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Conserved domains on  [gi|76677920|ref|NP_082648|]
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acyl-coenzyme A thioesterase MBLAC2 [Mus musculus]

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 4.75e-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: 262.18  E-value: 4.75e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  22 RFYESGNRANIWLVRGSEQDVVIDTGLGLRSLPEYLYSSGLLqdcgskedagrrPLLAVATHVHFDHSGGLYQFDQVAVH 101
Cdd:cd07712   1 LFIEEDDRVNIYLLRGRDRALLIDTGLGIGDLKEYVRTLTDL------------PLLVVATHGHFDHIGGLHEFEEVYVH 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920 102 RAEAEALARGDNFETVTWlsdsevvrapspgwRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKD 181
Cdd:cd07712  69 PADAEILAAPDNFETLTW--------------DAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRA 134

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 76677920 182 RKVLFSGDVVYDGSLIDWLPYSRISDYVGTCERLIELVDrgLVEKVLPGH 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 4.75e-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: 262.18  E-value: 4.75e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  22 RFYESGNRANIWLVRGSEQDVVIDTGLGLRSLPEYLYSSGLLqdcgskedagrrPLLAVATHVHFDHSGGLYQFDQVAVH 101
Cdd:cd07712   1 LFIEEDDRVNIYLLRGRDRALLIDTGLGIGDLKEYVRTLTDL------------PLLVVATHGHFDHIGGLHEFEEVYVH 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920 102 RAEAEALARGDNFETVTWlsdsevvrapspgwRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKD 181
Cdd:cd07712  69 PADAEILAAPDNFETLTW--------------DAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRA 134

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 76677920 182 RKVLFSGDVVYDGSLIDWLPYSRISDYVGTCERLIELVDrgLVEKVLPGH 231
Cdd:cd07712 135 NRLLFSGDVVYDGPLIMDLPHSDLDDYLASLEKLSKLPD--EFDKVLPGH 182
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 16-244 3.60e-41

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: 141.37  E-value: 3.60e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  16 IFWIQERFYESGNRANIWLVRGSEQDVVIDTGLGLRSLPEYLyssGLLqdcgskEDAGRRPLLAVATHVHFDHSGGLYQF 95
Cdd:COG0491   1 VYVLPGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEALL---AAL------AALGLDIKAVLLTHLHPDHVGGLAAL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  96 DQ-----VAVHRAEAEALARGDnfetvtwlsdsevvrapspgwRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGH 170
Cdd:COG0491  72 AEafgapVYAHAAEAEALEAPA---------------------AGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGH 130

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76677920 171 SRGSICLHDKDRKVLFSGDVVYDGSL-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 3.17e-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: 103.79  E-value: 3.17e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920     31 NIWLVRGSEQDVVIDTGLGlrslpeylYSSGLLqdcGSKEDAGRRPLLAV-ATHVHFDHSGGLYQF-----DQVAVHRAE 104
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPG--------EAEDLL---AELKKLGPKKIDAIiLTHGHPDHIGGLPELleapgAPVYAPEGT 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920    105 AEALargdnfetvtwlsdsevvRAPSPGWRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKV 184
Cdd:smart00849  70 AELL------------------KDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKI 131

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 76677920    185 LFSGDVVYDGSLIDWL-PYSRISDYVGTcERLIELVDRgLVEKVLPGH 231
Cdd:smart00849 132 LFTGDLLFAGGDGRTLvDGGDAAASDAL-ESLLKLLKL-LPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
31-231 2.40e-22

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 91.66  E-value: 2.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920    31 NIWLVRGSEQDVVIDTGLGLrslpeylySSGLLQDCGSKEDAGRRPLLAVATHVHFDHSGGLYQFDQVAVHRAEAEALar 110
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSA--------EAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAE-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920   111 gdnfETVTWLSDSEVVRAPSPGWRARQFRVQAVQPTLIlqDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKVLFSGDV 190
Cdd:pfam00753  77 ----EARELLDEELGLAASRLGLPGPPVVPLPPDVVLE--EGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 76677920   191 VYDGSLIDW-----LPYSRISDYVGTCERLIELVDRGLVEKVLPGH 231
Cdd:pfam00753 151 LFAGEIGRLdlplgGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 82-236 2.04e-04

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 42.14  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920   82 THVHFDHSGGLYQFDQvavhRAEAEALArgdnfetvtwlsdSEVVRAPSPGWrarqfrvqavqpTLILQDGDVINLGDRQ 161
Cdd:PLN02398 128 THHHYDHTGGNLELKA----RYGAKVIG-------------SAVDKDRIPGI------------DIVLKDGDKWMFAGHE 178

