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Conserved domains on  [gi|851302459|ref|WP_048165770|]
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MBL fold metallo-hydrolase [Palaeococcus pacificus]

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]; ...
 1-251 1.80e-56

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


:

Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 180.86  E-value: 1.80e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459   1 MKIIILGSGIYSGTPKPLCDCENCsrARKYPQYKRTRFSMYI--PKIKALIDPSPDLHYHLERLNM---PVKHVFITHAH 75
Cdd:COG1235    1 MKVTFLGSGSSGGVPQIGCDCPVC--ASTDPRYGRTRSSILVeaDGTRLLIDAGPDLREQLLRLGLdpsKIDAILLTHEH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  76 FDHIGGLPEL---QIFKHIKLYAHAKTLEVAEYLQKRFVGESRWNWEYFPLEFNRWYDFG-FKVYHFKVAHQPIEVAGgF 151
Cdd:COG1235   79 ADHIAGLDDLrprYGPNPIPVYATPGTLEALERRFPYLFAPYPGKLEFHEIEPGEPFEIGgLTVTPFPVPHDAGDPVG-Y 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459 152 IIQIGNKKIVITGDTGPEileDKKTLEEISNADLLVAEMTHKHSIPkTHLGVEDAIKLAQKVRAKKTVFVHISHTNYTHE 231
Cdd:COG1235  158 RIEDGGKKLAYATDTGYI---PEEVLELLRGADLLILDATYDDPEP-GHLSNEEALELLARLGPKRLVLTHLSPDNNDHE 233

                        250       260
                 ....*....|....*....|....*.
gi 851302459 232 ------ELEEKAKEYLIARDFMHLEI 251
Cdd:COG1235  234 ldydelEAALLPAGVEVAYDGMEIEL 259
 
Name Accession Description Interval E-value
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-251 1.80e-56

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 180.86  E-value: 1.80e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459   1 MKIIILGSGIYSGTPKPLCDCENCsrARKYPQYKRTRFSMYI--PKIKALIDPSPDLHYHLERLNM---PVKHVFITHAH 75
Cdd:COG1235    1 MKVTFLGSGSSGGVPQIGCDCPVC--ASTDPRYGRTRSSILVeaDGTRLLIDAGPDLREQLLRLGLdpsKIDAILLTHEH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  76 FDHIGGLPEL---QIFKHIKLYAHAKTLEVAEYLQKRFVGESRWNWEYFPLEFNRWYDFG-FKVYHFKVAHQPIEVAGgF 151
Cdd:COG1235   79 ADHIAGLDDLrprYGPNPIPVYATPGTLEALERRFPYLFAPYPGKLEFHEIEPGEPFEIGgLTVTPFPVPHDAGDPVG-Y 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459 152 IIQIGNKKIVITGDTGPEileDKKTLEEISNADLLVAEMTHKHSIPkTHLGVEDAIKLAQKVRAKKTVFVHISHTNYTHE 231
Cdd:COG1235  158 RIEDGGKKLAYATDTGYI---PEEVLELLRGADLLILDATYDDPEP-GHLSNEEALELLARLGPKRLVLTHLSPDNNDHE 233

                        250       260
                 ....*....|....*....|....*.
gi 851302459 232 ------ELEEKAKEYLIARDFMHLEI 251
Cdd:COG1235  234 ldydelEAALLPAGVEVAYDGMEIEL 259
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 1-187 5.38e-27

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


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 102.94  E-value: 5.38e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459   1 MKIIILGSGIYSGTPKPLCDCENCsrARKYPQYKRTRFSMYI--PKIKALIDPSPDLHYHLERLNMP-VKHVFITHAHFD 77
Cdd:cd16279    1 MKLTFLGTGTSSGVPVIGCDCGVC--DSSDPKNRRLRSSILIetGGKNILIDTGPDFRQQALRAGIRkLDAVLLTHAHAD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  78 HIGGLPELQIF-----KHIKLYAHAKTLevaEYLQKRF----VGESRWNWEYFPL----EFNRWYDFGFKVYHFKVAHQP 144
Cdd:cd16279   79 HIHGLDDLRPFnrlqqRPIPVYASEETL---DDLKRRFpyffAATGGGGVPKLDLhiiePDEPFTIGGLEITPLPVLHGK 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 851302459 145 IEVAgGFIIQignkKIVITGDTGpEIleDKKTLEEISNADLLV 187
Cdd:cd16279  156 LPSL-GFRFG----DFAYLTDVS-EI--PEESLEKLRGLDVLI 190
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 48-223 2.81e-22

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: 90.45  E-value: 2.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459   48 LIDPSPDLHYHLERLNMPVK-------HVFITHAHFDHIGGLPELQIFKHIKLYAHAKTLEVAEYLQKRFVGESRWNWEY 120
Cdd:pfam12706   4 LIDPGPDLRQQALPALQPGRlrddpidAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLRRNFPYLFLLEHYGVRV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  121 FPLEFNRWYDFG--------FKVYHF--KVAHQPIEVAGGFIIQIGNKKIVITGDTG---PEILEdkktleEISNADLLV 187
Cdd:pfam12706  84 HEIDWGESFTVGdggltvtaTPARHGspRGLDPNPGDTLGFRIEGPGKRVYYAGDTGyfpDEIGE------RLGGADLLL 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 851302459  188 AEMT---HKHSIPKTHLGVEDAIKLAQKVRAKKTVFVHI 223
Cdd:pfam12706 158 LDGGawrDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK02113 PRK02113
MBL fold metallo-hydrolase;
1-235 1.18e-21

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 90.23  E-value: 1.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459   1 MKIIILGSGIYSGTPKPLCDCENCSraRKYPQYKRTRFSMYIPK--IKALIDPSPDLHYHLERLNM-PVKHVFITHAHFD 77
Cdd:PRK02113   1 MKIRILGSGTSTGVPEIGCTCPVCT--SKDPRDNRLRTSALVETegARILIDCGPDFREQMLRLPFgKIDAVLITHEHYD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  78 HIGGLPELQIF---KHIKLYAHAKtleVAEYLQKR----FVGESRWNWEYFPLEfNRWYDFGFKVYHFKVahQPIEVAGG 150
Cdd:PRK02113  79 HVGGLDDLRPFcrfGEVPIYAEQY---VAERLRSRmpycFVEHSYPGVPNIPLR-EIEPDRPFLVNHTEV--TPLRVMHG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459 151 FI----IQIGNKKIVITGDTGPEiledkKTLEEISNADLLVAEMTHKHSIPkTHLGVEDAIKLAQKVRAKKTVFVHISHT 226
Cdd:PRK02113 153 KLpilgYRIGKMAYITDMLTMPE-----EEYEQLQGIDVLVMNALRIAPHP-THQSLEEALENIKRIGAKETYLIHMSHH 226


                 ....*....
gi 851302459 227 NYTHEELEE 235
Cdd:PRK02113 227 IGLHADVEK 235
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 47-169 6.31e-15

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: 70.66  E-value: 6.31e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459    47 ALIDP----SPDLHYHLERLN-MPVKHVFITHAHFDHIGGLPELQIFKHIKLYAHAKTLEVAEYLQKRFVGESRWNWeyf 121
Cdd:smart00849  12 ILIDTgpgeAEDLLAELKKLGpKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLALLGELGAEAE--- 88

