLLIDCGEGTQR---QLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLAGREKPLTiygppgtkefL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  84 EAILATQDMELPPE-RFIPLHPGRALDWQGWSILPFSIPHdAADPVGFRVERDGQAAGVVTDLGhPTALVADHCSGLDHL 162
Cdd:COG1234    98 EALLKASGTDLDFPlEFHEIEPGEVFEIGGFTVTAFPLDH-PVPAYGYRFEEPGRSLVYSGDTR-PCEALVELAKGADLL 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444 163 TLEAnhdvrmlregSYPPQLKSRILSRvGHLSNEAAAELLDRVWSPRLvsvVLAHLSEQNNLPDLARFAAGQVLRGRsTE 242
Cdd:COG1234   176 IHEA----------TFLDEEAELAKET-GHSTAKEAAELAAEAGVKRL---VLTHFSPRYDDPEELLAEARAVFPGP-VE 240


                  ..
gi 2624589444 243 LA 244
Cdd:COG1234   241 LA 242
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 24-211 6.51e-15

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: 71.19  E-value: 6.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  24 LLIDAGISFLQIRKRLEYLGLDLGQ-VGAVAITHEHSDHIAALPMILKRTRWTLMSTPATLeAILATQ--DMELPPERFI 100
Cdd:pfam12706   3 ILIDPGPDLRQQALPALQPGRLRDDpIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVL-AHLRRNfpYLFLLEHYGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444 101 PLHPgraLDWQ--------GWSILPFSIPHDAA--------DPVGFRVERDGQAAGVVTDLGHPTALVADHCSGLDHLTL 164
Cdd:pfam12706  82 RVHE---IDWGesftvgdgGLTVTATPARHGSPrgldpnpgDTLGFRIEGPGKRVYYAGDTGYFPDEIGERLGGADLLLL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2624589444 165 EAnhdvrmlreGSYPPQLKSRIlsrvGHLSNEAAAELLDRVWSPRLV 211
Cdd:pfam12706 159 DG---------GAWRDDEMIHM----GHMTPEEAVEAAADLGARRKV 192
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 8-136 9.92e-15

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: 70.75  E-value: 9.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444   8 SGSKGN-CHALASQDSILLIDAGISFLQirkRLEYLGLDLGQVGAVAITHEHSDHIAALPMIL-------KRTR-WTLMS 78
Cdd:cd07740    11 SGGRLNtCFHVASEAGRFLIDCGASSLI---ALKRAGIDPNAIDAIFITHLHGDHFGGLPFFLldaqfvaKRTRpLTIAG 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2624589444  79 TPATLEAILATQDMELP-----PERF----IPLHPGRALDWQGWSILPFSIPH-DAADPVGFRVERDG 136
Cdd:cd07740    88 PPGLRERLRRAMEALFPgsskvPRRFdlevIELEPGEPTTLGGVTVTAFPVVHpSGALPLALRLEAAG 155
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-136 3.47e-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: 60.65  E-value: 3.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444   13 NCHALASQDSILLIDAGISF-LQIRKRLEYLGLDlgQVGAVAITHEHSDHIAALPMILKRTRWTLMSTPATLEAILATQD 91
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEaEDLLAELKKLGPK--KIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2624589444   92 MEL-------PPERFIPLHPGRALDWQGWSILPFSIPHDAADPVGFRVERDG 136
Cdd:smart00849  79 LLGelgaeaePAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGK 130
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
12-217 5.74e-09