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 76677920  162 LTVMHMPGHSRGSICLHDKDRKVLFSGDVVYD---GSLIDWLPYSRISdyvgTCERLIELVDRglvEKVLPGHFNTFG 236
Cdd:PLN02398 179 VLVMETPGHTRGHISFYFPGSGAIFTGDTLFSlscGKLFEGTPEQMLS----SLQKIISLPDD---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 4.75e-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: 262.18  E-value: 4.75e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  22 RFYESGNRANIWLVRGSEQDVVIDTGLGLRSLPEYLYSSGLLqdcgskedagrrPLLAVATHVHFDHSGGLYQFDQVAVH 101
Cdd:cd07712   1 LFIEEDDRVNIYLLRGRDRALLIDTGLGIGDLKEYVRTLTDL------------PLLVVATHGHFDHIGGLHEFEEVYVH 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920 102 RAEAEALARGDNFETVTWlsdsevvrapspgwRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKD 181
Cdd:cd07712  69 PADAEILAAPDNFETLTW--------------DAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRA 134

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 76677920 182 RKVLFSGDVVYDGSLIDWLPYSRISDYVGTCERLIELVDrgLVEKVLPGH 231
Cdd:cd07712 135 NRLLFSGDVVYDGPLIMDLPHSDLDDYLASLEKLSKLPD--EFDKVLPGH 182
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 16-244 3.60e-41

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: 141.37  E-value: 3.60e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  16 IFWIQERFYESGNRANIWLVRGSEQDVVIDTGLGLRSLPEYLyssGLLqdcgskEDAGRRPLLAVATHVHFDHSGGLYQF 95
Cdd:COG0491   1 VYVLPGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEALL---AAL------AALGLDIKAVLLTHLHPDHVGGLAAL 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  96 DQ-----VAVHRAEAEALARGDnfetvtwlsdsevvrapspgwRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGH 170
Cdd:COG0491  72 AEafgapVYAHAAEAEALEAPA---------------------AGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGH 130

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 76677920 171 SRGSICLHDKDRKVLFSGDVVYDGSL-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 4.05e-32

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: 117.00  E-value: 4.05e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  30 ANIWLVRGSEQD-VVIDTGLGlrslpeylYSSGLLQDCgskEDAGRRPLLAVATHVHFDHSGGLYQFDQ-----VAVHRA 103
Cdd:cd06262  10 TNCYLVSDEEGEaILIDPGAG--------ALEKILEAI---EELGLKIKAILLTHGHFDHIGGLAELKEapgapVYIHEA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920 104 EAEALARGDNFetvtwlsdsevvrapspGWRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRK 183
Cdd:cd06262  79 DAELLEDPELN-----------------LAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEG 141

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 76677920 184 VLFSGDVVYDGSLIDW-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 5.39e-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: 106.88  E-value: 5.39e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  25 ESGNRANIWLVRGSEQDVVIDTGLGlrslpeYLYSSGLLQDcgSKEDAGRRPLLAVATHVHFDHSGGLYQFDQVAV---- 100
Cdd:cd16282  10 GGGFISNIGFIVGDDGVVVIDTGAS------PRLARALLAA--IRKVTDKPVRYVVNTHYHGDHTLGNAAFADAGApiia 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920 101 HRAEAEALARGdnfETVTWLSDSEVVRAPSPGwrarqfrVQAVQPTLILQDGDVINLGDRQLTVMHM-PGHSRGSICLHD 179
Cdd:cd16282  82 HENTREELAAR---GEAYLELMRRLGGDAMAG-------TELVLPDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWL 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 76677920 180 KDRKVLFSGDVVYDGsLIDWLPYSRISDYVGTCERLIELVDrglvEKVLPGH 231
Cdd:cd16282 152 PEEGVLFAGDLVFNG-RIPFLPDGSLAGWIAALDRLLALDA----TVVVPGH 198
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 31-231 3.17e-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: 103.79  E-value: 3.17e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920     31 NIWLVRGSEQDVVIDTGLGlrslpeylYSSGLLqdcGSKEDAGRRPLLAV-ATHVHFDHSGGLYQF-----DQVAVHRAE 104
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPG--------EAEDLL---AELKKLGPKKIDAIiLTHGHPDHIGGLPELleapgAPVYAPEGT 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920    105 AEALargdnfetvtwlsdsevvRAPSPGWRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKV 184
Cdd:smart00849  70 AELL------------------KDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKI 131

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 76677920    185 LFSGDVVYDGSLIDWL-PYSRISDYVGTcERLIELVDRgLVEKVLPGH 231
Cdd:smart00849 132 LFTGDLLFAGGDGRTLvDGGDAAASDAL-ESLLKLLKL-LPKLVVPGH 177
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 15-231 8.04e-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: 95.37  E-value: 8.04e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  15 GIFWIqerfyESGNRANIWLVRGSEQDVVIDTGlglrslpeYLYSSGLLQDCGSKEDAGRRPLLAVA-THVHFDHSGGLY 93
Cdd:cd07721   1 GVYQL-----PLLPPVNAYLIEDDDGLTLIDTG--------LPGSAKRILKALRELGLSPKDIRRILlTHGHIDHIGSLA 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  94 QFDQ-----VAVHRAEAEALARGDNFETVTWLSDSEVVRAPSPgwrarqfrVQAVQPTLILQDGDVINLGDRqLTVMHMP 168
Cdd:cd07721  68 ALKEapgapVYAHEREAPYLEGEKPYPPPVRLGLLGLLSPLLP--------VKPVPVDRTLEDGDTLDLAGG-LRVIHTP 138

