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Conserved domains on  [gi|815699165|ref|WP_046432495|]
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MULTISPECIES: MBL fold metallo-hydrolase [Stenotrophomonas]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869928)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme that may have substrate towards phosphotriesters, esters, and/or lactones

CATH:  3.60.15.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  17597585|12177301|11471246|11513844
SCOP:  3001057

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 43-297 5.32e-105

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: 307.17  E-value: 5.32e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  43 RVGALQVTALFDGVVALGRQEVVDVPPTLVSRLLEGRYVPEDkkGLQTAINAFLVRQGNHLTLVDTGTAQCFGPGLGQVL 122
Cdd:cd07720    2 KVGDFEVTALSDGTLPLPLDLLLGGAAPEAEAALLAAFLPPD--PVETSVNAFLVRTGGRLILVDTGAGGLFGPTAGKLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 123 GNLRASGVDPAEVDEVLLTHAHPDHLCGVLDAQGKPAYPNATVWLSKADADYWLSPASEATAPKGVRFAFPLARNAVAPY 202
Cdd:cd07720   80 ANLAAAGIDPEDIDDVLLTHLHPDHIGGLVDAGGKPVFPNAEVHVSEAEWDFWLDDANAAKAPEGAKRFFDAARDRLRPY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 203 QASGHlrtFSPGDALPGGAVAMDTHGHTPGHVSYRFDSQGQSLLVWGDVLHFHAVQFAHPEAAFEADSDRKAAIASRRGL 282
Cdd:cd07720  160 AAAGR---FEDGDEVLPGITAVPAPGHTPGHTGYRIESGGERLLIWGDIVHHPALQFAHPDWTIAFDVDPEQAAATRRRL 236

                        250
                 ....*....|....*
gi 815699165 283 LQQATANGWWVAGAH 297
Cdd:cd07720  237 LDRAAAEGLLVAGAH 251
 
Name Accession Description Interval E-value
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 43-297 5.32e-105

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: 307.17  E-value: 5.32e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  43 RVGALQVTALFDGVVALGRQEVVDVPPTLVSRLLEGRYVPEDkkGLQTAINAFLVRQGNHLTLVDTGTAQCFGPGLGQVL 122
Cdd:cd07720    2 KVGDFEVTALSDGTLPLPLDLLLGGAAPEAEAALLAAFLPPD--PVETSVNAFLVRTGGRLILVDTGAGGLFGPTAGKLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 123 GNLRASGVDPAEVDEVLLTHAHPDHLCGVLDAQGKPAYPNATVWLSKADADYWLSPASEATAPKGVRFAFPLARNAVAPY 202
Cdd:cd07720   80 ANLAAAGIDPEDIDDVLLTHLHPDHIGGLVDAGGKPVFPNAEVHVSEAEWDFWLDDANAAKAPEGAKRFFDAARDRLRPY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 203 QASGHlrtFSPGDALPGGAVAMDTHGHTPGHVSYRFDSQGQSLLVWGDVLHFHAVQFAHPEAAFEADSDRKAAIASRRGL 282
Cdd:cd07720  160 AAAGR---FEDGDEVLPGITAVPAPGHTPGHTGYRIESGGERLLIWGDIVHHPALQFAHPDWTIAFDVDPEQAAATRRRL 236

                        250
                 ....*....|....*
gi 815699165 283 LQQATANGWWVAGAH 297
Cdd:cd07720  237 LDRAAAEGLLVAGAH 251
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 80-322 7.34e-25

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: 99.76  E-value: 7.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  80 YVPEDKKGLQTAINAFLVRQGNHLTLVDTGTAqcfGPGLGQVLGNLRASGVDpaeVDEVLLTHAHPDHLCGVLDAQGKPa 159
Cdd:COG0491    3 VLPGGTPGAGLGVNSYLIVGGDGAVLIDTGLG---PADAEALLAALAALGLD---IKAVLLTHLHPDHVGGLAALAEAF- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 160 ypNATVWLSKADADYWLSPASEATapkgvrfafpLARNAVAPYqasghlRTFSPGDALPGGAV---AMDTHGHTPGHVSY 236
Cdd:COG0491   76 --GAPVYAHAAEAEALEAPAAGAL----------FGREPVPPD------RTLEDGDTLELGGPgleVIHTPGHTPGHVSF 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 237 RFDSQGqsLLVWGDVLHFHAVQFAHPeaafeADSDRKAAIASRRGLLQQataNGWWVAGAHLPFPGLGHVRGEGQAYAWV 316
Cdd:COG0491  138 YVPDEK--VLFTGDALFSGGVGRPDL-----PDGDLAQWLASLERLLAL---PPDLVIPGHGPPTTAEAIDYLEELLAAL 207


                 ....*.
gi 815699165 317 PAEYSP 322
Cdd:COG0491  208 GERANP 213
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 93-283 1.43e-20

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: 87.22  E-value: 1.43e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165    93 NAFLVRQGNHLTLVDTGTAQCFgpglgQVLGNLRASGvdPAEVDEVLLTHAHPDHLCGVLDAQgkpAYPNATVWLSKADA 172
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAE-----DLLAELKKLG--PKKIDAIILTHGHPDHIGGLPELL---EAPGAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165   173 DYWLSPASEATAPKGVRFAFPlarnavapyqasgHLRTFSPGDALPGGAVAMD---THGHTPGHVSYRFDsqGQSLLVWG 249
Cdd:smart00849  71 ELLKDLLALLGELGAEAEPAP-------------PDRTLKDGDELDLGGGELEvihTPGHTPGSIVLYLP--EGKILFTG 135