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 54.68  E-value: 5.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  12 GNCHALASQDSILLIDAGISFLQIRKR-LEYLGLDLGQVGAVAITHEHSDHIAALPMILKRTRWTLMSTPATLEAILATQ 90
Cdd:pfam00753   6 VNSYLIEGGGGAVLIDTGGSAEAALLLlLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  91 DMELPPERFIPLHPGRALDWQgwsilPFSIPHDAADPVGFRVER-----DGQAAGVVTDLGHPTALVADhcsgldhlTLE 165
Cdd:pfam00753  86 LGLAASRLGLPGPPVVPLPPD-----VVLEEGDGILGGGLGLLVthgpgHGPGHVVVYYGGGKVLFTGD--------LLF 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2624589444 166 ANHDVRMLREGSYPPQLKsrilsrvgHLSNEAAAELLDRVWSPRLVSVVLAH 217
Cdd:pfam00753 153 AGEIGRLDLPLGGLLVLH--------PSSAESSLESLLKLAKLKAAVIVPGH 196
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
19-227 1.31e-08

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 54.58  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  19 SQDSILLIDAGISFLQIRKRLEY------LGLDLGQVGAVAITHEHSDHIAALPMIL-KRTRWTLMSTPATLEAILAT-- 89
Cdd:COG5212    37 GSDDYVLLDAGTVVSGLELAEQKgafkgrQGYVLEHIKGYLISHAHLDHIAGLPILSpDDSPKTIYALPETIDALRNHyf 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  90 ------------QDMELPPERFIPLHPGR--ALDWQGWSILPFSIPHDAADpVGFRVERDGQAAGVVTDLGhPTALvaDH 155
Cdd:COG5212   117 nwviwpdftdigSAPHLPKYRYVPLKPGQtfPLGGTGLRVTAFPLSHSVPS-SAFLIESGGGAFLYSGDTG-PDEV--EK 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444 156 CSGLDHL-----TLEANHDVRML-REGSYPPQLKSRILSrvGHLsneaaaelldrvwSPRLVSVVLAHLSEQ--NNLPDL 227
Cdd:COG5212   193 STNLDALwealaPLVRSKKLKAIiIEVSFPNEQPDALLF--GHL-------------TPALLLEELAKLAKYagGALKGL 257
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 12-160 1.53e-08

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: 53.29  E-value: 1.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  12 GNCHALASQDSILLIDAGISFLQirkRLEYLGLDLGQVGAVAITHEHSDHIAALPMILKrTRWTLMST-------PATLE 84
Cdd:cd07719    18 GPSTLVVVGGRVYLVDAGSGVVR---RLAQAGLPLGDLDAVFLTHLHSDHVADLPALLL-TAWLAGRKtplpvygPPGTR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  85 AILATQDMELPPERFIPLH--------------------PGRALDWQGWSILPFSIPHDAADP-VGFRVERDGqaaGVVT 143
Cdd:cd07719    94 ALVDGLLAAYALDIDYRARigdegrpdpgalvevheiaaGGVVYEDDGVKVTAFLVDHGPVPPaLAYRFDTPG---RSVV 170

                         170       180
                  ....*....|....*....|
gi 2624589444 144 ---DLGhPTALVADHCSGLD 160
Cdd:cd07719   171 fsgDTG-PSENLIELAKGAD 189
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 18-138 1.61e-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: 54.14  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  18 ASQDSILLIDAG-----ISFLQIRKRLEYLGLDLGQ-----VGAVAITHEHSDHIAALPM------ILKRTRWTLMSTPA 81
Cdd:cd07735    25 AGSDGDILLDAGtgvgaLSLEEMFNDILFPSQKAAYelyqrIRHYLITHAHLDHIAGLPLlspndgGQRGSPKTIYGLPE 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  82 TLEAILAT-------------QDMELPPERFIPLHPGRALDWQGWSILPFSIPHDAADPVGFRVERDGQA 138
Cdd:cd07735   105 TIDALKKHifnwviwpdftsiPSGKYPYLRLEPIEPEYPIALTGLSVTAFPVSHGVPVSTAFLIRDGGDS 174
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 13-133 1.90e-08