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 76677920 169 GHSRGSICLHDKDRKVLFSGDVV--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 9.00e-23

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: 92.80  E-value: 9.00e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  31 NIWLVR--GSEQDVVIDTGLGlrslpeylySSGLLQDCGskeDAGRRPLLAVATHVHFDHSGGLyqfdqvavhraeaEAL 108
Cdd:cd16322  12 NTYLVAdeGGGEAVLVDPGDE---------SEKLLARFG---TTGLTLLYILLTHAHFDHVGGV-------------ADL 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920 109 ARGDNFETVTWLSDSEVVRAPSPGWRARQFRVQ-AVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKVLFS 187
Cdd:cd16322  67 RRHPGAPVYLHPDDLPLYEAADLGAKAFGLGIEpLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFS 146

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 76677920 188 GDVVYDGSL--IDwLPYSRISDYVGTCERLIELVDRglvEKVLPGHF--NTFGAERLF 241
Cdd:cd16322 147 GDLLFQGSIgrTD-LPGGDPKAMAASLRRLLTLPDE---TRVFPGHGppTTLGEERRT 200
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
31-231 2.40e-22

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 91.66  E-value: 2.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920    31 NIWLVRGSEQDVVIDTGLGLrslpeylySSGLLQDCGSKEDAGRRPLLAVATHVHFDHSGGLYQFDQVAVHRAEAEALar 110
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSA--------EAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAE-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920   111 gdnfETVTWLSDSEVVRAPSPGWRARQFRVQAVQPTLIlqDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKVLFSGDV 190
Cdd:pfam00753  77 ----EARELLDEELGLAASRLGLPGPPVVPLPPDVVLE--EGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 76677920   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 1.23e-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: 89.28  E-value: 1.23e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  28 NRANIWLVRGSEQDVVIDTGLGLRSLPEYLYSSglLQDCGSKEDAGRRPLLavaTHVHFDHSGGLYQFdqvavhRAEAEA 107
Cdd:cd07725  13 GHVNVYLLRDGDETTLIDTGLATEEDAEALWEG--LKELGLKPSDIDRVLL---THHHPDHIGLAGKL------QEKSGA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920 108 LARGDNFETVTwlsdsevvrapspgwrarqfrvqavqptlilqDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKVLFS 187
Cdd:cd07725  82 TVYILDVTPVK--------------------------------DGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFV 129

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 76677920 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 5.14e-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: 87.55  E-value: 5.14e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  31 NIWLVRGSEQDVVIDTGlglRSLPEYLyssgllqDCGSKEDAGRRPLLAVATHVHFDHSGGlyqfdqvavhraeAEALAR 110
Cdd:cd16278  19 NTYLLGAPDGVVVIDPG---PDDPAHL-------DALLAALGGGRVSAILVTHTHRDHSPG-------------AARLAE 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920 111 gdnfETvtwlsdSEVVRAPSPGWRARQFRvqAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKVLFSGDV 190
Cdd:cd16278  76 ----RT------GAPVRAFGPHRAGGQDT--DFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDH 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 76677920 191 VYDGS--LIDWlPYSRISDYVGTCERLIELVDRglveKVLPGH 231
Cdd:cd16278 144 VMGWSttVIAP-PDGDLGDYLASLERLLALDDR----LLLPGH 181
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 15-218 1.53e-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: 81.77  E-value: 1.53e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  15 GIFWIQERFYESGNRANIWLVRGSEQDVVIDTGLGLrSLPEYLyssGLLQDCGSKEDAGRRPLLavaTHVHFDHSGGLYQ 94
Cdd:cd07726   1 GIYLIDLGFLGFPGRIASYLLDGEGRPALIDTGPSS-SVPRLL---AALEALGIAPEDVDYIIL---THIHLDHAGGAGL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  95 FDQ------VAVHRAEAEALAR------------GDNFETVTWlsdsEVVRAPSPgwrarqfRVQAvqptliLQDGDVIN 156
Cdd:cd07726  74 LAEalpnakVYVHPRGARHLIDpsklwasaravyGDEADRLGG----EILPVPEE-------RVIV------LEDGETLD 136

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 76677920 157 LGDRQLTVMHMPGHSRGSICLHDKDRKVLFSGDVVydGSLIDWLPYSR----------ISDYVGTCERLIEL 218
Cdd:cd07726 137 LGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDAA--GVRYPELDVVGppstpppdfdPEAWLESLDRLLSL 206
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 33-231 2.30e-17

