NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|41327741|ref|NP_055112|]
View 

persulfide dioxygenase ETHE1, mitochondrial isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN02962 super family cl30130
hydroxyacylglutathione hydrolase
 13-254 3.04e-127

hydroxyacylglutathione hydrolase


The actual alignment was detected with superfamily member PLN02962:

Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 360.65  E-value: 3.04e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741   13 LSQRGGSGAPILLRQMFEPVSCTFTYLLGD--RESREAVLIDPVLETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGL 90
Cdd:PLN02962   1 SSSSSSSSSKLLFRQLFEKESSTYTYLLADvsHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741   91 LRSLLPGCQSVISRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHS------MAFTGDALLIRGCGRT 164
Cdd:PLN02962  81 LKTKLPGVKSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPdqpqprMAFTGDALLIRGCGRT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  165 DFQQGCAKTLYHSVHEKIFTLPGDCLIYPAHDYHGFTVSTVEEERTLNPRLTLSCEEFVKIMGNLNLPKPQQIDFAVPAN 244
Cdd:PLN02962 161 DFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPAN 240

                        250
                 ....*....|
gi 41327741  245 MRCGVQTPTA 254
Cdd:PLN02962 241 MVCGLQDPPA 250
 
Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 13-254 3.04e-127

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 360.65  E-value: 3.04e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741   13 LSQRGGSGAPILLRQMFEPVSCTFTYLLGD--RESREAVLIDPVLETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGL 90
Cdd:PLN02962   1 SSSSSSSSSKLLFRQLFEKESSTYTYLLADvsHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741   91 LRSLLPGCQSVISRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHS------MAFTGDALLIRGCGRT 164
Cdd:PLN02962  81 LKTKLPGVKSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPdqpqprMAFTGDALLIRGCGRT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  165 DFQQGCAKTLYHSVHEKIFTLPGDCLIYPAHDYHGFTVSTVEEERTLNPRLTLSCEEFVKIMGNLNLPKPQQIDFAVPAN 244
Cdd:PLN02962 161 DFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPAN 240

                        250
                 ....*....|
gi 41327741  245 MRCGVQTPTA 254
Cdd:PLN02962 241 MVCGLQDPPA 250
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 24-197 6.16e-83

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: 245.77  E-value: 6.16e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  24 LLRQMFEPVSCTFTYLLGDRESREAVLIDPVLETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRSLLpGCQSVIS 103
Cdd:cd07724   1 IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERT-GAPIVIG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741 104 RLSGA-QADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQ---GCAKTLYHSVH 179
Cdd:cd07724  80 EGAPAsFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPGeaeGLARQLYDSLQ 159

                       170
                ....*....|....*...
gi 41327741 180 EKIFTLPGDCLIYPAHDY 197
Cdd:cd07724 160 RKLLLLPDETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 35-197 9.72e-38

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: 131.74  E-value: 9.72e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  35 TFTYLLGDreSREAVLIDPVLETAPRDA--QLIKELGLRLLYAVNTHCHADHITGSGLLRSLLpGCQSVISR-------- 104
Cdd:COG0491  15 VNSYLIVG--GDGAVLIDTGLGPADAEAllAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAPVYAHAaeaealea 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741 105 --------LSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQGCAKTLYH 176
Cdd:COG0491  92 paagalfgREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLPDGDLAQWLA 171

                       170       180
                ....*....|....*....|.
gi 41327741 177 SVhEKIFTLPGDcLIYPAHDY 197
Cdd:COG0491 172 SL-ERLLALPPD-LVIPGHGP 190
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 37-195 1.39e-25

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: 98.78  E-value: 1.39e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741     37 TYLLGDREsrEAVLIDPVLETAPRDAQLIKELGLR-LLYAVNTHCHADHITGSG------------------LLRSLLPG 97
Cdd:smart00849   2 SYLVRDDG--GAILIDTGPGEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPelleapgapvyapegtaeLLKDLLAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741     98 CQSVISRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQG-CAKTLYH 176
Cdd:smart00849  80 LGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGdAAASDAL 159

