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Conserved domains on  [gi|957950905|gb|ALQ34024|]
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ethylmalonic encephalopathy 1 isoform 2, partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02962 super family cl30130
hydroxyacylglutathione hydrolase
 13-243 6.83e-115

hydroxyacylglutathione hydrolase


The actual alignment was detected with superfamily member PLN02962:

Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 329.07  E-value: 6.83e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  13 LSQRGGSGAPILLRQMFEPVSCTFTYLLGD--RESREAVLIDPVLETAPRDAQLIKELGLRLLYA-----------GSGL 79
Cdd:PLN02962   1 SSSSSSSSSKLLFRQLFEKESSTYTYLLADvsHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAmnthvhadhvtGTGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  80 LRSLLPGCQSVISRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHS------MAFTGDALLIRGCGRT 153
Cdd:PLN02962  81 LKTKLPGVKSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPdqpqprMAFTGDALLIRGCGRT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905 154 DFQQGCAKTLYHSVHEKIFTLPGDCLIYPAHDYHGFTVSTVEEERTLNPRLTLSCEEFVKIMGNLNLPKPQQIDFAVPAN 233
Cdd:PLN02962 161 DFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPAN 240

                        250
                 ....*....|
gi 957950905 234 MRCGVQTPTA 243
Cdd:PLN02962 241 MVCGLQDPPA 250
 
Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 13-243 6.83e-115

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 329.07  E-value: 6.83e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  13 LSQRGGSGAPILLRQMFEPVSCTFTYLLGD--RESREAVLIDPVLETAPRDAQLIKELGLRLLYA-----------GSGL 79
Cdd:PLN02962   1 SSSSSSSSSKLLFRQLFEKESSTYTYLLADvsHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAmnthvhadhvtGTGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  80 LRSLLPGCQSVISRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHS------MAFTGDALLIRGCGRT 153
Cdd:PLN02962  81 LKTKLPGVKSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPdqpqprMAFTGDALLIRGCGRT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905 154 DFQQGCAKTLYHSVHEKIFTLPGDCLIYPAHDYHGFTVSTVEEERTLNPRLTLSCEEFVKIMGNLNLPKPQQIDFAVPAN 233
Cdd:PLN02962 161 DFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPAN 240

                        250
                 ....*....|
gi 957950905 234 MRCGVQTPTA 243
Cdd:PLN02962 241 MVCGLQDPPA 250
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 24-186 7.71e-71

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: 214.57  E-value: 7.71e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  24 LLRQMFEPVSCTFTYLLGDRESREAVLIDPVLETAPRDAQLIKELGLRLLYA-----------GSGLLRSLLpGCQSVIS 92
Cdd:cd07724    1 IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRDSVDRYLDLAAELGLKITYVlethvhadhvsGARELAERT-GAPIVIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  93 RLSGA-QADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQ---GCAKTLYHSVH 168
Cdd:cd07724   80 EGAPAsFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPGeaeGLARQLYDSLQ 159

                        170
                 ....*....|....*...
gi 957950905 169 EKIFTLPGDCLIYPAHDY 186
Cdd:cd07724  160 RKLLLLPDETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 35-186 1.39e-26

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: 102.08  E-value: 1.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  35 TFTYLLGDreSREAVLIDPVLETAPRDA--QLIKELGLRLLY-----------AGSGLLRSLLpGCQSVISR-------- 93
Cdd:COG0491   15 VNSYLIVG--GDGAVLIDTGLGPADAEAllAALAALGLDIKAvllthlhpdhvGGLAALAEAF-GAPVYAHAaeaealea 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  94 --------LSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQGCAKTLYH 165
Cdd:COG0491   92 paagalfgREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLPDGDLAQWLA 171

                        170       180
                 ....*....|....*....|.
gi 957950905 166 SVhEKIFTLPGDcLIYPAHDY 186
Cdd:COG0491  172 SL-ERLLALPPD-LVIPGHGP 190
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 92-186 1.72e-17

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: 78.73  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905   92 SRLSGAqaDLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTdFqQGCAKTLYHSVhEKI 171
Cdd:TIGR03413  77 ERIPGI--THPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRL-F-EGTPEQMYDSL-QRL 151

                          90
                  ....*....|....*
gi 957950905  172 FTLPGDCLIYPAHDY 186
Cdd:TIGR03413 152 AALPDDTLVYCAHEY 166
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 37-184 6.39e-17