                          170       180       190
                   ....*....|....*....|....*....|....
gi 815699165   250 DVLHFHAVQFAHPEAAFEADSDRKAAIASRRGLL 283
Cdd:smart00849 136 DLLFAGGDGRTLVDGGDAAASDALESLLKLLKLL 169
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
92-297 3.39e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 70.09  E-value: 3.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165   92 INAFLVRQGNHLTLVDTGTaqcfgPGLGQVLGNLRASGVDPAEVDEVLLTHAHPDHLCGVLDAQGKpayPNATVWLSKAD 171
Cdd:pfam00753   6 VNSYLIEGGGGAVLIDTGG-----SAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEA---TDVPVIVVAEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  172 ADYWLspaseaTAPKGVRFAFPLARNAVAPYQASGHLRTFSPGDALPGGAVaMDTHGHTPGHVSYRFDSQGQSLLVWGDV 251
Cdd:pfam00753  78 ARELL------DEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGL-LVTHGPGHGPGHVVVYYGGGKVLFTGDL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 815699165  252 LHFHAVQFAHPEAAFEADSDRKAAIASRRGLLQQATANGWWVAGAH 297
Cdd:pfam00753 151 LFAGEIGRLDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
 
Name Accession Description Interval E-value
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 43-297 5.32e-105

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: 307.17  E-value: 5.32e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  43 RVGALQVTALFDGVVALGRQEVVDVPPTLVSRLLEGRYVPEDkkGLQTAINAFLVRQGNHLTLVDTGTAQCFGPGLGQVL 122
Cdd:cd07720    2 KVGDFEVTALSDGTLPLPLDLLLGGAAPEAEAALLAAFLPPD--PVETSVNAFLVRTGGRLILVDTGAGGLFGPTAGKLL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 123 GNLRASGVDPAEVDEVLLTHAHPDHLCGVLDAQGKPAYPNATVWLSKADADYWLSPASEATAPKGVRFAFPLARNAVAPY 202
Cdd:cd07720   80 ANLAAAGIDPEDIDDVLLTHLHPDHIGGLVDAGGKPVFPNAEVHVSEAEWDFWLDDANAAKAPEGAKRFFDAARDRLRPY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 203 QASGHlrtFSPGDALPGGAVAMDTHGHTPGHVSYRFDSQGQSLLVWGDVLHFHAVQFAHPEAAFEADSDRKAAIASRRGL 282
Cdd:cd07720  160 AAAGR---FEDGDEVLPGITAVPAPGHTPGHTGYRIESGGERLLIWGDIVHHPALQFAHPDWTIAFDVDPEQAAATRRRL 236

                        250
                 ....*....|....*
gi 815699165 283 LQQATANGWWVAGAH 297
Cdd:cd07720  237 LDRAAAEGLLVAGAH 251
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 92-297 2.45e-46

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 156.14  E-value: 2.45e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  92 INAFLVRQGNHLTLVDTgtaqCFGPGL------------GQVLGNLRASGVDPAEVDEVLLTHAHPDHlCG---VLDAqG 156
Cdd:cd16277   13 IHSWLVRTPGRTILVDT----GIGNDKprpgppafhnlnTPYLERLAAAGVRPEDVDYVLCTHLHVDH-VGwntRLVD-G 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 157 K--PAYPNATVWLSKADADYWLSPASEATAPKGVrfafplARNAVAPYQASGHLRTFSPGDALPGGAVAMDTHGHTPGHV 234
Cdd:cd16277   87 RwvPTFPNARYLFSRAEYDHWSSPDAGGPPNRGV------FEDSVLPVIEAGLADLVDDDHEILDGIRLEPTPGHTPGHV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 815699165 235 SYRFDSQGQSLLVWGDVLHfHAVQFAHPEAAFEADSDRKAAIASRRGLLQQATANGWWVAGAH 297
Cdd:cd16277  161 SVELESGGERALFTGDVMH-HPIQVARPDWSSVFDEDPAQAAATRRRLLERAADTDTLLFPAH 222
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 88-278 1.69e-25

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: 101.14  E-value: 1.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  88 LQTAINAFLVRQGNHLTLVDTGTAQCfgpgLGQVLGNLRASGVDPAEVDEVLLTHAHPDHLCGVLDAQGKpayPNATVWL 167
Cdd:cd07721    7 LLPPVNAYLIEDDDGLTLIDTGLPGS----AKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEA---PGAPVYA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 168 SKADADYwLspASEATAPKGVRFAFPLARNAVAPYQASGHLRTFSPGDALP--GGAVAMDTHGHTPGHVSYrFDSQGQSL 245
Cdd:cd07721   80 HEREAPY-L--EGEKPYPPPVRLGLLGLLSPLLPVKPVPVDRTLEDGDTLDlaGGLRVIHTPGHTPGHISL-YLEEDGVL 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 815699165 246 LVwGDVLHFHAVQFAHPEAAFEAdsDRKAAIAS 278
Cdd:cd07721  156 IA-GDALVTVGGELVPPPPPFTW--DMEEALES 185
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 80-322 7.34e-25

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: 99.76  E-value: 7.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  80 YVPEDKKGLQTAINAFLVRQGNHLTLVDTGTAqcfGPGLGQVLGNLRASGVDpaeVDEVLLTHAHPDHLCGVLDAQGKPa 159
Cdd:COG0491    3 VLPGGTPGAGLGVNSYLIVGGDGAVLIDTGLG---PADAEALLAALAALGLD---IKAVLLTHLHPDHVGGLAALAEAF- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 160 ypNATVWLSKADADYWLSPASEATapkgvrfafpLARNAVAPYqasghlRTFSPGDALPGGAV---AMDTHGHTPGHVSY 236
Cdd:COG0491   76 --GAPVYAHAAEAEALEAPAAGAL----------FGREPVPPD------RTLEDGDTLELGGPgleVIHTPGHTPGHVSF 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 237 RFDSQGqsLLVWGDVLHFHAVQFAHPeaafeADSDRKAAIASRRGLLQQataNGWWVAGAHLPFPGLGHVRGEGQAYAWV 316
Cdd:COG0491  138 YVPDEK--VLFTGDALFSGGVGRPDL-----PDGDLAQWLASLERLLAL---PPDLVIPGHGPPTTAEAIDYLEELLAAL 207