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: 78.80  E-value: 2.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  33 WLVRGSEQDVVIDTGLGlrslPEYLYSSGLLQDCGSKEDAGRRPLLA---------------VATHVHFDHSGGLYQFDQ 97
Cdd:cd07729  35 YLIEHPEGTILVDTGFH----PDAADDPGGLELAFPPGVTEEQTLEEqlarlgldpedidyvILSHLHFDHAGGLDLFPN 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  98 --VAVHRAEAEALARGDNFEtvtwlsdsevvRAPSPGWRARQFRVQAVQPTLIlqDGDVINLGDrqLTVMHMPGHSRGSI 175
Cdd:cd07729 111 atIIVQRAELEYATGPDPLA-----------AGYYEDVLALDDDLPGGRVRLV--DGDYDLFPG--VTLIPTPGHTPGHQ 175

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 76677920 176 CL--HDKDRKVLFSGDVVY-----DGSLIDWLPYSRIsDYVGTCERLIELVDRgLVEKVLPGH 231
Cdd:cd07729 176 SVlvRLPEGTVLLAGDAAYtyenlEEGRPPGINYDPE-AALASLERLKALAER-EGARVIPGH 236
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 82-189 7.10e-15

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: 70.57  E-value: 7.10e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  82 THVHFDHSGGlyqfdqvavhraeaealargdNFETVTWLSDSEVVrAPSPGwrarqfRVQAVqpTLILQDGDVINLGDRQ 161
Cdd:cd07723  50 THHHWDHTGG---------------------NAELKALFPDAPVY-GPAED------RIPGL--DHPVKDGDEIKLGGLE 99

                        90       100
                ....*....|....*....|....*...
gi 76677920 162 LTVMHMPGHSRGSICLHDKDRKVLFSGD 189
Cdd:cd07723 100 VKVLHTPGHTLGHICYYVPDEPALFTGD 127
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 82-195 2.18e-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: 69.89  E-value: 2.18e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  82 THVHFDHSGG------LYQFDQVAVHRAeaealargDNFetvtWLSDSEVvrapspgwRARQF---RVQAVQPTLILQDG 152
Cdd:cd07737  53 THGHLDHVGGaaelaeHYGVPIIGPHKE--------DKF----LLENLPE--------QSQMFgfpPAEAFTPDRWLEEG 112

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 76677920 153 DVINLGDRQLTVMHMPGHSRGSICLHDKDRKVLFSGDVVYDGS 195
Cdd:cd07737 113 DTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGS 155
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 2.59e-13

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: 68.12  E-value: 2.59e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  82 THVHFDHSGGLYQFDQ-----VAVHRAEAEALARGDNfetvtwlSDsevvrapsPGWRARQFRVQAVQPTLILQDGDVIN 156
Cdd:cd16288  67 SHAHLDHAGGLAALKKltgakLMASAEDAALLASGGK-------SD--------FHYGDDSLAFPPVKVDRVLKDGDRVT 131

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 76677920 157 LGDRQLTVMHMPGHSRGS------ICLHDKDRKVLF--SGDVVYDGSLIDWLPYSRIS-DYVGTCERL 215
Cdd:cd16288 132 LGGTTLTAHLTPGHTRGCttwtmtVKDDGKVYQVVFadSLTVNPGYKLVGNPTYPGIAeDYRHSFATL 199
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 31-192 4.25e-12

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: 64.49  E-value: 4.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  31 NIWLVRGSEQDVVIDTGLGLRSLPeylySSGLLQDcgSKEDAGRRP------LLavaTHVHFDHSGGLYQFD-------- 96
Cdd:cd07720  50 NAFLVRTGGRLILVDTGAGGLFGP----TAGKLLA--NLAAAGIDPediddvLL---THLHPDHIGGLVDAGgkpvfpna 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  97 QVAVHRAEAEAlargdnfetvtWLSDSEVVRAPSpgwRARQF------RVQAVQPTLILQDGDVINLGdrqLTVMHMPGH 170
Cdd:cd07720 121 EVHVSEAEWDF-----------WLDDANAAKAPE---GAKRFfdaardRLRPYAAAGRFEDGDEVLPG---ITAVPAPGH 183

                       170       180
                ....*....|....*....|....
gi 76677920 171 SRG--SICLHDKDRKVLFSGDVVY 192
Cdd:cd07720 184 TPGhtGYRIESGGERLLIWGDIVH 207
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 82-231 6.75e-11

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: 59.86  E-value: 6.75e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  82 THVHFDHSGG----LYQFD-QVAVHRAEAEALargdnfetvtwlsdsevvrapspgwrarQFRVQAVQPtliLQDGDVIN 156
Cdd:cd16275  54 THSHFDHVNLveplLAKYDaPVYMSKEEIDYY----------------------------GFRCPNLIP---LEDGDTIK 102

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 76677920 157 LGDRQLTVMHMPGHSRGSICLHDKDRkvLFSGDVVYDGS--LIDwLPYSRISDYVGTCERLIELVDRGLVekVLPGH 231
Cdd:cd16275 103 IGDTEITCLLTPGHTPGSMCYLLGDS--LFTGDTLFIEGcgRCD-LPGGDPEEMYESLQRLKKLPPPNTR--VYPGH 174
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 147-231 2.24e-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: 58.36  E-value: 2.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920 147 LILQDGDVINLGDrQLTVMHMPGHSRGSICLHDKDRKVLFSGDVVYDGSLIDWLPYSR------ISDYVGTCERLIELVd 220
Cdd:cd07727  90 IVLWGGDPWELDP-DLTLIPVPGHTRGSVVLLYKEKGVLFTGDHLAWSRRRGWLSAFRyvcwysWPEQAESVERLADLD- 167

                        90
                ....*....|.
gi 76677920 221 rglVEKVLPGH 231
Cdd:cd07727 168 ---FEWVLPGH 175
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 23-231 2.56e-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) 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: 58.70  E-value: 2.56e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  23 FYESGnRANIWLVRGSEQDV-VIDTGLG---LRSLPEYLyssgllqdcgskEDAGRRPLLAVATHVHFDHSGGLYQF--- 95
Cdd:cd07743   2 YYIPG-PTNIGVYVFGDKEAlLIDSGLDedaGRKIRKIL------------EELGWKLKAIINTHSHADHIGGNAYLqkk 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  96 --DQVAVHRAEAEALARGDNFETVTWLSdsevvrAPSPGWRARQFRVQAVQPTLILQDGDvINLGDRQLTVMHMPGHSRG 173
Cdd:cd07743  69 tgCKVYAPKIEKAFIENPLLEPSYLGGA------YPPKELRNKFLMAKPSKVDDIIEEGE-LELGGVGLEIIPLPGHSFG 141

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 76677920 174 SICLHDKDrKVLFSGDVVYDGSLID--WLPYSR-ISDYVGTCERLIELVdrglVEKVLPGH 231
Cdd:cd07743 142 QIGILTPD-GVLFAGDALFGEEVLEkyGIPFLYdVEEQLETLEKLEELD----ADYYVPGH 197
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 31-191 2.66e-10

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


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 58.31  E-value: 2.66e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  31 NIWLVRGSEQDVVIDTGLGLRSLPEYLYSsgLLQDCGSKE--DAgrrpllaVATHVHFDHSGGLyqfDQVavhraeaEAL 108
Cdd:cd07722  19 NTYLVGTGKRRILIDTGEGRPSYIPLLKS--VLDSEGNATisDI-------LLTHWHHDHVGGL---PDV-------LDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920 109 ARGDNFETVTWLSDSEVVRAPSPGwrarqfrvqavQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKVLFSG 188
Cdd:cd07722  80 LRGPSPRVYKFPRPEEDEDPDEDG-----------GDIHDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTG 148


                ...
gi 76677920 189 DVV 191
Cdd:cd07722 149 DCV 151
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 139-189 1.24e-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: 56.25  E-value: 1.24e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 76677920 139 RVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKVLFSGD 189
Cdd:cd07724  81 GAPASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGD 131
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 78-215 1.29e-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: 57.17  E-value: 1.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  78 LAVATHVHFDHSGGLYQFDQ-----VAVHRAEAEALARG----DNFE--TVTWLSDSEVVRApspgwrarqfrvqavqpt 146
Cdd:cd07708  63 LILISHAHFDHAGGSAEIKKqtgakVMAGAEDVSLLLSGgssdFHYAndSSTYFPQSTVDRA------------------ 124

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 76677920 147 liLQDGDVINLGDRQLTVMHMPGHSRGSI------CLHDKDRKVLF--SGDVVYDGSLIDWLPYSRI-SDYVGTCERL 215
Cdd:cd07708 125 --VHDGERVTLGGTVLTAHATPGHTPGCTtwtmtlKDHGKQYQVVFadSLTVNPGYRLVDNPTYPKIvEDYRHSFAVV 200
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 17-186 2.66e-09

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: 56.30  E-value: 2.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  17 FWIQERFYESGNRA-NIWLVRGSEQDVVIDTGL--GLRSLPEYLYSSGL-LQDCGskedagrrplLAVATHVHFDHSGGL 92
Cdd:cd16310   8 FRIVDNIYYVGTKGiGSYLITSNHGAILLDGGLeeNAALIEQNIKALGFkLSDIK----------IIINTHAHYDHAGGL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  93 YQFDQ-----VAVHRAEAEALARGdnfetvTWLSDSEVVRAPSPgwrarqfrvqAVQPTLILQDGDVINLGDRQLTVMHM 167
Cdd:cd16310  78 AQLKAdtgakLWASRGDRPALEAG------KHIGDNITQPAPFP----------AVKVDRILGDGEKIKLGDITLTATLT 141

                       170       180
                ....*....|....*....|....*
gi 76677920 168 PGHSRG------SICLHDKDRKVLF 186
Cdd:cd16310 142 PGHTKGcttwstTVKENGRPLRVVF 166
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 42-174 3.07e-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: 56.32  E-value: 3.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  42 VVIDTGLGlRSLPEYLYSsglLQDCGSK-EDAgrRPLLAvaTHVHFDHSGGLYQFDQ-----VAVHRAEAEALARGDNFE 115
Cdd:cd16308  34 ILINTGLA-ESVPLIKKN---IQALGFKfKDI--KILLT--TQAHYDHVGAMAAIKQqtgakMMVDEKDAKVLADGGKSD 105