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 851302459   122 PLEFNRWYDFG----FKVYHFKVAHQPIEVAGGFIIQIGNKKIVITGDTGPE 169
Cdd:smart00849  89 PAPPDRTLKDGdeldLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFA 140
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 64-251 4.13e-12

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: 64.55  E-value: 4.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459   64 MPVKHVFITHAHFDHIGGLPELqiFKHIKLYAHAKTLEV------AEYLQKRF-VGESRWNweyFPLEF-------NRWY 129
Cdd:TIGR02651  50 MKIDRIFITHLHGDHILGLPGL--LSTMSFQGRKEPLTIygppgiKEFIETSLrVSYTYLN---YPIKIheieeggLVFE 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  130 DFGFKVYHFKVAHQ------------------------------PI--EVAGGFIIQIGN----------------KKIV 161
Cdd:TIGR02651 125 DDGFKVEAFPLDHSipslgyrfeekdrpgkfdrekakelgippgPLygKLKRGETVTLIDgriidpedvlgpprkgRKIA 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  162 ITGDTGPEiledKKTLEEISNADLLVAEMT-----HKHSIPKTHLGVEDAIKLAQKVRAKKTVFVHIShTNYT--HEELE 234
Cdd:TIGR02651 205 YTGDTRPC----EEVIEFAKNADLLIHEATfldedKKLAKEYGHSTAAQAAEIAKEANVKRLILTHIS-PRYSdeEELLE 279

                         250       260
                  ....*....|....*....|
gi 851302459  235 EKAKEY---LIARDFMHLEI 251
Cdd:TIGR02651 280 EAKKIFpntYIAEDFMEIEI 299
 
Name Accession Description Interval E-value
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 1-251 1.80e-56

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 180.86  E-value: 1.80e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459   1 MKIIILGSGIYSGTPKPLCDCENCsrARKYPQYKRTRFSMYI--PKIKALIDPSPDLHYHLERLNM---PVKHVFITHAH 75
Cdd:COG1235    1 MKVTFLGSGSSGGVPQIGCDCPVC--ASTDPRYGRTRSSILVeaDGTRLLIDAGPDLREQLLRLGLdpsKIDAILLTHEH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  76 FDHIGGLPEL---QIFKHIKLYAHAKTLEVAEYLQKRFVGESRWNWEYFPLEFNRWYDFG-FKVYHFKVAHQPIEVAGgF 151
Cdd:COG1235   79 ADHIAGLDDLrprYGPNPIPVYATPGTLEALERRFPYLFAPYPGKLEFHEIEPGEPFEIGgLTVTPFPVPHDAGDPVG-Y 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459 152 IIQIGNKKIVITGDTGPEileDKKTLEEISNADLLVAEMTHKHSIPkTHLGVEDAIKLAQKVRAKKTVFVHISHTNYTHE 231
Cdd:COG1235  158 RIEDGGKKLAYATDTGYI---PEEVLELLRGADLLILDATYDDPEP-GHLSNEEALELLARLGPKRLVLTHLSPDNNDHE 233

                        250       260
                 ....*....|....*....|....*.
gi 851302459 232 ------ELEEKAKEYLIARDFMHLEI 251
Cdd:COG1235  234 ldydelEAALLPAGVEVAYDGMEIEL 259
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
1-251 3.74e-36

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 128.39  E-value: 3.74e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459   1 MKIIILGSGiySGTPKPlcdCENCS----RARKypqykrTRFsmyipkikaLIDPSPDLHYHLERLNMP---VKHVFITH 73
Cdd:COG1234    1 MKLTFLGTG--GAVPTP---GRATSsyllEAGG------ERL---------LIDCGEGTQRQLLRAGLDprdIDAIFITH 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  74 AHFDHIGGLPELQIF-------KHIKLYAHAKTLEVAEYLQKRFVGESRWNWEYFPLEFNRWYDFG-FKVYHFKVAHqPI 145
Cdd:COG1234   61 LHGDHIAGLPGLLSTrslagreKPLTIYGPPGTKEFLEALLKASGTDLDFPLEFHEIEPGEVFEIGgFTVTAFPLDH-PV 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459 146 EvAGGFIIQIGNKKIVITGDTGPeileDKKTLEEISNADLLVAEMTHKHSIPKT-----HLGVEDAIKLAQKVRAKKTVF 220
Cdd:COG1234  140 P-AYGYRFEEPGRSLVYSGDTRP----CEALVELAKGADLLIHEATFLDEEAELaketgHSTAKEAAELAAEAGVKRLVL 214

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 851302459 221 VHISHTNYTHEELEEKAKEY-----LIARDFMHLEI 251
Cdd:COG1234  215 THFSPRYDDPEELLAEARAVfpgpvELAEDGMVIEL 250
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 1-187 5.38e-27

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


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 102.94  E-value: 5.38e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459   1 MKIIILGSGIYSGTPKPLCDCENCsrARKYPQYKRTRFSMYI--PKIKALIDPSPDLHYHLERLNMP-VKHVFITHAHFD 77
Cdd:cd16279    1 MKLTFLGTGTSSGVPVIGCDCGVC--DSSDPKNRRLRSSILIetGGKNILIDTGPDFRQQALRAGIRkLDAVLLTHAHAD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  78 HIGGLPELQIF-----KHIKLYAHAKTLevaEYLQKRF----VGESRWNWEYFPL----EFNRWYDFGFKVYHFKVAHQP 144
Cdd:cd16279   79 HIHGLDDLRPFnrlqqRPIPVYASEETL---DDLKRRFpyffAATGGGGVPKLDLhiiePDEPFTIGGLEITPLPVLHGK 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 851302459 145 IEVAgGFIIQignkKIVITGDTGpEIleDKKTLEEISNADLLV 187
Cdd:cd16279  156 LPSL-GFRFG----DFAYLTDVS-EI--PEESLEKLRGLDVLI 190
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 64-250 2.42e-23

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: 94.82  E-value: 2.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  64 MPVKHVFITHAHFDHIGGLPEL-------QIFKHIKLYAHAKTLEVAEYLQKRFVGESRwnweyFPLEFN--------RW 128
Cdd:cd07717   49 SKIDRIFITHLHGDHILGLPGLlstmsllGRTEPLTIYGPKGLKEFLETLLRLSASRLP-----YPIEVHelepdpglVF 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459 129 YDFGFKVYHFKVAHqPIEvAGGFIIQIGnKKIVITGDTGPeileDKKTLEEISNADLLVAEMTHKHS-----IPKTHLGV 203
Cdd:cd07717  124 EDDGFTVTAFPLDH-RVP-CFGYRFEEG-RKIAYLGDTRP----CEGLVELAKGADLLIHEATFLDDdaekaKETGHSTA 196

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 851302459 204 EDAIKLAQKVRAKKTVFVHIShTNYTH-EELEEKAKEY----LIARDFMHLE 250
Cdd:cd07717  197 KQAAEIAKKAGVKKLVLTHFS-ARYKDpEELLKEARAVfpntILAEDFMTIE 247
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 48-223 2.81e-22