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: 53.56  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  13 NCHALASQDSILLIDAGISFLqirkRLEYLGLDL------------GQVGAVAITHEHSDHIAALPMILKR-------TR 73
Cdd:cd07714    12 NMYVVEYDDDIIIIDCGLKFP----DEDMPGVDYiipdfsyleenkDKIKGIFITHGHEDHIGALPYLLPElnvpiyaTP 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  74 WTLmstpATLEAILATQDMELPPErFIPLHPGRALDWQGWSILPFSIPHDAADPVGFRVE 133
Cdd:cd07714    88 LTL----ALIKKKLEEFKLIKKVK-LNEIKPGERIKLGDFEVEFFRVTHSIPDSVGLAIK 142
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 14-136 2.03e-08

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: 52.65  E-value: 2.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  14 CHALASQDSILLIDAGISFLQirkRLEYLGLDLGQVGAVAITHEHSDHIAALPMILKRTRWTLMSTP----------ATL 83
Cdd:cd16272    19 SYLLETGGTRILLDCGEGTVY---RLLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRKKPltiygpkgikEFL 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2624589444  84 EAILATQDMELPPERFIPLHP----GRALDWQGWSILPFSIPHdaADP-VGFRVERDG 136
Cdd:cd16272    96 EKLLNFPVEILPLGFPLEIEEleegGEVLELGDLKVEAFPVKH--SVEsLGYRIEAEG 151
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 13-72 3.82e-08

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: 52.22  E-value: 3.82e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2624589444  13 NCHALASQDSILLIDAGI--SFLQIRKRLEYLGLDLGQVGAVAITHEHSDHIAALPMILKRT 72
Cdd:cd07721    12 NAYLIEDDDGLTLIDTGLpgSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAP 73
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 12-84 4.65e-08

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 53.27  E-value: 4.65e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2624589444  12 GNCHALASQDSILLIDAGISFLQIRKRLEYLGLDLGQVGAVAITHEHSDHIAALPMILKRT-RWTLMSTPATLE 84
Cdd:COG1236    14 GSCYLLETGGTRILIDCGLFQGGKERNWPPFPFRPSDVDAVVLTHAHLDHSGALPLLVKEGfRGPIYATPATAD 87
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 38-137 2.11e-07

Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase domain; Includes Dictyostelium discoideum cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A (also known as cyclic GMP-binding protein A, phosphodiesterase 5, phosphodiesterase D, and PDE5) and cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B (also known as cyclic GMP-binding protein B, phosphodiesterase 6, phosphodiesterase E, and PDE6. 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: 293824  Cd Length: 189  Bit Score: 49.99  E-value: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  38 RLEYLGLDLGQVGAVAITHEHSDHIAALP-MILKRTRWTLMSTPATLEAIL--ATQDMELPPER------FIPLHPGRAL 108
Cdd:cd07738    38 YLRQNGISPRLVDHVILTHCHADHDAGTFqKILEEEKITLYTTRTINESFLrkYAALTGLPPDFleelfdFRPVIIGEKT 117

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2624589444 109 DWQGWSILPF----SIPhdaadPVGFRVERDGQ 137
Cdd:cd07738   118 KINGAEFEFDysfhSIP-----TIRFKVSYGGK 145
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 13-136 7.45e-07

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: 48.53  E-value: 7.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  13 NCHALASQDSILLIDAGISFL---QIRKRLEYLGLDlgqVGAVAITHEHSDHIAALPMILKRTRWTLMSTPATLEAILAT 89
Cdd:COG0491    16 NSYLIVGGDGAVLIDTGLGPAdaeALLAALAALGLD---IKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEAP 92

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2624589444  90 QDMELPPERFIP----LHPGRALDWQGWSILPFSIPHDAADPVGFRVERDG 136
Cdd:COG0491    93 AAGALFGREPVPpdrtLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEK 143
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 24-134 8.11e-07