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 76677920 116 TVtwLSDSEVVRAPspgwrarqfrvqaVQPTLILQDGDVINLGDRQLTVMHMPGHSRGS 174
Cdd:cd16308 106 YE--MGGYGSTFAP-------------VKADKLLHDGDTIKLGGTKLTLLHHPGHTKGS 149
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 82-245 2.69e-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: 2.69e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  82 THVHFDHSGGlyqfdqvavhraeAEALArgDNFETVTWLS--DSEVVRAPsPGWRARQFRVQAVQPTLILQDGDVINLGD 159
Cdd:cd16280  68 THGHGDHYGG-------------AAYLK--DLYGAKVVMSeaDWDMMEEP-PEEGDNPRWGPPPERDIVIKDGDTLTLGD 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920 160 RQLTVMHMPGHSRGSICL----HDKDRK---VLFSGdvvydGSLIDWLPYSRISDYVGTCERLIELVDRGLVEKVLPGH- 231
Cdd:cd16280 132 TTITVYLTPGHTPGTLSLifpvKDGGKThraGLWGG-----TGLNTGPNLERREQYIASLERFKKIAEEAGVDVFLSNHp 206

                       170
                ....*....|....
gi 76677920 232 FNTFGAERLFRLAS 245
Cdd:cd16280 207 FQDGSLEKREALRN 220
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 145-231 2.72e-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: 53.26  E-value: 2.72e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920 145 PTLILQDGDVINLGDRQLTVMHMPG-HSRGSICLHDKDRKVLFSGDV---------VYDGSLIDWLPYSR--ISDYVGT- 211
Cdd:cd07709 117 RFVVVKDGDTLDLGKHTLKFIPAPMlHWPDTMVTYDPEDKILFSGDAfgahgasgeLFDDEVEDYLEEARryYANIMGPf 196

                        90       100
                ....*....|....*....|....
gi 76677920 212 ---CERLIELVdRGL-VEKVLPGH 231
Cdd:cd07709 197 skqVRKALEKL-EALdIKMIAPSH 219
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 1.73e-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: 51.19  E-value: 1.73e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  80 VATHVHFDHSGGL--YQFD---QVAVHRAEAEALARGDNfetvtwlSDSEvvraPSPGWRARqfrVQAVQPTLILQDGDV 154
Cdd:cd16290  65 LNSHAHFDHAGGIaaLQRDsgaTVAASPAGAAALRSGGV-------DPDD----PQAGAADP---FPPVAKVRVVADGEV 130

                        90       100
                ....*....|....*....|.
gi 76677920 155 INLGDRQLTVMHMPGHSRGSI 175
Cdd:cd16290 131 VKLGPLAVTAHATPGHTPGGT 151
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 80-205 3.60e-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: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 49.51  E-value: 3.60e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  80 VATHVHFDHSGGLYQF-DQVAV---HRAEAEALARgdnfetvtwlsdsevvrAPSPgwrarqfrvQAVQPTLILQDGDVI 155
Cdd:cd16276  50 VYSHNHADHIGGASIFkDEGATiiaHEATAELLKR-----------------NPDP---------KRPVPTVTFDDEYTL 103

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 76677920 156 NLGDRQLTVM-HMPGHSRGSICLHDKDRKVLFSGDVVYdgslIDWLPYSRI 205
Cdd:cd16276 104 EVGGQTLELSyFGPNHGPGNIVIYLPKQKVLMAVDLIN----PGWVPFFNF 150
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 42-231 8.54e-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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 48.80  E-value: 8.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  42 VVIDTGLG------LRSLPEYLYSSGLLQDCG-----SKEDAGRRPL---LAVATHVHFDHSGGLYQFDQVA--VHRAEA 105
Cdd:cd07730  36 ILFDLGYRkdfeeyTPRVPERLYRTPVPLEVEedvaeQLAAGGIDPEdidAVILSHLHWDHIGGLSDFPNARliVGPGAK 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920 106 EALARGDnfetvtwlsdseVVRAPSPGWRARQFRVQAVQPTLILQDGDVIN--------LGDRQLTVMHMPGHSRGSICL 177
Cdd:cd07730 116 EALRPPG------------YPSGFLPELLPSDFEGRLVRWEEDDFLWVPLGpfpraldlFGDGSLYLVDLPGHAPGHLGL 183

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 76677920 178 H---DKDRKVLFSGDVVYDGS----------LIDWLPYSRISDYVGTCERLIELVDRGLVEkVLPGH 231
Cdd:cd07730 184 LartTSGTWVFLAGDACHHRIgllrpspllpLPDLDDGADREAARETLARLRELDAAPDVR-VVLAH 249
NorV COG0426
Flavorubredoxin [Energy production and conversion];
138-231 1.57e-05