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: 75.67  E-value: 6.39e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905    37 TYLLGDREsrEAVLIDPVLETAPRDAQLIKELGLR---------------------------LLYAGSG---LLRSLLPG 86
Cdd:smart00849   2 SYLVRDDG--GAILIDTGPGEAEDLLAELKKLGPKkidaiilthghpdhigglpelleapgaPVYAPEGtaeLLKDLLAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905    87 CQSVISRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQG-CAKTLYH 165
Cdd:smart00849  80 LGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGdAAASDAL 159

                          170
                   ....*....|....*....
gi 957950905   166 SVHEKIFTLPGDcLIYPAH 184
Cdd:smart00849 160 ESLLKLLKLLPK-LVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
103-184 1.43e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 58.92  E-value: 1.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  103 IEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQGCAKTLYHSVHE-------KIFTLP 175
Cdd:pfam00753 109 LEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPLGGLLVLHPSSAEsslesllKLAKLK 188


                  ....*....
gi 957950905  176 GDcLIYPAH 184
Cdd:pfam00753 189 AA-VIVPGH 196
B3_Acin_new1 NF033184
putative subclass B3 metallo-beta-lactamase; This is one of two families of putative ...
 98-131 2.68e-04

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: 41.25  E-value: 2.68e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 957950905  98 QADLHIEDGDSIRFGRFALETRASPGHTPGCVTF 131
Cdd:NF033184 145 KVDKVIHDGEVVKLGKFKLKATLTPGHTPGCTTW 178
 
Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 13-243 6.83e-115

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 329.07  E-value: 6.83e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  13 LSQRGGSGAPILLRQMFEPVSCTFTYLLGD--RESREAVLIDPVLETAPRDAQLIKELGLRLLYA-----------GSGL 79
Cdd:PLN02962   1 SSSSSSSSSKLLFRQLFEKESSTYTYLLADvsHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAmnthvhadhvtGTGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  80 LRSLLPGCQSVISRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHS------MAFTGDALLIRGCGRT 153
Cdd:PLN02962  81 LKTKLPGVKSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPdqpqprMAFTGDALLIRGCGRT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905 154 DFQQGCAKTLYHSVHEKIFTLPGDCLIYPAHDYHGFTVSTVEEERTLNPRLTLSCEEFVKIMGNLNLPKPQQIDFAVPAN 233
Cdd:PLN02962 161 DFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPAN 240

                        250
                 ....*....|
gi 957950905 234 MRCGVQTPTA 243
Cdd:PLN02962 241 MVCGLQDPPA 250
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 24-186 7.71e-71

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: 214.57  E-value: 7.71e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  24 LLRQMFEPVSCTFTYLLGDRESREAVLIDPVLETAPRDAQLIKELGLRLLYA-----------GSGLLRSLLpGCQSVIS 92
Cdd:cd07724    1 IFRQFFDPGLGTLSYLVGDPETGEAAVIDPVRDSVDRYLDLAAELGLKITYVlethvhadhvsGARELAERT-GAPIVIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  93 RLSGA-QADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQ---GCAKTLYHSVH 168
Cdd:cd07724   80 EGAPAsFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPGeaeGLARQLYDSLQ 159

                        170
                 ....*....|....*...
gi 957950905 169 EKIFTLPGDCLIYPAHDY 186
Cdd:cd07724  160 RKLLLLPDETLVYPGHDY 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 37-184 6.69e-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: 115.46  E-value: 6.69e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  37 TYLLGDrESREAVLIDPVLETAPRDAQLIKELGLRLLY-----------AGSGLLRSLlPGCQSVISR------------ 93
Cdd:cd06262   12 CYLVSD-EEGEAILIDPGAGALEKILEAIEELGLKIKAillthghfdhiGGLAELKEA-PGAPVYIHEadaelledpeln 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  94 --------LSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQGCAKTLYH 165
Cdd:cd06262   90 laffgggpLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDLPGGDPEQLIE 169

                        170
                 ....*....|....*....
gi 957950905 166 SVHEKIFTLPGDCLIYPAH 184
Cdd:cd06262  170 SIKKLLLLLPDDTVVYPGH 188
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 36-184 1.43e-29