                          170
                   ....*....|....*....
gi 41327741    177 SVHEKIFTLPGDcLIYPAH 195
Cdd:smart00849 160 ESLLKLLKLLPK-LVVPGH 177
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 38-197 5.63e-24

hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione hydrolase, a detoxification enzyme known as glyoxalase II. It follows lactoylglutathione lyase, or glyoxalase I, and acts to remove the toxic metabolite methylglyoxal and related compounds. This protein belongs to the broader metallo-beta-lactamase family (pfam00753). [Cellular processes, Detoxification]


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 96.45  E-value: 5.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741    38 YLLGDrESREAVLID-----PVLETaprdaqlIKELGLRLLYAVNTHCHADHITG-SGLLRSLlpGCQsVI----SRLSG 107
Cdd:TIGR03413  13 WLLHD-PDGQAAVVDpgeaePVLDA-------LEARGLTLTAILLTHHHHDHVGGvAELLEAF--PAP-VYgpaeERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741   108 AqaDLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTdFqQGCAKTLYHSVhEKIFTLPG 187
Cdd:TIGR03413  82 I--THPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRL-F-EGTPEQMYDSL-QRLAALPD 156

                         170
                  ....*....|
gi 41327741   188 DCLIYPAHDY 197
Cdd:TIGR03413 157 DTLVYCAHEY 166
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
35-195 4.45e-19

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 82.42  E-value: 4.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741    35 TFTYLLGDREsrEAVLIDPVLETAPRDAQLIKELGLRLL---YAVNTHCHADHITGSGLLRSLLPGCQSVISRLSGAQAD 111
Cdd:pfam00753   6 VNSYLIEGGG--GAVLIDTGGSAEAALLLLLAALGLGPKdidAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741   112 LH-----------------------IEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQ 168
Cdd:pfam00753  84 EElglaasrlglpgppvvplppdvvLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPL 163

                         170       180       190
                  ....*....|....*....|....*....|....
gi 41327741   169 GCAKTLYHSVHE-------KIFTLPGDcLIYPAH 195
Cdd:pfam00753 164 GGLLVLHPSSAEsslesllKLAKLKAA-VIVPGH 196
B3_Acin_new1 NF033184
putative subclass B3 metallo-beta-lactamase; This is one of two families of putative ...
 37-142 1.53e-07

putative subclass B3 metallo-beta-lactamase; This is one of two families of putative metallo-beta-lactamases of subclass B3 that are restricted to the genus Acinetobacter, and undescribed as of January 2017.


Pssm-ID: 439394  Cd Length: 283  Bit Score: 51.26  E-value: 1.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741   37 TYLLGdrESREAVLIDPVL-ETAPRDAQLIKELGLRLL---YAVNTHCHADHI---------TGSGLL------RSLLPG 97
Cdd:NF033184  51 AYLLA--SGHQALLIDTGLpENTEQIEQNIKQLGFKLSdvkIMVTSHAHWDHVgalarikqdTGAKLIamqqdvKALEIG 128

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 41327741   98 -------CQSVisRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTF 142
Cdd:NF033184 129 kpigentFQTI--PFTPVKVDKVIHDGEVVKLGKFKLKATLTPGHTPGCTTW 178
 
Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 13-254 3.04e-127

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 360.65  E-value: 3.04e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741   13 LSQRGGSGAPILLRQMFEPVSCTFTYLLGD--RESREAVLIDPVLETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGL 90
Cdd:PLN02962   1 SSSSSSSSSKLLFRQLFEKESSTYTYLLADvsHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741   91 LRSLLPGCQSVISRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHS------MAFTGDALLIRGCGRT 164
Cdd:PLN02962  81 LKTKLPGVKSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPdqpqprMAFTGDALLIRGCGRT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  165 DFQQGCAKTLYHSVHEKIFTLPGDCLIYPAHDYHGFTVSTVEEERTLNPRLTLSCEEFVKIMGNLNLPKPQQIDFAVPAN 244
Cdd:PLN02962 161 DFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPAN 240

                        250
                 ....*....|
gi 41327741  245 MRCGVQTPTA 254
Cdd:PLN02962 241 MVCGLQDPPA 250
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 24-197 6.16e-83

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: 245.77  E-value: 6.16e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  24 LLRQMFEPVSCTFTYLLGDRESREAVLIDPVLETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRSLLpGCQSVIS 103
Cdd:cd07724   1 IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERT-GAPIVIG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741 104 RLSGA-QADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQ---GCAKTLYHSVH 179
Cdd:cd07724  80 EGAPAsFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPGeaeGLARQLYDSLQ 159

                       170
                ....*....|....*...
gi 41327741 180 EKIFTLPGDCLIYPAHDY 197
Cdd:cd07724 160 RKLLLLPDETLVYPGHDY 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 37-195 4.70e-43

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: 144.35  E-value: 4.70e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  37 TYLLGDrESREAVLIDPVLETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRSLlPGCQSVISR------------ 104
Cdd:cd06262  12 CYLVSD-EEGEAILIDPGAGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEA-PGAPVYIHEadaelledpeln 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741 105 --------LSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQGCAKTLYH 176
Cdd:cd06262  90 laffgggpLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDLPGGDPEQLIE 169

                       170
                ....*....|....*....
gi 41327741 177 SVHEKIFTLPGDCLIYPAH 195
Cdd:cd06262 170 SIKKLLLLLPDDTVVYPGH 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 35-197 9.72e-38

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: 131.74  E-value: 9.72e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  35 TFTYLLGDreSREAVLIDPVLETAPRDA--QLIKELGLRLLYAVNTHCHADHITGSGLLRSLLpGCQSVISR-------- 104
Cdd:COG0491  15 VNSYLIVG--GDGAVLIDTGLGPADAEAllAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAPVYAHAaeaealea 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741 105 --------LSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQGCAKTLYH 176
Cdd:COG0491  92 paagalfgREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLPDGDLAQWLA 171

                       170       180
                ....*....|....*....|.
gi 41327741 177 SVhEKIFTLPGDcLIYPAHDY 197
Cdd:COG0491 172 SL-ERLLALPPD-LVIPGHGP 190
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 36-195 1.43e-37

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: 129.50  E-value: 1.43e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  36 FTYLLGDRESREAVLIDPVletaprDAQLI----KELGLRLLYAVNTHCHADHITGSGLLRSLLPGCQsVI----SRLSG 107
Cdd:cd07723  10 YIYLIVDEATGEAAVVDPG------EAEPVlaalEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAP-VYgpaeDRIPG 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741 108 AqaDLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRtdFQQGCAKTLYHSvHEKIFTLPG 187
Cdd:cd07723  83 L--DHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGR--FFEGTAEQMYAS-LQKLLALPD 157


                ....*...
gi 41327741 188 DCLIYPAH 195
Cdd:cd07723 158 DTLVYCGH 165
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 36-195 1.24e-36

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: 127.27  E-value: 1.24e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  36 FTYLLGDRESREAVLIDPV--LETAprdAQLIKELGLRLLYAVNTHCHADHITGSGLLRSLlPGCQSVISR----LSGAQ 109
Cdd:cd16275  13 YSYIIIDKATREAAVVDPAwdIEKI---LAKLNELGLTLTGILLTHSHFDHVNLVEPLLAK-YDAPVYMSKeeidYYGFR 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741 110 A-DLH-IEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHsmAFTGDALLIRGCGRTDFQQGCAKTLYHSVHEKIFTLPG 187
Cdd:cd16275  89 CpNLIpLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGDS--LFTGDTLFIEGCGRCDLPGGDPEEMYESLQRLKKLPPP 166


                ....*...
gi 41327741 188 DCLIYPAH 195
Cdd:cd16275 167 NTRVYPGH 174
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 37-215 4.82e-31

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: 113.98  E-value: 4.82e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  37 TYLLGDRESREAVLIDPVLEtAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRsLLPGCQSVISRL---------SG 107
Cdd:cd16322  13 TYLVADEGGGEAVLVDPGDE-SEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLR-RHPGAPVYLHPDdlplyeaadLG 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741 108 AQA-----------DLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFqQGCAKTLYH 176
Cdd:cd16322  91 AKAfglgieplpppDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRTDL-PGGDPKAMA 169

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 41327741 177 SVHEKIFTLPGDCLIYPAHDyhgfTVSTVEEERTLNPRL 215
Cdd:cd16322 170 ASLRRLLTLPDETRVFPGHG----PPTTLGEERRTNPFL 204
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 37-195 1.39e-25