                 ....*.
gi 815699165 317 PAEYSP 322
Cdd:COG0491  208 GERANP 213
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 93-283 1.43e-20

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: 87.22  E-value: 1.43e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165    93 NAFLVRQGNHLTLVDTGTAQCFgpglgQVLGNLRASGvdPAEVDEVLLTHAHPDHLCGVLDAQgkpAYPNATVWLSKADA 172
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAE-----DLLAELKKLG--PKKIDAIILTHGHPDHIGGLPELL---EAPGAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165   173 DYWLSPASEATAPKGVRFAFPlarnavapyqasgHLRTFSPGDALPGGAVAMD---THGHTPGHVSYRFDsqGQSLLVWG 249
Cdd:smart00849  71 ELLKDLLALLGELGAEAEPAP-------------PDRTLKDGDELDLGGGELEvihTPGHTPGSIVLYLP--EGKILFTG 135

                          170       180       190
                   ....*....|....*....|....*....|....
gi 815699165   250 DVLHFHAVQFAHPEAAFEADSDRKAAIASRRGLL 283
Cdd:smart00849 136 DLLFAGGDGRTLVDGGDAAASDALESLLKLLKLL 169
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 92-293 2.58e-20

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: 88.04  E-value: 2.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  92 INAFLVRQGNHLTLVDTG-------------TAQCFGPGLGQVLGN-LRASGVDPAEVDEVLLTHAHPDHlCGVLDaqgk 157
Cdd:cd07729   32 VYAYLIEHPEGTILVDTGfhpdaaddpggleLAFPPGVTEEQTLEEqLARLGLDPEDIDYVILSHLHFDH-AGGLD---- 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 158 pAYPNATVWLSKADADYwlspaseATAPKGVRFAFPLARNAVAPYQASGHLRTFSpGDA-LPGGAVAMDTHGHTPGHVSY 236
Cdd:cd07729  107 -LFPNATIIVQRAELEY-------ATGPDPLAAGYYEDVLALDDDLPGGRVRLVD-GDYdLFPGVTLIPTPGHTPGHQSV 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 815699165 237 RFDSQGQSLLVWGDVLHFHAvQFAHpEAAFEADSDRKAAIASRRGLLQQATANGWWV 293
Cdd:cd07729  178 LVRLPEGTVLLAGDAAYTYE-NLEE-GRPPGINYDPEAALASLERLKALAEREGARV 232
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 93-257 5.50e-20

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: 85.80  E-value: 5.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  93 NAFLVR-QGNHLTLVDTGtaqcfGPGLGQVLGNLRASGVDpaeVDEVLLTHAHPDHLCGVLDAQgkpAYPNATVWLSKAD 171
Cdd:cd06262   11 NCYLVSdEEGEAILIDPG-----AGALEKILEAIEELGLK---IKAILLTHGHFDHIGGLAELK---EAPGAPVYIHEAD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 172 ADYWLSPASEATAPKGVRFAFPLArnavapyqasghLRTFSPGDALPGGAV---AMDTHGHTPGHVSYRFDSQGqsLLVW 248
Cdd:cd06262   80 AELLEDPELNLAFFGGGPLPPPEP------------DILLEDGDTIELGGLeleVIHTPGHTPGSVCFYIEEEG--VLFT 145


                 ....*....
gi 815699165 249 GDVLHFHAV 257
Cdd:cd06262  146 GDTLFAGSI 154
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 91-256 1.17e-14

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


Pssm-ID: 293839  Cd Length: 252  Bit Score: 72.53  E-value: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  91 AINAFLVRQGNHLTLVDTGTAQCFGP---------GLGQVLGNLRASGVDPAEVDEVLLTHAHPDHLCGVL----DAQGK 157
Cdd:cd16281   42 AMRCLLIETGGRNILIDTGIGDKQDPkfrsiyvqhSEHSLLKSLARLGLSPEDITDVILTHLHFDHCGGATraddDGLVE 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 158 PAYPNATVWLSKADADYWLSP-----ASeatapkgvrFafpLARNaVAPYQASGHLRTFSPGDALPGGAVAMD-THGHTP 231
Cdd:cd16281  122 LLFPNATYWVQKRHWEWALNPnprerAS---------F---LPEN-IEPLEESGRLKLIDGSDAELGPGIRFHlSDGHTP 188

                        170       180
                 ....*....|....*....|....*
gi 815699165 232 GHVSYRFDSQGQSLLVWGDVLHFHA 256
Cdd:cd16281  189 GQMLPEISTPGGTVVFAADLIPTSA 213
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
92-297 3.39e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 70.09  E-value: 3.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165   92 INAFLVRQGNHLTLVDTGTaqcfgPGLGQVLGNLRASGVDPAEVDEVLLTHAHPDHLCGVLDAQGKpayPNATVWLSKAD 171
Cdd:pfam00753   6 VNSYLIEGGGGAVLIDTGG-----SAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEA---TDVPVIVVAEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  172 ADYWLspaseaTAPKGVRFAFPLARNAVAPYQASGHLRTFSPGDALPGGAVaMDTHGHTPGHVSYRFDSQGQSLLVWGDV 251
Cdd:pfam00753  78 ARELL------DEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGL-LVTHGPGHGPGHVVVYYGGGKVLFTGDL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 815699165  252 LHFHAVQFAHPEAAFEADSDRKAAIASRRGLLQQATANGWWVAGAH 297
Cdd:pfam00753 151 LFAGEIGRLDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 125-252 6.80e-14