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: 48.24  E-value: 8.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  24 LLIDAGISFlqirkRLEYLGLDLGQVGAVAITHEHSDHIAALPMIlkRtRWTLMS--------TPATLEAILATQDMELP 95
Cdd:cd16279    47 ILIDTGPDF-----RQQALRAGIRKLDAVLLTHAHADHIHGLDDL--R-PFNRLQqrpipvyaSEETLDDLKRRFPYFFA 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2624589444  96 PE--------RFIPLHPGRALDWQGWSILPFSIPHDAADPVGFRVER 134
Cdd:cd16279   119 ATggggvpklDLHIIEPDEPFTIGGLEITPLPVLHGKLPSLGFRFGD 165
MG423 TIGR00649
beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and ...
 12-130 1.83e-06

beta-CASP ribonuclease, RNase J family; This family of metalloenzymes includes RNase J1 and RNase J2, involved in mRNA degradation in a wide range of organism. [Transcription, Degradation of RNA]


Pssm-ID: 273195 [Multi-domain]  Cd Length: 422  Bit Score: 48.50  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  12 GNCHALASQDSILLIDAGISFlqirKRLEYLGLDL------------GQVGAVAITHEHSDHIAALPMILKRTR-WTLMS 78
Cdd:TIGR00649  14 KNMYVVEIDDEIVIFDAGILF----PEDEMLGVDGvipdftylqeneDKVKGIFITHGHEDHIGAVPYLLHQVGfFPIYG 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2624589444  79 TPATLEAILATQDME--LPPERFIPLHPGRALDW-QGWSILPFSIPHDAADPVGF 130
Cdd:TIGR00649  90 TPLTIALIKSKIKEHglNVRTDLLEIHEGEPVEFgENTAIEFFRITHSIPDSVGF 144
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 21-72 2.77e-06

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: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 46.75  E-value: 2.77e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2624589444  21 DSILLIDAGI---SFLQIRKRLEYLGLdlgQVGAVAITHEHSDHIAALPMILKRT 72
Cdd:cd07743    18 KEALLIDSGLdedAGRKIRKILEELGW---KLKAIINTHSHADHIGGNAYLQKKT 69
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 13-121 4.31e-06

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: 46.12  E-value: 4.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  13 NCHALAS-QDSILLIDAGISFL-QIRKRLEYLGLDlgqVGAVAITHEHSDHIAALPMILKRTRWTLMSTPATLEAI---- 86
Cdd:cd06262    11 NCYLVSDeEGEAILIDPGAGALeKILEAIEELGLK---IKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAELLedpe 87

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2624589444  87 ----LATQDMELPPERFIPLHPGRALDWQGWSILPFSIP 121
Cdd:cd06262    88 lnlaFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTP 126
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 12-136 4.33e-06

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: 46.45  E-value: 4.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  12 GNCHALASQDSILLIDAGISF----------LQIRK-----------RLEYLGLDLGQ-----VGAVAITHEHSDHIAAL 65
Cdd:cd07732    13 GNCIEVETGGTRILLDFGLPLdpeskyfdevLDFLElgllpdivglyRDPLLLGGLRSeedpsVDAVLLSHAHLDHYGLL 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2624589444  66 PMIlkRTRWTLMSTPAT---LEAILATQDMELPPER-FIPLHPGRALDWQGWSILPFSIPHDAADPVGFRVERDG 136
Cdd:cd07732    93 NYL--RPDIPVYMGEATkriLKALLPFFGEGDPVPRnIRVFESGKSFTIGDFTVTPYLVDHSAPGAYAFLIEAPG 165
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 12-84 1.27e-05

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: 44.76  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  12 GNCHALASQDSILLIDAGISflQIRKRLEY-----LGLDLGQVGAVAITHEHSDHIAALPMILKRTR----WTlmsTPAT 82
Cdd:cd16295    12 GSCYLLETGGKRILLDCGLF--QGGKELEElnnepFPFDPKEIDAVILTHAHLDHSGRLPLLVKEGFrgpiYA---TPAT 86


                  ..
gi 2624589444  83 LE 84
Cdd:cd16295    87 KD 88
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-108 1.64e-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.


