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Conserved domains on  [gi|492583249|ref|WP_005894592|]
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MULTISPECIES: MBL fold metallo-hydrolase [Pseudomonas syringae group]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869981)

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

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List of domain hits

 Name Accession Description Interval E-value
bifunc_ST_SDO super family cl48920
bifunctional sulfur transferase/dioxygenase Blh;
8-294 2.36e-126

bifunctional sulfur transferase/dioxygenase Blh;


The actual alignment was detected with superfamily member NF040641:

Pssm-ID: 468609 [Multi-domain]  Cd Length: 423  Bit Score: 366.53  E-value: 2.36e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249   8 HVEALFDSETGTISYLVMDLESKQCALIDSVLDYDPKSGRTRTESADRMIDRVRALQASVQWIFETHVHADHLSAAPYLK 87
Cdd:NF040641 143 QVKGFFDPRTGSVQYVVSDPATRRCAIIDPVLDFDEKSGATSTTNADAILAYVAEEGLTVEWILDTHPHADHFSAAHYLK 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  88 QNLGGKIVIGSHITVVQKTFGALFNASsDFARNGSQFDVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLVqvGEqtVAF 167
Cdd:NF040641 223 EKTGAPTAIGEHVVDVQKLWKGIYNWP-DLPTDGSQWDRLFADGDTFKVGSIDARVMFSPGHTLASITYVI--GD--AAF 297

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 168 VGDTLFMPDYGTARCDFPGADARTLYRSIRKLLALPPQTLLFMCHDYLPNGRALKYMTTVAEQRASNIHVhDGVDEDTFV 247
Cdd:NF040641 298 VHDTLFMPDSGTARADFPGGSARALWRSIQAILALPDETRLFTGHDYQPGGRAPRWESTVAEQKRSNPHL-AGQDEASFV 376

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 492583249 248 SMREARDVTLEMPVLMLPSVQVNMRCGHFPEPEDNGVVYLKIPLNAL 294
Cdd:NF040641 377 ALREARDKTLPMPKLILHALQVNIRGGRLPEPEANGRRYLKIPLDAL 423
 
Name Accession Description Interval E-value
bifunc_ST_SDO NF040641
bifunctional sulfur transferase/dioxygenase Blh;
8-294 2.36e-126

bifunctional sulfur transferase/dioxygenase Blh;


Pssm-ID: 468609 [Multi-domain]  Cd Length: 423  Bit Score: 366.53  E-value: 2.36e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249   8 HVEALFDSETGTISYLVMDLESKQCALIDSVLDYDPKSGRTRTESADRMIDRVRALQASVQWIFETHVHADHLSAAPYLK 87
Cdd:NF040641 143 QVKGFFDPRTGSVQYVVSDPATRRCAIIDPVLDFDEKSGATSTTNADAILAYVAEEGLTVEWILDTHPHADHFSAAHYLK 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  88 QNLGGKIVIGSHITVVQKTFGALFNASsDFARNGSQFDVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLVqvGEqtVAF 167
Cdd:NF040641 223 EKTGAPTAIGEHVVDVQKLWKGIYNWP-DLPTDGSQWDRLFADGDTFKVGSIDARVMFSPGHTLASITYVI--GD--AAF 297

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 168 VGDTLFMPDYGTARCDFPGADARTLYRSIRKLLALPPQTLLFMCHDYLPNGRALKYMTTVAEQRASNIHVhDGVDEDTFV 247
Cdd:NF040641 298 VHDTLFMPDSGTARADFPGGSARALWRSIQAILALPDETRLFTGHDYQPGGRAPRWESTVAEQKRSNPHL-AGQDEASFV 376

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 492583249 248 SMREARDVTLEMPVLMLPSVQVNMRCGHFPEPEDNGVVYLKIPLNAL 294
Cdd:NF040641 377 ALREARDKTLPMPKLILHALQVNIRGGRLPEPEANGRRYLKIPLDAL 423
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 8-214 1.16e-73

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: 223.43  E-value: 1.16e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249   8 HVEALFDSETGTISYLVMDLESKQCALIDSVLDydpksgrtrteSADRMIDRVRALQASVQWIFETHVHADHLSAAPYLK 87
Cdd:cd07724    1 IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRD-----------SVDRYLDLAAELGLKITYVLETHVHADHVSGARELA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  88 QNLGGKIVIGSHItvvqktfgalfnassdfarNGSQFDVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLvqVGEQTVAF 167
Cdd:cd07724   70 ERTGAPIVIGEGA-------------------PASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYL--VGDPDAVF 128

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 492583249 168 VGDTLFMPDygTARCDFPGA---DARTLYRSIRKLLALPP-QTLLFMCHDY 214
Cdd:cd07724  129 TGDTLFVGD--VGRPDLPGEaegLARQLYDSLQRKLLLLPdETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 8-229 8.40e-42

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: 143.29  E-value: 8.40e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249   8 HVEALFDSETGTISYLVMDleSKQCALIDSVLDydpksgrtrTESADRMIDRVRALQASVQWIFETHVHADHLSAAPYLK 87
Cdd:COG0491    4 LPGGTPGAGLGVNSYLIVG--GDGAVLIDTGLG---------PADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  88 QNLGGKIVIGSHITVVQKTFGalfnASSDFARNGSQFDVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLvqVGEQTVAF 167
Cdd:COG0491   73 EAFGAPVYAHAAEAEALEAPA----AGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFY--VPDEKVLF 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492583249 168 VGDTLFMPDYGtaRCDFPGADARTLYRSIRKLLALPPQTLLFmCHDYLPNGRALKYMTTVAE 229
Cdd:COG0491  147 TGDALFSGGVG--RPDLPDGDLAQWLASLERLLALPPDLVIP-GHGPPTTAEAIDYLEELLA 205
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 6-274 2.34e-26

