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Conserved domains on  [gi|1519312219|ref|NP_981951|]
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acyl-coenzyme A thioesterase MBLAC2 [Homo sapiens]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869773)

uncharacterized MBL fold metallo-hydrolase similar to uncharacterized human metallo-beta-lactamase domain-containing protein 2 (MBLAC2 )

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 22-231 2.36e-89

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: 262.95  E-value: 2.36e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  22 RFYESGNRANIWLVRGSEQDVVIDTGLGLRSLPEYLYSSGLLqdreakedaarrPLLAVATHVHFDHSGGLYQFDRVAVH 101
Cdd:cd07712     1 LFIEEDDRVNIYLLRGRDRALLIDTGLGIGDLKEYVRTLTDL------------PLLVVATHGHFDHIGGLHEFEEVYVH 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 102 HAEAEALARGDNFETVTWlsdsevvrtpspgwRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKD 181
Cdd:cd07712    69 PADAEILAAPDNFETLTW--------------DAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRA 134

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1519312219 182 RKILFSGDVVYDGSLIDWLPYSRISDYVGTCERLIELVDrgLVEKVLPGH 231
Cdd:cd07712   135 NRLLFSGDVVYDGPLIMDLPHSDLDDYLASLEKLSKLPD--EFDKVLPGH 182
 
Name Accession Description Interval E-value
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 22-231 2.36e-89

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: 262.95  E-value: 2.36e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  22 RFYESGNRANIWLVRGSEQDVVIDTGLGLRSLPEYLYSSGLLqdreakedaarrPLLAVATHVHFDHSGGLYQFDRVAVH 101
Cdd:cd07712     1 LFIEEDDRVNIYLLRGRDRALLIDTGLGIGDLKEYVRTLTDL------------PLLVVATHGHFDHIGGLHEFEEVYVH 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 102 HAEAEALARGDNFETVTWlsdsevvrtpspgwRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKD 181
Cdd:cd07712    69 PADAEILAAPDNFETLTW--------------DAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRA 134

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1519312219 182 RKILFSGDVVYDGSLIDWLPYSRISDYVGTCERLIELVDrgLVEKVLPGH 231
Cdd:cd07712   135 NRLLFSGDVVYDGPLIMDLPHSDLDDYLASLEKLSKLPD--EFDKVLPGH 182
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 16-244 7.31e-40

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: 137.90  E-value: 7.31e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  16 IFWIQERFYESGNRANIWLVRGSEQDVVIDTGLGLRSLPEYLyssgllqdrEAKEDAARRPLLAVATHVHFDHSGGLYQF 95
Cdd:COG0491     1 VYVLPGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEALL---------AALAALGLDIKAVLLTHLHPDHVGGLAAL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  96 D-----RVAVHHAEAEALARGDnfetvtwlsdsevvrtpspgwRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGH 170
Cdd:COG0491    72 AeafgaPVYAHAAEAEALEAPA---------------------AGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGH 130

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519312219 171 SRGSICLHDKDRKILFSGDVVYDGSL-IDWLPYSRISDYVGTCERLIELVDrglvEKVLPGHFNTFGAERLFRLA 244
Cdd:COG0491   131 TPGHVSFYVPDEKVLFTGDALFSGGVgRPDLPDGDLAQWLASLERLLALPP----DLVIPGHGPPTTAEAIDYLE 201
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 31-231 1.91e-27

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: 104.56  E-value: 1.91e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219   31 NIWLVRGSEQDVVIDTGLGlrslpeylYSSGLLqdREAKEDAARRPLLAVATHVHFDHSGGLYQF-----DRVAVHHAEA 105
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPG--------EAEDLL--AELKKLGPKKIDAIILTHGHPDHIGGLPELleapgAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  106 EALargdnfetvtwlsdsevvRTPSPGWRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKIL 185
Cdd:smart00849  71 ELL------------------KDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKIL 132

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1519312219  186 FSGDVVYDGSLIDWLPYSRISDYVGTCERLIELVDRgLVEKVLPGH 231
Cdd:smart00849 133 FTGDLLFAGGDGRTLVDGGDAAASDALESLLKLLKL-LPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
31-231 8.45e-22

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 90.12  E-value: 8.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  31 NIWLVRGSEQDVVIDTGLGLrslpeylySSGLLQDREAKEDAARRPLLAVATHVHFDHSGGLYQFDRVAVHHAEAEALar 110
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSA--------EAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAE-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 111 gdnfETVTWLSDSEVVRTPSPGWRARQFRVQAVQPTLIlqDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKILFSGDV 190
Cdd:pfam00753  77 ----EARELLDEELGLAASRLGLPGPPVVPLPPDVVLE--EGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1519312219 191 VYDGSLIDW-----LPYSRISDYVGTCERLIELVDRGLVEKVLPGH 231
Cdd:pfam00753 151 LFAGEIGRLdlplgGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 147-236 3.12e-04

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 41.75  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 147 LILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKILFSGDVVYD---GSLIDWLPYSRISdyvgTCERLIELVDRgl 223
Cdd:PLN02398  164 IVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSlscGKLFEGTPEQMLS----SLQKIISLPDD-- 237

                          90
                  ....*....|...
gi 1519312219 224 vEKVLPGHFNTFG 236
Cdd:PLN02398  238 -TNIYCGHEYTLS 249
 
Name Accession Description Interval E-value
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 22-231 2.36e-89