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: 108.70  E-value: 1.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  36 FTYLLGDRESREAVLIDPVletaprDAQLI----KELGLRLLY-----------AGSGLLRSLLPGCQsVI----SRLSG 96
Cdd:cd07723   10 YIYLIVDEATGEAAVVDPG------EAEPVlaalEKNGLTLTAiltthhhwdhtGGNAELKALFPDAP-VYgpaeDRIPG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  97 AqaDLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRtdFQQGCAKTLYHSvHEKIFTLPG 176
Cdd:cd07723   83 L--DHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGR--FFEGTAEQMYAS-LQKLLALPD 157


                 ....*...
gi 957950905 177 DCLIYPAH 184
Cdd:cd07723  158 DTLVYCGH 165
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 36-184 1.18e-28

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: 106.47  E-value: 1.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  36 FTYLLGDRESREAVLIDPV--LETAprdAQLIKELGLRLlyAGS----------GLLRSLL--PGCQSVISR----LSGA 97
Cdd:cd16275   13 YSYIIIDKATREAAVVDPAwdIEKI---LAKLNELGLTL--TGIllthshfdhvNLVEPLLakYDAPVYMSKeeidYYGF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  98 QA-DLH-IEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHsmAFTGDALLIRGCGRTDFQQGCAKTLYHSVHEKIFTLP 175
Cdd:cd16275   88 RCpNLIpLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGDS--LFTGDTLFIEGCGRCDLPGGDPEEMYESLQRLKKLPP 165


                 ....*....
gi 957950905 176 GDCLIYPAH 184
Cdd:cd16275  166 PNTRVYPGH 174
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 35-186 1.39e-26

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: 102.08  E-value: 1.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  35 TFTYLLGDreSREAVLIDPVLETAPRDA--QLIKELGLRLLY-----------AGSGLLRSLLpGCQSVISR-------- 93
Cdd:COG0491   15 VNSYLIVG--GDGAVLIDTGLGPADAEAllAALAALGLDIKAvllthlhpdhvGGLAALAEAF-GAPVYAHAaeaealea 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  94 --------LSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQGCAKTLYH 165
Cdd:COG0491   92 paagalfgREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDLPDGDLAQWLA 171

                        170       180
                 ....*....|....*....|.
gi 957950905 166 SVhEKIFTLPGDcLIYPAHDY 186
Cdd:COG0491  172 SL-ERLLALPPD-LVIPGHGP 190
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 37-204 5.01e-22

uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 90.10  E-value: 5.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  37 TYLLGDRESREAVLIDPVLEtAPRDAQLIKELGLRLLY-----------AGSGLLRsLLPGCQSVISRL---------SG 96
Cdd:cd16322   13 TYLVADEGGGEAVLVDPGDE-SEKLLARFGTTGLTLLYillthahfdhvGGVADLR-RHPGAPVYLHPDdlplyeaadLG 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  97 AQA-----------DLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFqQGCAKTLYH 165
Cdd:cd16322   91 AKAfglgieplpppDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRTDL-PGGDPKAMA 169

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 957950905 166 SVHEKIFTLPGDCLIYPAHDyhgfTVSTVEEERTLNPRL 204
Cdd:cd16322  170 ASLRRLLTLPDETRVFPGHG----PPTTLGEERRTNPFL 204
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 34-184 3.90e-19

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: 81.83  E-value: 3.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  34 CTftyLLGDRESREAVLIDPVLEtAPRDAQLIKELGLRL---------------------LYA----GSG-----LLRSL 83
Cdd:cd07737   13 CS---LIWCEETKEAAVIDPGGD-ADKILQAIEDLGLTLkkillthghldhvggaaelaeHYGvpiiGPHkedkfLLENL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  84 LPgcQSVISRLSGAQA---DLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQGCA 160
Cdd:cd07737   89 PE--QSQMFGFPPAEAftpDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTDFPGGNH 166

                        170       180
                 ....*....|....*....|....
gi 957950905 161 KTLYHSVHEKIFTLPGDCLIYPAH 184
Cdd:cd07737  167 AQLIASIKEKLLPLGDDVTFIPGH 190
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 92-186 1.72e-17

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: 78.73  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905   92 SRLSGAqaDLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTdFqQGCAKTLYHSVhEKI 171
Cdd:TIGR03413  77 ERIPGI--THPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRL-F-EGTPEQMYDSL-QRL 151

                          90
                  ....*....|....*
gi 957950905  172 FTLPGDCLIYPAHDY 186
Cdd:TIGR03413 152 AALPDDTLVYCAHEY 166
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 37-184 6.39e-17

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: 75.67  E-value: 6.39e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905    37 TYLLGDREsrEAVLIDPVLETAPRDAQLIKELGLR---------------------------LLYAGSG---LLRSLLPG 86
Cdd:smart00849   2 SYLVRDDG--GAILIDTGPGEAEDLLAELKKLGPKkidaiilthghpdhigglpelleapgaPVYAPEGtaeLLKDLLAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905    87 CQSVISRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQG-CAKTLYH 165
Cdd:smart00849  80 LGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGdAAASDAL 159

                          170
                   ....*....|....*....
gi 957950905   166 SVHEKIFTLPGDcLIYPAH 184
Cdd:smart00849 160 ESLLKLLKLLPK-LVVPGH 177
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 31-202 1.64e-13

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 67.86  E-value: 1.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  31 PVSC---TFTYLLGDRESREAVLIDPVLETAPRDAQLIKELGLRLL--------YAGSGL-LRSLLPGCQSVISRLSGAQ 98
Cdd:PLN02469   5 PVPCledNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVltthhhwdHAGGNEkIKKLVPGIKVYGGSLDNVK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  99 ADLH-IEDGDSIRFGR----FALETrasPGHTPGCVTFVL----NDHSMAFTGDALLIRGCGRtdFQQGCAKTLYHSVHE 169
Cdd:PLN02469  85 GCTHpVENGDKLSLGKdvniLALHT---PCHTKGHISYYVtgkeGEDPAVFTGDTLFIAGCGK--FFEGTAEQMYQSLCV 159

                        170       180       190
                 ....*....|....*....|....*....|...
gi 957950905 170 KIFTLPGDCLIYPAHDYhgfTVSTVEEERTLNP 202
Cdd:PLN02469 160 TLGSLPKPTQVYCGHEY---TVKNLKFALTVEP 189
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
103-184 1.43e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 58.92  E-value: 1.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  103 IEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQGCAKTLYHSVHE-------KIFTLP 175
Cdd:pfam00753 109 LEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPLGGLLVLHPSSAEsslesllKLAKLK 188


                  ....*....
gi 957950905  176 GDcLIYPAH 184
Cdd:pfam00753 189 AA-VIVPGH 196
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 103-201 9.47e-10

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 57.14  E-value: 9.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905 103 IEDGDSIRFGRFALETRASPGHTPGCVTFVlnDHSMAFTGDALLIRGCGRtdFQQGCAKTLYHSVhEKIFTLPGDCLIYP 182
Cdd:PRK10241  89 VKDGETAFVLGHEFSVFATPGHTLGHICYF--SKPYLFCGDTLFSGGCGR--LFEGTASQMYQSL-KKINALPDDTLICC 163

                         90       100
                 ....*....|....*....|...
gi 957950905 183 AHDYH----GFTVSTVEEERTLN 201
Cdd:PRK10241 164 AHEYTlsnmKFALSILPHDLSIN 186
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 76-186 5.93e-08

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 52.54  E-value: 5.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  76 GSGLLRSLLPGCqsvisrlsgaqaDLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRtdF 155
Cdd:PLN02398 151 GSAVDKDRIPGI------------DIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGK--L 216

                         90       100       110
                 ....*....|....*....|....*....|.
gi 957950905 156 QQGCAKTLYHSVhEKIFTLPGDCLIYPAHDY 186
Cdd:PLN02398 217 FEGTPEQMLSSL-QKIISLPDDTNIYCGHEY 246
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 100-132 4.76e-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: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 49.12  E-value: 4.76e-07
                         10        20        30
                 ....*....|....*....|....*....|...
gi 957950905 100 DLHIEDGDSIRFGRFALETRASPGHTPGCVTFV 132
Cdd:cd16280  118 DIVIKDGDTLTLGDTTITVYLTPGHTPGTLSLI 150
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 98-149 5.72e-07

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: 48.76  E-value: 5.72e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 957950905  98 QADLHIEDGDSIRFGrFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRG 149
Cdd:cd07721  115 PVDRTLEDGDTLDLA-GGLRVIHTPGHTPGHISLYLEEDGVLIAGDALVTVG 165
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 103-184 3.62e-06