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 44.88  E-value: 1.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  14 CHALASQDSILLIDAGISF---LQIRKRLEYLGLDLGQVGAVAITHEHSDHI--AAL-------PMILKRTRWTLMSTPA 81
Cdd:cd16280    24 AWAIDTGDGLILIDALNNNeaaDLIVDGLEKLGLDPADIKYILITHGHGDHYggAAYlkdlygaKVVMSEADWDMMEEPP 103

                          90       100
                  ....*....|....*....|....*..
gi 2624589444  82 TLEailATQDMELPPERFIPLHPGRAL 108
Cdd:cd16280   104 EEG---DNPRWGPPPERDIVIKDGDTL 127
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 21-112 2.43e-05

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. 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: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 43.66  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  21 DSIL--------LIDAG----------ISFLQIR--KRLEYLgldlgqvgavAITHEHSDHIAALPMILKR--TRWTLMS 78
Cdd:cd07731    11 DAILiqtpgktiLIDTGprdsfgedvvVPYLKARgiKKLDYL----------ILTHPDADHIGGLDAVLKNfpVKEVYMP 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2624589444  79 -----TPATLEAILATQDMELPperFIPLHPGRALDWQG 112
Cdd:cd07731    81 gvthtTKTYEDLLDAIKEKGIP---VTPCKAGDRWQLGG 116
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 13-109 2.85e-05

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: 43.83  E-value: 2.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  13 NCHALASQDSILLIDAGI----SFLQIRKRLEYLGLDLGQVGAVAITHEHSDHIAALPMILKRTRWTLMStpATLEAILA 88
Cdd:cd07725    16 NVYLLRDGDETTLIDTGLateeDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGATVYI--LDVTPVKD 93

                          90       100
                  ....*....|....*....|..
gi 2624589444  89 TQDMELPPERFIPLH-PGRALD 109
Cdd:cd07725    94 GDKIDLGGLRLKVIEtPGHTPG 115
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
13-76 4.40e-05

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 44.28  E-value: 4.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  13 NCHALASQDSILLIDAGISF------------------LQIRKRLEylgldlgqvgAVAITHEHSDHIAALPMILKR--- 71
Cdd:COG0595    20 NMYVYEYDDDIIIVDCGLKFpedempgvdlvipdisylEENKDKIK----------GIVLTHGHEDHIGALPYLLKElnv 89


                  ....*....
gi 2624589444  72 ----TRWTL 76
Cdd:COG0595    90 pvygTPLTL 98
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 24-115 1.20e-04

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: 42.54  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  24 LLIDAGISFLQ------IRKRLEYLGLDlgQVGAVAITHEHSDHIAALPMILKR--TRWTLMSTPATLEAILAT--QDME 93
Cdd:COG2333    24 ILIDTGPRPSFdagervVLPYLRALGIR--RLDLLVLTHPDADHIGGLAAVLEAfpVGRVLVSGPPDTSETYERllEALK 101

                          90       100
                  ....*....|....*....|..
gi 2624589444  94 LPPERFIPLHPGRALDWQGWSI 115
Cdd:COG2333   102 EKGIPVRPCRAGDTWQLGGVRF 123
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
24-73 1.68e-04

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 42.18  E-value: 1.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2624589444  24 LLIDAGISFLqIRKRLEYLGLDLGQVGAVAITHEHSDHIAALPMILKRTR 73
Cdd:COG1237    34 ILFDTGQSDV-LLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLPALLELNP 82
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 24-73 2.33e-04

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: 41.84  E-value: 2.33e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2624589444  24 LLIDAGIS--FLQ-IRKrleyLGLDLGQVGAVAITHEHSDHIAALPMILKRTR 73
Cdd:cd07713    32 ILFDTGQSgvLLHnAKK----LGIDLSDIDAVVLSHGHYDHTGGLKALLELNP 80
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 14-83 4.49e-04