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: 262.95  E-value: 2.36e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  22 RFYESGNRANIWLVRGSEQDVVIDTGLGLRSLPEYLYSSGLLqdreakedaarrPLLAVATHVHFDHSGGLYQFDRVAVH 101
Cdd:cd07712     1 LFIEEDDRVNIYLLRGRDRALLIDTGLGIGDLKEYVRTLTDL------------PLLVVATHGHFDHIGGLHEFEEVYVH 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 102 HAEAEALARGDNFETVTWlsdsevvrtpspgwRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKD 181
Cdd:cd07712    69 PADAEILAAPDNFETLTW--------------DAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRA 134

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1519312219 182 RKILFSGDVVYDGSLIDWLPYSRISDYVGTCERLIELVDrgLVEKVLPGH 231
Cdd:cd07712   135 NRLLFSGDVVYDGPLIMDLPHSDLDDYLASLEKLSKLPD--EFDKVLPGH 182
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 16-244 7.31e-40

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: 137.90  E-value: 7.31e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  16 IFWIQERFYESGNRANIWLVRGSEQDVVIDTGLGLRSLPEYLyssgllqdrEAKEDAARRPLLAVATHVHFDHSGGLYQF 95
Cdd:COG0491     1 VYVLPGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEALL---------AALAALGLDIKAVLLTHLHPDHVGGLAAL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  96 D-----RVAVHHAEAEALARGDnfetvtwlsdsevvrtpspgwRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGH 170
Cdd:COG0491    72 AeafgaPVYAHAAEAEALEAPA---------------------AGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGH 130

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519312219 171 SRGSICLHDKDRKILFSGDVVYDGSL-IDWLPYSRISDYVGTCERLIELVDrglvEKVLPGHFNTFGAERLFRLA 244
Cdd:COG0491   131 TPGHVSFYVPDEKVLFTGDALFSGGVgRPDLPDGDLAQWLASLERLLALPP----DLVIPGHGPPTTAEAIDYLE 201
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 30-231 1.36e-31

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: 115.46  E-value: 1.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  30 ANIWLVRGSEQD-VVIDTGLGLRslpEYLyssgllqdREAKEDAARRPLLAVATHVHFDHSGGLYQFDR-----VAVHHA 103
Cdd:cd06262    10 TNCYLVSDEEGEaILIDPGAGAL---EKI--------LEAIEELGLKIKAILLTHGHFDHIGGLAELKEapgapVYIHEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 104 EAEALARGDNFetvtwlsdsevvrtpspGWRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRK 183
Cdd:cd06262    79 DAELLEDPELN-----------------LAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEG 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1519312219 184 ILFSGDVVYDGSLIDW-LPYSRISDYVGTCERLIELVDRGLVekVLPGH 231
Cdd:cd06262   142 VLFTGDTLFAGSIGRTdLPGGDPEQLIESIKKLLLLLPDDTV--VYPGH 188
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 25-231 1.01e-28

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: 108.81  E-value: 1.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  25 ESGNRANIWLVRGSEQDVVIDTGLGLRSLPEYLyssgllqdREAKEDAARRPLLAVATHVHFDHSGGLYQFDRVAV---- 100
Cdd:cd16282    10 GGGFISNIGFIVGDDGVVVIDTGASPRLARALL--------AAIRKVTDKPVRYVVNTHYHGDHTLGNAAFADAGApiia 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 101 HHAEAEALARgdnfetvtwlsDSEVVRTPSPGWRARQFR-VQAVQPTLILQDGDVINLGDRQLTVMHM-PGHSRGSICLH 178
Cdd:cd16282    82 HENTREELAA-----------RGEAYLELMRRLGGDAMAgTELVLPDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVW 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1519312219 179 DKDRKILFSGDVVYDGsLIDWLPYSRISDYVGTCERLIELVDrglvEKVLPGH 231
Cdd:cd16282   151 LPEEGVLFAGDLVFNG-RIPFLPDGSLAGWIAALDRLLALDA----TVVVPGH 198
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 31-231 1.91e-27

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: 104.56  E-value: 1.91e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219   31 NIWLVRGSEQDVVIDTGLGlrslpeylYSSGLLqdREAKEDAARRPLLAVATHVHFDHSGGLYQF-----DRVAVHHAEA 105
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPG--------EAEDLL--AELKKLGPKKIDAIILTHGHPDHIGGLPELleapgAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  106 EALargdnfetvtwlsdsevvRTPSPGWRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKIL 185
Cdd:smart00849  71 ELL------------------KDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKIL 132

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1519312219  186 FSGDVVYDGSLIDWLPYSRISDYVGTCERLIELVDRgLVEKVLPGH 231
Cdd:smart00849 133 FTGDLLFAGGDGRTLVDGGDAAASDALESLLKLLKL-LPKLVVPGH 177
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 15-231 6.87e-24

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: 95.75  E-value: 6.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  15 GIFWIqerfyESGNRANIWLVRGSEQDVVIDTGlglrslpeYLYSSGLLQDREAKEDAARRPLLAVA-THVHFDHSGGLY 93
Cdd:cd07721     1 GVYQL-----PLLPPVNAYLIEDDDGLTLIDTG--------LPGSAKRILKALRELGLSPKDIRRILlTHGHIDHIGSLA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  94 QFDR-----VAVHHAEAEALARGDNFETVTWLSDSEVVRTPSPgwrarqfrVQAVQPTLILQDGDVINLGDRqLTVMHMP 168
Cdd:cd07721    68 ALKEapgapVYAHEREAPYLEGEKPYPPPVRLGLLGLLSPLLP--------VKPVPVDRTLEDGDTLDLAGG-LRVIHTP 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519312219 169 GHSRGSICLHDKDRKILFSGDVV--YDGSLidWLPYSRISD----YVGTCERLIELVdrglVEKVLPGH 231
Cdd:cd07721   139 GHTPGHISLYLEEDGVLIAGDALvtVGGEL--VPPPPPFTWdmeeALESLRKLAELD----PEVLAPGH 201
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 31-241 3.77e-22