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: 68.72  E-value: 6.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 125 LRASGVDPAEVDEVLLTHAHPDHLCGVLDAqgkPAYPNATVWLSKADADYWlspaseatapkgvRFAFPlarnavapyqa 204
Cdd:cd16275   38 LAKLNELGLTLTGILLTHSHFDHVNLVEPL---LAKYDAPVYMSKEEIDYY-------------GFRCP----------- 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 815699165 205 sgHLRTFSPGDALPGGAV---AMDTHGHTPGHVSYRFDSQgqslLVWGDVL 252
Cdd:cd16275   91 --NLIPLEDGDTIKIGDTeitCLLTPGHTPGSMCYLLGDS----LFTGDTL 135
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 94-239 2.96e-12

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: 65.30  E-value: 2.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  94 AFLVRQGNHLTLVDTGTAQCFGpglGQVLGNLRASGVDPAEVDEVLLTHAHPDHLCGvldAQGKPAYPNATVWLSKADAD 173
Cdd:cd16280   24 AWAIDTGDGLILIDALNNNEAA---DLIVDGLEKLGLDPADIKYILITHGHGDHYGG---AAYLKDLYGAKVVMSEADWD 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 815699165 174 YWLSPASEATAPkgvRFAFPLARNAVApyqasghlrtfSPGDALPGGAVAMDTH---GHTPGHVSYRFD 239
Cdd:cd16280   98 MMEEPPEEGDNP---RWGPPPERDIVI-----------KDGDTLTLGDTTITVYltpGHTPGTLSLIFP 152
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 92-252 7.75e-11

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 60.39  E-value: 7.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  92 INAFLVRQGNHLTLVDTGTAQcfGPGLGQVLGNLRASGVDPAEVDEVLLTHAHPDHlCGVLdaqgkpaypnatvwlskad 171
Cdd:cd07725   15 VNVYLLRDGDETTLIDTGLAT--EEDAEALWEGLKELGLKPSDIDRVLLTHHHPDH-IGLA------------------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 172 adYWLSPASEATapkgVRFAFPlarnavapyqasghlRTFSPGDALPGGAV---AMDTHGHTPGHVSYRFDSQGqsLLVW 248
Cdd:cd07725   73 --GKLQEKSGAT----VYILDV---------------TPVKDGDKIDLGGLrlkVIETPGHTPGHIVLYDEDRR--ELFV 129


                 ....
gi 815699165 249 GDVL 252
Cdd:cd07725  130 GDAV 133
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 67-256 7.84e-11

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. 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: 293814  Cd Length: 249  Bit Score: 61.12  E-value: 7.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  67 VPPTLVSRllegRYVPEDKKGLQTAINAFLVRQGNHLTLVDTGtaqcFGPGL--------------GQVLGNLRASGVDP 132
Cdd:cd07728   22 VPKPLWSK----KYPANEKNQIELRTDPILIQYQGKNYLIDAG----IGNGKltekqkrnfgvteeSSIEESLAELGLTP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 133 AEVDEVLLTHAHPDHLCGVLDAQG---KPAYPNATVWLSKADADYWLSPA--SEATapkgvrfafPLARNavapYQA-SG 206
Cdd:cd07728   94 EDIDYVLMTHLHFDHASGLTKVKGeqlVSVFPNATIYVSEIEWEEMRNPNirSKNT---------YWKEN----WEPiED 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 815699165 207 HLRTFSpGDALPGGAVAM-DTHGHTPGHVSYRFDSQGQSLLVWGDVLHFHA 256
Cdd:cd07728  161 QVKTFS-DEIEIVPGITMiHTGGHSDGHSIIEIEQGGETAIHMADLMPTHA 210
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 72-286 3.27e-10

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: 58.37  E-value: 3.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  72 VSRLLEGRYVPEDKKGLQTAINAFLVRQGNHLTLVDTGTAQCfGPGLgqvLGNLRASGVDPAEVDEVLLTHAHPDHlCGV 151
Cdd:cd07711    2 VKVLVEGYARRDSDGGFRASSTVTLIKDGGKNILVDTGTPWD-RDLL---LKALAEHGLSPEDIDYVVLTHGHPDH-IGN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 152 LDaqgkpAYPNATVWLSKADADYWLSPASEATAPkgvrfafplarnavaPYQASGHLRTFSpgdalpggavamdTHGHTP 231
Cdd:cd07711   77 LN-----LFPNATVIVGWDICGDSYDDHSLEEGD---------------GYEIDENVEVIP-------------TPGHTP 123

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 815699165 232 GHVS--YRFDSQGQSLLVwGDVLHFH--AVQFAHPEAAFEadsDRKAAIASRRGLLQQA 286
Cdd:cd07711  124 EDVSvlVETEKKGTVAVA-GDLFEREedLEDPILWDPLSE---DPELQEESRKRILALA 178
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
94-250 4.56e-10

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 59.05  E-value: 4.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  94 AFLVRQGNHLTLVDtgtaqcFGPGlgqVLGNLRASGVDPAEVDEVLLTHAHPDH---LCGVLDA---QGKPayPNATVWL 167
Cdd:COG1234   21 SYLLEAGGERLLID------CGEG---TQRQLLRAGLDPRDIDAIFITHLHGDHiagLPGLLSTrslAGRE--KPLTIYG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 168 SKADADYWlspaSEATAPKGVRFAFPLarnavapyqasgHLRTFSPGDALPGGAV---AMDTHgHTPGHVSYRFDSQGQS 244
Cdd:COG1234   90 PPGTKEFL----EALLKASGTDLDFPL------------EFHEIEPGEVFEIGGFtvtAFPLD-HPVPAYGYRFEEPGRS 152


                 ....*.
gi 815699165 245 LLVWGD 250
Cdd:COG1234  153 LVYSGD 158
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 93-235 7.23e-10

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: 57.54  E-value: 7.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  93 NAFLVRQGNHLTLVDTG-TAQCFGPGLGQVLGNLrasgvDPAEVDEVLLTHAHPDHLCGVLDAQGKPAYPNATVWlsKad 171
Cdd:cd07722   19 NTYLVGTGKRRILIDTGeGRPSYIPLLKSVLDSE-----GNATISDILLTHWHHDHVGGLPDVLDLLRGPSPRVY--K-- 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 815699165 172 adywlspaseatapkgvrfaFPLARNAVAPYQASGHLRTFSPGDALPGGAV---AMDTHGHTPGHVS 235
Cdd:cd07722   90 --------------------FPRPEEDEDPDEDGGDIHDLQDGQVFKVEGAtlrVIHTPGHTTDHVC 136
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 93-254 1.03e-09