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: 90.45  E-value: 2.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459   48 LIDPSPDLHYHLERLNMPVK-------HVFITHAHFDHIGGLPELQIFKHIKLYAHAKTLEVAEYLQKRFVGESRWNWEY 120
Cdd:pfam12706   4 LIDPGPDLRQQALPALQPGRlrddpidAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLRRNFPYLFLLEHYGVRV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  121 FPLEFNRWYDFG--------FKVYHF--KVAHQPIEVAGGFIIQIGNKKIVITGDTG---PEILEdkktleEISNADLLV 187
Cdd:pfam12706  84 HEIDWGESFTVGdggltvtaTPARHGspRGLDPNPGDTLGFRIEGPGKRVYYAGDTGyfpDEIGE------RLGGADLLL 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 851302459  188 AEMT---HKHSIPKTHLGVEDAIKLAQKVRAKKTVFVHI 223
Cdd:pfam12706 158 LDGGawrDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK02113 PRK02113
MBL fold metallo-hydrolase;
1-235 1.18e-21

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 90.23  E-value: 1.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459   1 MKIIILGSGIYSGTPKPLCDCENCSraRKYPQYKRTRFSMYIPK--IKALIDPSPDLHYHLERLNM-PVKHVFITHAHFD 77
Cdd:PRK02113   1 MKIRILGSGTSTGVPEIGCTCPVCT--SKDPRDNRLRTSALVETegARILIDCGPDFREQMLRLPFgKIDAVLITHEHYD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  78 HIGGLPELQIF---KHIKLYAHAKtleVAEYLQKR----FVGESRWNWEYFPLEfNRWYDFGFKVYHFKVahQPIEVAGG 150
Cdd:PRK02113  79 HVGGLDDLRPFcrfGEVPIYAEQY---VAERLRSRmpycFVEHSYPGVPNIPLR-EIEPDRPFLVNHTEV--TPLRVMHG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459 151 FI----IQIGNKKIVITGDTGPEiledkKTLEEISNADLLVAEMTHKHSIPkTHLGVEDAIKLAQKVRAKKTVFVHISHT 226
Cdd:PRK02113 153 KLpilgYRIGKMAYITDMLTMPE-----EEYEQLQGIDVLVMNALRIAPHP-THQSLEEALENIKRIGAKETYLIHMSHH 226


                 ....*....
gi 851302459 227 NYTHEELEE 235
Cdd:PRK02113 227 IGLHADVEK 235
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 42-190 5.42e-17

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: 76.15  E-value: 5.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  42 IPKIKALIDPSPDLHYHLERLNMP---VKHVFITHAHFDHIGGLPELQIFKH-------IKLYAHAKTLEVAEYLQKRFV 111
Cdd:cd16272   24 TGGTRILLDCGEGTVYRLLKAGVDpdkLDAIFLSHFHLDHIGGLPTLLFARRyggrkkpLTIYGPKGIKEFLEKLLNFPV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459 112 GESrwnWEYFPLEFNRW------YDFG-FKVYHFKVAHQPIEVagGFIIQIGNKKIVITGDTGPeileDKKTLEEISNAD 184
Cdd:cd16272  104 EIL---PLGFPLEIEELeeggevLELGdLKVEAFPVKHSVESL--GYRIEAEGKSIVYSGDTGP----CENLVELAKGAD 174


                 ....*.
gi 851302459 185 LLVAEM 190
Cdd:cd16272  175 LLIHEC 180
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 47-166 3.32e-15

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: 71.55  E-value: 3.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  47 ALIDPSPDLHY----HLERLNMPVKHVFITHAHFDHIGGLPELQIFKHIKLYAHAKTlevAEYLQKRFVGESRWNWEYFP 122
Cdd:cd06262   23 ILIDPGAGALEkileAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEAD---AELLEDPELNLAFFGGGPLP 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 851302459 123 LEFN-RWYDFGFKvyhFKVAHQPIEV-------AGGFIIQIGNKKIVITGDT 166
Cdd:cd06262  100 PPEPdILLEDGDT---IELGGLELEVihtpghtPGSVCFYIEEEGVLFTGDT 148
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 47-169 6.31e-15

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: 70.66  E-value: 6.31e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459    47 ALIDP----SPDLHYHLERLN-MPVKHVFITHAHFDHIGGLPELQIFKHIKLYAHAKTLEVAEYLQKRFVGESRWNWeyf 121
Cdd:smart00849  12 ILIDTgpgeAEDLLAELKKLGpKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLALLGELGAEAE--- 88

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 851302459   122 PLEFNRWYDFG----FKVYHFKVAHQPIEVAGGFIIQIGNKKIVITGDTGPE 169
Cdd:smart00849  89 PAPPDRTLKDGdeldLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFA 140
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 47-166 2.37e-13

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: 67.02  E-value: 2.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  47 ALIDPSPDLHYH------LERLNMPVKHVFITHAHFDHIGGLPELQIFKHIKLYAHAKTLEVAEYLQKRFVgesrwnWEY 120
Cdd:COG0491   27 VLIDTGLGPADAeallaaLAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEAPAAGAL------FGR 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 851302459 121 FPLEFNRWYDFGfkvYHFKVAHQPIEV-------AGGFIIQIGNKKIVITGDT 166
Cdd:COG0491  101 EPVPPDRTLEDG---DTLELGGPGLEVihtpghtPGHVSFYVPDEKVLFTGDA 150
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 66-187 8.94e-13

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: 64.84  E-value: 8.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  66 VKHVFITHAHFDHIGGLPELQIF-------KHIKLYAHAKTLEVAEYLQK--RFVGESRWNWEYFPLEFNRWY----DF- 131
Cdd:cd07719   52 LDAVFLTHLHSDHVADLPALLLTawlagrkTPLPVYGPPGTRALVDGLLAayALDIDYRARIGDEGRPDPGALvevhEIa 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 851302459 132 ---------GFKVYHFKVAHQPIEVAGGFIIQIGNKKIVITGDTGPEiledkKTLEEIS-NADLLV 187
Cdd:cd07719  132 aggvvyeddGVKVTAFLVDHGPVPPALAYRFDTPGRSVVFSGDTGPS-----ENLIELAkGADLLV 192
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 48-222 1.86e-12

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 64.55  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  48 LIDP--------SPDLHYHLERLNmPVKHVFITHAHFDHIGGLPELQI-FKHIKLYAhakTLEVAEYLQKRfvGESRW-- 116
Cdd:COG2220   24 LIDPvfsgraspVNPLPLDPEDLP-KIDAVLVTHDHYDHLDDATLRALkRTGATVVA---PLGVAAWLRAW--GFPRVte 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459 117 --NWEYFPLEfnrwydfGFKVYHFKVAHQPIEV------AGGFIIQIGNKKIVITGDTGpeILEDKKTLEEISNADLLVA 188
Cdd:COG2220   98 ldWGESVELG-------GLTVTAVPARHSSGRPdrngglWVGFVIETDGKTIYHAGDTG--YFPEMKEIGERFPIDVALL 168