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: 91.26  E-value: 3.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  31 NIWLVR--GSEQDVVIDTGLGlrslpeylySSGLLqdrEAKEDAARRPLLAVATHVHFDHSGGLYQFDRvavhHAEAEAL 108
Cdd:cd16322    12 NTYLVAdeGGGEAVLVDPGDE---------SEKLL---ARFGTTGLTLLYILLTHAHFDHVGGVADLRR----HPGAPVY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 109 ARGDnfetvtwlsDSEVVRTPSPGWRARQFRVQ-AVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKILFS 187
Cdd:cd16322    76 LHPD---------DLPLYEAADLGAKAFGLGIEpLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFS 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1519312219 188 GDVVYDGSL--IDwLPYSRISDYVGTCERLIELVDRglvEKVLPGHF--NTFGAERLF 241
Cdd:cd16322   147 GDLLFQGSIgrTD-LPGGDPKAMAASLRRLLTLPDE---TRVFPGHGppTTLGEERRT 200
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
31-231 8.45e-22

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 90.12  E-value: 8.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  31 NIWLVRGSEQDVVIDTGLGLrslpeylySSGLLQDREAKEDAARRPLLAVATHVHFDHSGGLYQFDRVAVHHAEAEALar 110
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSA--------EAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAE-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 111 gdnfETVTWLSDSEVVRTPSPGWRARQFRVQAVQPTLIlqDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKILFSGDV 190
Cdd:pfam00753  77 ----EARELLDEELGLAASRLGLPGPPVVPLPPDVVLE--EGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1519312219 191 VYDGSLIDW-----LPYSRISDYVGTCERLIELVDRGLVEKVLPGH 231
Cdd:pfam00753 151 LFAGEIGRLdlplgGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 28-235 2.38e-21

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: 88.51  E-value: 2.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  28 NRANIWLVRGSEQDVVIDTGLGLRSLPEYLYSSglLQDREAKEDAARRPLLavaTHVHFDHSGGLYQFdrvavhHAEAEA 107
Cdd:cd07725    13 GHVNVYLLRDGDETTLIDTGLATEEDAEALWEG--LKELGLKPSDIDRVLL---THHHPDHIGLAGKL------QEKSGA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 108 LARGDNFETVTwlsdsevvrtpspgwrarqfrvqavqptlilqDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKILFS 187
Cdd:cd07725    82 TVYILDVTPVK--------------------------------DGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFV 129

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1519312219 188 GDVV--YDGSLIDWLPYSRI---SDYVGTCERLIELvdrgLVEKVLPGHFNTF 235
Cdd:cd07725   130 GDAVlpKITPNVSLWAVRVEdplGAYLESLDKLEKL----DVDLAYPGHGGPI 178
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 31-231 6.87e-21

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: 87.16  E-value: 6.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  31 NIWLVRGSEQDVVIDTGlglRSLPEYLyssgllqDREAKEDAARRPLLAVATHVHFDHSGGlyqfdrvavhhaeAEALAR 110
Cdd:cd16278    19 NTYLLGAPDGVVVIDPG---PDDPAHL-------DALLAALGGGRVSAILVTHTHRDHSPG-------------AARLAE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 111 gdnfetvtwlsdsevvRTPSP--GWRARQFRVQ--AVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKILF 186
Cdd:cd16278    76 ----------------RTGAPvrAFGPHRAGGQdtDFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALF 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1519312219 187 SGDVVYDGS--LIDWlPYSRISDYVGTCERLIELVDRglveKVLPGH 231
Cdd:cd16278   140 TGDHVMGWSttVIAP-PDGDLGDYLASLERLLALDDR----LLLPGH 181
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 15-218 3.05e-18

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: 81.00  E-value: 3.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  15 GIFWIQERFYESGNRANIWLVRGSEQDVVIDTGlglrslpeylYSSGLLQDREAKEDAARRP--LLAVA-THVHFDHSGG 91
Cdd:cd07726     1 GIYLIDLGFLGFPGRIASYLLDGEGRPALIDTG----------PSSSVPRLLAALEALGIAPedVDYIIlTHIHLDHAGG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  92 LYQFDR------VAVHHAEAEALAR------------GDNFETVTWlsdsEVVRTPSPgwrarqfRVQAvqptliLQDGD 153
Cdd:cd07726    71 AGLLAEalpnakVYVHPRGARHLIDpsklwasaravyGDEADRLGG----EILPVPEE-------RVIV------LEDGE 133

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519312219 154 VINLGDRQLTVMHMPGHSRGSICLHDKDRKILFSGDVVydGSLIDWLPYSR----------ISDYVGTCERLIEL 218
Cdd:cd07726   134 TLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDAA--GVRYPELDVVGppstpppdfdPEAWLESLDRLLSL 206
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 33-231 1.12e-15