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 57.98  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  93 NAFLVRQGNHLTLVDTGtaqcfgPGLGQVLgnlRASGVDPAEVDEVLLTHAHPDHLCGVLDAqgKPAYPNATVwlskada 172
Cdd:COG1235   36 SSILVEADGTRLLIDAG------PDLREQL---LRLGLDPSKIDAILLTHEHADHIAGLDDL--RPRYGPNPI------- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 173 DYWLSPASEATAPKGVRFAFPLARNAVAPYQASGHlRTFSPGD------ALPGGAVamDTHGhtpghvsYRFDSQGQSLL 246
Cdd:COG1235   98 PVYATPGTLEALERRFPYLFAPYPGKLEFHEIEPG-EPFEIGGltvtpfPVPHDAG--DPVG-------YRIEDGGKKLA 167


                 ....*...
gi 815699165 247 VWGDVLHF 254
Cdd:COG1235  168 YATDTGYI 175
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 94-278 1.24e-09

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: 57.12  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  94 AFLVRQGNHLTLVDTGTAqcfgPGLGQVLGNLRASGVDPAEVDEVLLTHAHPDH--LCGVLdAQgkpAYPNATVWLskad 171
Cdd:cd07726   18 SYLLDGEGRPALIDTGPS----SSVPRLLAALEALGIAPEDVDYIILTHIHLDHagGAGLL-AE---ALPNAKVYV---- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 172 adywlspaseatAPKGVRF-AFP--LARNAVAPYQASGHLRTFSP-------------GDALPGGAV---AMDTHGHTPG 232
Cdd:cd07726   86 ------------HPRGARHlIDPskLWASARAVYGDEADRLGGEIlpvpeervivledGETLDLGGRtleVIDTPGHAPH 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 815699165 233 HVSYrFDSQGQSLLVwGDV--LHFHAVQFAHPEAAFEADSDRKAAIAS 278
Cdd:cd07726  154 HLSF-LDEESDGLFT-GDAagVRYPELDVVGPPSTPPPDFDPEAWLES 199
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 92-236 1.04e-08

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. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B3 MBLs include Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Stenotrophomonas Maltophilia L1, and Bradyrhizobium diazoefficiens BJP-1, Serratia marcescens SMB-1, and Pseudomonas Aeruginosa AIM-1. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 55.24  E-value: 1.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  92 INAFLVRQGNHLTLVDTGTAQcfgpGLGQVLGNLRASGVDPAEVDEVLLTHAHPDHLCGVLDAQGKPAypnATVWLSKAD 171
Cdd:cd07708   22 LAAYLIVTPQGNILIDGDMEQ----NAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAEIKKQTG---AKVMAGAED 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 815699165 172 ADYWLSpaseatapkGVRFAFPLARNAVAPYQASGHLRTFSPGDALPGGAVAMDTH---GHTPGHVSY 236
Cdd:cd07708   95 VSLLLS---------GGSSDFHYANDSSTYFPQSTVDRAVHDGERVTLGGTVLTAHatpGHTPGCTTW 153
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 125-235 1.89e-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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 54.20  E-value: 1.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 125 LRASGVDPAEVDEVLLTHAHPDHLCGVLDaqgkpaYPNATVWLSKADADYWLSPASEATAPKGVRfafplarnavaPYQA 204
Cdd:cd07730   74 LAAGGIDPEDIDAVILSHLHWDHIGGLSD------FPNARLIVGPGAKEALRPPGYPSGFLPELL-----------PSDF 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 815699165 205 SGHLRTFSPGDALP----GGAVAMD-----------THGHTPGHVS 235
Cdd:cd07730  137 EGRLVRWEEDDFLWvplgPFPRALDlfgdgslylvdLPGHAPGHLG 182
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 93-252 4.69e-08

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: 52.35  E-value: 4.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  93 NAFLVR--QGNHLTLVDTGTAQcfgpglGQVLGNLRASGVDpaeVDEVLLTHAHPDHLCGVLDAQgkpAYPNATVWLSKA 170
Cdd:cd16322   12 NTYLVAdeGGGEAVLVDPGDES------EKLLARFGTTGLT---LLYILLTHAHFDHVGGVADLR---RHPGAPVYLHPD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 171 DadywlSPASEATAPKGVRFAFplarNAVAPYQASGHLRTfspGDALPGGAV---AMDTHGHTPGHVSYRFDSQGqsLLV 247
Cdd:cd16322   80 D-----LPLYEAADLGAKAFGL----GIEPLPPPDRLLED---GQTLTLGGLefkVLHTPGHSPGHVCFYVEEEG--LLF 145


                 ....*
gi 815699165 248 WGDVL 252
Cdd:cd16322  146 SGDLL 150
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 130-242 5.57e-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: 51.69  E-value: 5.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 130 VDPAEVDEV--------------LLTHAHPDHLCGVLDAQGKpaYPNATVWLSKADadywlspaseatapkgvrfafpla 195
Cdd:cd07723   25 VDPGEAEPVlaalekngltltaiLTTHHHWDHTGGNAELKAL--FPDAPVYGPAED------------------------ 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 815699165 196 rnavapyQASGHLRTFSPGDALPGGAV---AMDTHGHTPGHVSYRFDSQG 242
Cdd:cd07723   79 -------RIPGLDHPVKDGDEIKLGGLevkVLHTPGHTLGHICYYVPDEP 121
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 94-173 1.01e-07