                        170       180       190
                 ....*....|....*....|....*....|....
gi 851302459 189 EMthkhSIPKTHLGVEDAIKLAQKVRAKKTVFVH 222
Cdd:COG2220  169 PI----GAYPFTMGPEEAAEAARDLKPKVVIPIH 198
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 66-225 2.50e-12

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: 64.93  E-value: 2.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  66 VKHVFITHAHFDHIGGLPEL------QIFKHIKLYAHAKTLEVaeyLQKRFvgesrWNW--------------EYFPLEF 125
Cdd:cd07735   66 IRHYLITHAHLDHIAGLPLLspndggQRGSPKTIYGLPETIDA---LKKHI-----FNWviwpdftsipsgkyPYLRLEP 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459 126 N-RWYD---FGFKVYHFKVAHqPIEVAGGFIIQIGNKKIVITGDTGPEILEDKKTLEEI-------------------SN 182
Cdd:cd07735  138 IePEYPialTGLSVTAFPVSH-GVPVSTAFLIRDGGDSFLFFGDTGPDSVSKSPRLDALwralaplipkklkaiiiecSF 216

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 851302459 183 ADLLVAEMTHKHSIPKtHLgVEDAIKLAQKVR--AKKTVFVHISH 225
Cdd:cd07735  217 PNSRPDALLYGHLTPK-LL-AEELAKLAKEVLkgALKGLNVIITH 259
PRK00055 PRK00055
ribonuclease Z; Reviewed
 64-251 3.48e-12

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 64.43  E-value: 3.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  64 MPVKHVFITHAHFDHIGGLPELqifkhiklyahaktlevaeyLQkrfvgeSRWNWE-------YFP------LE-FNRWY 129
Cdd:PRK00055  52 RKIDKIFITHLHGDHIFGLPGL--------------------LS------TRSLSGrtepltiYGPkgikefVEtLLRAS 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459 130 DF-GFKVYH--------------FKVAHQP----------IEVAGGFII---------QIGnKKIVITGDTGP--EIled 173
Cdd:PRK00055 106 GSlGYRIAEkdkpgkldaeklkaLGVPPGPlfgklkrgedVTLEDGRIInpadvlgppRKG-RKVAYCGDTRPceAL--- 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459 174 kktLEEISNADLLVAEMTHKHS-----IPKTHLGVEDAIKLAQKVRAKKTVFVHIShTNYTH--EELEEKAKEY----LI 242
Cdd:PRK00055 182 ---VELAKGADLLVHEATFGDEdeelaKEYGHSTARQAAEIAKEAGVKRLILTHFS-PRYTGdpEELLKEAREIfpntEL 257


                 ....*....
gi 851302459 243 ARDFMHLEI 251
Cdd:PRK00055 258 AEDLMRVEV 266
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 64-251 4.13e-12

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: 64.55  E-value: 4.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459   64 MPVKHVFITHAHFDHIGGLPELqiFKHIKLYAHAKTLEV------AEYLQKRF-VGESRWNweyFPLEF-------NRWY 129
Cdd:TIGR02651  50 MKIDRIFITHLHGDHILGLPGL--LSTMSFQGRKEPLTIygppgiKEFIETSLrVSYTYLN---YPIKIheieeggLVFE 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  130 DFGFKVYHFKVAHQ------------------------------PI--EVAGGFIIQIGN----------------KKIV 161
Cdd:TIGR02651 125 DDGFKVEAFPLDHSipslgyrfeekdrpgkfdrekakelgippgPLygKLKRGETVTLIDgriidpedvlgpprkgRKIA 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  162 ITGDTGPEiledKKTLEEISNADLLVAEMT-----HKHSIPKTHLGVEDAIKLAQKVRAKKTVFVHIShTNYT--HEELE 234
Cdd:TIGR02651 205 YTGDTRPC----EEVIEFAKNADLLIHEATfldedKKLAKEYGHSTAAQAAEIAKEANVKRLILTHIS-PRYSdeEELLE 279

                         250       260
                  ....*....|....*....|
gi 851302459  235 EKAKEY---LIARDFMHLEI 251
Cdd:TIGR02651 280 EAKKIFpntYIAEDFMEIEI 299
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 1-95 2.07e-11

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: 61.10  E-value: 2.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459   1 MKIIILGSGIYSGTPKPLCDCENCSRARKYPQYKRTRFSMYIP--KIKALIDP-SPDLHyhlERLNmPVK--HVFITHAH 75
Cdd:cd07736    1 MKLTFLGTGDAGGVPVYGCDCSACQRARQDPSYRRRPCSALIEvdGERILLDAgLTDLA---ERFP-PGSidAILLTHFH 76

                         90       100
                 ....*....|....*....|..
gi 851302459  76 FDHIGGLPELQ--IFKHIKLYA 95
Cdd:cd07736   77 MDHVQGLFHLRwgVGDPIPVYG 98
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
47-225 3.43e-11

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 60.85  E-value: 3.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459   47 ALIDPSPDLHYHLERLNM-------PVKHVFITHAHFDHIGGLPELQ------IFKHIKLYAHAKTLEVAEYLQKRFVGE 113
Cdd:pfam00753  18 VLIDTGGSAEAALLLLLAalglgpkDIDAVILTHGHFDHIGGLGELAeatdvpVIVVAEEARELLDEELGLAASRLGLPG 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  114 SRWNWEYFPLEFNRWYDFGFKVYHFKVAHQPIEVAGGFIIQIGNKKIVITGDTGPeiledkkTLEEISNADLLVAEMTHK 193
Cdd:pfam00753  98 PPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLF-------AGEIGRLDLPLGGLLVLH 170

                         170       180       190
                  ....*....|....*....|....*....|..
gi 851302459  194 HSIpkthlgVEDAIKLAQKVRAKKTVFVHISH 225
Cdd:pfam00753 171 PSS------AESSLESLLKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-222 4.24e-11

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: 60.67  E-value: 4.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  48 LIDPSPDLHYHLERLNMPVKH---VFITHAHFDH-------IGGLPELQIFKHIKLYAHAKTL----EVAEYLQKRFVGE 113
Cdd:cd07741   33 HIDPGPGALVRMCRPKLDPTKldaIILSHRHLDHsndanvlIEAMTEGGFKKRGTLLAPEDALngepVVLLYYHRRKLEE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459 114 SRwNWEyfplEFNRWYDFGFKVYHFKVAHQPiEVAGGFIIQIGNKKIVITGDTgpEILEDkkTLEEISNADLLVAEMTHK 193
Cdd:cd07741  113 IE-ILE----EGDEYELGGIKIEATRHKHSD-PTTYGFIFRTSDKKIGYISDT--RYFEE--LIEYYSNCDVLIINVTRP 182

                        170       180       190
                 ....*....|....*....|....*....|
gi 851302459 194 HSIP-KTHLGVEDAIKLAQKVRAKKTVFVH 222
Cdd:cd07741  183 RPRKgVDHLSVEDVEKILKEIKPKLAILTH 212
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
66-180 4.90e-11