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: 74.17  E-value: 1.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  33 WLVRGSEQDVVIDTGLGlrslPEYLYSSGLLQDREAKEDAARRPLLA---------------VATHVHFDHSGGLYQFD- 96
Cdd:cd07729    35 YLIEHPEGTILVDTGFH----PDAADDPGGLELAFPPGVTEEQTLEEqlarlgldpedidyvILSHLHFDHAGGLDLFPn 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  97 -RVAVHHAEAEALARGDNFEtvtwlsdsevvRTPSPGWRARQFRVQAVQPTLIlqDGDVINLGDrqLTVMHMPGHSRGSI 175
Cdd:cd07729   111 aTIIVQRAELEYATGPDPLA-----------AGYYEDVLALDDDLPGGRVRLV--DGDYDLFPG--VTLIPTPGHTPGHQ 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519312219 176 CL--HDKDRKILFSGDVVY-----DGSLIDWLPYSRIsDYVGTCERLIELVDRgLVEKVLPGH 231
Cdd:cd07729   176 SVlvRLPEGTVLLAGDAAYtyenlEEGRPPGINYDPE-AALASLERLKALAER-EGARVIPGH 236
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 82-195 2.38e-14

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: 69.50  E-value: 2.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  82 THVHFDHSGGLyqfDRVAVHH-AEAEALARGDNFetvtWLSDSEVvrtpspgwRARQF---RVQAVQPTLILQDGDVINL 157
Cdd:cd07737    53 THGHLDHVGGA---AELAEHYgVPIIGPHKEDKF----LLENLPE--------QSQMFgfpPAEAFTPDRWLEEGDTVTV 117

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1519312219 158 GDRQLTVMHMPGHSRGSICLHDKDRKILFSGDVVYDGS 195
Cdd:cd07737   118 GNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGS 155
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 82-189 1.05e-13

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: 67.49  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  82 THVHFDHSGGlyqfdrvavhhaeaealargdNFETVTWLSDSEVV---RTPSPGWrarqfrvqavqpTLILQDGDVINLG 158
Cdd:cd07723    50 THHHWDHTGG---------------------NAELKALFPDAPVYgpaEDRIPGL------------DHPVKDGDEIKLG 96

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1519312219 159 DRQLTVMHMPGHSRGSICLHDKDRKILFSGD 189
Cdd:cd07723    97 GLEVKVLHTPGHTLGHICYYVPDEPALFTGD 127
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 82-215 1.51e-12

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: 65.81  E-value: 1.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  82 THVHFDHSGGLYQFD-----RVAVHHAEAEALARGDNfetvtwlSDsevvrtpsPGWRARQFRVQAVQPTLILQDGDVIN 156
Cdd:cd16288    67 SHAHLDHAGGLAALKkltgaKLMASAEDAALLASGGK-------SD--------FHYGDDSLAFPPVKVDRVLKDGDRVT 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1519312219 157 LGDRQLTVMHMPGHSRGS------ICLHDKDRKILF--SGDVVYDGSLIDWLPYSRIS-DYVGTCERL 215
Cdd:cd16288   132 LGGTTLTAHLTPGHTRGCttwtmtVKDDGKVYQVVFadSLTVNPGYKLVGNPTYPGIAeDYRHSFATL 199
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 147-231 5.68e-10

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: 57.21  E-value: 5.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 147 LILQDGDVINLGDrQLTVMHMPGHSRGSICLHDKDRKILFSGDVVYDGSLIDWLPYSR------ISDYVGTCERLIELVd 220
Cdd:cd07727    90 IVLWGGDPWELDP-DLTLIPVPGHTRGSVVLLYKEKGVLFTGDHLAWSRRRGWLSAFRyvcwysWPEQAESVERLADLD- 167

                          90
                  ....*....|.
gi 1519312219 221 rglVEKVLPGH 231
Cdd:cd07727   168 ---FEWVLPGH 175
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 82-231 7.15e-10

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: 56.78  E-value: 7.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  82 THVHFDHSGGlyqfdrvavhhaeAEALARgdNFETVTWLSDSEVvrtpspgwRARQFRVQAVQPtliLQDGDVINLGDRQ 161
Cdd:cd16275    54 THSHFDHVNL-------------VEPLLA--KYDAPVYMSKEEI--------DYYGFRCPNLIP---LEDGDTIKIGDTE 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519312219 162 LTVMHMPGHSRGSICLHDKDRkiLFSGDVVYDGS--LIDwLPYSRISDYVGTCERLIELVDRGLVekVLPGH 231
Cdd:cd16275   108 ITCLLTPGHTPGSMCYLLGDS--LFTGDTLFIEGcgRCD-LPGGDPEEMYESLQRLKKLPPPNTR--VYPGH 174
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 31-192 1.33e-09

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: 57.17  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  31 NIWLVRGSEQDVVIDTGLGLRSLPeylySSGLLQDReakedaarrplLAVA------------THVHFDHSGGLYQ---- 94
Cdd:cd07720    50 NAFLVRTGGRLILVDTGAGGLFGP----TAGKLLAN-----------LAAAgidpediddvllTHLHPDHIGGLVDaggk 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  95 --FDRVAVHHAEAEAlargdNFetvtWLSDSEVVRTPSpgwRARQF------RVQAVQPTLILQDGDVINLGdrqLTVMH 166
Cdd:cd07720   115 pvFPNAEVHVSEAEW-----DF----WLDDANAAKAPE---GAKRFfdaardRLRPYAAAGRFEDGDEVLPG---ITAVP 179

                         170       180
                  ....*....|....*....|....*...
gi 1519312219 167 MPGHSRG--SICLHDKDRKILFSGDVVY 192
Cdd:cd07720   180 APGHTPGhtGYRIESGGERLLIWGDIVH 207
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 78-215 1.66e-09

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: 56.78  E-value: 1.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  78 LAVATHVHFDHSGGLYQFDR-----VAVHHAEAEALARG----DNFEtvtwlSDSEVVRTPSPGWRArqfrvqavqptli 148
Cdd:cd07708    63 LILISHAHFDHAGGSAEIKKqtgakVMAGAEDVSLLLSGgssdFHYA-----NDSSTYFPQSTVDRA------------- 124