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: 40.39  E-value: 4.49e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2624589444  14 CHALASQDSILLIDAGI--SFLQIRKRLEYLGLDLGQVGAVAITHEHSDHIAALPMILKRT--RWTLMSTPATL 83
Cdd:cd07734    13 CFLVEFKGRTVLLDCGMnpGKEDPEACLPQFELLPPEIDAILISHFHLDHCGALPYLFRGFifRGPIYATHPTV 86
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 12-148 9.04e-04

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: 39.40  E-value: 9.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  12 GN--CHALASQDSILLIDAGISflqIRKrleyLGLDLGQVGAVA-----ITHEHSDHIAALP----MILKRTRWTLMS-- 78
Cdd:cd07715    21 GNtsCVEVRAGGELLILDAGTG---IRE----LGNELMKEGPPGeahllLSHTHWDHIQGFPffapAYDPGNRIHIYGph 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  79 -TPATLEAILATQdMELP--P---------ERFIPLHPGRALDWQGWSILPFSIPHdaadP---VGFRVERDGQAAGVVT 143
Cdd:cd07715    94 kDGGSLEEVLRRQ-MSPPyfPvpleellaaIEFHDLEPGEPFSIGGVTVTTIPLNH----PggaLGYRIEEDGKSVVYAT 168


                  ....*
gi 2624589444 144 DLGHP 148
Cdd:cd07715   169 DTEHY 173
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 13-219 1.14e-03

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: 39.35  E-value: 1.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  13 NCHALASQDSILLIDAG----IsflQIRKrleyLGLDLGQVGAVAITHEHSDHIAALPMIL------KRTRwTLM----- 77
Cdd:cd07717    18 SSIALRLEGELWLFDCGegtqR---QLLR----AGLSPSKIDRIFITHLHGDHILGLPGLLstmsllGRTE-PLTiygpk 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  78 STPATLEAILATQDMELP-PERFIPLHPGRALDW--QGWSILPFSIPHDaADPVGFRVErDGQAAGVVTDLGhPTALVAD 154
Cdd:cd07717    90 GLKEFLETLLRLSASRLPyPIEVHELEPDPGLVFedDGFTVTAFPLDHR-VPCFGYRFE-EGRKIAYLGDTR-PCEGLVE 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2624589444 155 HCSGLD---HltleanhdvrmlrEGSYPPQLKSRILSRvGHLSNEAAAELLDRVWSPRLvsvVLAHLS 219
Cdd:cd07717   167 LAKGADlliH-------------EATFLDDDAEKAKET-GHSTAKQAAEIAKKAGVKKL---VLTHFS 217
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 14-71 1.29e-03

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 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: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 39.01  E-value: 1.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  14 CHALASQDSILLIDAGI--SFLQIRKRLEYLGLDLGQVGAVAITHEHSDHIAALPMILKR 71
Cdd:cd07726    18 SYLLDGEGRPALIDTGPssSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLAEA 77
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 24-138 1.33e-03

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: 38.58  E-value: 1.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  24 LLIDAGI-SFLQIRKRLEYLGLDlgqvgAVAITHEHSDHIAALPMILKRTRWTLMST---------PATLEAILATQDME 93
Cdd:cd07716    30 ILLDCGSgVLSRLQRYIDPEDLD-----AVVLSHLHPDHCADLGVLQYARRYHPRGArkpplplygPAGPAERLAALYGL 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2624589444  94 LPPERFIPLHPGRALDWQGWSILPFSIPHdaadPV---GFRVERDGQA 138
Cdd:cd07716   105 EDVFDFHPIEPGEPLEIGPFTITFFRTVH----PVpcyAMRIEDGGKV 148
PRK02113 PRK02113
MBL fold metallo-hydrolase;
19-217 1.67e-03