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 61.51  E-value: 4.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  66 VKHVFITHAHFDHIGGLPEL-QIFKHIKLYAHAKTLEVaeyLQKRFvgesrWNWEYFPlefnrwyDFG-------FKVYH 137
Cdd:COG5212   73 IKGYLISHAHLDHIAGLPILsPDDSPKTIYALPETIDA---LRNHY-----FNWVIWP-------DFTdigsaphLPKYR 137

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 851302459 138 FKVAH--QPIEVAG-----------------GFIIQIGNKKIVITGDTGPEILEDKKTLEEI 180
Cdd:COG5212  138 YVPLKpgQTFPLGGtglrvtafplshsvpssAFLIESGGGAFLYSGDTGPDEVEKSTNLDAL 199
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 65-191 2.15e-09

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 57.12  E-value: 2.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  65 PVKHVFITHAHFDHIGGLPELQI-FKHIKLYAHAKTLEVAE-------YLQKRfvgESRWNWEYFPLEFNRWYDFgFKVY 136
Cdd:COG1236   50 DVDAVVLTHAHLDHSGALPLLVKeGFRGPIYATPATADLARillgdsaKIQEE---EAEAEPLYTEEDAERALEL-FQTV 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 851302459 137 HFkvaHQPIEVAG--------GFI-------IQIGNKKIVITGDTGPeilEDKKTL---EEISNADLLVAEMT 191
Cdd:COG1236  126 DY---GEPFEIGGvrvtfhpaGHIlgsaqveLEVGGKRIVFSGDYGR---EDDPLLappEPVPPADVLITEST 192
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 25-165 5.01e-09

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: 54.54  E-value: 5.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  25 SRARKYPQYKRTRFSM-YIPKIKALIDPSPDLHYHLERLNMPVKHVFITHAHFDHIGGLPELQifKHIKLYAHAKTLEVA 103
Cdd:cd07732   34 DPESKYFDEVLDFLELgLLPDIVGLYRDPLLLGGLRSEEDPSVDAVLLSHAHLDHYGLLNYLR--PDIPVYMGEATKRIL 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 851302459 104 EYLQKRFVGESRWNWEYFPLEFNRWYDFG-FKVyhfkvahQPIEV------AGGFIIQIGNKKIVITGD 165
Cdd:cd07732  112 KALLPFFGEGDPVPRNIRVFESGKSFTIGdFTV-------TPYLVdhsapgAYAFLIEAPGKRIFYTGD 173
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 65-104 8.25e-09

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: 54.15  E-value: 8.25e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 851302459  65 PVKHVFITHAHFDHIGGLPELQIFKHIKLYAHAKTLEVAE 104
Cdd:cd07721   49 DIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEREAPYLE 88
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 56-189 1.19e-08

uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. Members of this bacterial subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 53.21  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  56 HYHLERLNmpvkHVFITHAHFDHIGGLPELQIF----------KHIKLYAHAKT---LEVAEYLQKRFVGesrwnweyFP 122
Cdd:cd07716   45 YIDPEDLD----AVVLSHLHPDHCADLGVLQYArryhprgarkPPLPLYGPAGPaerLAALYGLEDVFDF--------HP 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 851302459 123 LEFNRWYDFG-FKVYHFKVAHqPIEvAGGFIIQIGNKKIVITGDTGPEilEDkktLEEIS-NADLLVAE 189
Cdd:cd07716  113 IEPGEPLEIGpFTITFFRTVH-PVP-CYAMRIEDGGKVLVYTGDTGYC--DE---LVEFArGADLLLCE 174
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 39-189 1.24e-08

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


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 53.23  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  39 SMY---IPKIKALID----PSPDLHYHLERLNMPVKH-----VFITHAHFDHIGGLPELqiFKH---IKLYAHAKTLEVA 103
Cdd:cd16295   13 SCYlleTGGKRILLDcglfQGGKELEELNNEPFPFDPkeidaVILTHAHLDHSGRLPLL--VKEgfrGPIYATPATKDLA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459 104 EYLQKRFV---GESRWNWEYFPLefnrwYDFG--------FKVYHFkvaHQPIEVAGGF--------------IIQI--- 155
Cdd:cd16295   91 ELLLLDSAkiqEEEAEHPPAEPL-----YTEEdvekalkhFRPVEY---GEPFEIGPGVkvtfydaghilgsaSVELeig 162

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 851302459 156 GNKKIVITGDTGPE---ILEDKktlEEISNADLLVAE 189
Cdd:cd16295  163 GGKRILFSGDLGRKntpLLRDP---APPPEADYLIME 196
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 47-99 4.57e-08

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 51.31  E-value: 4.57e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 851302459  47 ALIDPS---PDLHYhLERLNMPVKHVFITHAHFDHIGGLPEL-QIFKHIKLYAHAKT 99
Cdd:cd07723   23 AVVDPGeaePVLAA-LEKNGLTLTAILTTHHHWDHTGGNAELkALFPDAPVYGPAED 78
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 47-86 7.07e-08

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 50.95  E-value: 7.07e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 851302459  47 ALIDPSPDLHYHLERL-----NMPVKHVFITHAHFDHIGGLPELQ 86
Cdd:cd16278   30 VVIDPGPDDPAHLDALlaalgGGRVSAILVTHTHRDHSPGAARLA 74
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 60-104 1.44e-07

metallo-beta-lactamases, subclass B1; 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. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. Includes chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1.


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 50.36  E-value: 1.44e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 851302459  60 ERLNMPVKHVFITHAHFDHIGGLPELQIfKHIKLYAHAKTLEVAE 104
Cdd:cd16285   58 KKLGKPVTAAISTHSHDDRTGGIKALNA-RGIPTYATALTNELAK 101
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 38-175 1.60e-07

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: 51.08  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  38 FSMYI--PKIKALID--PSPDLHYHLERLNMP---VKHVFITHAHFDHIGGLPE-LQIFKHIKLYAHAKTLEvaEYLQKR 109
Cdd:cd07713   21 LSLLIetEGKKILFDtgQSGVLLHNAKKLGIDlsdIDAVVLSHGHYDHTGGLKAlLELNPKAPVYAHPDAFE--PRYSKR 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 851302459 110 FVGESRWNWEYFPLEFNrwydfGFKVYHFKvahQPIEVAGGFII--QIGNKKIVITGDTGPEILEDKK 175
Cdd:cd07713   99 GGGKKGIGIGREELEKA-----GARLVLVE---EPTEIAPGVYLtgEIPRVTDFEKGNPGLFVKEDGG 158
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 47-165 1.66e-07

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: 50.43  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  47 ALIDP---SPDLHYHLERLNMPVKHVFITHAHFDHIGGLPELQIFKHIKLYAHAKTLEVAEYLQKrfvGESRWNWEYFPL 123
Cdd:cd16322   25 VLVDPgdeSEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDLPLYEAADL---GAKAFGLGIEPL 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 851302459 124 ----------EFNRWYDFGFKVYHFKvAHQPIEVAggFIIQigNKKIVITGD 165
Cdd:cd16322  102 pppdrlledgQTLTLGGLEFKVLHTP-GHSPGHVC--FYVE--EEGLLFSGD 148
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 47-165 3.98e-07