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: 98.78  E-value: 1.39e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741     37 TYLLGDREsrEAVLIDPVLETAPRDAQLIKELGLR-LLYAVNTHCHADHITGSG------------------LLRSLLPG 97
Cdd:smart00849   2 SYLVRDDG--GAILIDTGPGEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPelleapgapvyapegtaeLLKDLLAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741     98 CQSVISRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQG-CAKTLYH 176
Cdd:smart00849  80 LGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGdAAASDAL 159

                          170
                   ....*....|....*....
gi 41327741    177 SVHEKIFTLPGDcLIYPAH 195
Cdd:smart00849 160 ESLLKLLKLLPK-LVVPGH 177
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 34-195 1.95e-25

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: 98.78  E-value: 1.95e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  34 CTftyLLGDRESREAVLIDPVLEtAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRSL------------------L 95
Cdd:cd07737  13 CS---LIWCEETKEAAVIDPGGD-ADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHygvpiigphkedkfllenL 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  96 PGcQSVISRLSGAQA---DLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQGCAK 172
Cdd:cd07737  89 PE-QSQMFGFPPAEAftpDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTDFPGGNHA 167

                       170       180
                ....*....|....*....|...
gi 41327741 173 TLYHSVHEKIFTLPGDCLIYPAH 195
Cdd:cd07737 168 QLIASIKEKLLPLGDDVTFIPGH 190
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 38-197 5.63e-24

hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione hydrolase, a detoxification enzyme known as glyoxalase II. It follows lactoylglutathione lyase, or glyoxalase I, and acts to remove the toxic metabolite methylglyoxal and related compounds. This protein belongs to the broader metallo-beta-lactamase family (pfam00753). [Cellular processes, Detoxification]


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 96.45  E-value: 5.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741    38 YLLGDrESREAVLID-----PVLETaprdaqlIKELGLRLLYAVNTHCHADHITG-SGLLRSLlpGCQsVI----SRLSG 107
Cdd:TIGR03413  13 WLLHD-PDGQAAVVDpgeaePVLDA-------LEARGLTLTAILLTHHHHDHVGGvAELLEAF--PAP-VYgpaeERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741   108 AqaDLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTdFqQGCAKTLYHSVhEKIFTLPG 187
Cdd:TIGR03413  82 I--THPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRL-F-EGTPEQMYDSL-QRLAALPD 156

                         170
                  ....*....|
gi 41327741   188 DCLIYPAHDY 197
Cdd:TIGR03413 157 DTLVYCAHEY 166
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 31-213 3.15e-20

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 86.74  E-value: 3.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741   31 PVSC---TFTYLLGDRESREAVLIDPVLETAPRDAQliKELGLRLLYAVNTHCHADHITGSGLLRSLLPGCQSVISRLSG 107
Cdd:PLN02469   5 PVPCledNYAYLIIDESTKDAAVVDPVDPEKVLQAA--HEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSLDN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  108 AQADLH-IEDGDSIRFGR----FALETrasPGHTPGCVTFVL----NDHSMAFTGDALLIRGCGRtdFQQGCAKTLYHSV 178
Cdd:PLN02469  83 VKGCTHpVENGDKLSLGKdvniLALHT---PCHTKGHISYYVtgkeGEDPAVFTGDTLFIAGCGK--FFEGTAEQMYQSL 157

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 41327741  179 HEKIFTLPGDCLIYPAHDYhgfTVSTVEEERTLNP 213
Cdd:PLN02469 158 CVTLGSLPKPTQVYCGHEY---TVKNLKFALTVEP 189
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
35-195 4.45e-19

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 82.42  E-value: 4.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741    35 TFTYLLGDREsrEAVLIDPVLETAPRDAQLIKELGLRLL---YAVNTHCHADHITGSGLLRSLLPGCQSVISRLSGAQAD 111
Cdd:pfam00753   6 VNSYLIEGGG--GAVLIDTGGSAEAALLLLLAALGLGPKdidAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741   112 LH-----------------------IEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQ 168
Cdd:pfam00753  84 EElglaasrlglpgppvvplppdvvLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPL 163

                         170       180       190
                  ....*....|....*....|....*....|....
gi 41327741   169 GCAKTLYHSVHE-------KIFTLPGDcLIYPAH 195
Cdd:pfam00753 164 GGLLVLHPSSAEsslesllKLAKLKAA-VIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 30-197 1.42e-13