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519312219 149 LQDGDVINLGDRQLTVMHMPGHSRGSI------CLHDKDRKILF--SGDVVYDGSLIDWLPYSRI-SDYVGTCERL 215
Cdd:cd07708   125 VHDGERVTLGGTVLTAHATPGHTPGCTtwtmtlKDHGKQYQVVFadSLTVNPGYRLVDNPTYPKIvEDYRHSFAVV 200
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 31-191 2.95e-09

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: 55.23  E-value: 2.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  31 NIWLVRGSEQDVVIDTGLGLRSLPEYLYSsgLLQDREAKEDAArrpllAVATHVHFDHSGGLyqfdrvavhhAEAEALAR 110
Cdd:cd07722    19 NTYLVGTGKRRILIDTGEGRPSYIPLLKS--VLDSEGNATISD-----ILLTHWHHDHVGGL----------PDVLDLLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 111 GDNFETVTWLSDSEVVRTPSPGwrarqfrvqavQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKILFSGDV 190
Cdd:cd07722    82 GPSPRVYKFPRPEEDEDPDEDG-----------GDIHDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGDC 150


                  .
gi 1519312219 191 V 191
Cdd:cd07722   151 V 151
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 139-189 3.53e-09

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: 54.71  E-value: 3.53e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1519312219 139 RVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKILFSGD 189
Cdd:cd07724    81 GAPASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGD 131
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 80-174 9.99e-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: 54.78  E-value: 9.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  80 VATHVHFDHSGGLYQFDR-----VAVHHAEAEALARGDNfetvtwlSDSEVvrtpspGWRARQFrvQAVQPTLILQDGDV 154
Cdd:cd16308    65 LTTQAHYDHVGAMAAIKQqtgakMMVDEKDAKVLADGGK-------SDYEM------GGYGSTF--APVKADKLLHDGDT 129

                          90       100
                  ....*....|....*....|
gi 1519312219 155 INLGDRQLTVMHMPGHSRGS 174
Cdd:cd16308   130 IKLGGTKLTLLHHPGHTKGS 149
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 145-231 1.66e-08

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: 54.03  E-value: 1.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 145 PTLILQDGDVINLGDRQLTVMHMPG-HSRGSICLHDKDRKILFSGDV---------VYDGSLIDWLPYSR--ISDYVGT- 211
Cdd:cd07709   117 RFVVVKDGDTLDLGKHTLKFIPAPMlHWPDTMVTYDPEDKILFSGDAfgahgasgeLFDDEVEDYLEEARryYANIMGPf 196

                          90       100
                  ....*....|....*....|....
gi 1519312219 212 ---CERLIELVdRGL-VEKVLPGH 231
Cdd:cd07709   197 skqVRKALEKL-EALdIKMIAPSH 219
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 23-231 1.93e-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) 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: 53.30  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  23 FYESGnRANIWLVRGSEQDV-VIDTGLG---LRSLPEYLyssgllqdreakEDAARRPLLAVATHVHFDHSGGLYQF--- 95
Cdd:cd07743     2 YYIPG-PTNIGVYVFGDKEAlLIDSGLDedaGRKIRKIL------------EELGWKLKAIINTHSHADHIGGNAYLqkk 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  96 --DRVAVHHAEAEALARGDNFETVTWLSdsevvrTPSPGWRARQFRVQAVQPTLILQDGDvINLGDRQLTVMHMPGHSRG 173
Cdd:cd07743    69 tgCKVYAPKIEKAFIENPLLEPSYLGGA------YPPKELRNKFLMAKPSKVDDIIEEGE-LELGGVGLEIIPLPGHSFG 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519312219 174 SICLHDKDrKILFSGDVVYDGSLID--WLPYSR-ISDYVGTCERLIELVdrglVEKVLPGH 231
Cdd:cd07743   142 QIGILTPD-GVLFAGDALFGEEVLEkyGIPFLYdVEEQLETLEKLEELD----ADYYVPGH 197
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 82-245 2.72e-08

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 53.36  E-value: 2.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  82 THVHFDHSGGlyqfdrvavhhaeAEALArgDNFETVTWLS--DSEVVRTPsPGWRARQFRVQAVQPTLILQDGDVINLGD 159
Cdd:cd16280    68 THGHGDHYGG-------------AAYLK--DLYGAKVVMSeaDWDMMEEP-PEEGDNPRWGPPPERDIVIKDGDTLTLGD 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 160 RQLTVMHMPGHSRGSICL----HDKDRK---ILFSGdvvydGSLIDWLPYSRISDYVGTCERLIELVDRGLVEKVLPGH- 231
Cdd:cd16280   132 TTITVYLTPGHTPGTLSLifpvKDGGKThraGLWGG-----TGLNTGPNLERREQYIASLERFKKIAEEAGVDVFLSNHp 206

                         170
                  ....*....|....
gi 1519312219 232 FNTFGAERLFRLAS 245
Cdd:cd16280   207 FQDGSLEKREALRN 220
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 17-186 3.75e-08