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 45.59  E-value: 1.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920 138 FRVQAVQptlilqDGDVINLGDRQLTV--MHMPgHSRGSICLHDKDRKVLFSGDV---------VYDGSLID-------- 198
Cdd:COG0426 118 FRFIVVK------EGDTLDLGGHTLQFipAPML-HWPDTMFTYDPEDKILFSGDAfgshgasdeLFDDEVDEhleeearr 190

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 76677920 199 -----WLPYSRIsdyvgtCERLIELVdRGL-VEKVLPGH 231
Cdd:COG0426 191 yyaniMMPFSKQ------VLKALKKV-RGLdIDMIAPSH 222
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 34-196 3.72e-05

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: 44.04  E-value: 3.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  34 LVRGSEQDVVIDTGLglrslPEYlySSGLLQDCGSKEDAGRRPLLAVATHVHFDHSGGLYQFD-----QVAVHRAEAEAL 108
Cdd:cd16289  26 LVKTPDGAVLLDGGM-----PQA--ADMLLDNMRALGVAPGDLKLILHSHAHADHAGPLAALKratgaRVAANAESAVLL 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920 109 ARGDNFETvtwLSDSEVVRAPspgwrarqfrvqaVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKVLFSG 188
Cdd:cd16289  99 ARGGSDDI---HFGDGITFPP-------------VQADRIVMDGEVVTLGGVTFTAHFTPGHTPGSTSWTWTDTRDGKPV 162


                ....*...
gi 76677920 189 DVVYDGSL 196
Cdd:cd16289 163 RIAYADSL 170
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 82-203 4.33e-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: 4.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  82 THVHFDHSGGLyqfdqvavhraeaEALARGDNFETVTWLSDSEVVRAPSPGWRARQFR------VQAVQPTLILQDGDVI 155
Cdd:cd16312  67 SHAHWDHAGGI-------------AALQKASGATVAASAHGAQVLQSGTNGKDDPQYQakpvvhVAKVAKVKEVGEGDTL 133

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 76677920 156 NLGDRQLTVMHMPGHSRGSI------ClhdKDRKVLfsgDVVYDGSLIdwlPYS 203
Cdd:cd16312 134 KVGPLRLTAHMTPGHTPGGTtwtwtsC---EGQRCL---DVVYADSLN---PYS 178
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 80-231 4.59e-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: 43.70  E-value: 4.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  80 VATHVHFDHSGGLyqfdqvavhraeaEALARGDNFETVTWLSDSEVVRAPSPGWRARQF----------RVQAVQptlil 149
Cdd:cd16313  65 LSSHDHWDHAGGI-------------AALQKLTGAQVLASPATVAVLRSGSMGKDDPQFggltpmppvaSVRAVR----- 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920 150 qDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKVLFSGDVVYDGSLI----DWLPYSRISDYVGTCERLIELVDRGLVE 225
Cdd:cd16313 127 -DGEVVKLGPLAVTAHATPGHTTGGTSWTWQSCEQGRCANMVFADSLTavsaDGYRFSAHPAVLADVEQSIAAVEKLACD 205


                ....*.
gi 76677920 226 KVLPGH 231
Cdd:cd16313 206 ILVSAH 211
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 80-174 4.86e-05

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


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 43.49  E-value: 4.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  80 VATHVHFDHSGGLYQFDQVAVHRAEAEALARgdnfetvtwlsdsEVVRAPSPGWRARQFRV----QAVQPTLILQDGDVI 155
Cdd:cd16315  65 LSSHEHFDHVGGLAALQRATGARVAASAAAA-------------PVLESGKPAPDDPQAGLhepfPPVRVDRIVEDGDTV 131

                        90
                ....*....|....*....
gi 76677920 156 NLGDRQLTVMHMPGHSRGS 174
Cdd:cd16315 132 ALGSLRLTAHATPGHTPGA 150
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 32-189 5.07e-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: 43.69  E-value: 5.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  32 IWLVRGSEQDVVIDTG------LGLRSLPEYLYSSGLlqdcgskedagRRPLLAVATHVHFDHSGGLyqfdqvavhraea 105
Cdd:COG2333  14 ILIRTPDGKTILIDTGprpsfdAGERVVLPYLRALGI-----------RRLDLLVLTHPDADHIGGL------------- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920 106 EALARgdNFEtVTWLSDSEVVRAPSPGWRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHmPGHSR--------GSICL 177
Cdd:COG2333  70 AAVLE--AFP-VGRVLVSGPPDTSETYERLLEALKEKGIPVRPCRAGDTWQLGGVRFEVLW-PPEDLlegsdennNSLVL 145

                       170
                ....*....|....
gi 76677920 178 H--DKDRKVLFSGD 189
Cdd:COG2333 146 RltYGGFSFLLTGD 159
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 82-236 2.04e-04

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 42.14  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920   82 THVHFDHSGGLYQFDQvavhRAEAEALArgdnfetvtwlsdSEVVRAPSPGWrarqfrvqavqpTLILQDGDVINLGDRQ 161
Cdd:PLN02398 128 THHHYDHTGGNLELKA----RYGAKVIG-------------SAVDKDRIPGI------------DIVLKDGDKWMFAGHE 178

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 76677920  162 LTVMHMPGHSRGSICLHDKDRKVLFSGDVVYD---GSLIDWLPYSRISdyvgTCERLIELVDRglvEKVLPGHFNTFG 236
Cdd:PLN02398 179 VLVMETPGHTRGHISFYFPGSGAIFTGDTLFSlscGKLFEGTPEQMLS----SLQKIISLPDD---TNIYCGHEYTLS 249
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 34-189 2.49e-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: 40.97  E-value: 2.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  34 LVRGSEQDVVIDTG----LGLRSLPEYLYSSGllqdcgskedaGRRPLLAVATHVHFDHSGGLyqfdqvavhraeAEALa 109
Cdd:cd07731  14 LIQTPGKTILIDTGprdsFGEDVVVPYLKARG-----------IKKLDYLILTHPDADHIGGL------------DAVL- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920 110 rgDNFEtVTWLSDSEVVRAPSPGWRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHmPGHSRG------SICLH--DKD 181
Cdd:cd07731  70 --KNFP-VKEVYMPGVTHTTKTYEDLLDAIKEKGIPVTPCKAGDRWQLGGVSFEVLS-PPKDDYddlnnnSCVLRltYGG 145


                ....*...
gi 76677920 182 RKVLFSGD 189
Cdd:cd07731 146 TSFLLTGD 153
SPM-1-like_MBL-B1-B2-like cd16286
Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; ...
 10-240 2.51e-04

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: 41.36  E-value: 2.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  10 KSLGDGIFWIQERFYESGNranIWLVRGSEQDVVI----DTGLGLRSLPEYLyssgllqdcgsKEDAGRRPLLAVATHVH 85
Cdd:cd16286  10 REIDPDVFVITHRDPWSSN---VLVVKMLDGTVVIvdspYTNLATQTVLDWI-----------AKTMGPRKVVAINTHFH 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  86 FDHSGG----------LYQFDQVAVHRAEAealARGDNFETVTWLSDSEVVRapspgwraRQFRVQAVQPTLILQ--DGD 153
Cdd:cd16286  76 LDGTGGnealkkrgipTWGSDLTKQLLLER---GKADRIKAAEFLKNEDLKR--------RIESSPPVPPDNVFDlkEGK 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920 154 VINLGDRQLTVmHMPG--HSRGSICLHDKDRKVLFSGDVVYDGSLIDWLPYSRISDYVGTCERLIELVDRglveKVLPGH 231
Cdd:cd16286 145 VFSFGNELVEV-SFPGpaHAPDNVVVYFPERKILFGGCMIKPGKELGNLGDANMKAWPDSVRRLKKFDAK----IVIPGH 219


                ....*....
gi 76677920 232 FNTFGAERL 240
Cdd:cd16286 220 GERGDPGMV 228
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 80-221 2.75e-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) 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: 41.46  E-value: 2.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  80 VATHVHFDHSGGLYQFDQVAVHRAEAE---ALARGDNFE----TVTWLSDS-EVVRAPSPGWRARQFRvqAVQPTLILQD 151
Cdd:cd07742  85 VLTHLDLDHAGGLADFPHATVHVHAAEldaATSPRTRYErrryRPQQLAHGpWWVTYAAGGERWFGFE--AVRPLDGLPP 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920 152 GdvinlgdrqLTVMHMPGHSRG--SICLHDKDRKVLFSGDVVYDGSLID--------WLPYSRISD-----YVGTCERLI 216
Cdd:cd07742 163 E---------ILLVPLPGHTRGhcGVAVRTGDRWLLHAGDAYFHHGELDplppppppLRLFQRLLAvdrsaRLANLARLR 233


                ....*
gi 76677920 217 ELVDR 221
Cdd:cd07742 234 ELARD 238
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 28-191 3.97e-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: 293839  Cd Length: 252  Bit Score: 40.94  E-value: 3.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  28 NR----ANIWLVRGSEQDVVIDTGLGLRSLPEYLYSSGLLQDCG---SKEDAGRRP------LLavaTHVHFDHSGGLyq 94
Cdd:cd16281  37 NRitlaMRCLLIETGGRNILIDTGIGDKQDPKFRSIYVQHSEHSllkSLARLGLSPeditdvIL---THLHFDHCGGA-- 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 76677920  95 fdqVAVHRAEAEALArgdnFETVT-WLSDSEVVRA--PSPGWRARQFR--VQAVQPT--LILQDGDVINLGDR-QLTVMH 166
Cdd:cd16281 112 ---TRADDDGLVELL----FPNATyWVQKRHWEWAlnPNPRERASFLPenIEPLEESgrLKLIDGSDAELGPGiRFHLSD 184

                       170       180
                ....*....|....*....|....*..
gi 76677920 167 mpGHSRGSIC--LHDKDRKVLFSGDVV 191
Cdd:cd16281 185 --GHTPGQMLpeISTPGGTVVFAADLI 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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