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 69.10  E-value: 1.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741   30 EPVSC---TFTYLLGDRESREAVLIDPVlETAPRDAQLIKElGLRLLYAVNTHCHADHITGSGLLRSLLpGCQSVIS--- 103
Cdd:PLN02398  79 ELVPClkdNYAYLLHDEDTGTVGVVDPS-EAVPVIDALSRK-NRNLTYILNTHHHYDHTGGNLELKARY-GAKVIGSavd 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  104 --RLSGAqaDLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRtdFQQGCAKTLYHSVhEK 181
Cdd:PLN02398 156 kdRIPGI--DIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGK--LFEGTPEQMLSSL-QK 230

                        170
                 ....*....|....*.
gi 41327741  182 IFTLPGDCLIYPAHDY 197
Cdd:PLN02398 231 IISLPDDTNIYCGHEY 246
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 36-212 1.76e-13

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 67.93  E-value: 1.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741   36 FTYLLGDRESReAVLIDPVlETAPRdAQLIKELGLRLLYAVNTHCHADHITGSGLLRSLLPgcQSVISRLSGAQ---ADL 112
Cdd:PRK10241  13 YIWVLNDEAGR-CLIVDPG-EAEPV-LNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFP--QIVVYGPQETQdkgTTQ 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  113 HIEDGDSIRFGRFALETRASPGHTPGCVTFVlnDHSMAFTGDALLIRGCGRtdFQQGCAKTLYHSVhEKIFTLPGDCLIY 192
Cdd:PRK10241  88 VVKDGETAFVLGHEFSVFATPGHTLGHICYF--SKPYLFCGDTLFSGGCGR--LFEGTASQMYQSL-KKINALPDDTLIC 162

                        170       180
                 ....*....|....*....|....
gi 41327741  193 PAHDYH----GFTVSTVEEERTLN 212
Cdd:PRK10241 163 CAHEYTlsnmKFALSILPHDLSIN 186
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 44-156 3.85e-13

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 66.01  E-value: 3.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  44 ESREAVLIDPVL--ETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRSlLPGCQSVISR---------------LS 106
Cdd:cd07743  16 GDKEALLIDSGLdeDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQK-KTGCKVYAPKiekafienpllepsyLG 94

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41327741 107 GA----------------QADLHIEDGDsIRFGRFALETRASPGHTPGCVTfVLNDHSMAFTGDAL 156
Cdd:cd07743  95 GAyppkelrnkflmakpsKVDDIIEEGE-LELGGVGLEIIPLPGHSFGQIG-ILTPDGVLFAGDAL 158
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 38-195 1.78e-12

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: 63.86  E-value: 1.78e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  38 YLLGDREsrEAVLIDPVLETaPRDAQL----IKELGLRLL---YAVNTHCHADHITGSGLLRSLLpGCQSVISRLSGaqa 110
Cdd:cd07725  18 YLLRDGD--ETTLIDTGLAT-EEDAEAlwegLKELGLKPSdidRVLLTHHHPDHIGLAGKLQEKS-GATVYILDVTP--- 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741 111 dlhIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIR----GCGRTDFQQGCAKTLYHSVhEKIFTLP 186
Cdd:cd07725  91 ---VKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLPKitpnVSLWAVRVEDPLGAYLESL-DKLEKLD 166


                ....*....
gi 41327741 187 GDcLIYPAH 195
Cdd:cd07725 167 VD-LAYPGH 174
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 49-143 2.22e-11

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 61.83  E-value: 2.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  49 VLIDpVLETAPRDAQL---IKELGL---RLLYAVNTHCHADHITGSGLLRSLlPGCQSVISR----LSGAQA-------- 110
Cdd:cd16280  34 ILID-ALNNNEAADLIvdgLEKLGLdpaDIKYILITHGHGDHYGGAAYLKDL-YGAKVVMSEadwdMMEEPPeegdnprw 111

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 41327741 111 ------DLHIEDGDSIRFGRFALETRASPGHTPGCVTFV 143
Cdd:cd16280 112 gppperDIVIKDGDTLTLGDTTITVYLTPGHTPGTLSLI 150
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-160 2.39e-11