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: 52.17  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  94 AFLVRQGNHLT-LVDTGTAQCFGPGLGQVLGNLRASGVDpaEVDEVLLTHAHPDHLCGVLDAQGkpAYPNATVWLSKADA 172
Cdd:COG2333   13 AILIRTPDGKTiLIDTGPRPSFDAGERVVLPYLRALGIR--RLDLLVLTHPDADHIGGLAAVLE--AFPVGRVLVSGPPD 88


                 .
gi 815699165 173 D 173
Cdd:COG2333   89 T 89
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 94-173 1.22e-07

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: 50.98  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  94 AFLVRQGNHLTLVDTGTAqcFGPGLGQVLGNLRASGVDpaEVDEVLLTHAHPDHLCG---VLDaqgkpAYPNATVWLSKA 170
Cdd:cd07731   12 AILIQTPGKTILIDTGPR--DSFGEDVVVPYLKARGIK--KLDYLILTHPDADHIGGldaVLK-----NFPVKEVYMPGV 82


                 ...
gi 815699165 171 DAD 173
Cdd:cd07731   83 THT 85
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 90-242 2.04e-07

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: 51.33  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  90 TAINAFLVRQGNHLTLVDTGTAQcfgpGLGQVLGNLRASGVDPAEVDEVLLTHAHPDHLCGVldAQGKPAyPNATVWLSK 169
Cdd:cd16309   20 AGLGVFLITTPEGHILIDGAMPQ----STPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGL--AELKKA-TGAQLVASA 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 815699165 170 ADadywlSPASEAtapkGVRFAFPLARNAVAPYQASghlRTFSPGDALPGGAVAMDTH---GHTPGHVSYRFDSQG 242
Cdd:cd16309   93 AD-----KPLLES----GYVGSGDTKNLQFPPVRVD---RVIGDGDKVTLGGTTLTAHltpGHSPGCTSWTTTVKD 156
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 94-169 2.57e-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: 2.57e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 815699165  94 AFLVRQGNHLTLVDTGtaqcFGPGLgqvLGNLRASGVDPAEVDEVLLTHAHPDH---LCGVLDaqgkpAYPNATVWLSK 169
Cdd:cd07713   22 SLLIETEGKKILFDTG----QSGVL---LHNAKKLGIDLSDIDAVVLSHGHYDHtggLKALLE-----LNPKAPVYAHP 88
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 94-250 5.78e-07

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: 49.05  E-value: 5.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  94 AFLVRQGNHLTLVDtgtaqcFGPGlgqVLGNLRASGVDPAEVDEVLLTHAHPDHLCGVLDaqgkpaypnatVWLSkadad 173
Cdd:cd07719   20 STLVVVGGRVYLVD------AGSG---VVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPA-----------LLLT----- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 174 YWLSPASEATA---PKGVRfafPLARNAVAPYQASGHLRTFSPGDALP------------GGAVAMD-----------TH 227
Cdd:cd07719   75 AWLAGRKTPLPvygPPGTR---ALVDGLLAAYALDIDYRARIGDEGRPdpgalvevheiaAGGVVYEddgvkvtaflvDH 151

                        170       180
                 ....*....|....*....|...
gi 815699165 228 GHTPGHVSYRFDSQGQSLLVWGD 250
Cdd:cd07719  152 GPVPPALAYRFDTPGRSVVFSGD 174
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 93-152 3.68e-06

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 48.26  E-value: 3.68e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  93 NAFLVRQGNHLTLVDTGTAQcfgpglGQVLGNLRASGVDPAEVDEVLLTHAHPDHlCGVL 152
Cdd:COG1236   15 SCYLLETGGTRILIDCGLFQ------GGKERNWPPFPFRPSDVDAVVLTHAHLDH-SGAL 67
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 125-282 5.68e-06

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


Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 46.85  E-value: 5.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 125 LRASGVDPAEVDEVLLTHAHPDHLCGVLDaqgkpaYPNATVWLSKADADywlspASEATAPKGVRFAFPLARNAVAP--- 201
Cdd:cd07742   71 IEALGFDPSDVRHIVLTHLDLDHAGGLAD------FPHATVHVHAAELD-----AATSPRTRYERRRYRPQQLAHGPwwv 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 202 -YQASGH----LRTFSPGDALPGGAVAMDTHGHTPGHVSYRFDSQGQSLLVWGDVLHFHAVQFAHPEAAFEADS------ 270
Cdd:cd07742  140 tYAAGGErwfgFEAVRPLDGLPPEILLVPLPGHTRGHCGVAVRTGDRWLLHAGDAYFHHGELDPLPPPPPPLRLfqrlla 219

                        170
                 ....*....|...
gi 815699165 271 -DRKAAIASRRGL 282
Cdd:cd07742  220 vDRSARLANLARL 232
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 134-252 1.11e-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: 45.24  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 134 EVDEVLLTHAHPDHLCGVldAQGKPAYpNATVWLSKADADYWLspasEATAPKGVRFAFPLARNAVAPyqasghlRTFSP 213
Cdd:cd07737   46 TLKKILLTHGHLDHVGGA--AELAEHY-GVPIIGPHKEDKFLL----ENLPEQSQMFGFPPAEAFTPD-------RWLEE 111

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 815699165 214 GDALPGGAVAMD---THGHTPGHVSYrFDSQGQSLLVwGDVL 252
Cdd:cd07737  112 GDTVTVGNLTLEvlhCPGHTPGHVVF-FNRESKLAIV-GDVL 151
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 91-240 1.16e-05

Pseudomonas Aeruginosa AIM-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 AIM-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: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 46.04  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  91 AINAFLVRQGNHLTLVDTGTAQCfGPglgQVLGNLRASGVDPAEVDEVLLTHAHPDHLCGVLDAQgkpAYPNATVWLSKA 170
Cdd:cd16314   21 GISALLVTSDAGHILIDGGTDKA-AP---LIEANIRALGFRPEDVRYIVSSHEHFDHAGGIARLQ---RATGAPVVAREP 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 815699165 171 DADYWLSPASEATAPKgvrFAfplarnAVAPYQASGHLRTFSPGDALPGGAVAMDTH---GHTPGHVSYRFDS 240
Cdd:cd16314   94 AATTLERGRSDRSDPQ---FL------VVEKFPPVASVQRIGDGEVLRVGPLALTAHatpGHTPGGTSWTWRS 157
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 93-151 2.39e-05

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


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 43.79  E-value: 2.39e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 815699165  93 NAFLVRQGNHLTLVDTGTaqcfgpGLGQVLGNLRASGVDPAEVDEVLLTHAHPDHLCGV 151
Cdd:cd07733   10 NCTYLETEDGKLLIDAGL------SGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGL 62
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 94-150 3.72e-05

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: 43.79  E-value: 3.72e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 815699165  94 AFLVRQGNHLTLVDTGTAQCFGpglgqvlgnLRASGVDPAEVDEVLLTHAHPDHLCG 150
Cdd:cd16272   19 SYLLETGGTRILLDCGEGTVYR---------LLKAGVDPDKLDAIFLSHFHLDHIGG 66
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 95-155 4.18e-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: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 43.79  E-value: 4.18e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815699165  95 FLVRQGNHLTLVDTGtaqcfgpglGQVLGNLRASGVDPAEVDEVLLTHAHPDHLCG----VLDAQ 155
Cdd:cd07740   19 FHVASEAGRFLIDCG---------ASSLIALKRAGIDPNAIDAIFITHLHGDHFGGlpffLLDAQ 74
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 92-240 6.43e-05

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


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 43.49  E-value: 6.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  92 INAFLVRQGNHLTLVDTGTAqcfgPGLGQVLGNLRASGVDPAEVDEVLLTHAHPDHLCGVLDAQgkpAYPNATVWLSKAD 171
Cdd:cd16315   22 ISAILITGDDGHVLIDSGTE----EAAPLVLANIRKLGFDPKDVRWLLSSHEHFDHVGGLAALQ---RATGARVAASAAA 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 815699165 172 ADYWLSPASEATAPK-GVRFAFPLARNAvapyqasghlRTFSPGDALPGGAVAMDTH---GHTPGHVSYRFDS 240
Cdd:cd16315   95 APVLESGKPAPDDPQaGLHEPFPPVRVD----------RIVEDGDTVALGSLRLTAHatpGHTPGALSWTWRS 157
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 92-236 1.04e-04

Caulobacter crescentus Mbl1b 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 Mbl1b-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: 293868  Cd Length: 252  Bit Score: 43.21  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  92 INAFLVRQGNHLTLVDTGTAQcfgpGLGQVLGNLRASGVDPAEVDEVLLTHAHPDHLCGVldAQGKpAYPNATVWLSKAD 171
Cdd:cd16310   22 IGSYLITSNHGAILLDGGLEE----NAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGL--AQLK-ADTGAKLWASRGD 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 815699165 172 AdywlsPASEATAPKGVRFAFPlarnavAPYQASGHLRTFSPGDALPGGAVAMDTH---GHTPGHVSY 236
Cdd:cd16310   95 R-----PALEAGKHIGDNITQP------APFPAVKVDRILGDGEKIKLGDITLTATltpGHTKGCTTW 151
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 138-251 1.25e-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: 42.00  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 138 VLLTHAHPDHLCGVLDAQGKPaypNATVWLSKADadywlspaseatapkGVRFAFplarnavapyqasghlRTFSPGDAL 217
Cdd:cd07724   52 VLETHVHADHVSGARELAERT---GAPIVIGEGA---------------PASFFD----------------RLLKDGDVL 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 815699165 218 PGGAV---AMDTHGHTPGHVSYRFDSQ-----GQSLLVwGDV 251
Cdd:cd07724   98 ELGNLtleVLHTPGHTPESVSYLVGDPdavftGDTLFV-GDV 138
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 92-252 1.91e-04

SMB-1, THIN-B 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 SMB-1- and 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: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 42.16  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  92 INAFLVRQGNHLTLVDTGTAQcfgpGLGQVLGNLRASGVDPAEVDEVLLTHAHPDHLCGVLDAQgkpAYPNATVWLSKAD 171
Cdd:cd16313   22 ISAVLITSPQGHILIDGGFPK----SPEQIAASIRQLGFKLEDVKYILSSHDHWDHAGGIAALQ---KLTGAQVLASPAT 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 172 ADYWLSPASEATAPKgvrfaFPlarnAVAPYQASGHLRTFSPGDALPGGAVAMDTH---GHTPGHVSYRFDS--QGQSL- 245
Cdd:cd16313   95 VAVLRSGSMGKDDPQ-----FG----GLTPMPPVASVRAVRDGEVVKLGPLAVTAHatpGHTTGGTSWTWQSceQGRCAn 165


                 ....*..
gi 815699165 246 LVWGDVL 252
Cdd:cd16313  166 MVFADSL 172
NorV COG0426
Flavorubredoxin [Energy production and conversion];
74-169 2.09e-04

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 42.51  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  74 RLLEGRYVPEdkKGlqTAINAFLVRqGNHLTLVDTGTAQCFGpglgQVLGNLRASgVDPAEVDEVLLTHAHPDHlCG--- 150
Cdd:COG0426   20 RLFEGEYPTP--RG--TTYNSYLIV-DEKTALIDTVGESFFE----EFLENLSKV-IDPKKIDYIIVNHQEPDH-SGslp 88

                         90       100
                 ....*....|....*....|
gi 815699165 151 -VLDaqgkpAYPNATVWLSK 169
Cdd:COG0426   89 eLLE-----LAPNAKIVCSK 103
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 93-242 2.78e-04

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 40.94  E-value: 2.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  93 NAFLVRQGNHLTLVDTGtaqcfgPGLGQVLGNLrASGVDPAEVDEVLLTHAHPDHlcgvldaqgkpaypnatvwlskada 172
Cdd:cd16278   19 NTYLLGAPDGVVVIDPG------PDDPAHLDAL-LAALGGGRVSAILVTHTHRDH------------------------- 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 815699165 173 dywlspaSEATAPKGVRFAFPLArnAVAPYQASGHLRTFSPGDALPGGAV---------AMDTHGHTPGHVSYRFDSQG 242
Cdd:cd16278   67 -------SPGAARLAERTGAPVR--AFGPHRAGGQDTDFAPDRPLADGEVieggglrltVLHTPGHTSDHLCFALEDEG 136
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 97-271 3.48e-04

MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain; Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 40.94  E-value: 3.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  97 VRQGNHLTLVDTGTaqcfgpGLgQVLGN-LRASGvDPAEVDeVLLTHAHPDHLcgvldaQG----KPAY-PNATVwlska 170
Cdd:cd07715   28 VRAGGELLILDAGT------GI-RELGNeLMKEG-PPGEAH-LLLSHTHWDHI------QGfpffAPAYdPGNRI----- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 171 daDYWlspaSEATAPKGVRFA---------FPlarnaVAPYQASGHLR--TFSPGDALPGGAVAMDTHG--HTPGHVSYR 237
Cdd:cd07715   88 --HIY----GPHKDGGSLEEVlrrqmsppyFP-----VPLEELLAAIEfhDLEPGEPFSIGGVTVTTIPlnHPGGALGYR 156

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 815699165 238 FDSQGQSLLVWGDVLHFHAVQFAHPE-AAFEADSD 271
Cdd:cd07715  157 IEEDGKSVVYATDTEHYPDDGESDEAlLEFARGAD 191
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 94-152 3.77e-04

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: 40.91  E-value: 3.77e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 815699165  94 AFLVRQGNHLTLVDtgtaqCfgpGLGQVLGNLRAS-----GVDPAEVDEVLLTHAHPDHlCGVL 152
Cdd:cd16295   14 CYLLETGGKRILLD-----C---GLFQGGKELEELnnepfPFDPKEIDAVILTHAHLDH-SGRL 68
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 74-170 3.95e-04

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: 41.32  E-value: 3.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  74 RLLEGRYVPEDkkglQTAINAFLVRqGNHLTLVDTGTAQCFGpglgQVLGNLRaSGVDPAEVDEVLLTHAHPDHlCGVLd 153
Cdd:cd07709   18 RLFEGEYPTPR----GTSYNSYLIK-DEKTALIDTVKEPFFD----EFLENLE-EVIDPRKIDYIVVNHQEPDH-SGSL- 85

                         90       100
                 ....*....|....*....|.
gi 815699165 154 aqgkPA----YPNATVWLSKA 170
Cdd:cd07709   86 ----PEllelAPNAKIVCSKK 102
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 92-236 5.83e-04

Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-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 L1- and Pom-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: 293847  Cd Length: 239  Bit Score: 40.57  E-value: 5.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165  92 INAFLVRQGNHLTLVDTGTAQcfgpGLGQVLGNLRASGVDPAEVDEVLLTHAHPDH---LCGVLDAQGKPAYPNA--TVW 166
Cdd:cd16289   22 LTALLVKTPDGAVLLDGGMPQ----AADMLLDNMRALGVAPGDLKLILHSHAHADHagpLAALKRATGARVAANAesAVL 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 815699165 167 LSKADADywlspaseaTAPKGVRFAFPlarnavaPYQASghlRTFSPGDALPGGAVAMDTH---GHTPGHVSY 236
Cdd:cd16289   98 LARGGSD---------DIHFGDGITFP-------PVQAD---RIVMDGEVVTLGGVTFTAHftpGHTPGSTSW 151
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 96-153 9.56e-04

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: 39.76  E-value: 9.56e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815699165  96 LVRQGNHLTLVDTGT---AQCfgpglgqvlgnLRAsGVDpaEVDEVLLTHAHPDHLCGvLD 153
Cdd:cd16279   39 LIETGGKNILIDTGPdfrQQA-----------LRA-GIR--KLDAVLLTHAHADHIHG-LD 84
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 95-147 1.17e-03

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


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 38.96  E-value: 1.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 815699165  95 FLVRQGNHLTLVDtgtaqcFGPGlgqVLGNLRASgVDPAEVDEVLLTHAHPDH 147
Cdd:cd07716   21 YLLEADGFRILLD------CGSG---VLSRLQRY-IDPEDLDAVVLSHLHPDH 63
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 93-148 3.99e-03

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 37.97  E-value: 3.99e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 815699165  93 NAFLVRQGNHLTLVDtgtaqcfgPGLGQVLGNLRASGVDPAEVDE---VLLTHAHPDHL 148
Cdd:COG2220   12 ATFLIETGGKRILID--------PVFSGRASPVNPLPLDPEDLPKidaVLVTHDHYDHL 62
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 105-239 4.30e-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: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 37.51  E-value: 4.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815699165 105 LVDTGTAQCFGPGLGQVLGNLRAsgvdpaEVDEVLLTHAHPDHLCGVLDAQGKpayPNATVWLSKADADYWLSPASEATA 184
Cdd:cd07743   22 LIDSGLDEDAGRKIRKILEELGW------KLKAIINTHSHADHIGGNAYLQKK---TGCKVYAPKIEKAFIENPLLEPSY 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 815699165 185 PKGVRFAFPLaRNAVAPYQASGHLRTFSPGDALPGGA--VAMDTHGHTPGHVSYRFD 239
Cdd:cd07743   93 LGGAYPPKEL-RNKFLMAKPSKVDDIIEEGELELGGVglEIIPLPGHSFGQIGILTP 148
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 129-147 7.11e-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: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 37.17  E-value: 7.11e-03
                         10
                 ....*....|....*....
gi 815699165 129 GVDPAEVDEVLLTHAHPDH 147
Cdd:cd07741   48 KLDPTKLDAIILSHRHLDH 66
 
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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