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: 49.10  E-value: 3.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  47 ALID--PSPDLHYHL-----ERLNMPVKHVFITHAHFDHIGGlpeLQIFK--HIKLYAHAKTlevAEYLQKRfvGESRWN 117
Cdd:cd16282   27 VVIDtgASPRLARALlaairKVTDKPVRYVVNTHYHGDHTLG---NAAFAdaGAPIIAHENT---REELAAR--GEAYLE 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 851302459 118 WEYFPLEF----------NRWY------DFG---FKVYHFKVAHQPievaGGFIIQIGNKKIVITGD 165
Cdd:cd16282   99 LMRRLGGDamagtelvlpDRTFddgltlDLGgrtVELIHLGPAHTP----GDLVVWLPEEGVLFAGD 161
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 53-165 6.94e-07

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 48.94  E-value: 6.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  53 PDLHYHLERLNmPVKHVFITHAHFDHIGGLPELqIFKH-IKLYAHAKTLEVAEYLQKRFVGESRWNweYFPLEFNRWYDF 131
Cdd:cd07714   44 PDFSYLEENKD-KIKGIFITHGHEDHIGALPYL-LPELnVPIYATPLTLALIKKKLEEFKLIKKVK--LNEIKPGERIKL 119

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 851302459 132 G-FKVYHFKVAHQPIEvAGGFIIQIGNKKIVITGD 165
Cdd:cd07714  120 GdFEVEFFRVTHSIPD-SVGLAIKTPEGTIVHTGD 153
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
53-104 7.57e-07

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 49.68  E-value: 7.57e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 851302459  53 PDLHYHLERLNMpVKHVFITHAHFDHIGGLPELqiFKHIK--LYAHAKTLEVAE 104
Cdd:COG0595   52 PDISYLEENKDK-IKGIVLTHGHEDHIGALPYL--LKELNvpVYGTPLTLALLE 102
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 47-105 8.42e-07

Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; Bacillus amyloliquefaciens BaeB may play a role in the synthesis of the antibiotic polyketide bacillaene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293833 [Multi-domain]  Cd Length: 174  Bit Score: 47.92  E-value: 8.42e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 851302459  47 ALIDPSPDLHYHLERLNMP---VKHVFITHAHFDHIGGLPELQIFKHIKLYAHAKTLEVAEY 105
Cdd:cd16275   26 AVVDPAWDIEKILAKLNELgltLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDYYGF 87
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-189 9.08e-07

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: 48.02  E-value: 9.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  35 RTRFSMYIPKIKALIDPSPDLHYHLERLNM---PVKHVFITHAHFDHIGGLP----ELQIF----KHIKLYAHAKTLEVA 103
Cdd:cd07740   16 NTCFHVASEAGRFLIDCGASSLIALKRAGIdpnAIDAIFITHLHGDHFGGLPffllDAQFVakrtRPLTIAGPPGLRERL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459 104 EY-LQKRFVGESR------WNWEYF----PLEFNRWydfgfKVYHFKVAHQPIEVAGGFIIQIGNKKIVITGDTGPeile 172
Cdd:cd07740   96 RRaMEALFPGSSKvprrfdLEVIELepgePTTLGGV-----TVTAFPVVHPSGALPLALRLEAAGRVLAYSGDTEW---- 166

                        170
                 ....*....|....*...
gi 851302459 173 dKKTLEEIS-NADLLVAE 189
Cdd:cd07740  167 -TDALVPLArGADLFICE 183
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 54-165 9.90e-07

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: 48.36  E-value: 9.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  54 DLHYHLERLNM-P--VKHVFITHAHFDHIGGLPElqiFKHIKLYAHAKTLEVAeylqkrfvgESRWNWEYFPLEFNRWYD 130
Cdd:cd07729   74 TLEEQLARLGLdPedIDYVILSHLHFDHAGGLDL---FPNATIIVQRAELEYA---------TGPDPLAAGYYEDVLALD 141

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 851302459 131 FGFKVYHFKVAHQPIEVAGG---------------FIIQIGNKKIVITGD 165
Cdd:cd07729  142 DDLPGGRVRLVDGDYDLFPGvtliptpghtpghqsVLVRLPEGTVLLAGD 191
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
66-153 1.66e-06

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 47.96  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  66 VKHVFITHAHFDHIGGLPE-LQIFKHIKLYAHAKTLEvaeylqKRFVGesRWNWEYFPLEFNRwYDFGFKVYHFKVAHQP 144
Cdd:COG1237   58 IDAVVLSHGHYDHTGGLPAlLELNPKAPVYAHPDAFE------KRYSK--RPGGKYIGIPFSR-EELEKLGARLILVKEP 128


                 ....*....
gi 851302459 145 IEVAGGFII 153
Cdd:COG1237  129 TEIAPGVYL 137
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 47-96 3.03e-06

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: 46.72  E-value: 3.03e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 851302459  47 ALID--PSPDLHYHLERLN----MP--VKHVFITHAHFDHIGGLPEL-QIFKHIKLYAH 96
Cdd:cd07726   28 ALIDtgPSSSVPRLLAALEalgiAPedVDYIILTHIHLDHAGGAGLLaEALPNAKVYVH 86
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 68-187 3.81e-06

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: 46.34  E-value: 3.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  68 HVFITHAHFDHIGGLPelqIFK-------HIKLYAHAKTLEVAEYLQKRFVGESrwnweYFPLEFNrwYDFGFKVYHFKV 140
Cdd:cd07715   60 HLLLSHTHWDHIQGFP---FFApaydpgnRIHIYGPHKDGGSLEEVLRRQMSPP-----YFPVPLE--ELLAAIEFHDLE 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 851302459 141 AHQPIEVAG---------------GFIIQIGNKKIVITGDTGPEILE---DKKTLEEISNADLLV 187
Cdd:cd07715  130 PGEPFSIGGvtvttiplnhpggalGYRIEEDGKSVVYATDTEHYPDDgesDEALLEFARGADLLI 194
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-101 6.05e-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) 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: 46.11  E-value: 6.05e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 851302459  35 RTRFSMYIPKIKALI-------DPSPDLHYHLERLNMP---VKHVFITHAHFDHIGGLPElqiFKHIKLYAHAKTLE 101
Cdd:cd07730   43 RKDFEEYTPRVPERLyrtpvplEVEEDVAEQLAAGGIDpedIDAVILSHLHWDHIGGLSD---FPNARLIVGPGAKE 116
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 69-174 8.18e-06

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: 44.56  E-value: 8.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  69 VFITHAHFDHIGGLPELQIFKHIKLYAHAKTLEVAEylQKRFVGESRwnwEYFPLEFNRWYDFG-FKVYHFKVAHQPIEV 147
Cdd:cd07733   49 ILVTHEHADHIKGLGVLARKYNVPIYATAGTLRAME--RKVGLIDVD---QKQIFEPGETFSIGdFDVESFGVSHDAADP 123

                         90       100
                 ....*....|....*....|....*..
gi 851302459 148 AgGFIIQIGNKKIVITGDTGPEILEDK 174
Cdd:cd07733  124 V-GYRFEEGGRRFGMLTDLKQRILSDR 149
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 44-166 1.01e-05

Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Salmonella enterica serovar typhimurium YcbL which has type II hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as glyoxalase II) activity, and has a single metal ion binding site, and Thermus thermophilus TTHA1623 which does not have GLX2 activity and has two metal ion binding sites with a glyoxalase II-type metal coordination. 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: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 44.85  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  44 KIKALIDP---SPDLHYHLERLNMPVKHVFITHAHFDHIGGLPELQIFKHIKLY----AHAKTLEVAEYLQKRFVGEsrw 116
Cdd:cd07737   22 KEAAVIDPggdADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIgphkEDKFLLENLPEQSQMFGFP--- 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 851302459 117 nwEYFPLEFNRWYDFGFKV----YHFKVAHQPIEVAGGFIIQIGNKKIVITGDT 166
Cdd:cd07737   99 --PAEAFTPDRWLEEGDTVtvgnLTLEVLHCPGHTPGHVVFFNRESKLAIVGDV 150
PQQB-like_MBL-fold cd16274
Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold ...
 1-102 1.03e-05

Coenzyme pyrroloquinoline quinone (PQQ) synthesis protein B and related proteins; MBL-fold metallo hydrolase domainhydrolase domain; PQQB is essential for the synthesis of the cofactor pyrroloquinoline quinone (PQQ) in Klebsiella pneumonia. PqqB is not directly involved in the PQQ biosynthesis but may serve as a carrier for PQQ when PQQ is released from PqqC. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293832 [Multi-domain]  Cd Length: 220  Bit Score: 45.30  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459   1 MKIIILGSGIYSGTPKPLCDCENCSRARKY-PQYK-RTRFSMYI-------------PKIKALIDPSPDLHYHLERLNMP 65
Cdd:cd16274    1 MRIKVLGSAAGGGFPQWNCNCPNCALARAGdGRATaRTQSSIAVsadgenwvlinasPDIRQQIEATPELQPRPGLRDTP 80

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 851302459  66 VKHVFITHAHFDHIGGLPELQIFKHIKLYAHAKTLEV 102
Cdd:cd16274   81 IAAVLLTDAEIDHTTGLLSLREGQPLTVYATAPVLED 117
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 59-105 1.36e-05

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 44.44  E-value: 1.36e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 851302459  59 LERLNMPVKHVFITHAHFDHIGGLPELQIFKHIKLYAHAKTLEVAEY 105
Cdd:cd07743   39 LEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAFIEN 85
PRK05184 PRK05184
pyrroloquinoline quinone biosynthesis protein PqqB; Provisional
 1-102 4.11e-05

pyrroloquinoline quinone biosynthesis protein PqqB; Provisional


Pssm-ID: 235361 [Multi-domain]  Cd Length: 302  Bit Score: 44.04  E-value: 4.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459   1 MKIIILGSGIYSGTPKPLCDCENCSRARK-YPQYK-RTRFSMYI-------------PKIKALIDPSPDLH-YHLERlNM 64
Cdd:PRK05184   1 MRIIVLGSAAGGGFPQWNCNCPNCRGARAgTIRAKpRTQSSIAVsadgedwvllnasPDIRQQIQATPALQpARGLR-DT 79

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 851302459  65 PVKHVFITHAHFDHIGGLPELQIFKHIKLYAHAKTLEV 102
Cdd:PRK05184  80 PIAAVVLTDGQIDHTTGLLTLREGQPFPVYATPAVLED 117
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 39-160 4.34e-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: 43.73  E-value: 4.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  39 SMYIPKIKALIDPSpdlhyhLERLNM---PVKHVFITHAHFDHIGGlpelqifkhiklyahaktlevAEYLQKRF---VG 112
Cdd:cd16280   38 ALNNNEAADLIVDG------LEKLGLdpaDIKYILITHGHGDHYGG---------------------AAYLKDLYgakVV 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 851302459 113 ESRWNWEyfplEFNRWYDFGFKVYHFKVAHQPIEVAGGFIIQIGNKKI 160
Cdd:cd16280   91 MSEADWD----MMEEPPEEGDNPRWGPPPERDIVIKDGDTLTLGDTTI 134
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 65-122 8.44e-05

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


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 42.10  E-value: 8.44e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 851302459  65 PVKHVFITHAHFDHIGGLPELQ-IFKHIKLYAHAKTlevAEYLQKRFVGESRWNWEYFP 122
Cdd:cd07739   52 TLTTIYITHGHPDHYFGLEVLLeAFPDAKVVATPAV---VAHIKAQLEPKLAFWGPLLG 107
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 40-96 8.92e-05

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 42.14  E-value: 8.92e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  40 MYIPKIKALIDpspdlhyhlERLNMPVKHVFITHAHFDHIGGLPELQ---IFKHIKLYAH 96
Cdd:cd07722   40 SYIPLLKSVLD---------SEGNATISDILLTHWHHDHVGGLPDVLdllRGPSPRVYKF 90
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-101 1.12e-04

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 41.80  E-value: 1.12e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 851302459  48 LIDPSPDLHYHL-----ERLNMPVKHVFITHAHFDHIGGlpeLQIFK--HIKLYAHAKTLE 101
Cdd:cd16276   23 VVDAPPSLGENLlaairKVTDKPVTHVVYSHNHADHIGG---ASIFKdeGATIIAHEATAE 80
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 47-98 1.76e-04

ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; MBL-fold metallo-hydrolase domain; Persulfide dioxygenase (PDO, also known as sulfur dioxygenase, SDO, EC 1.13.11.18) is a non-heme iron-dependent oxygenase which catalyzes the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria. Mutations in ethe1 (the human PDO gene) are responsible for a rare autosomal recessive metabolic disorder called ethylmalonic encephalopathy. Arabidopsis thaliana ETHE1 is essential for embryo and endosperm development. Bacterial ETHE1-type PDOs are also called Type 1 PDOs. Type II PDOs (also called PDOAs), are mainly proteobacterial. 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: 293810 [Multi-domain]  Cd Length: 177  Bit Score: 41.23  E-value: 1.76e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 851302459  47 ALIDPSPDL--HY--HLERLNMPVKHVFITHAHFDHIGGLPELQIFKHIKLYAHAK 98
Cdd:cd07724   26 AVIDPVRDSvdRYldLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGEG 81
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 66-222 2.22e-04

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 41.34  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  66 VKHVFITHAHFDHIGGLPELQIFKHIKLYAHAktlEVAEYLQKRFVGESRwnweyfPLEFNRWYDF-GFKVYHFKVAH-- 142
Cdd:PRK00685  41 VDYILLTHGHGDHLGDTVEIAKRTGATVIANA---ELANYLSEKGVEKTH------PMNIGGTVEFdGGKVKLTPALHss 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459 143 --------QPIEVAGGFIIQIGNKKIVITGDTGpeILEDKKTLEEISNADLLVaemthkhsIP---KTHLGVEDAIKLAQ 211
Cdd:PRK00685 112 sfidedgiTYLGNPTGFVITFEGKTIYHAGDTG--LFSDMKLIGELHKPDVAL--------LPigdNFTMGPEDAALAVE 181

                        170
                 ....*....|.
gi 851302459 212 KVRAKKTVFVH 222
Cdd:PRK00685 182 LIKPKIVIPMH 192
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 60-104 4.05e-04

Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Bacillus cereus Beta-lactamase 2, also called BcII. MBLs (class B of the Ambler beta-lactamase classification) 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. BcII is a chromosome-encoded B1 MBL. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293862 [Multi-domain]  Cd Length: 212  Bit Score: 40.35  E-value: 4.05e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 851302459  60 ERLNMPVKHVFITHAHFDHIGGLPELQifKH-IKLYAHAKTLEVAE 104
Cdd:cd16304   58 KKLKKPVTLAIVTHAHDDRIGGIKALQ--KRgIPVYSTKLTAQLAK 101
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 31-173 4.81e-04

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: 39.97  E-value: 4.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  31 PQYKRTRFSMYIPKIKALIDPSPDLHYHLERLNMP---VKHVFITHAHFDHIGGLPELQIF-KHIKLYA----------- 95
Cdd:cd07738   11 PKGHTSGFIIWINGRGIMVDPPVNSTSYLRQNGISprlVDHVILTHCHADHDAGTFQKILEeEKITLYTtrtinesflrk 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  96 -HAKTLEVAEYLQKRFvgesrwNWE----YFPLEFNRwYDFGFkvyHFKVAHQPievAGGFIIQIGNKKIVITGDT--GP 168
Cdd:cd07738   91 yAALTGLPPDFLEELF------DFRpviiGEKTKING-AEFEF---DYSFHSIP---TIRFKVSYGGKSIAYSGDTryDP 157


                 ....*
gi 851302459 169 EILED 173
Cdd:cd07738  158 DGLKS 162
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 66-82 5.65e-04

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: 40.22  E-value: 5.65e-04
                         10
                 ....*....|....*..
gi 851302459  66 VKHVFITHAHFDHIGGL 82
Cdd:cd07720   92 IDDVLLTHLHPDHIGGL 108
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 68-188 5.79e-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: 40.23  E-value: 5.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 851302459  68 HVFITHAHFDHIGGLPEL-------QIFKHIKLYAHAKTLEVAEYLQKRFV-------GEsRWNWEyfplefnrwyDFGF 133
Cdd:COG2333   55 LLVLTHPDADHIGGLAAVleafpvgRVLVSGPPDTSETYERLLEALKEKGIpvrpcraGD-TWQLG----------GVRF 123

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 851302459 134 KVYHfkvahqPIEVAGG----------FIIQIGNKKIVITGDTGPE----ILEDKKTLeeisNADLLVA 188
Cdd:COG2333  124 EVLW------PPEDLLEgsdennnslvLRLTYGGFSFLLTGDAEAEaeaaLLARGPDL----KADVLKV 182
PRK11539 PRK11539
ComEC family competence protein; Provisional
 53-86 9.46e-04

ComEC family competence protein; Provisional


Pssm-ID: 236924 [Multi-domain]  Cd Length: 755  Bit Score: 40.36  E-value: 9.46e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 851302459  53 PDLHYHlerlNMPVKHVFITHAHFDHIGGLPELQ 86
Cdd:PRK11539 543 PWLRWH----GLTPEGIILSHEHLDHRGGLASLL 572
NorV COG0426
Flavorubredoxin [Energy production and conversion];
47-117 1.75e-03

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 39.04  E-value: 1.75e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 851302459  47 ALIDPSPDLHYH--LERLNM-----PVKHVFITHAHFDHIGGLPE-LQIFKHIKLYAHAKTlevAEYLqKRFVGESRWN 117
Cdd:COG0426   45 ALIDTVGESFFEefLENLSKvidpkKIDYIIVNHQEPDHSGSLPElLELAPNAKIVCSKKA---ARFL-PHFYGIPDFR 119
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 34-101 2.22e-03

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. 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. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 38.24  E-value: 2.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 851302459  34 KRTRFSMYIPKIKALIDPSPdlhyhlerlnmpVKHVFITHAHFDHIGGLPE-LQIFKHIKLYAHAKTLE 101
Cdd:cd07709   49 KEPFFDEFLENLEEVIDPRK------------IDYIVVNHQEPDHSGSLPElLELAPNAKIVCSKKAAR 105
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 66-133 2.60e-03

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


Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 38.37  E-value: 2.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 851302459  66 VKHVFITHAHFDHIGGLPElqiFKHIKLYAHAKTLEVAE-----YLQKRFVG----ESRWnWEYFPLEFNRWydFGF 133
Cdd:cd07742   81 VRHIVLTHLDLDHAGGLAD---FPHATVHVHAAELDAATsprtrYERRRYRPqqlaHGPW-WVTYAAGGERW--FGF 151
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 69-99 3.11e-03

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 37.88  E-value: 3.11e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 851302459  69 VFITHAHFDHIGGLPEL-QIFKHIKLYAHAKT 99
Cdd:PRK10241  49 IFLTHHHHDHVGGVKELvEKFPQIVVYGPQET 80
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 68-92 3.83e-03

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: 37.11  E-value: 3.83e-03
                         10        20
                 ....*....|....*....|....*
gi 851302459  68 HVFITHAHFDHIGGLPElqIFKHIK 92
Cdd:cd07731   51 YLILTHPDADHIGGLDA--VLKNFP 73
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 66-96 4.36e-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: 4.36e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 851302459  66 VKHVFITHAHFDHIGGLPelqIFKHIKLYAH 96
Cdd:cd07711   61 IDYVVLTHGHPDHIGNLN---LFPNATVIVG 88
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 60-103 4.94e-03

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. 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: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 37.09  E-value: 4.94e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 851302459  60 ERLNMPVKHVFITHAHFDHIGG----LPELQIFKhIKLYAHAKTLEVA 103
Cdd:cd07710   51 HTGDKPVKAIIYTHSHPDHFGGaggfVEEEDSGK-VPIIAPEGFMEEA 97
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 66-86 5.55e-03

AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Pseudomonas Aeruginosa AIM-1, Serratia marcescens SMB-1, Erythrobacter vulgaris EVM-1, and Janthinobacterium lividum THIN-B. 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 of AIM-1-,SMB-1-, EVM-1-, THIN-B-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: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 37.33  E-value: 5.55e-03
                         10        20
                 ....*....|....*....|.
gi 851302459  66 VKHVFITHAHFDHIGGLPELQ 86
Cdd:cd16290   61 VKLILNSHAHFDHAGGIAALQ 81
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 66-86 6.50e-03

Bradyrhizobium diazoefficiens BJP-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 of BJP-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: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 37.08  E-value: 6.50e-03
                         10        20
                 ....*....|....*....|.
gi 851302459  66 VKHVFITHAHFDHIGGLPELQ 86
Cdd:cd16309   61 VKYLLNTHAHFDHAGGLAELK 81
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 60-103 8.20e-03

Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; 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 of MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293860  Cd Length: 212  Bit Score: 36.45  E-value: 8.20e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 851302459  60 ERLNMPVKHVFITHAHFDHIGGLPELQifKH-IKLYAHAKTLEVA 103
Cdd:cd16302   59 NSLKAKVKAVVPTHFHDDCLGGLKAFH--RRgIPSYANQKTIALA 101
 
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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