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: 52.84  E-value: 3.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  17 FWIQERFYESGNRA-NIWLVRGSEQDVVIDTGL--GLRSLPEYLYSSGL-LQDREakedaarrplLAVATHVHFDHSGGL 92
Cdd:cd16310     8 FRIVDNIYYVGTKGiGSYLITSNHGAILLDGGLeeNAALIEQNIKALGFkLSDIK----------IIINTHAHYDHAGGL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  93 YQFDR-----VAVHHAEAEALARGdnfetvTWLSDSEVVRTPSPgwrarqfrvqAVQPTLILQDGDVINLGDRQLTVMHM 167
Cdd:cd16310    78 AQLKAdtgakLWASRGDRPALEAG------KHIGDNITQPAPFP----------AVKVDRILGDGEKIKLGDITLTATLT 141

                         170       180
                  ....*....|....*....|....*
gi 1519312219 168 PGHSRG------SICLHDKDRKILF 186
Cdd:cd16310   142 PGHTKGcttwstTVKENGRPLRVVF 166
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 ...
 80-175 1.19e-07

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: 51.58  E-value: 1.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  80 VATHVHFDHSGGLYQFDR-----VAVHHAEAEALARGDNFETvtwlsdsevvrTPSPGWRARqfrVQAVQPTLILQDGDV 154
Cdd:cd16290    65 LNSHAHFDHAGGIAALQRdsgatVAASPAGAAALRSGGVDPD-----------DPQAGAADP---FPPVAKVRVVADGEV 130

                          90       100
                  ....*....|....*....|.
gi 1519312219 155 INLGDRQLTVMHMPGHSRGSI 175
Cdd:cd16290   131 VKLGPLAVTAHATPGHTPGGT 151
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 42-231 2.20e-06

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


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 47.65  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  42 VVIDTGLG------LRSLPEYLYssGLLQDREAKEDAARrpLLAVA------------THVHFDHSGGLYQF--DRVAVH 101
Cdd:cd07730    36 ILFDLGYRkdfeeyTPRVPERLY--RTPVPLEVEEDVAE--QLAAGgidpedidavilSHLHWDHIGGLSDFpnARLIVG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 102 HAEAEALARGDnfetvtwlsdseVVRTPSPGWRARQFRVQAVQPTLILQDGDVIN--------LGDRQLTVMHMPGHSRG 173
Cdd:cd07730   112 PGAKEALRPPG------------YPSGFLPELLPSDFEGRLVRWEEDDFLWVPLGpfpraldlFGDGSLYLVDLPGHAPG 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519312219 174 SICL---HDKDRKILFSGDVVYDGS----------LIDWLPYSRISDYVGTCERLIELVDRGLVEkVLPGH 231
Cdd:cd07730   180 HLGLlarTTSGTWVFLAGDACHHRIgllrpspllpLPDLDDGADREAARETLARLRELDAAPDVR-VVLAH 249
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 34-196 6.13e-06

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: 46.35  E-value: 6.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  34 LVRGSEQDVVIDTGLglrslPEYlySSGLLQDREAKEDAARRPLLAVATHVHFDHSGGLYQFDR-----VAVHHAEAEAL 108
Cdd:cd16289    26 LVKTPDGAVLLDGGM-----PQA--ADMLLDNMRALGVAPGDLKLILHSHAHADHAGPLAALKRatgarVAANAESAVLL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 109 ARGDNFETvtwLSDSEVVRTPspgwrarqfrvqaVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKILFSG 188
Cdd:cd16289    99 ARGGSDDI---HFGDGITFPP-------------VQADRIVMDGEVVTLGGVTFTAHFTPGHTPGSTSWTWTDTRDGKPV 162


                  ....*...
gi 1519312219 189 DVVYDGSL 196
Cdd:cd16289   163 RIAYADSL 170
NorV COG0426
Flavorubredoxin [Energy production and conversion];
138-231 6.96e-06

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 46.75  E-value: 6.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 138 FRVQAVQptlilqDGDVINLGDRQLTV--MHMPgHSRGSICLHDKDRKILFSGDV---------VYDGSLID-------- 198
Cdd:COG0426   118 FRFIVVK------EGDTLDLGGHTLQFipAPML-HWPDTMFTYDPEDKILFSGDAfgshgasdeLFDDEVDEhleeearr 190

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1519312219 199 -----WLPYSRIsdyvgtCERLIELVdRGL-VEKVLPGH 231
Cdd:COG0426   191 yyaniMMPFSKQ------VLKALKKV-RGLdIDMIAPSH 222
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 80-174 6.97e-06

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: 46.19  E-value: 6.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  80 VATHVHFDHSGGLYQFDRVAVHHAEAEALARgdnfetvtwlsdsEVVRTPSPGWRARQFRV----QAVQPTLILQDGDVI 155
Cdd:cd16315    65 LSSHEHFDHVGGLAALQRATGARVAASAAAA-------------PVLESGKPAPDDPQAGLhepfPPVRVDRIVEDGDTV 131

                          90
                  ....*....|....*....
gi 1519312219 156 NLGDRQLTVMHMPGHSRGS 174
Cdd:cd16315   132 ALGSLRLTAHATPGHTPGA 150
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 80-175 1.54e-05

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: 45.24  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  80 VATHVHFDHSGGLYQFDRVAvhhaEAEALARGDNfetvtwlsdSEVVRTPSPGWRARQF----------RVQAVQptlil 149
Cdd:cd16313    65 LSSHDHWDHAGGIAALQKLT----GAQVLASPAT---------VAVLRSGSMGKDDPQFggltpmppvaSVRAVR----- 126

                          90       100
                  ....*....|....*....|....*.
gi 1519312219 150 qDGDVINLGDRQLTVMHMPGHSRGSI 175
Cdd:cd16313   127 -DGEVVKLGPLAVTAHATPGHTTGGT 151
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 80-205 1.56e-05

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 44.50  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  80 VATHVHFDHSGGLYQFD----RVAVHHAEAEALARgdnfetvtwlsdsevvrTPSPgwrarqfrvQAVQPTLILQDGDVI 155
Cdd:cd16276    50 VYSHNHADHIGGASIFKdegaTIIAHEATAELLKR-----------------NPDP---------KRPVPTVTFDDEYTL 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1519312219 156 NLGDRQLTVM-HMPGHSRGSICLHDKDRKILFSGDVVYdgslIDWLPYSRI 205
Cdd:cd16276   104 EVGGQTLELSyFGPNHGPGNIVIYLPKQKVLMAVDLIN----PGWVPFFNF 150
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 42-221 2.44e-05

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


Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 44.54  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  42 VVIDTGLGL--------RSLPEYLYSSGLLQDREakeDAARRPLLA-----------VATHVHFDHSGGLYQFDRVAVHH 102
Cdd:cd07742    31 VLVDTGFGLadvadpkrRLGGPFRRLLRPRLDED---ETAVRQIEAlgfdpsdvrhiVLTHLDLDHAGGLADFPHATVHV 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 103 AEAE---ALARGDNFE----TVTWLSDSEVVRTPSPGwRARQFRVQAVQPTLILQDGdvinlgdrqLTVMHMPGHSRG-- 173
Cdd:cd07742   108 HAAEldaATSPRTRYErrryRPQQLAHGPWWVTYAAG-GERWFGFEAVRPLDGLPPE---------ILLVPLPGHTRGhc 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519312219 174 SICLHDKDRKILFSGDVVYDGSLID--------WLPYSRISD-----YVGTCERLIELVDR 221
Cdd:cd07742   178 GVAVRTGDRWLLHAGDAYFHHGELDplppppppLRLFQRLLAvdrsaRLANLARLRELARD 238
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 32-189 2.50e-05

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 44.46  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  32 IWLVRGSEQDVVIDTG------LGLRSLPEYLYSSGLlqdreakedaaRRPLLAVATHVHFDHSGGLyqfdrvavhhaea 105
Cdd:COG2333    14 ILIRTPDGKTILIDTGprpsfdAGERVVLPYLRALGI-----------RRLDLLVLTHPDADHIGGL------------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 106 EALARgdNFEtVTWLSDSEVVRTPSPGWRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHmPGHSR--------GSICL 177
Cdd:COG2333    70 AAVLE--AFP-VGRVLVSGPPDTSETYERLLEALKEKGIPVRPCRAGDTWQLGGVRFEVLW-PPEDLlegsdennNSLVL 145

                         170
                  ....*....|....
gi 1519312219 178 H--DKDRKILFSGD 189
Cdd:COG2333   146 RltYGGFSFLLTGD 159
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 82-203 4.45e-05

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: 43.82  E-value: 4.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  82 THVHFDHSGGLyqfdrvavhhaeaEALARGDNFETVTWLSDSEVVRTPSPGWRARQFR------VQAVQPTLILQDGDVI 155
Cdd:cd16312    67 SHAHWDHAGGI-------------AALQKASGATVAASAHGAQVLQSGTNGKDDPQYQakpvvhVAKVAKVKEVGEGDTL 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1519312219 156 NLGDRQLTVMHMPGHSRGSI------ClhdKDRKILfsgDVVYDGSLIdwlPYS 203
Cdd:cd16312   134 KVGPLRLTAHMTPGHTPGGTtwtwtsC---EGQRCL---DVVYADSLN---PYS 178
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 34-189 1.67e-04

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: 41.35  E-value: 1.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  34 LVRGSEQDVVIDTG----LGLRSLPEYLYSSGLlqdreakedaaRRPLLAVATHVHFDHSGGLyqfdrvavhhaeAEALa 109
Cdd:cd07731    14 LIQTPGKTILIDTGprdsFGEDVVVPYLKARGI-----------KKLDYLILTHPDADHIGGL------------DAVL- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 110 rgDNFEtVTWLSDSEVVRTPSPGWRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHmPGHSRG------SICLH--DKD 181
Cdd:cd07731    70 --KNFP-VKEVYMPGVTHTTKTYEDLLDAIKEKGIPVTPCKAGDRWQLGGVSFEVLS-PPKDDYddlnnnSCVLRltYGG 145


                  ....*...
gi 1519312219 182 RKILFSGD 189
Cdd:cd07731   146 TSFLLTGD 153
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 34-276 1.78e-04

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: 41.90  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  34 LVRGSEQDVVIDTGLGlRSLPEYLYSSGLLQDReaKEDAArrplLAVATHVHFDHSGGLYQFDR-----VAVHHAEAEAL 108
Cdd:cd16311    26 LVTSPQGHVLVDGGLP-ESAPKIIANIEALGFR--IEDVK----LILNSHGHIDHAGGLAELQRrsgalVAASPSAALDL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 109 ARGDnfetvtwlsdsevVRTPSPGWRARQfRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSI-----------CL 177
Cdd:cd16311    99 ASGE-------------VGPDDPQYHALP-KYPPVKDMRLARDGGQFNVGPVSLTAHATPGHTPGGLswtwqscdgprCL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 178 hdkdrkilfsgDVVYDGSLI----DWLPYSRISDY---VGTCERLIELVDRGLVEKVLPGHFNtfgAERLF-RLASNyiS 249
Cdd:cd16311   165 -----------NMVYADSQNavsrPGFKFSASSEYpnaVADLRRSFETLEKLPCDVLISAHPE---ASQLWeRLEAS--D 228