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 60.97  E-value: 2.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  35 TFTYLLGDREsrEAVLIDPvletAPRDAQLIKEL-----GLRLLYAVNTHCHADHITGSGLLRSLL------PGCQSVIS 103
Cdd:cd16278  18 TNTYLLGAPD--GVVVIDP----GPDDPAHLDALlaalgGGRVSAILVTHTHRDHSPGAARLAERTgapvraFGPHRAGG 91

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 41327741 104 RLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRG 160
Cdd:cd16278  92 QDTDFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVMGWS 148
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 45-146 1.91e-10

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: 59.48  E-value: 1.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  45 SREAVLIDPVLE-TAPRDAQLIKELGLRLL---YAVNTHCHADHITGSGLLR-----SLLPGCQSVISRLSGAQADLH-- 113
Cdd:cd07708  30 PQGNILIDGDMEqNAPMIKANIKKLGFKFSdtkLILISHAHFDHAGGSAEIKkqtgaKVMAGAEDVSLLLSGGSSDFHya 109

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 41327741 114 ---------------IEDGDSIRFGRFALETRASPGHTPGCVTFVLND 146
Cdd:cd07708 110 ndsstyfpqstvdraVHDGERVTLGGTVLTAHATPGHTPGCTTWTMTL 157
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 38-195 2.53e-10

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: 58.02  E-value: 2.53e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  38 YLLgdRESREAVLIDPVLETAPRDaQLIKELGLRLLYAVNTHCHADHITG-------------SGLLRSLLPGCQSVIS- 103
Cdd:cd07712  12 YLL--RGRDRALLIDTGLGIGDLK-EYVRTLTDLPLLVVATHGHFDHIGGlhefeevyvhpadAEILAAPDNFETLTWDa 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741 104 ---RLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDAL----LIRGCGRTDFqqgcakTLYH 176
Cdd:cd07712  89 atySVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVydgpLIMDLPHSDL------DDYL 162

                       170       180
                ....*....|....*....|
gi 41327741 177 SVHEKIFTLPGDC-LIYPAH 195
Cdd:cd07712 163 ASLEKLSKLPDEFdKVLPGH 182
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-142 2.42e-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: 2.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  37 TYLLGdrESREAVLIDPVL-ETAPRDAQLIKELGLRLL---YAVNTHCHADHITGSGLLRSlLPGCQSVISR-------- 104
Cdd:cd16310  24 SYLIT--SNHGAILLDGGLeENAALIEQNIKALGFKLSdikIIINTHAHYDHAGGLAQLKA-DTGAKLWASRgdrpalea 100

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 41327741 105 -------------LSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTF 142
Cdd:cd16310 101 gkhigdnitqpapFPAVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTW 151
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 35-195 2.76e-09

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


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 55.23  E-value: 2.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  35 TFTYLLGDRESReaVLID---------PVLETAprdaqLIKELGLRLLYAVNTHCHADHITGSGLLRSLLPGCQSVISRL 105
Cdd:cd07722  18 TNTYLVGTGKRR--ILIDtgegrpsyiPLLKSV-----LDSEGNATISDILLTHWHHDHVGGLPDVLDLLRGPSPRVYKF 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741 106 ---------SGAQADLH-IEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLirGCGRTDFQqgCAKTLY 175
Cdd:cd07722  91 prpeededpDEDGGDIHdLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGDCVL--GHGTAVFE--DLAAYM 166

                       170       180
                ....*....|....*....|
gi 41327741 176 HSVHeKIFTLPGDcLIYPAH 195
Cdd:cd07722 167 ASLK-KLLSLGPG-RIYPGH 184
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 38-160 4.11e-09

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: 54.92  E-value: 4.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  38 YLLGDreSREAVLIDP-VLETAPRDAQLIKELGLR-------LLyavnTHCHADHItGS--------------------- 88
Cdd:cd07721  14 YLIED--DDGLTLIDTgLPGSAKRILKALRELGLSpkdirriLL----THGHIDHI-GSlaalkeapgapvyahereapy 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  89 --GLLRSLLPGCQSVISRLSG------AQADLHIEDGDSIRFGrFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRG 160
Cdd:cd07721  87 leGEKPYPPPVRLGLLGLLSPllpvkpVPVDRTLEDGDTLDLA-GGLRVIHTPGHTPGHISLYLEEDGVLIAGDALVTVG 165
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-145 9.81e-09