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 39.00  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  19 SQDSILLIDAGISFlqirkRLEYLGLDLGQVGAVAITHEHSDHIAALPMILKRTRWTLMSTPA---TLEAI-----LATQ 90
Cdd:PRK02113   42 TEGARILIDCGPDF-----REQMLRLPFGKIDAVLITHEHYDHVGGLDDLRPFCRFGEVPIYAeqyVAERLrsrmpYCFV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  91 DMELPPERFIPLH---PGRALDWQGWSILPFSIPHDAADPVGFRVERdgqaAGVVTDLGHPTALVADHCSGLDHLTLEAn 167
Cdd:PRK02113  117 EHSYPGVPNIPLReiePDRPFLVNHTEVTPLRVMHGKLPILGYRIGK----MAYITDMLTMPEEEYEQLQGIDVLVMNA- 191

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2624589444 168 hdvrmLREGSYPpqlksrilsrvGHLSNEAAAELLDRVWSPRLVSVVLAH 217
Cdd:PRK02113  192 -----LRIAPHP-----------THQSLEEALENIKRIGAKETYLIHMSH 225
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 45-136 2.63e-03

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 38.36  E-value: 2.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2624589444  45 DLGQVGAVAITHEHSDHI--AALPMILKRTrwTLMSTPATLEAILATQDMelppERFIPLHPGRALDWQGWSI--LP--- 117
Cdd:COG2220    45 DLPKIDAVLVTHDHYDHLddATLRALKRTG--ATVVAPLGVAAWLRAWGF----PRVTELDWGESVELGGLTVtaVParh 118

                          90       100
                  ....*....|....*....|.
gi 2624589444 118 FSIPHDAA--DPVGFRVERDG 136
Cdd:COG2220   119 SSGRPDRNggLWVGFVIETDG 139
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 13-65 2.69e-03

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: 38.30  E-value: 2.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2624589444  13 NCHALASQDSILLIDAGISFL------QIRKRLEYLGLDLGQVGAVAITHEHSDHIAAL 65
Cdd:cd07720    50 NAFLVRTGGRLILVDTGAGGLfgptagKLLANLAAAGIDPEDIDDVLLTHLHPDHIGGL 108
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 17-81 2.78e-03

Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup EVM-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 38.10  E-value: 2.78e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2624589444  17 LASQDSILLIDAGI--SFLQIRKRLEYLGLDLGQVGAVAITHEHSDHIAALPMILKRTRWTLMSTPA 81
Cdd:cd16315    27 ITGDDGHVLIDSGTeeAAPLVLANIRKLGFDPKDVRWLLSSHEHFDHVGGLAALQRATGARVAASAA 93
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 14-86 3.32e-03

BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Bradyrhizobium diazoefficiens BJP-1, Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Caulobacter crescentus Mbl1b. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 38.07  E-value: 3.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2624589444  14 CHALASQDSILLIDAGI--SFLQIRKRLEYLGLDLGQVGAVAITHEHSDHIAALPMILKRTRWTLMSTPATLEAI 86
Cdd:cd16288    24 SYLITTPQGLILIDTGLesSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAALKKLTGAKLMASAEDAALL 98
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 13-72 4.76e-03

uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 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. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 37.33  E-value: 4.76e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2624589444  13 NCHALASQDS--ILLIDAGISFLQIRKRLEYLGLDLGqvgAVAITHEHSDHIAALPMILKRT 72
Cdd:cd16322    12 NTYLVADEGGgeAVLVDPGDESEKLLARFGTTGLTLL---YILLTHAHFDHVGGVADLRRHP 70
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 45-73 8.00e-03

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: 36.41  E-value: 8.00e-03
                          10        20
                  ....*....|....*....|....*....
gi 2624589444  45 DLGQVGAVAITHEHSDHIAALPMILKRTR 73
Cdd:cd16292    49 DLSEIDLLLITHFHLDHCGALPYFLQKTN 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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