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: 46.14  E-value: 3.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905 103 IEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIR----GCGRTDFQQGCAKTLYHSVhEKIFTLPGDc 178
Cdd:cd07725   91 VKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLPKitpnVSLWAVRVEDPLGAYLESL-DKLEKLDVD- 168


                 ....*.
gi 957950905 179 LIYPAH 184
Cdd:cd07725  169 LAYPGH 174
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 103-184 5.45e-06

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: 45.31  E-value: 5.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905 103 IEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDAL----LIRGCGRTDFqqgcakTLYHSVHEKIFTLPGDC 178
Cdd:cd07712  102 LRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVydgpLIMDLPHSDL------DDYLASLEKLSKLPDEF 175


                 ....*..
gi 957950905 179 -LIYPAH 184
Cdd:cd07712  176 dKVLPGH 182
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-149 1.80e-05

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 44.02  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  35 TFTYLLGDREsrEAVLIDPvletAPRDAQLIKELgLRLLYAG--------------SGLLRSLlpgcqsviSRLSGA--- 97
Cdd:cd16278   18 TNTYLLGAPD--GVVVIDP----GPDDPAHLDAL-LAALGGGrvsailvththrdhSPGAARL--------AERTGApvr 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 957950905  98 --------------QADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRG 149
Cdd:cd16278   83 afgphraggqdtdfAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVMGWS 148
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 90-182 1.08e-04

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: 42.34  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905  90 VISRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPG-------------CVTFVLNDHSMAFTGDALliRGCGRTDFQ 156
Cdd:cd16315  112 LHEPFPPVRVDRIVEDGDTVALGSLRLTAHATPGHTPGalswtwrscegadCRTIVYADSLSPVSADGY--RFSDHPDYV 189

                         90       100
                 ....*....|....*....|....*.
gi 957950905 157 QGCAKTLyhsvhEKIFTLPGDCLIYP 182
Cdd:cd16315  190 AAYRAGL-----AKVAALPCDILLTP 210
B3_Acin_new1 NF033184
putative subclass B3 metallo-beta-lactamase; This is one of two families of putative ...
 98-131 2.68e-04

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: 41.25  E-value: 2.68e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 957950905  98 QADLHIEDGDSIRFGRFALETRASPGHTPGCVTF 131
Cdd:NF033184 145 KVDKVIHDGEVVKLGKFKLKATLTPGHTPGCTTW 178
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 96-135 8.30e-04

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: 39.45  E-value: 8.30e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 957950905  96 GAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLND 135
Cdd:cd07708  118 QSTVDRAVHDGERVTLGGTVLTAHATPGHTPGCTTWTMTL 157
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 98-134 1.00e-03

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: 39.23  E-value: 1.00e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 957950905  98 QADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLN 134
Cdd:cd16288  119 KVDRVLKDGDRVTLGGTTLTAHLTPGHTRGCTTWTMT 155
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 100-133 1.88e-03

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: 38.62  E-value: 1.88e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 957950905 100 DLHIEDGDSIRFGRFALETRASPGHTPGCVTFVL 133
Cdd:cd16309  119 DRVIGDGDKVTLGGTTLTAHLTPGHSPGCTSWTT 152
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 ...
 103-130 2.47e-03

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: 38.10  E-value: 2.47e-03
                         10        20
                 ....*....|....*....|....*...
gi 957950905 103 IEDGDSIRFGRFALETRASPGHTPGCVT 130
Cdd:cd16290  125 VADGEVVKLGPLAVTAHATPGHTPGGTS 152
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 97-131 4.39e-03

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: 37.43  E-value: 4.39e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 957950905  97 AQADLHIEDGDSIRFGRFALETRASPGHTPGCVTF 131
Cdd:cd16310  117 VKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTW 151
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 102-184 5.09e-03

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: 36.74  E-value: 5.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 957950905 102 HIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLirGCGRTDFQqgCAKTLYHSVHeKIFTLPGDcLIY 181
Cdd:cd07722  108 DLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEENALFTGDCVL--GHGTAVFE--DLAAYMASLK-KLLSLGPG-RIY 181


                 ...
gi 957950905 182 PAH 184
Cdd:cd07722  182 PGH 184
 
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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