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


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 54.25  E-value: 9.81e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  49 VLIDPVLE-TAPRDAQLIKELGLR---LLYAVNTHCHADHITGSGLLRSLlPGCQSVISR------LSGAQADLH----- 113
Cdd:cd16288  34 ILIDTGLEsSAPMIKANIRKLGFKpsdIKILLNSHAHLDHAGGLAALKKL-TGAKLMASAedaallASGGKSDFHygdds 112

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 41327741 114 -----------IEDGDSIRFGRFALETRASPGHTPGCVTFVLN 145
Cdd:cd16288 113 lafppvkvdrvLKDGDRVTLGGTTLTAHLTPGHTRGCTTWTMT 155
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 ...
 49-141 3.41e-08

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: 52.74  E-value: 3.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  49 VLIDPVLE-TAPRDAQLIKELGLRL---LYAVNTHCHADHITGSGLLRSLlPGCQsVISRLSGAQA-------------- 110
Cdd:cd16290  34 ILIDGALPqSAPQIEANIRALGFRLedvKLILNSHAHFDHAGGIAALQRD-SGAT-VAASPAGAAAlrsggvdpddpqag 111

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 41327741 111 ----------DLHIEDGDSIRFGRFALETRASPGHTPGCVT 141
Cdd:cd16290 112 aadpfppvakVRVVADGEVVKLGPLAVTAHATPGHTPGGTS 152
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 37-162 4.61e-08

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 52.11  E-value: 4.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  37 TYLLgdRESREAVLIDP-VLETAPRDAQLIKELGLRLL---YAVNTHCHADHITGSGLLRSLLPGCQSVI---------- 102
Cdd:cd07726  18 SYLL--DGEGRPALIDTgPSSSVPRLLAALEALGIAPEdvdYIILTHIHLDHAGGAGLLAEALPNAKVYVhprgarhlid 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741 103 -SRL-------SGAQADLH--------------IEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRG 160
Cdd:cd07726  96 pSKLwasaravYGDEADRLggeilpvpeervivLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDAAGVRY 175


                ..
gi 41327741 161 CG 162
Cdd:cd07726 176 PE 177
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-144 1.47e-07

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


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 50.95  E-value: 1.47e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  49 VLIDPVL-ETAPRDAQLIKELGLR---LLYAVNTHCHADHITGSGLLRSLlPGCQSVISRL-----------SGAQADLH 113
Cdd:cd16309  34 ILIDGAMpQSTPLIKDNIKKLGFDvkdVKYLLNTHAHFDHAGGLAELKKA-TGAQLVASAAdkpllesgyvgSGDTKNLQ 112

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 41327741 114 ---------IEDGDSIRFGRFALETRASPGHTPGCVTFVL 144
Cdd:cd16309 113 fppvrvdrvIGDGDKVTLGGTTLTAHLTPGHSPGCTSWTT 152
B3_Acin_new1 NF033184
putative subclass B3 metallo-beta-lactamase; This is one of two families of putative ...
 37-142 1.53e-07

putative subclass B3 metallo-beta-lactamase; This is one of two families of putative metallo-beta-lactamases of subclass B3 that are restricted to the genus Acinetobacter, and undescribed as of January 2017.


Pssm-ID: 439394  Cd Length: 283  Bit Score: 51.26  E-value: 1.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741   37 TYLLGdrESREAVLIDPVL-ETAPRDAQLIKELGLRLL---YAVNTHCHADHI---------TGSGLL------RSLLPG 97
Cdd:NF033184  51 AYLLA--SGHQALLIDTGLpENTEQIEQNIKQLGFKLSdvkIMVTSHAHWDHVgalarikqdTGAKLIamqqdvKALEIG 128

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 41327741   98 -------CQSVisRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTF 142
Cdd:NF033184 129 kpigentFQTI--PFTPVKVDKVIHDGEVVKLGKFKLKATLTPGHTPGCTTW 178
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-193 4.72e-07