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 104.11  E-value: 2.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249   6 KLHVEALFDSETGTISYLVMDLE--SKQCALIDSVldydpksgrtrTESADRMIDRVRALQASVQWIFETHVHADHLSAA 83
Cdd:PLN02962  10 KLLFRQLFEKESSTYTYLLADVShpDKPALLIDPV-----------DKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  84 PYLKQNLGG-KIVIGshitvvqktfgalfNASsdfarnGSQFDVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLVQVGE 162
Cdd:PLN02962  79 GLLKTKLPGvKSIIS--------------KAS------GSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGP 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 163 QT----VAFVGDTLFMpdYGTARCDFPGADARTLYRSIR-KLLALPPQTLLFMCHDYLPNGralkyMTTVAEQRASNIHV 237
Cdd:PLN02962 139 DQpqprMAFTGDALLI--RGCGRTDFQGGSSDQLYKSVHsQIFTLPKDTLIYPAHDYKGFT-----VSTVGEEMLYNPRL 211

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 492583249 238 HDgvDEDTFVSMREarDVTLEMPVLMLPSVQVNMRCG 274
Cdd:PLN02962 212 TK--DEETFKTIME--NLNLPYPKMIDVAVPANMVCG 244
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 21-209 1.74e-23

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: 94.54  E-value: 1.74e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249    21 SYLVMDleSKQCALIDSVLDYdpksgrtrtesADRMIDRVRALQ-ASVQWIFETHVHADHLSAAPYLKQNLGGKIVIGSH 99
Cdd:smart00849   2 SYLVRD--DGGAILIDTGPGE-----------AEDLLAELKKLGpKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEG 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249   100 ITVVQKTFGALFNASSDFARNGSqFDVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLvqVGEQTVAFVGDTLFMPDYGT 179
Cdd:smart00849  69 TAELLKDLLALLGELGAEAEPAP-PDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLY--LPEGKILFTGDLLFAGGDGR 145

                          170       180       190
                   ....*....|....*....|....*....|
gi 492583249   180 ARCDFPGADARTLYRSIRKLLALPPQTLLF 209
Cdd:smart00849 146 TLVDGGDAAASDALESLLKLLKLLPKLVVP 175
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
21-200 4.30e-16

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 75.10  E-value: 4.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249   21 SYLVMDleSKQCALIDSvldydpksGRTRTESADRMIDRVRALQASVQWIFETHVHADHLSAAPYLKQNLGGKIVIGSHI 100
Cdd:pfam00753   8 SYLIEG--GGGAVLIDT--------GGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  101 TVVQKTFGALFNASSDFARNGSQF----DVLLDDDAAFAIGTLQVKAMHTPGHTPACMSylVQVGEQTVAFVGDTLFMPD 176
Cdd:pfam00753  78 ARELLDEELGLAASRLGLPGPPVVplppDVVLEEGDGILGGGLGLLVTHGPGHGPGHVV--VYYGGGKVLFTGDLLFAGE 155

                         170       180
                  ....*....|....*....|....
gi 492583249  177 ygTARCDFPGADARTLYRSIRKLL 200
Cdd:pfam00753 156 --IGRLDLPLGGLLVLHPSSAESS 177
 
Name Accession Description Interval E-value
bifunc_ST_SDO NF040641
bifunctional sulfur transferase/dioxygenase Blh;
8-294 2.36e-126

bifunctional sulfur transferase/dioxygenase Blh;


Pssm-ID: 468609 [Multi-domain]  Cd Length: 423  Bit Score: 366.53  E-value: 2.36e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249   8 HVEALFDSETGTISYLVMDLESKQCALIDSVLDYDPKSGRTRTESADRMIDRVRALQASVQWIFETHVHADHLSAAPYLK 87
Cdd:NF040641 143 QVKGFFDPRTGSVQYVVSDPATRRCAIIDPVLDFDEKSGATSTTNADAILAYVAEEGLTVEWILDTHPHADHFSAAHYLK 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  88 QNLGGKIVIGSHITVVQKTFGALFNASsDFARNGSQFDVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLVqvGEqtVAF 167
Cdd:NF040641 223 EKTGAPTAIGEHVVDVQKLWKGIYNWP-DLPTDGSQWDRLFADGDTFKVGSIDARVMFSPGHTLASITYVI--GD--AAF 297

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 168 VGDTLFMPDYGTARCDFPGADARTLYRSIRKLLALPPQTLLFMCHDYLPNGRALKYMTTVAEQRASNIHVhDGVDEDTFV 247
Cdd:NF040641 298 VHDTLFMPDSGTARADFPGGSARALWRSIQAILALPDETRLFTGHDYQPGGRAPRWESTVAEQKRSNPHL-AGQDEASFV 376

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 492583249 248 SMREARDVTLEMPVLMLPSVQVNMRCGHFPEPEDNGVVYLKIPLNAL 294
Cdd:NF040641 377 ALREARDKTLPMPKLILHALQVNIRGGRLPEPEANGRRYLKIPLDAL 423
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 8-214 1.16e-73

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: 223.43  E-value: 1.16e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249   8 HVEALFDSETGTISYLVMDLESKQCALIDSVLDydpksgrtrteSADRMIDRVRALQASVQWIFETHVHADHLSAAPYLK 87
Cdd:cd07724    1 IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRD-----------SVDRYLDLAAELGLKITYVLETHVHADHVSGARELA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  88 QNLGGKIVIGSHItvvqktfgalfnassdfarNGSQFDVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLvqVGEQTVAF 167
Cdd:cd07724   70 ERTGAPIVIGEGA-------------------PASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYL--VGDPDAVF 128

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 492583249 168 VGDTLFMPDygTARCDFPGA---DARTLYRSIRKLLALPP-QTLLFMCHDY 214
Cdd:cd07724  129 TGDTLFVGD--VGRPDLPGEaegLARQLYDSLQRKLLLLPdETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 8-229 8.40e-42

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: 143.29  E-value: 8.40e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249   8 HVEALFDSETGTISYLVMDleSKQCALIDSVLDydpksgrtrTESADRMIDRVRALQASVQWIFETHVHADHLSAAPYLK 87
Cdd:COG0491    4 LPGGTPGAGLGVNSYLIVG--GDGAVLIDTGLG---------PADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  88 QNLGGKIVIGSHITVVQKTFGalfnASSDFARNGSQFDVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLvqVGEQTVAF 167
Cdd:COG0491   73 EAFGAPVYAHAAEAEALEAPA----AGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFY--VPDEKVLF 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492583249 168 VGDTLFMPDYGtaRCDFPGADARTLYRSIRKLLALPPQTLLFmCHDYLPNGRALKYMTTVAE 229
Cdd:COG0491  147 TGDALFSGGVG--RPDLPDGDLAQWLASLERLLALPPDLVIP-GHGPPTTAEAIDYLEELLA 205
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 21-212 3.76e-37

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: 130.48  E-value: 3.76e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  21 SYLVMDlESKQCALIDsvldydpksgrTRTESADRMIDRVRALQASVQWIFETHVHADHLSAAPYLKQNLGGKIVIGshi 100
Cdd:cd06262   12 CYLVSD-EEGEAILID-----------PGAGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIH--- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 101 tvvQKTFGALFNASSDFARNGSQF------DVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLvqVGEQTVAFVGDTLFM 174
Cdd:cd06262   77 ---EADAELLEDPELNLAFFGGGPlpppepDILLEDGDTIELGGLELEVIHTPGHTPGSVCFY--IEEEGVLFTGDTLFA 151

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 492583249 175 PDYGtaRCDFPGADARTLYRSIRKLLA-LPPQTLLFMCH 212
Cdd:cd06262  152 GSIG--RTDLPGGDPEQLIESIKKLLLlLPDDTVVYPGH 188
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 22-234 3.14e-29

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: 110.13  E-value: 3.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  22 YLVMDLESKQCALIDSVLDydpksgrtrtesADRMIDRVRALQASVQWIFETHVHADHLSAAPYLKQNLGGKIVI---GS 98
Cdd:cd16322   14 YLVADEGGGEAVLVDPGDE------------SEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLhpdDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  99 HITVVQKTFGALFNASSDFarnGSQFDVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLVQvgEQTVAFVGDTLFmpdYG 178
Cdd:cd16322   82 PLYEAADLGAKAFGLGIEP---LPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVE--EEGLLFSGDLLF---QG 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492583249 179 T-ARCDFPGADARTLYRSIRKLLALPPQTLLFMCHdylpnGRAlkymTTVAEQRASN 234
Cdd:cd16322  154 SiGRTDLPGGDPKAMAASLRRLLTLPDETRVFPGH-----GPP----TTLGEERRTN 201
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 20-209 5.53e-29

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: 108.78  E-value: 5.53e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  20 ISYLVMDLESKQCALIDSVLDydpksgrtrtesADRMIDRVRALQASVQWIFETHVHADHLSAAPYLKQNLGGKIVIGSH 99
Cdd:cd16275   13 YSYIIIDKATREAAVVDPAWD------------IEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 100 -ITVVQKTFGALfnassdfarngsqfdVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLVqvgeQTVAFVGDTLFMpdYG 178
Cdd:cd16275   81 eIDYYGFRCPNL---------------IPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLL----GDSLFTGDTLFI--EG 139

                        170       180       190
                 ....*....|....*....|....*....|..
gi 492583249 179 TARCDFPGADARTLYRSIRKLLAL-PPQTLLF 209
Cdd:cd16275  140 CGRCDLPGGDPEEMYESLQRLKKLpPPNTRVY 171
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 21-209 3.56e-28

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: 106.39  E-value: 3.56e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  21 SYLVMDLESKQCALIDSVldydpksgrtrteSADRMIDRVRALQASVQWIFETHVHADHLSAAPYLKQNLGGKIVIGSHI 100
Cdd:cd07723   11 IYLIVDEATGEAAVVDPG-------------EAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 101 TVVQKTfgalfnassdfarngsqfDVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLVQvgEQTVAFVGDTLFMpdYGTA 180
Cdd:cd07723   78 DRIPGL------------------DHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVP--DEPALFTGDTLFS--GGCG 135

                        170       180
                 ....*....|....*....|....*....
gi 492583249 181 RCdFPGaDARTLYRSIRKLLALPPQTLLF 209
Cdd:cd07723  136 RF-FEG-TAEQMYASLQKLLALPDDTLVY 162
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 6-274 2.34e-26

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 104.11  E-value: 2.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249   6 KLHVEALFDSETGTISYLVMDLE--SKQCALIDSVldydpksgrtrTESADRMIDRVRALQASVQWIFETHVHADHLSAA 83
Cdd:PLN02962  10 KLLFRQLFEKESSTYTYLLADVShpDKPALLIDPV-----------DKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  84 PYLKQNLGG-KIVIGshitvvqktfgalfNASsdfarnGSQFDVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLVQVGE 162
Cdd:PLN02962  79 GLLKTKLPGvKSIIS--------------KAS------GSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGP 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 163 QT----VAFVGDTLFMpdYGTARCDFPGADARTLYRSIR-KLLALPPQTLLFMCHDYLPNGralkyMTTVAEQRASNIHV 237
Cdd:PLN02962 139 DQpqprMAFTGDALLI--RGCGRTDFQGGSSDQLYKSVHsQIFTLPKDTLIYPAHDYKGFT-----VSTVGEEMLYNPRL 211

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 492583249 238 HDgvDEDTFVSMREarDVTLEMPVLMLPSVQVNMRCG 274
Cdd:PLN02962 212 TK--DEETFKTIME--NLNLPYPKMIDVAVPANMVCG 244
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 21-209 1.74e-23

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: 94.54  E-value: 1.74e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249    21 SYLVMDleSKQCALIDSVLDYdpksgrtrtesADRMIDRVRALQ-ASVQWIFETHVHADHLSAAPYLKQNLGGKIVIGSH 99
Cdd:smart00849   2 SYLVRD--DGGAILIDTGPGE-----------AEDLLAELKKLGpKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEG 68

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249   100 ITVVQKTFGALFNASSDFARNGSqFDVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLvqVGEQTVAFVGDTLFMPDYGT 179
Cdd:smart00849  69 TAELLKDLLALLGELGAEAEPAP-PDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLY--LPEGKILFTGDLLFAGGDGR 145

                          170       180       190
                   ....*....|....*....|....*....|
gi 492583249   180 ARCDFPGADARTLYRSIRKLLALPPQTLLF 209
Cdd:smart00849 146 TLVDGGDAAASDALESLLKLLKLLPKLVVP 175
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 21-206 5.78e-21

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: 87.99  E-value: 5.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  21 SYLVMDLESKQCALIDSVLDydpksgrtrtesADRMIDRVRALQASVQWIFETHVHADHLSAAPYLKQNLGGKIvIGSHI 100
Cdd:cd07737   13 CSLIWCEETKEAAVIDPGGD------------ADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPI-IGPHK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 101 ---------TVVQKTFGalFNASSDFARngsqfDVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLVQvgEQTVAFVGDT 171
Cdd:cd07737   80 edkfllenlPEQSQMFG--FPPAEAFTP-----DRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNR--ESKLAIVGDV 150

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 492583249 172 LFmpDYGTARCDFPGADARTLYRSIR-KLLALPPQT 206
Cdd:cd07737  151 LF--KGSIGRTDFPGGNHAQLIASIKeKLLPLGDDV 184
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
21-200 4.30e-16

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 75.10  E-value: 4.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249   21 SYLVMDleSKQCALIDSvldydpksGRTRTESADRMIDRVRALQASVQWIFETHVHADHLSAAPYLKQNLGGKIVIGSHI 100
Cdd:pfam00753   8 SYLIEG--GGGAVLIDT--------GGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  101 TVVQKTFGALFNASSDFARNGSQF----DVLLDDDAAFAIGTLQVKAMHTPGHTPACMSylVQVGEQTVAFVGDTLFMPD 176
Cdd:pfam00753  78 ARELLDEELGLAASRLGLPGPPVVplppDVVLEEGDGILGGGLGLLVTHGPGHGPGHVV--VYYGGGKVLFTGDLLFAGE 155

                         170       180
                  ....*....|....*....|....
gi 492583249  177 ygTARCDFPGADARTLYRSIRKLL 200
Cdd:pfam00753 156 --IGRLDLPLGGLLVLHPSSAESS 177
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 7-227 1.10e-15

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 75.18  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249   7 LHVEALFDSetgtISYLVMDLESKQCALIDSVldyDPksgrtrtesaDRMIDRVRALQASVQWIFETHVHADHLSAAPYL 86
Cdd:PLN02469   4 IPVPCLEDN----YAYLIIDESTKDAAVVDPV---DP----------EKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKI 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  87 KQNLGGKIVIGshitvvqktfGALFNAS--SDFARNGSQFdvlldddaafAIG-TLQVKAMHTPGHTPACMSYLV--QVG 161
Cdd:PLN02469  67 KKLVPGIKVYG----------GSLDNVKgcTHPVENGDKL----------SLGkDVNILALHTPCHTKGHISYYVtgKEG 126

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492583249 162 EQTVAFVGDTLFMPDYGtarcDFPGADARTLYRSIRKLLA-LPPQTLLFMCHDYlpNGRALKYMTTV 227
Cdd:PLN02469 127 EDPAVFTGDTLFIAGCG----KFFEGTAEQMYQSLCVTLGsLPKPTQVYCGHEY--TVKNLKFALTV 187
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 17-208 5.22e-13

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: 65.98  E-value: 5.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  17 TGTISYLVMDleSKQCALIDsvldydPksGRTRTESADRMIDRVRAlqASVQWIFETHVHADHLSAAPYLKQnLGGKIVI 96
Cdd:cd16278   16 DGTNTYLLGA--PDGVVVID------P--GPDDPAHLDALLAALGG--GRVSAILVTHTHRDHSPGAARLAE-RTGAPVR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  97 GshitvvqktFGALFNASSDFARngsQFDVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLVQvgEQTVAFVGDTLFmpD 176
Cdd:cd16278   83 A---------FGPHRAGGQDTDF---APDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALE--DEGALFTGDHVM--G 146

                        170       180       190
                 ....*....|....*....|....*....|..
gi 492583249 177 YGTARCDFPGADARTLYRSIRKLLALPPQTLL 208
Cdd:cd16278  147 WSTTVIAPPDGDLGDYLASLERLLALDDRLLL 178
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 52-212 7.88e-13

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: 66.09  E-value: 7.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  52 SADRMIDRVRALQAS---VQWIFETHVHADHLSAAPYLKQNLGGKIVIGS----HIT-----VVQKTFGALFNASSDFAR 119
Cdd:cd07721   32 SAKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEreapYLEgekpyPPPVRLGLLGLLSPLLPV 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 120 NGSQFDVLLDDDAAFAI-GTLQVkaMHTPGHTPACMSYLvqVGEQTVAFVGDTLF--------MPDYGTarcdfpgADAR 190
Cdd:cd07721  112 KPVPVDRTLEDGDTLDLaGGLRV--IHTPGHTPGHISLY--LEEDGVLIAGDALVtvggelvpPPPPFT-------WDME 180

                        170       180
                 ....*....|....*....|..
gi 492583249 191 TLYRSIRKLLALPPQTLLFmCH 212
Cdd:cd07721  181 EALESLRKLAELDPEVLAP-GH 201
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 27-173 2.33e-11

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 61.78  E-value: 2.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  27 LESKQCALIDSVLDydpksgrtrtESADRMIDRV-RALQASVQWIFETHVHADHLSAAPYLKQNLGGKIVIGSH-ITVVQ 104
Cdd:cd07743   15 FGDKEALLIDSGLD----------EDAGRKIRKIlEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIeKAFIE 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492583249 105 KTF---GALFNASSDFARNG-------SQFDVLLDDDaAFAIGTLQVKAMHTPGHTPACMSYLVQVGeqtVAFVGDTLF 173
Cdd:cd07743   85 NPLlepSYLGGAYPPKELRNkflmakpSKVDDIIEEG-ELELGGVGLEIIPLPGHSFGQIGILTPDG---VLFAGDALF 159
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 53-235 1.16e-10

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 61.40  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  53 ADRMIDRVRALQASVQWIFETHVHADHLSAAPYLKQNLGGKiVIGSHItvvqktfgalfnassDFARNGSqFDVLLDDDA 132
Cdd:PLN02398 108 AVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAK-VIGSAV---------------DKDRIPG-IDIVLKDGD 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 133 AFAIGTLQVKAMHTPGHTPACMSYLVQvGEQTVaFVGDTLFMPDYGTArcdFPGAdARTLYRSIRKLLALPPQTLLFMCH 212
Cdd:PLN02398 171 KWMFAGHEVLVMETPGHTRGHISFYFP-GSGAI-FTGDTLFSLSCGKL---FEGT-PEQMLSSLQKIISLPDDTNIYCGH 244

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 492583249 213 DYL-----------PNGRALK-YMTTVAEQRASNI 235
Cdd:PLN02398 245 EYTlsnskfalsiePNNEVLQsYAAHVAHLRSKGL 279
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 34-173 2.22e-10

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 59.52  E-value: 2.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  34 LIDSvLDYDpksgrtrtESADRMIDRVRAL---QASVQWIFETHVHADHLSAAPYLKQNLGGKIVIGS---HITVVQKTF 107
Cdd:cd16280   35 LIDA-LNNN--------EAADLIVDGLEKLgldPADIKYILITHGHGDHYGGAAYLKDLYGAKVVMSEadwDMMEEPPEE 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 108 GALFNASSDFARngsqfDVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLVQV---GEQ-TVAFVGDTLF 173
Cdd:cd16280  106 GDNPRWGPPPER-----DIVIKDGDTLTLGDTTITVYLTPGHTPGTLSLIFPVkdgGKThRAGLWGGTGL 170
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 65-213 8.59e-10

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: 57.99  E-value: 8.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  65 ASVQWIFETHVHADHLSAAPYLKqnlggkiviGSHItVVQKT-FGALFNASSDFARNGSQFDVLLDDDAAFAIGTLQ--- 140
Cdd:cd07729   87 EDIDYVILSHLHFDHAGGLDLFP---------NATI-IVQRAeLEYATGPDPLAAGYYEDVLALDDDLPGGRVRLVDgdy 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 141 -----VKAMHTPGHTPACMSYLVQVGEQTVAFVGDTLFMPD-YGTARCDFPGADARTLYRSIRKLLAL---PPQTLLFmC 211
Cdd:cd07729  157 dlfpgVTLIPTPGHTPGHQSVLVRLPEGTVLLAGDAAYTYEnLEEGRPPGINYDPEAALASLERLKALaerEGARVIP-G 235


                 ..
gi 492583249 212 HD 213
Cdd:cd07729  236 HD 237
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 67-162 6.17e-09

Elizabethkingia meningoseptica GOB-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 GOB-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: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 55.55  E-value: 6.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  67 VQWIFETHVHADHLSAAPYLKQNLGGKIVIGSHITVVQKTFGAlfnasSDFA--RNGSQF-----DVLLDDDAAFAIGTL 139
Cdd:cd16308   61 IKILLTTQAHYDHVGAMAAIKQQTGAKMMVDEKDAKVLADGGK-----SDYEmgGYGSTFapvkaDKLLHDGDTIKLGGT 135

                         90       100
                 ....*....|....*....|...
gi 492583249 140 QVKAMHTPGHTPACMSYLVQVGE 162
Cdd:cd16308  136 KLTLLHHPGHTKGSCSFLFDVKD 158
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 17-208 7.31e-09

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


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 55.40  E-value: 7.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  17 TGTISYLVMDleSKQCALIDSVLDydpksgrtrtESADRMIDRVRALQ---ASVQWIFETHVHADHLSAAPYLKQNLGGK 93
Cdd:cd16288   20 SGLASYLITT--PQGLILIDTGLE----------SSAPMIKANIRKLGfkpSDIKILLNSHAHLDHAGGLAALKKLTGAK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  94 IVIGShitvvqKTFGALFN-ASSDFARNG-------SQFDVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLVQV---GE 162
Cdd:cd16288   88 LMASA------EDAALLASgGKSDFHYGDdslafppVKVDRVLKDGDRVTLGGTTLTAHLTPGHTRGCTTWTMTVkddGK 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 492583249 163 Q-TVAFVGDTLFMPDYGTA-RCDFPGAdARTLYRSIRKLLALPPQTLL 208
Cdd:cd16288  162 VyQVVFADSLTVNPGYKLVgNPTYPGI-AEDYRHSFATLRALQCDIFL 208
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 21-209 1.49e-08

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: 54.04  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  21 SYLVMDleSKQCALIDSvldyDPKSgrtrteSADRMIDRVRALQ---ASVQWIFETHVHADHLSAAPYLKQNLGgkivig 97
Cdd:cd07726   18 SYLLDG--EGRPALIDT----GPSS------SVPRLLAALEALGiapEDVDYIILTHIHLDHAGGAGLLAEALP------ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  98 sHITVVQKTFGA--------LFNASSDFArnGSQFDVL--------------LDDDAAFAIGTLQVKAMHTPGHTPACMS 155
Cdd:cd07726   80 -NAKVYVHPRGArhlidpskLWASARAVY--GDEADRLggeilpvpeervivLEDGETLDLGGRTLEVIDTPGHAPHHLS 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492583249 156 YLvqVGEQTVAFVGDT--LFMPDYGTARC------DFpgaDARTLYRSIRKLLALPPQTLLF 209
Cdd:cd07726  157 FL--DEESDGLFTGDAagVRYPELDVVGPpstpppDF---DPEAWLESLDRLLSLKPERIYL 213
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 51-208 1.75e-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: 54.09  E-value: 1.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  51 ESADRMIDRVRALQ---ASVQWIFETHVHADHLSAAPYLKQNLGGKIVIGSHITVVQKTFGAL---FNASSDFARNGSQF 124
Cdd:cd07708   42 QNAPMIKANIKKLGfkfSDTKLILISHAHFDHAGGSAEIKKQTGAKVMAGAEDVSLLLSGGSSdfhYANDSSTYFPQSTV 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 125 DVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLVQVGEQ----TVAFVGDTLFMPDYG-TARCDFPG--ADARtlyRSIR 197
Cdd:cd07708  122 DRAVHDGERVTLGGTVLTAHATPGHTPGCTTWTMTLKDHgkqyQVVFADSLTVNPGYRlVDNPTYPKivEDYR---HSFA 198

                        170
                 ....*....|.
gi 492583249 198 KLLALPPQTLL 208
Cdd:cd07708  199 VVEAMRCDILL 209
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 68-234 2.25e-08

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 53.67  E-value: 2.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  68 QW----IFETHVHADHLSAAPYLKQNLGGKIVIGSHITvvqKTFGAlfnasSDFARNGSQFDVLLDDDAAFAigtlqvka 143
Cdd:PRK10241  43 NWqpeaIFLTHHHHDHVGGVKELVEKFPQIVVYGPQET---QDKGT-----TQVVKDGETAFVLGHEFSVFA-------- 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 144 mhTPGHTPACMSYLvqvgEQTVAFVGDTLFmpDYGTARCdFPGAdARTLYRSIRKLLALPPQTLLFMCHDY--------- 214
Cdd:PRK10241 107 --TPGHTLGHICYF----SKPYLFCGDTLF--SGGCGRL-FEGT-ASQMYQSLKKINALPDDTLICCAHEYtlsnmkfal 176

                        170       180
                 ....*....|....*....|...
gi 492583249 215 --LPNGRAL-KYMTTVAEQRASN 234
Cdd:PRK10241 177 siLPHDLSInDYYRKVKELRAKN 199
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 19-177 3.03e-07

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


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 49.60  E-value: 3.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  19 TISYLVMDLESKqcALIDSVLDYdpksgRTRTESADRMIDRVRALQASVQWIFETHVHADHLSAAPYLKQNLGgkivigs 98
Cdd:cd07725   15 VNVYLLRDGDET--TLIDTGLAT-----EEDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSG------- 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492583249  99 hITVVQKTFGALfnassdfaRNGSQFDVlldddaafaiGTLQVKAMHTPGHTPACMSYLvqVGEQTVAFVGDTLfMPDY 177
Cdd:cd07725   81 -ATVYILDVTPV--------KDGDKIDL----------GGLRLKVIETPGHTPGHIVLY--DEDRRELFVGDAV-LPKI 137
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 53-207 3.78e-07

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 49.87  E-value: 3.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  53 ADRMIDRVRAL-QASVQWIFETHVHADHLSAAPYLKQnlGGKIVIGSHITV-----VQKTFGALFNASSDFARNGSQF-- 124
Cdd:cd16282   38 ARALLAAIRKVtDKPVRYVVNTHYHGDHTLGNAAFAD--AGAPIIAHENTReelaaRGEAYLELMRRLGGDAMAGTELvl 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 125 -DVLLDDDAAFAIGTLQVKAMHT-PGHTPAcmSYLVQVGEQTVAFVGDTLFMPDYGTarcdFPGADARTLYRSIRKLLAL 202
Cdd:cd16282  116 pDRTFDDGLTLDLGGRTVELIHLgPAHTPG--DLVVWLPEEGVLFAGDLVFNGRIPF----LPDGSLAGWIAALDRLLAL 189


                 ....*
gi 492583249 203 PPQTL 207
Cdd:cd16282  190 DATVV 194
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 51-208 7.27e-07

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: 49.04  E-value: 7.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  51 ESADRMIDRVRAL---QASVQWIFETHVHADHLSAAPYLKQNLGGKIVIGSHITVVQKTFGA---LFNASSDFARngSQF 124
Cdd:cd16289   42 QAADMLLDNMRALgvaPGDLKLILHSHAHADHAGPLAALKRATGARVAANAESAVLLARGGSddiHFGDGITFPP--VQA 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 125 DVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLVQVGEQ----TVAFVgDTLFMPDY---GTARCDFPGADARTLYRSIR 197
Cdd:cd16289  120 DRIVMDGEVVTLGGVTFTAHFTPGHTPGSTSWTWTDTRDgkpvRIAYA-DSLSAPGYqllGNPRYPRIVEDYRRTFATVR 198

                        170
                 ....*....|.
gi 492583249 198 kllALPPQTLL 208
Cdd:cd16289  199 ---ALPCDVLL 206
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 18-168 3.04e-06

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: 47.45  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  18 GTISYLVMdlESKQCALIDSVLDydpksgrTRTESADRMIDRVRALQASVQWIFETHVHADHLSAAPYLKQNLGGKIVI- 96
Cdd:cd16310   21 GIGSYLIT--SNHGAILLDGGLE-------ENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQLKADTGAKLWAs 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  97 ---------GSHITVvQKTFGALFNASsdfarngsQFDVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLVQVGEQ---- 163
Cdd:cd16310   92 rgdrpaleaGKHIGD-NITQPAPFPAV--------KVDRILGDGEKIKLGDITLTATLTPGHTKGCTTWSTTVKENgrpl 162


                 ....*
gi 492583249 164 TVAFV 168
Cdd:cd16310  163 RVVFP 167
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 50-203 3.44e-06

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


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 47.34  E-value: 3.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  50 TESADRMIDRVRALQAS---VQWIFETHVHADH---------LSAAPYLKQNLGGKIVIGSHITVVQKTFGALfnasSDF 117
Cdd:cd16290   41 PQSAPQIEANIRALGFRledVKLILNSHAHFDHaggiaalqrDSGATVAASPAGAAALRSGGVDPDDPQAGAA----DPF 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 118 ArnGSQFDVLLDDDAAFAIGTLQVKAMHTPGHTPACMSYLVQVGEQ----TVAFvGDTL---------FMPDYGTARCdf 184
Cdd:cd16290  117 P--PVAKVRVVADGEVVKLGPLAVTAHATPGHTPGGTSWTWRSCEGgrclDIVY-ADSLtavsadgfrFSDDAHPARV-- 191

                        170
                 ....*....|....*....
gi 492583249 185 pgADARtlyRSIRKLLALP 203
Cdd:cd16290  192 --AAFR---RSIATVAALP 205
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 34-156 2.28e-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: 44.65  E-value: 2.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  34 LIDSVLDydpksgrtrtESADRMIDRVRAL---QASVQWIFETHVHADHLSAAPYLKQNLGGKIVIGSHITVVQKT---- 106
Cdd:cd16315   35 LIDSGTE----------EAAPLVLANIRKLgfdPKDVRWLLSSHEHFDHVGGLAALQRATGARVAASAAAAPVLESgkpa 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 492583249 107 -----FGALfnasSDFArnGSQFDVLLDDDAAFAIGTLQVKAMHTPGHTPACMSY 156
Cdd:cd16315  105 pddpqAGLH----EPFP--PVRVDRIVEDGDTVALGSLRLTAHATPGHTPGALSW 153
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 67-203 7.24e-05

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: 42.57  E-value: 7.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  67 VQWIFETHVHADHLsaapylkQNLGgkivigshitvvqktfgaLF-NA----SSDFARNGSQFDVLLDDDAaFAIGTlQV 141
Cdd:cd07711   61 IDYVVLTHGHPDHI-------GNLN------------------LFpNAtvivGWDICGDSYDDHSLEEGDG-YEIDE-NV 113

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492583249 142 KAMHTPGHTPACMSYLVQVGEQ-TVAFVGDtLFM---PDYGTARCDFPGADARTLYRSIRKLLALP 203
Cdd:cd07711  114 EVIPTPGHTPEDVSVLVETEKKgTVAVAGD-LFEreeDLEDPILWDPLSEDPELQEESRKRILALA 178
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 51-208 8.15e-05

Janthinobacterium lividum THIN-B2 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 THIN-B2-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: 293869  Cd Length: 257  Bit Score: 43.05  E-value: 8.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  51 ESADRMIDRVRALQ---ASVQWIFETHVHADHLSAAPYLkQNLGGKIVIGSHITVVQKTFGALFNASSDFARNGSQFDV- 126
Cdd:cd16311   42 ESAPKIIANIEALGfriEDVKLILNSHGHIDHAGGLAEL-QRRSGALVAASPSAALDLASGEVGPDDPQYHALPKYPPVk 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 127 ---LLDDDAAFAIGTLQVKAMHTPGHTPACMSYLVQV--GEQTVAFV-GDTL---FMPDYG-TARCDFPGADArTLYRSI 196
Cdd:cd16311  121 dmrLARDGGQFNVGPVSLTAHATPGHTPGGLSWTWQScdGPRCLNMVyADSQnavSRPGFKfSASSEYPNAVA-DLRRSF 199

                        170
                 ....*....|..
gi 492583249 197 RKLLALPPQTLL 208
Cdd:cd16311  200 ETLEKLPCDVLI 211
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 45-176 8.87e-05

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 42.96  E-value: 8.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  45 SGRTRTESADRMIDRVRAlqasvqwIFETHVHADHLSAAPYLkqnlgGKIVIGSHITVV--QKTFGALFNA-SSDFARNG 121
Cdd:COG1235   54 DLREQLLRLGLDPSKIDA-------ILLTHEHADHIAGLDDL-----RPRYGPNPIPVYatPGTLEALERRfPYLFAPYP 121

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 492583249 122 SQFDV-LLDDDAAFAIGTLQVKAMHTPGHTPACMSYLVQVGEQTVAFVGDTLFMPD 176
Cdd:COG1235  122 GKLEFhEIEPGEPFEIGGLTVTPFPVPHDAGDPVGYRIEDGGKKLAYATDTGYIPE 177
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 67-203 1.10e-04

uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YmaE and Nostoc all1228 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. 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: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 42.18  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  67 VQWIFETHVH--ADHLSAApylkQNLGGKIVIgsH---ITVVQKTFgalfnassDFARNGSQFDVLLDDDaafaigtlqV 141
Cdd:cd07727   48 IRYIFLTHRDdvADHAKWA----ERFGAKRII--HeddVNAVTRPD--------EVIVLWGGDPWELDPD---------L 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492583249 142 KAMHTPGHTPACMSYLVQvgEQTVAFVGDTLF-MPDYG--TARCDFPGADARTLYRSIRKLLALP 203
Cdd:cd07727  105 TLIPVPGHTRGSVVLLYK--EKGVLFTGDHLAwSRRRGwlSAFRYVCWYSWPEQAESVERLADLD 167
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
70-176 1.10e-04

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 42.87  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  70 IFETHVHADHLSAAPYLKQ--NLGGKIvigSHITV-----VQKTFGALFNASSDFARNGSQFdVLLDDDAAFAIGTLQVK 142
Cdd:COG1234   56 IFITHLHGDHIAGLPGLLStrSLAGRE---KPLTIygppgTKEFLEALLKASGTDLDFPLEF-HEIEPGEVFEIGGFTVT 131

                         90       100       110
                 ....*....|....*....|....*....|....
gi 492583249 143 AMHTPgHTPACMSYLVQVGEQTVAFVGDTLFMPD 176
Cdd:COG1234  132 AFPLD-HPVPAYGYRFEEPGRSLVYSGDTRPCEA 164
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 126-212 1.45e-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: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 42.12  E-value: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 126 VLLDDDAAFAIGtlqVKAMHTPGHTPACMSYLVQVGEQTVAFVGDTL------FMPDYGTARCDFPGADARTlyRsiRKL 199
Cdd:cd16277  135 DLVDDDHEILDG---IRLEPTPGHTPGHVSVELESGGERALFTGDVMhhpiqvARPDWSSVFDEDPAQAAAT--R--RRL 207

                         90
                 ....*....|....*
gi 492583249 200 LAL--PPQTLLFMCH 212
Cdd:cd16277  208 LERaaDTDTLLFPAH 222
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 15-171 1.56e-04

class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293821  Cd Length: 259  Bit Score: 42.20  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  15 SETGTISYLVMDLESKQCALID--------SVLDYDPKSGRTRTESADRMIDRVRAlqasvqwIFETHVHADHLSA---- 82
Cdd:cd07735   13 DEGNTSSFLLDPAGSDGDILLDagtgvgalSLEEMFNDILFPSQKAAYELYQRIRH-------YLITHAHLDHIAGlpll 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  83 APYLKQNLGGKIVI---GSHITVVQKTfgaLFNASS--DFARNGSQFDVLLD-----DDAAFAIGTLQVKAM---HTpgh 149
Cdd:cd07735   86 SPNDGGQRGSPKTIyglPETIDALKKH---IFNWVIwpDFTSIPSGKYPYLRlepiePEYPIALTGLSVTAFpvsHG--- 159

                        170       180
                 ....*....|....*....|..
gi 492583249 150 TPACMSYLVQVGEQTVAFVGDT 171
Cdd:cd07735  160 VPVSTAFLIRDGGDSFLFFGDT 181
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 141-175 4.03e-04

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 40.99  E-value: 4.03e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 492583249 141 VKAMHTPGHTPACMSYLVQVGEQTVAFVGDTLFMP 175
Cdd:cd07720  175 ITAVPAPGHTPGHTGYRIESGGERLLIWGDIVHHP 209
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 64-207 4.32e-04

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: 40.21  E-value: 4.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  64 QASVQWIFETHVHADHLSAAPYLKqnlggKIVIGSHITVVQktFGALFNASSDFARNGSQFDvlLDDDAAFAIGTLQVKA 143
Cdd:cd07722   54 NATISDILLTHWHHDHVGGLPDVL-----DLLRGPSPRVYK--FPRPEEDEDPDEDGGDIHD--LQDGQVFKVEGATLRV 124

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492583249 144 MHTPGHTPACMSyLVQVGEQTVaFVGDTLFmpdyGTARCDFpgADARTLYRSIRKLLALPPQTL 207
Cdd:cd07722  125 IHTPGHTTDHVC-FLLEEENAL-FTGDCVL----GHGTAVF--EDLAAYMASLKKLLSLGPGRI 180
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 52-163 5.09e-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: 40.62  E-value: 5.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  52 SADRMIDRVRALQ---ASVQWIFETHVHADHLSAAPYLkQNLGGKIVIGSHITVvqktfGALFNASSDfaRNGSQFDVL- 127
Cdd:cd16313   43 SPEQIAASIRQLGfklEDVKYILSSHDHWDHAGGIAAL-QKLTGAQVLASPATV-----AVLRSGSMG--KDDPQFGGLt 114

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 492583249 128 ----------LDDDAAFAIGTLQVKAMHTPGHTPACMSYLVQVGEQ 163
Cdd:cd16313  115 pmppvasvraVRDGEVVKLGPLAVTAHATPGHTTGGTSWTWQSCEQ 160
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 51-203 8.80e-04

Janthinobacterium lividum 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 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: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 39.97  E-value: 8.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  51 ESADRMIDRVRAL---QASVQWIFETHVHADHLSAAPYLKQNLGGkivigshiTVVQKTFGALFNASSDFARNGSQFDV- 126
Cdd:cd16312   42 QSAPLIIANIEALgfrIEDVKLILNSHAHWDHAGGIAALQKASGA--------TVAASAHGAQVLQSGTNGKDDPQYQAk 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 127 ------------LLDDDAAFAIGTLQVKAMHTPGHTPACMSYLVQVGEQTVAF---VGDTLFMPDYG----TARCDFPGA 187
Cdd:cd16312  114 pvvhvakvakvkEVGEGDTLKVGPLRLTAHMTPGHTPGGTTWTWTSCEGQRCLdvvYADSLNPYSSGdfyyTGKGGYPDI 193

                        170
                 ....*....|....*.
gi 492583249 188 DArTLYRSIRKLLALP 203
Cdd:cd16312  194 SA-SFRASIAKVAALP 208
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 127-205 8.87e-04

uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 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: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 39.53  E-value: 8.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249 127 LLDDDAAFAIGTLQVKAMHTPGHTPACMSYLVQvgEQTVAFVGDT-----LFMpdygtarcDFPGADARTLYRSIRKLLA 201
Cdd:cd07712  101 PLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDR--ANRLLFSGDVvydgpLIM--------DLPHSDLDDYLASLEKLSK 170


                 ....
gi 492583249 202 LPPQ 205
Cdd:cd07712  171 LPDE 174
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 73-185 2.16e-03

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 38.74  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  73 THVHADHLSAAPYlkqnlggKIVIGSHITVVqktfgALFNASSDFARNGSQFDVLLDDDAAFAIGTLQVK---AMHTPGH 149
Cdd:COG2220   55 THDHYDHLDDATL-------RALKRTGATVV-----APLGVAAWLRAWGFPRVTELDWGESVELGGLTVTavpARHSSGR 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 492583249 150 TPAC----MSYLVQVGEQTVAFVGDTLFMPDYGTARCDFP 185
Cdd:COG2220  123 PDRNgglwVGFVIETDGKTIYHAGDTGYFPEMKEIGERFP 162
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
21-171 2.67e-03

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 38.79  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  21 SYLVMDLESKQCALID--SVLdydpkSGRTRTESADRMIDRVRALQASVQWIFETHVHADHLSAAPYLKQNLGGKIVIG- 97
Cdd:COG5212   30 TYLLRPLGSDDYVLLDagTVV-----SGLELAEQKGAFKGRQGYVLEHIKGYLISHAHLDHIAGLPILSPDDSPKTIYAl 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  98 -SHITVVQKTFgalFNASS--DFARNGSQFD------VLLDDDAAFAIG--TLQVKAM---HTpghTPACMsYLVQVGEQ 163
Cdd:COG5212  105 pETIDALRNHY---FNWVIwpDFTDIGSAPHlpkyryVPLKPGQTFPLGgtGLRVTAFplsHS---VPSSA-FLIESGGG 177


                 ....*...
gi 492583249 164 TVAFVGDT 171
Cdd:COG5212  178 AFLYSGDT 185
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 70-171 4.41e-03

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: 37.24  E-value: 4.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492583249  70 IFETHVHADH---LSAAPYLKQNLGGK---IVIGShiTVVQKTFGALFNASSDFARNGSQFDVLLDDDAA--FAIGTLQV 141
Cdd:cd16272   54 IFLSHFHLDHiggLPTLLFARRYGGRKkplTIYGP--KGIKEFLEKLLNFPVEILPLGFPLEIEELEEGGevLELGDLKV 131

                         90       100       110
                 ....*....|....*....|....*....|
gi 492583249 142 KAMHTPgHTPACMSYLVQVGEQTVAFVGDT 171
Cdd:cd16272  132 EAFPVK-HSVESLGYRIEAEGKSIVYSGDT 160
 
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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