                         250       260
                  ....*....|....*....|....*..
gi 1519312219 250 KAGICHKVSTFAMRSLASLALRVTNSR 276
Cdd:cd16311   229 RSARPALVDREACRRYASRAREALEKR 255
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 34-190 2.76e-04

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: 41.48  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  34 LVRGSEQDVVIDTGLGLRSLPEYLYSS-GLLQDREAKEDAARRPL------LAVATHVHFDHSGGLYQFD---RV----- 98
Cdd:cd07728    47 LIQYQGKNYLIDAGIGNGKLTEKQKRNfGVTEESSIEESLAELGLtpedidYVLMTHLHFDHASGLTKVKgeqLVsvfpn 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  99 AVHHAEAealargdnfetVTWlsdsEVVRTPS---------PGWRARQFRVQAVQPTLILQDGdvinlgdrqLTVMHMPG 169
Cdd:cd07728   127 ATIYVSE-----------IEW----EEMRNPNirskntywkENWEPIEDQVKTFSDEIEIVPG---------ITMIHTGG 182

                         170       180
                  ....*....|....*....|...
gi 1519312219 170 HSRGS--ICLHDKDRKILFSGDV 190
Cdd:cd07728   183 HSDGHsiIEIEQGGETAIHMADL 205
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 147-236 3.12e-04

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 41.75  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 147 LILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKILFSGDVVYD---GSLIDWLPYSRISdyvgTCERLIELVDRgl 223
Cdd:PLN02398  164 IVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSlscGKLFEGTPEQMLS----SLQKIISLPDD-- 237

                          90
                  ....*....|...
gi 1519312219 224 vEKVLPGHFNTFG 236
Cdd:PLN02398  238 -TNIYCGHEYTLS 249
ODP pfam19583
ODP family beta lactamase; The ODP (Oxygen-binding Di-iron Protein) domain is a distinct ...
 152-190 7.59e-04

ODP family beta lactamase; The ODP (Oxygen-binding Di-iron Protein) domain is a distinct member of the metallo-beta-lactamase superfamily recruited to various bacterial and archaeal signal transduction pathways, including chemotaxis, to function as oxygen and iron sensors (1). ODP was shown to act as a sensor for chemotactic responses to both iron and oxygen in the human pathogen Treponema denticola (Td). The ODP di-iron site binds oxygen at high affinity to reversibly form an unusually stable peroxo adduct.


Pssm-ID: 437415  Cd Length: 194  Bit Score: 39.77  E-value: 7.59e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1519312219 152 GDVINLGD-RQLTVMHMP-GHSRGSICLHDKDRKILFSGDV 190
Cdd:pfam19583  96 GGRITLGSgRRLEFIPAHfLHSPGNFVTYDPVSKILFSGDI 136
SPM-1-like_MBL-B1-B2-like cd16286
Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; ...
 10-240 1.16e-03

Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; MBL-fold metallo-hydrolase domain; SPM-1 was first identified in a Pseudomonas aeruginosa strain from a paediatric leukaemia patient and is a major clinical problem. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs are most closely related to each other. SPM-1 appears to be a hybrid B1/B2 MBL.


Pssm-ID: 293844 [Multi-domain]  Cd Length: 236  Bit Score: 39.44  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  10 KSLGDGIFWIQERFYESGNranIWLVRGSEQDVVI----DTGLGLRSLPEYLyssgllqdreAKEDAARRpLLAVATHVH 85
Cdd:cd16286    10 REIDPDVFVITHRDPWSSN---VLVVKMLDGTVVIvdspYTNLATQTVLDWI----------AKTMGPRK-VVAINTHFH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  86 FDHSGG----------LYQFDRVAVHHAEAealARGDNFETVTWLSDSEVVRtpspgwraRQFRVQAVQPTLILQ--DGD 153
Cdd:cd16286    76 LDGTGGnealkkrgipTWGSDLTKQLLLER---GKADRIKAAEFLKNEDLKR--------RIESSPPVPPDNVFDlkEGK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 154 VINLGDRQLTVmHMPG--HSRGSICLHDKDRKILFSGDVVYDGSLIDWLPYSRISDYVGTCERLIELVDRglveKVLPGH 231
Cdd:cd16286   145 VFSFGNELVEV-SFPGpaHAPDNVVVYFPERKILFGGCMIKPGKELGNLGDANMKAWPDSVRRLKKFDAK----IVIPGH 219


                  ....*....
gi 1519312219 232 FNTFGAERL 240
Cdd:cd16286   220 GERGDPGMV 228
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 30-191 4.36e-03

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


Pssm-ID: 293839  Cd Length: 252  Bit Score: 37.86  E-value: 4.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219  30 ANIWLVRGSEQDVVIDTGLGLRSLPEYLYSSGLLQDREAKEDAARRPLLA------VATHVHFDHSGGLYQFDrvavhha 103
Cdd:cd16281    43 MRCLLIETGGRNILIDTGIGDKQDPKFRSIYVQHSEHSLLKSLARLGLSPeditdvILTHLHFDHCGGATRAD------- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519312219 104 eaealarGDNFETVT------WLSDS--EVVRTPSPGWRARQFR--VQAVQPT--LILQDGDVINLGDR-QLTVMHmpGH 170
Cdd:cd16281   116 -------DDGLVELLfpnatyWVQKRhwEWALNPNPRERASFLPenIEPLEESgrLKLIDGSDAELGPGiRFHLSD--GH 186

                         170       180
                  ....*....|....*....|...
gi 1519312219 171 SRGSIC--LHDKDRKILFSGDVV 191
Cdd:cd16281   187 TPGQMLpeISTPGGTVVFAADLI 209
 
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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