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: 49.27  E-value: 4.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  49 VLIDP-VLETAPRDAQLIKELGLRLL---YAVNTHCHADHITGSGLLRSL-------LPGCQSVISR------------- 104
Cdd:cd16315  34 VLIDSgTEEAAPLVLANIRKLGFDPKdvrWLLSSHEHFDHVGGLAALQRAtgarvaaSAAAAPVLESgkpapddpqaglh 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741 105 --LSGAQADLHIEDGDSIRFGRFALETRASPGHTPG-------------CVTFVLNDHSMAFTGDALliRGCGRTDFQQG 169
Cdd:cd16315 114 epFPPVRVDRIVEDGDTVALGSLRLTAHATPGHTPGalswtwrscegadCRTIVYADSLSPVSADGY--RFSDHPDYVAA 191

                       170       180
                ....*....|....*....|....
gi 41327741 170 CAKTLyhsvhEKIFTLPGDCLIYP 193
Cdd:cd16315 192 YRAGL-----AKVAALPCDILLTP 210
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-160 3.36e-05

Fluoribacter gormanii FEZ-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 FEZ-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: 293865  Cd Length: 255  Bit Score: 43.97  E-value: 3.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  49 VLIDPVLETA-PRDAQLIKELGLRLL---YAVNTHCHADHITGSGLLRSL-------LPGCQSVIsrLSGAQADLH---- 113
Cdd:cd16307  34 ILINSNLESSvPQIKASIEKLGFKFSdtkILLISHAHFDHAAGSALIKREthakymvMDGDVDVV--ESGGKSDFFygnd 111

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741 114 -------------IEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRG 160
Cdd:cd16307 112 pstyfppahvdkvLHDGEQVELGGTVLTAHLTAGHTKGCTTWTMKVKDHGKTYDVVIVGS 171
VIM_type_MBL-B1 cd16303
VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona ...
 43-164 7.27e-05

VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona integron-encoded metallo-beta-lactamase)-type MBLs are integron-associated and are widely distributed acquired MBLs. 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 being most closely related to each other. This subgroup of VIM-type MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293861 [Multi-domain]  Cd Length: 218  Bit Score: 42.54  E-value: 7.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  43 RESREAVLIDPV---LETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRS------LLPGCQSVISRLSGAQADLH 113
Cdd:cd16303  34 RDGDELLLIDTAwgaKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLRAagvatyASPSTRRLAEAEGNEIPTHS 113

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41327741 114 IED----GDSIRFGRFALeTRASPGHTPGCVTFVLNDHSMAFTGDAllIRGCGRT 164
Cdd:cd16303 114 LEGlsssGDAVRFGPVEL-FYPGAAHSTDNLVVYVPSARVLYGGCA--VRELSST 165
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 27-97 1.13e-03

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


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 39.02  E-value: 1.13e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41327741  27 QMFEPVSCTFTYllGDREsreAVLIDPVLETAprDAQ----LIKELGLRLLYAVNTHCHADHITGSGLLRSLLPG 97
Cdd:cd07739  11 ISSFPVTSTLIY--GETE---AVLVDAQFTRA--DAErladWIKASGKTLTTIYITHGHPDHYFGLEVLLEAFPD 78
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
78-154 2.09e-03

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 38.64  E-value: 2.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  78 THCHADHITG-SGLLRSLL-------------PGCQSVISRLSGAQA-------DLH-IEDGDSIRFGRFALETRASPgH 135
Cdd:COG1234  59 THLHGDHIAGlPGLLSTRSlagrekpltiygpPGTKEFLEALLKASGtdldfplEFHeIEPGEVFEIGGFTVTAFPLD-H 137

                        90       100
                ....*....|....*....|.
gi 41327741 136 TPGCV--TFVLNDHSMAFTGD 154
Cdd:COG1234 138 PVPAYgyRFEEPGRSLVYSGD 158
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 47-154 6.51e-03

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 37.18  E-value: 6.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327741  47 EAVLIDpvletAPRDA-QLIKELGLR------LLYavnTHCHADHITGSGLLRSLLPGCQ-----------------SVI 102
Cdd:COG1235  45 TRLLID-----AGPDLrEQLLRLGLDpskidaILL---THEHADHIAGLDDLRPRYGPNPipvyatpgtlealerrfPYL 116

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 41327741 103 SRLSGAQADLH-IEDGDSIRFGRFALETRASPGHTPGCVTFVL--NDHSMAFTGD 154
Cdd:COG1235 117 FAPYPGKLEFHeIEPGEPFEIGGLTVTPFPVPHDAGDPVGYRIedGGKKLAYATD 171
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH