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Conserved domains on  [gi|157821863|ref|NP_001102404|]
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acyl-coenzyme A thioesterase MBLAC2 [Rattus norvegicus]

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 157821863  22 RFYESGNRANIWLVRGSEQDVVIDTGLGLRSLPEYLYSSGLLqdcgakedagrrPLLAVATHVHFDHSGGLYQFDQVAVH 101
Cdd:cd07712    1 LFIEEDDRVNIYLLRGRDRALLIDTGLGIGDLKEYVRTLTDL------------PLLVVATHGHFDHIGGLHEFEEVYVH 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863 102 RAEAEALARGDNFETVTWlsdsevvrapspgwRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKD 181
Cdd:cd07712   69 PADAEILAAPDNFETLTW--------------DAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRA 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 157821863 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 157821863  22 RFYESGNRANIWLVRGSEQDVVIDTGLGLRSLPEYLYSSGLLqdcgakedagrrPLLAVATHVHFDHSGGLYQFDQVAVH 101
Cdd:cd07712    1 LFIEEDDRVNIYLLRGRDRALLIDTGLGIGDLKEYVRTLTDL------------PLLVVATHGHFDHIGGLHEFEEVYVH 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863 102 RAEAEALARGDNFETVTWlsdsevvrapspgwRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKD 181
Cdd:cd07712   69 PADAEILAAPDNFETLTW--------------DAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRA 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 157821863 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 5.41e-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: 140.98  E-value: 5.41e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  16 IFWIQERFYESGNRANIWLVRGSEQDVVIDTGLGLRSLPEYLyssgllqdcGAKEDAGRRPLLAVATHVHFDHSGGLYQF 95
Cdd:COG0491    1 VYVLPGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEALL---------AALAALGLDIKAVLLTHLHPDHVGGLAAL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  96 DQ-----VAVHRAEAEALARGDnfetvtwlsdsevvrapspgwRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGH 170
Cdd:COG0491   72 AEafgapVYAHAAEAEALEAPA---------------------AGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGH 130

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157821863 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 3.04e-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: 3.04e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863    31 NIWLVRGSEQDVVIDTGLGlrslpeylYSSGLLQDcgAKEDAGRRPLLAVATHVHFDHSGGLYQF-----DQVAVHRAEA 105
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPG--------EAEDLLAE--LKKLGPKKIDAIILTHGHPDHIGGLPELleapgAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863   106 EALargdnfetvtwlsdsevvRAPSPGWRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKVL 185
Cdd:smart00849  71 ELL------------------KDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKIL 132

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 157821863   186 FSGDVVYDGSLIDWL-PYSRISDYVGTcERLIELVDRgLVEKVLPGH 231
Cdd:smart00849 133 FTGDLLFAGGDGRTLvDGGDAAASDAL-ESLLKLLKL-LPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
31-231 1.62e-22

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 92.05  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863   31 NIWLVRGSEQDVVIDTGLGLrslpeylySSGLLQDCGAKEDAGRRPLLAVATHVHFDHSGGLYQFDQVAVHRAEAEALar 110
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSA--------EAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAE-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  111 gdnfETVTWLSDSEVVRAPSPGWRARQFRVQAVQPTLIlqDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKVLFSGDV 190
Cdd:pfam00753  77 ----EARELLDEELGLAASRLGLPGPPVVPLPPDVVLE--EGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 157821863  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 157821863  82 THVHFDHSGGLYQFDQvavhRAEAEALArgdnfetvtwlsdSEVVRAPSPGWrarqfrvqavqpTLILQDGDVINLGDRQ 161
Cdd:PLN02398 128 THHHYDHTGGNLELKA----RYGAKVIG-------------SAVDKDRIPGI------------DIVLKDGDKWMFAGHE 178

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157821863 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 157821863  22 RFYESGNRANIWLVRGSEQDVVIDTGLGLRSLPEYLYSSGLLqdcgakedagrrPLLAVATHVHFDHSGGLYQFDQVAVH 101
Cdd:cd07712    1 LFIEEDDRVNIYLLRGRDRALLIDTGLGIGDLKEYVRTLTDL------------PLLVVATHGHFDHIGGLHEFEEVYVH 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863 102 RAEAEALARGDNFETVTWlsdsevvrapspgwRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKD 181
Cdd:cd07712   69 PADAEILAAPDNFETLTW--------------DAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRA 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 157821863 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 5.41e-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: 140.98  E-value: 5.41e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  16 IFWIQERFYESGNRANIWLVRGSEQDVVIDTGLGLRSLPEYLyssgllqdcGAKEDAGRRPLLAVATHVHFDHSGGLYQF 95
Cdd:COG0491    1 VYVLPGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEALL---------AALAALGLDIKAVLLTHLHPDHVGGLAAL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  96 DQ-----VAVHRAEAEALARGDnfetvtwlsdsevvrapspgwRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGH 170
Cdd:COG0491   72 AEafgapVYAHAAEAEALEAPA---------------------AGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGH 130

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157821863 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 2.40e-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: 117.39  E-value: 2.40e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  30 ANIWLVRGSEQD-VVIDTGLGlrslpeylYSSGLLQdcgAKEDAGRRPLLAVATHVHFDHSGGLYQFDQ-----VAVHRA 103
Cdd:cd06262   10 TNCYLVSDEEGEaILIDPGAG--------ALEKILE---AIEELGLKIKAILLTHGHFDHIGGLAELKEapgapVYIHEA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863 104 EAEALARGDNFetvtwlsdsevvrapspGWRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRK 183
Cdd:cd06262   79 DAELLEDPELN-----------------LAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEG 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 157821863 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 ...
 15-231 4.53e-29

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: 109.58  E-value: 4.53e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  15 GIFWIQERfYESGNRANIWLVRGSEQDVVIDTGLGlrslpeYLYSSGLLQDcgAKEDAGRRPLLAVATHVHFDHSGGLYQ 94
Cdd:cd16282    1 GVYALIGP-DGGGFISNIGFIVGDDGVVVIDTGAS------PRLARALLAA--IRKVTDKPVRYVVNTHYHGDHTLGNAA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  95 FDQVAV----HRAEAEALARGdnfETVTWLSDSEVVRAPSPGwrarqfrVQAVQPTLILQDGDVINLGDRQLTVMHM-PG 169
Cdd:cd16282   72 FADAGApiiaHENTREELAAR---GEAYLELMRRLGGDAMAG-------TELVLPDRTFDDGLTLDLGGRTVELIHLgPA 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157821863 170 HSRGSICLHDKDRKVLFSGDVVYDGsLIDWLPYSRISDYVGTCERLIELVDrglvEKVLPGH 231
Cdd:cd16282  142 HTPGDLVVWLPEEGVLFAGDLVFNG-RIPFLPDGSLAGWIAALDRLLALDA----TVVVPGH 198
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 31-231 3.04e-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: 3.04e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863    31 NIWLVRGSEQDVVIDTGLGlrslpeylYSSGLLQDcgAKEDAGRRPLLAVATHVHFDHSGGLYQF-----DQVAVHRAEA 105
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPG--------EAEDLLAE--LKKLGPKKIDAIILTHGHPDHIGGLPELleapgAPVYAPEGTA 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863   106 EALargdnfetvtwlsdsevvRAPSPGWRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKVL 185
Cdd:smart00849  71 ELL------------------KDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKIL 132

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 157821863   186 FSGDVVYDGSLIDWL-PYSRISDYVGTcERLIELVDRgLVEKVLPGH 231
Cdd:smart00849 133 FTGDLLFAGGDGRTLvDGGDAAASDAL-ESLLKLLKL-LPKLVVPGH 177
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 15-231 3.14e-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: 96.52  E-value: 3.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  15 GIFWIqerfyESGNRANIWLVRGSEQDVVIDTGlglrslpeYLYSSGLLQDCGAKEDAGRRPLLAVA-THVHFDHSGGLY 93
Cdd:cd07721    1 GVYQL-----PLLPPVNAYLIEDDDGLTLIDTG--------LPGSAKRILKALRELGLSPKDIRRILlTHGHIDHIGSLA 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  94 QFDQ-----VAVHRAEAEALARGDNFETVTWLSDSEVVRAPSPgwrarqfrVQAVQPTLILQDGDVINLGDRqLTVMHMP 168
Cdd:cd07721   68 ALKEapgapVYAHEREAPYLEGEKPYPPPVRLGLLGLLSPLLP--------VKPVPVDRTLEDGDTLDLAGG-LRVIHTP 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157821863 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 6.79e-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: 93.18  E-value: 6.79e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  31 NIWLVR--GSEQDVVIDTGLGlrslpeylySSGLLQDCGAKedaGRRPLLAVATHVHFDHSGGLyqfdqvavhraeaEAL 108
Cdd:cd16322   12 NTYLVAdeGGGEAVLVDPGDE---------SEKLLARFGTT---GLTLLYILLTHAHFDHVGGV-------------ADL 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863 109 ARGDNFETVTWLSDSEVVRAPSPGWRARQFRVQ-AVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKVLFS 187
Cdd:cd16322   67 RRHPGAPVYLHPDDLPLYEAADLGAKAFGLGIEpLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFS 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157821863 188 GDVVYDGSL--IDwLPYSRISDYVGTCERLIELVDRglvEKVLPGHF--NTFGAERLF 241
Cdd:cd16322  147 GDLLFQGSIgrTD-LPGGDPKAMAASLRRLLTLPDE---TRVFPGHGppTTLGEERRT 200
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
31-231 1.62e-22

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 92.05  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863   31 NIWLVRGSEQDVVIDTGLGLrslpeylySSGLLQDCGAKEDAGRRPLLAVATHVHFDHSGGLYQFDQVAVHRAEAEALar 110
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSA--------EAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAE-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  111 gdnfETVTWLSDSEVVRAPSPGWRARQFRVQAVQPTLIlqDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKVLFSGDV 190
Cdd:pfam00753  77 ----EARELLDEELGLAASRLGLPGPPVVPLPPDVVLE--EGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDL 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 157821863  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 5.92e-22

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: 90.05  E-value: 5.92e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  28 NRANIWLVRGSEQDVVIDTGLGLRSLPEYLYSSglLQDCGAKEDAGRRPLLavaTHVHFDHSGGLYQFdqvavhRAEAEA 107
Cdd:cd07725   13 GHVNVYLLRDGDETTLIDTGLATEEDAEALWEG--LKELGLKPSDIDRVLL---THHHPDHIGLAGKL------QEKSGA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863 108 LARGDNFETVTwlsdsevvrapspgwrarqfrvqavqptlilqDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKVLFS 187
Cdd:cd07725   82 TVYILDVTPVK--------------------------------DGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFV 129

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157821863 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 9.36e-22

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: 89.47  E-value: 9.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  31 NIWLVRGSEQDVVIDTGlglRSLPEYLyssgllqDCGAKEDAGRRPLLAVATHVHFDHSGGlyqfdqvavhraeAEALAR 110
Cdd:cd16278   19 NTYLLGAPDGVVVIDPG---PDDPAHL-------DALLAALGGGRVSAILVTHTHRDHSPG-------------AARLAE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863 111 gdnfETvtwlsdSEVVRAPSPGWRARQFRvqAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKVLFSGDV 190
Cdd:cd16278   76 ----RT------GAPVRAFGPHRAGGQDT--DFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDH 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 157821863 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 2.27e-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: 81.38  E-value: 2.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  15 GIFWIQERFYESGNRANIWLVRGSEQDVVIDTGLGLrSLPEYLyssGLLQDCGAKEDAGRRPLLavaTHVHFDHSGGLYQ 94
Cdd:cd07726    1 GIYLIDLGFLGFPGRIASYLLDGEGRPALIDTGPSS-SVPRLL---AALEALGIAPEDVDYIIL---THIHLDHAGGAGL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  95 FDQ------VAVHRAEAEALAR------------GDNFETVTWlsdsEVVRAPSPgwrarqfRVQAvqptliLQDGDVIN 156
Cdd:cd07726   74 LAEalpnakVYVHPRGARHLIDpsklwasaravyGDEADRLGG----EILPVPEE-------RVIV------LEDGETLD 136

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157821863 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 1.07e-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: 79.95  E-value: 1.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  33 WLVRGSEQDVVIDTGLGlrslPEYLYSSGLLQDCGAKEDAGRRPLLA---------------VATHVHFDHSGGLYQFDQ 97
Cdd:cd07729   35 YLIEHPEGTILVDTGFH----PDAADDPGGLELAFPPGVTEEQTLEEqlarlgldpedidyvILSHLHFDHAGGLDLFPN 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  98 --VAVHRAEAEALARGDNFEtvtwlsdsevvRAPSPGWRARQFRVQAVQPTLIlqDGDVINLGDrqLTVMHMPGHSRGSI 175
Cdd:cd07729  111 atIIVQRAELEYATGPDPLA-----------AGYYEDVLALDDDLPGGRVRLV--DGDYDLFPG--VTLIPTPGHTPGHQ 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157821863 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 7.47e-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: 7.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  82 THVHFDHSGGlyqfdqvavhraeaealargdNFETVTWLSDSEVVrAPSPGwrarqfRVQAVqpTLILQDGDVINLGDRQ 161
Cdd:cd07723   50 THHHWDHTGG---------------------NAELKALFPDAPVY-GPAED------RIPGL--DHPVKDGDEIKLGGLE 99

                         90       100
                 ....*....|....*....|....*...
gi 157821863 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 2.31e-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: 2.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  82 THVHFDHSGG------LYQFDQVAVHRAeaealargDNFetvtWLSDSEVvrapspgwRARQF---RVQAVQPTLILQDG 152
Cdd:cd07737   53 THGHLDHVGGaaelaeHYGVPIIGPHKE--------DKF----LLENLPE--------QSQMFgfpPAEAFTPDRWLEEG 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 157821863 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 3.00e-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: 67.73  E-value: 3.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  82 THVHFDHSGGLYQFDQ-----VAVHRAEAEALARGDNfetvtwlSDsevvrapsPGWRARQFRVQAVQPTLILQDGDVIN 156
Cdd:cd16288   67 SHAHLDHAGGLAALKKltgakLMASAEDAALLASGGK-------SD--------FHYGDDSLAFPPVKVDRVLKDGDRVT 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157821863 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 7.75e-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: 63.72  E-value: 7.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  31 NIWLVRGSEQDVVIDTGLGLRSLPeylySSGLLQDcgAKEDAGRRP------LLavaTHVHFDHSGGLYQFD-------- 96
Cdd:cd07720   50 NAFLVRTGGRLILVDTGAGGLFGP----TAGKLLA--NLAAAGIDPediddvLL---THLHPDHIGGLVDAGgkpvfpna 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  97 QVAVHRAEAEAlargdnfetvtWLSDSEVVRAPSpgwRARQF------RVQAVQPTLILQDGDVINLGdrqLTVMHMPGH 170
Cdd:cd07720  121 EVHVSEAEWDF-----------WLDDANAAKAPE---GAKRFfdaardRLRPYAAAGRFEDGDEVLPG---ITAVPAPGH 183

                        170       180
                 ....*....|....*....|....
gi 157821863 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 157821863  82 THVHFDHSGG----LYQFD-QVAVHRAEAEALargdnfetvtwlsdsevvrapspgwrarQFRVQAVQPtliLQDGDVIN 156
Cdd:cd16275   54 THSHFDHVNLveplLAKYDaPVYMSKEEIDYY----------------------------GFRCPNLIP---LEDGDTIK 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157821863 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 2.31e-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: 2.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863 147 LILQDGDVINLGDrQLTVMHMPGHSRGSICLHDKDRKVLFSGDVVYDGSLIDWLPYSR------ISDYVGTCERLIELVd 220
Cdd:cd07727   90 IVLWGGDPWELDP-DLTLIPVPGHTRGSVVLLYKEKGVLFTGDHLAWSRRRGWLSAFRyvcwysWPEQAESVERLADLD- 167

                         90
                 ....*....|.
gi 157821863 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 157821863  23 FYESGnRANIWLVRGSEQDV-VIDTGLG---LRSLPEYLyssgllqdcgakEDAGRRPLLAVATHVHFDHSGGLYQF--- 95
Cdd:cd07743    2 YYIPG-PTNIGVYVFGDKEAlLIDSGLDedaGRKIRKIL------------EELGWKLKAIINTHSHADHIGGNAYLqkk 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  96 --DQVAVHRAEAEALARGDNFETVTWLSdsevvrAPSPGWRARQFRVQAVQPTLILQDGDvINLGDRQLTVMHMPGHSRG 173
Cdd:cd07743   69 tgCKVYAPKIEKAFIENPLLEPSYLGGA------YPPKELRNKFLMAKPSKVDDIIEEGE-LELGGVGLEIIPLPGHSFG 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157821863 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 2.61e-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: 2.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  31 NIWLVRGSEQDVVIDTGLGLRSLPEYLYSsgLLQDCGAKE--DAgrrpllaVATHVHFDHSGGLyqfDQVavhraeaEAL 108
Cdd:cd07722   19 NTYLVGTGKRRILIDTGEGRPSYIPLLKS--VLDSEGNATisDI-------LLTHWHHDHVGGL---PDV-------LDL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863 109 ARGDNFETVTWLSDSEVVRAPSPGwrarqfrvqavQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKVLFSG 188
Cdd:cd07722   80 LRGPSPRVYKFPRPEEDEDPDEDG-----------GDIHDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTG 148


                 ...
gi 157821863 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; ...
 42-189 9.19e-10

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: 56.64  E-value: 9.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  42 VVIDTGLGlrSLPEYLyssGLLQDCGAKedagrrpLLAVA-THVHFDH-SGGLYqfdqvavhraeaeaLARgdnfetvtw 119
Cdd:cd07724   26 AVIDPVRD--SVDRYL---DLAAELGLK-------ITYVLeTHVHADHvSGARE--------------LAE--------- 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863 120 LSDSEVVRAPspgwrarqfRVQAVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKVLFSGD 189
Cdd:cd07724   71 RTGAPIVIGE---------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 157821863  78 LAVATHVHFDHSGGLYQFDQ-----VAVHRAEAEALARG----DNFE--TVTWLSDSEVVRApspgwrarqfrvqavqpt 146
Cdd:cd07708   63 LILISHAHFDHAGGSAEIKKqtgakVMAGAEDVSLLLSGgssdFHYAndSSTYFPQSTVDRA------------------ 124

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157821863 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 157821863  17 FWIQERFYESGNRA-NIWLVRGSEQDVVIDTGL--GLRSLPEYLYSSGL-LQDCGakedagrrplLAVATHVHFDHSGGL 92
Cdd:cd16310    8 FRIVDNIYYVGTKGiGSYLITSNHGAILLDGGLeeNAALIEQNIKALGFkLSDIK----------IIINTHAHYDHAGGL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  93 YQFDQ-----VAVHRAEAEALARGdnfetvTWLSDSEVVRAPSPgwrarqfrvqAVQPTLILQDGDVINLGDRQLTVMHM 167
Cdd:cd16310   78 AQLKAdtgakLWASRGDRPALEAG------KHIGDNITQPAPFP----------AVKVDRILGDGEKIKLGDITLTATLT 141

                        170       180
                 ....*....|....*....|....*
gi 157821863 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 2.90e-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: 2.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  42 VVIDTGLGlRSLPEYLYSsglLQDCGAK-EDAgrRPLLAvaTHVHFDHSGGLYQFDQ-----VAVHRAEAEALARGDNFE 115
Cdd:cd16308   34 ILINTGLA-ESVPLIKKN---IQALGFKfKDI--KILLT--TQAHYDHVGAMAAIKQqtgakMMVDEKDAKVLADGGKSD 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157821863 116 TVtwLSDSEVVRAPspgwrarqfrvqaVQPTLILQDGDVINLGDRQLTVMHMPGHSRGS 174
Cdd:cd16308  106 YE--MGGYGSTFAP-------------VKADKLLHDGDTIKLGGTKLTLLHHPGHTKGS 149
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 145-231 2.74e-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: 2.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863 145 PTLILQDGDVINLGDRQLTVMHMPG-HSRGSICLHDKDRKVLFSGDV---------VYDGSLIDWLPYSR--ISDYVGT- 211
Cdd:cd07709  117 RFVVVKDGDTLDLGKHTLKFIPAPMlHWPDTMVTYDPEDKILFSGDAfgahgasgeLFDDEVEDYLEEARryYANIMGPf 196

                         90       100
                 ....*....|....*....|....
gi 157821863 212 ---CERLIELVdRGL-VEKVLPGH 231
Cdd:cd07709  197 skqVRKALEKL-EALdIKMIAPSH 219
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 82-245 2.93e-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) 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: 2.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  82 THVHFDHSGGlyqfdqvavhraeAEALArgDNFETVTWLS--DSEVVRAPsPGWRARQFRVQAVQPTLILQDGDVINLGD 159
Cdd:cd16280   68 THGHGDHYGG-------------AAYLK--DLYGAKVVMSeaDWDMMEEP-PEEGDNPRWGPPPERDIVIKDGDTLTLGD 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863 160 RQLTVMHMPGHSRGSICL----HDKDRK---VLFSGdvvydGSLIDWLPYSRISDYVGTCERLIELVDRGLVEKVLPGH- 231
Cdd:cd16280  132 TTITVYLTPGHTPGTLSLifpvKDGGKThraGLWGG-----TGLNTGPNLERREQYIASLERFKKIAEEAGVDVFLSNHp 206

                        170
                 ....*....|....
gi 157821863 232 FNTFGAERLFRLAS 245
Cdd:cd16280  207 FQDGSLEKREALRN 220
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 2.00e-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: 50.81  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  80 VATHVHFDHSGGL--YQFD---QVAVHRAEAEALARGDNfetvtwlSDSEvvraPSPGWRARqfrVQAVQPTLILQDGDV 154
Cdd:cd16290   65 LNSHAHFDHAGGIaaLQRDsgaTVAASPAGAAALRSGGV-------DPDD----PQAGAADP---FPPVAKVRVVADGEV 130

                         90       100
                 ....*....|....*....|.
gi 157821863 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 3.88e-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: 49.12  E-value: 3.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  80 VATHVHFDHSGGLYQF-DQVAV---HRAEAEALARgdnfetvtwlsdsevvrAPSPgwrarqfrvQAVQPTLILQDGDVI 155
Cdd:cd16276   50 VYSHNHADHIGGASIFkDEGATiiaHEATAELLKR-----------------NPDP---------KRPVPTVTFDDEYTL 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157821863 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 1.49e-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: 48.42  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  42 VVIDTGLG------LRSLPEYLYssGLLQDCGAKEDAgrRPLLAVA------------THVHFDHSGGLYQFDQVA--VH 101
Cdd:cd07730   36 ILFDLGYRkdfeeyTPRVPERLY--RTPVPLEVEEDV--AEQLAAGgidpedidavilSHLHWDHIGGLSDFPNARliVG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863 102 RAEAEALARGDnfetvtwlsdseVVRAPSPGWRARQFRVQAVQPTLILQDGDVIN--------LGDRQLTVMHMPGHSRG 173
Cdd:cd07730  112 PGAKEALRPPG------------YPSGFLPELLPSDFEGRLVRWEEDDFLWVPLGpfpraldlFGDGSLYLVDLPGHAPG 179

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157821863 174 SICLH---DKDRKVLFSGDVVYDGS----------LIDWLPYSRISDYVGTCERLIELVDRGLVEkVLPGH 231
Cdd:cd07730  180 HLGLLartTSGTWVFLAGDACHHRIgllrpspllpLPDLDDGADREAARETLARLRELDAAPDVR-VVLAH 249
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 33-190 1.99e-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.


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 47.52  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  33 WLVRGSEQDVVIDTGLG---LRSLPEYL--YSSGLLQDCGAkedAGRRPL---LAVATHVHFDHSGGLYQFD-------- 96
Cdd:cd16277   16 WLVRTPGRTILVDTGIGndkPRPGPPAFhnLNTPYLERLAA---AGVRPEdvdYVLCTHLHVDHVGWNTRLVdgrwvptf 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  97 ---QVAVHRAEAEAlargdnfetvtWLSDSEVVRAPSPGWrarqfrVQAVQP------TLILQDGDVINLGdrqLTVMHM 167
Cdd:cd16277   93 pnaRYLFSRAEYDH-----------WSSPDAGGPPNRGVF------EDSVLPvieaglADLVDDDHEILDG---IRLEPT 152

                        170       180
                 ....*....|....*....|....*
gi 157821863 168 PGHSRG--SICLHDKDRKVLFSGDV 190
Cdd:cd16277  153 PGHTPGhvSVELESGGERALFTGDV 177
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 157821863 138 FRVQAVQptlilqDGDVINLGDRQLTV--MHMPgHSRGSICLHDKDRKVLFSGDV---------VYDGSLID-------- 198
Cdd:COG0426  118 FRFIVVK------EGDTLDLGGHTLQFipAPML-HWPDTMFTYDPEDKILFSGDAfgshgasdeLFDDEVDEhleeearr 190

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 157821863 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 2.14e-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: 44.81  E-value: 2.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  34 LVRGSEQDVVIDTGLglrslPEYlySSGLLQDCGAKEDAGRRPLLAVATHVHFDHSGGLYQFD-----QVAVHRAEAEAL 108
Cdd:cd16289   26 LVKTPDGAVLLDGGM-----PQA--ADMLLDNMRALGVAPGDLKLILHSHAHADHAGPLAALKratgaRVAANAESAVLL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863 109 ARGDNFETvtwLSDSEVVRAPspgwrarqfrvqaVQPTLILQDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKVLFSG 188
Cdd:cd16289   99 ARGGSDDI---HFGDGITFPP-------------VQADRIVMDGEVVTLGGVTFTAHFTPGHTPGSTSWTWTDTRDGKPV 162


                 ....*...
gi 157821863 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 157821863  82 THVHFDHSGGLyqfdqvavhraeaEALARGDNFETVTWLSDSEVVRAPSPGWRARQFR------VQAVQPTLILQDGDVI 155
Cdd:cd16312   67 SHAHWDHAGGI-------------AALQKASGATVAASAHGAQVLQSGTNGKDDPQYQakpvvhVAKVAKVKEVGEGDTL 133

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157821863 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 4.80e-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: 4.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  80 VATHVHFDHSGGLyqfdqvavhraeaEALARGDNFETVTWLSDSEVVRAPSPGWRARQF----------RVQAVQptlil 149
Cdd:cd16313   65 LSSHDHWDHAGGI-------------AALQKLTGAQVLASPATVAVLRSGSMGKDDPQFggltpmppvaSVRAVR----- 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863 150 qDGDVINLGDRQLTVMHMPGHSRGSICLHDKDRKVLFSGDVVYDGSLI----DWLPYSRISDYVGTCERLIELVDRGLVE 225
Cdd:cd16313  127 -DGEVVKLGPLAVTAHATPGHTTGGTSWTWQSCEQGRCANMVFADSLTavsaDGYRFSAHPAVLADVEQSIAAVEKLACD 205


                 ....*.
gi 157821863 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 5.09e-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: 5.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  80 VATHVHFDHSGGLYQFDQVAVHRAEAEALARgdnfetvtwlsdsEVVRAPSPGWRARQFRV----QAVQPTLILQDGDVI 155
Cdd:cd16315   65 LSSHEHFDHVGGLAALQRATGARVAASAAAA-------------PVLESGKPAPDDPQAGLhepfPPVRVDRIVEDGDTV 131

                         90
                 ....*....|....*....
gi 157821863 156 NLGDRQLTVMHMPGHSRGS 174
Cdd:cd16315  132 ALGSLRLTAHATPGHTPGA 150
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 32-189 5.26e-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: 5.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  32 IWLVRGSEQDVVIDTG------LGLRSLPEYLYSSGLlqdcgakedagRRPLLAVATHVHFDHSGGLyqfdqvavhraea 105
Cdd:COG2333   14 ILIRTPDGKTILIDTGprpsfdAGERVVLPYLRALGI-----------RRLDLLVLTHPDADHIGGL------------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863 106 EALARgdNFEtVTWLSDSEVVRAPSPGWRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHmPGHSR--------GSICL 177
Cdd:COG2333   70 AAVLE--AFP-VGRVLVSGPPDTSETYERLLEALKEKGIPVRPCRAGDTWQLGGVRFEVLW-PPEDLlegsdennNSLVL 145

                        170
                 ....*....|....
gi 157821863 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 157821863  82 THVHFDHSGGLYQFDQvavhRAEAEALArgdnfetvtwlsdSEVVRAPSPGWrarqfrvqavqpTLILQDGDVINLGDRQ 161
Cdd:PLN02398 128 THHHYDHTGGNLELKA----RYGAKVIG-------------SAVDKDRIPGI------------DIVLKDGDKWMFAGHE 178

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157821863 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 2.53e-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: 2.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  34 LVRGSEQDVVIDTG----LGLRSLPEYLYSSGllqdcgakedaGRRPLLAVATHVHFDHSGGLyqfdqvavhraeAEALa 109
Cdd:cd07731   14 LIQTPGKTILIDTGprdsFGEDVVVPYLKARG-----------IKKLDYLILTHPDADHIGGL------------DAVL- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863 110 rgDNFEtVTWLSDSEVVRAPSPGWRARQFRVQAVQPTLILQDGDVINLGDRQLTVMHmPGHSRG------SICLH--DKD 181
Cdd:cd07731   70 --KNFP-VKEVYMPGVTHTTKTYEDLLDAIKEKGIPVTPCKAGDRWQLGGVSFEVLS-PPKDDYddlnnnSCVLRltYGG 145


                 ....*...
gi 157821863 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 2.58e-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: 2.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  10 KSLGDGIFWIQERFYESGNranIWLVRGSEQDVVI----DTGLGLRSLPEYLyssgllqdcgaKEDAGRRPLLAVATHVH 85
Cdd:cd16286   10 REIDPDVFVITHRDPWSSN---VLVVKMLDGTVVIvdspYTNLATQTVLDWI-----------AKTMGPRKVVAINTHFH 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  86 FDHSGG----------LYQFDQVAVHRAEAealARGDNFETVTWLSDSEVVRapspgwraRQFRVQAVQPTLILQ--DGD 153
Cdd:cd16286   76 LDGTGGnealkkrgipTWGSDLTKQLLLER---GKADRIKAAEFLKNEDLKR--------RIESSPPVPPDNVFDlkEGK 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863 154 VINLGDRQLTVmHMPG--HSRGSICLHDKDRKVLFSGDVVYDGSLIDWLPYSRISDYVGTCERLIELVDRglveKVLPGH 231
Cdd:cd16286  145 VFSFGNELVEV-SFPGpaHAPDNVVVYFPERKILFGGCMIKPGKELGNLGDANMKAWPDSVRRLKKFDAK----IVIPGH 219


                 ....*....
gi 157821863 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 2.98e-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: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  80 VATHVHFDHSGGLYQFDQVAVHRAEAE---ALARGDNFE----TVTWLSDS-EVVRAPSPGWRARQFRvqAVQPTLILQD 151
Cdd:cd07742   85 VLTHLDLDHAGGLADFPHATVHVHAAEldaATSPRTRYErrryRPQQLAHGpWWVTYAAGGERWFGFE--AVRPLDGLPP 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863 152 GdvinlgdrqLTVMHMPGHSRG--SICLHDKDRKVLFSGDVVYDGSLID--------WLPYSRISD-----YVGTCERLI 216
Cdd:cd07742  163 E---------ILLVPLPGHTRGhcGVAVRTGDRWLLHAGDAYFHHGELDplppppppLRLFQRLLAvdrsaRLANLARLR 233


                 ....*
gi 157821863 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 ...
 30-191 7.45e-04

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


Pssm-ID: 293839  Cd Length: 252  Bit Score: 40.17  E-value: 7.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863  30 ANIWLVRGSEQDVVIDTGLGLRSLPEYLYSSGLLQDCGAKEDAGRRPLLA------VATHVHFDHSGGLyqfdqVAVHRA 103
Cdd:cd16281   43 MRCLLIETGGRNILIDTGIGDKQDPKFRSIYVQHSEHSLLKSLARLGLSPeditdvILTHLHFDHCGGA-----TRADDD 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157821863 104 EAEALArgdnFETVT-WLSDSEVVRA--PSPGWRARQFR--VQAVQPT--LILQDGDVINLGDR-QLTVMHmpGHSRGSI 175
Cdd:cd16281  118 GLVELL----FPNATyWVQKRHWEWAlnPNPRERASFLPenIEPLEESgrLKLIDGSDAELGPGiRFHLSD--GHTPGQM 191

                        170
                 ....*....|....*...
gi 157821863 176 C--LHDKDRKVLFSGDVV 191
Cdd:cd16281  192 LpeISTPGGTVVFAADLI 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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