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Conserved domains on  [gi|731409215|ref|XP_002279121|]
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persulfide dioxygenase ETHE1 homolog, mitochondrial [Vitis vinifera]

Protein Classification

PLN02962 family protein( domain architecture ID 11477331)

PLN02962 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
36-286 0e+00

hydroxyacylglutathione hydrolase


:

Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 544.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  36 STSFGQSSKKLLFRQLFEQESSTYTYLLADVSHPDKPALLIDPVDKKVERDLSLVKELGLKLIYAMNTHVHADHVTGTGL 115
Cdd:PLN02962   1 SSSSSSSSSKLLFRQLFEKESSTYTYLLADVSHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 116 IKTKVPGVKSIISKMSKSKADLLVENGDKIYFGDLYLEVRATPGHTIGCVTYVTGDAPDQPEPRMAFTGDALLIRGCGRT 195
Cdd:PLN02962  81 LKTKLPGVKSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPDQPQPRMAFTGDALLIRGCGRT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 196 DFQGGCSHQLYNSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKDIMENLNLSYPKMIDLAVPAN 275
Cdd:PLN02962 161 DFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPAN 240
                        250
                 ....*....|.
gi 731409215 276 MVCGLQDLSAK 286
Cdd:PLN02962 241 MVCGLQDPPAK 251
 
Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
36-286 0e+00

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 544.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  36 STSFGQSSKKLLFRQLFEQESSTYTYLLADVSHPDKPALLIDPVDKKVERDLSLVKELGLKLIYAMNTHVHADHVTGTGL 115
Cdd:PLN02962   1 SSSSSSSSSKLLFRQLFEKESSTYTYLLADVSHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 116 IKTKVPGVKSIISKMSKSKADLLVENGDKIYFGDLYLEVRATPGHTIGCVTYVTGDAPDQPEPRMAFTGDALLIRGCGRT 195
Cdd:PLN02962  81 LKTKLPGVKSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPDQPQPRMAFTGDALLIRGCGRT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 196 DFQGGCSHQLYNSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKDIMENLNLSYPKMIDLAVPAN 275
Cdd:PLN02962 161 DFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPAN 240
                        250
                 ....*....|.
gi 731409215 276 MVCGLQDLSAK 286
Cdd:PLN02962 241 MVCGLQDPPAK 251
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
47-228 4.67e-76

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: 229.59  E-value: 4.67e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  47 LFRQLFEQESSTYTYLLADVShpDKPALLIDPVDKKVERDLSLVKELGLKLIYAMNTHVHADHVTGTGLIKTKvPGVKSI 126
Cdd:cd07724    1 IFRQFFDPGLGTLSYLVGDPE--TGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAER-TGAPIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 127 ISKMSK-SKADLLVENGDKIYFGDLYLEVRATPGHTIGCVTYVTGDapdqpePRMAFTGDALLIRGCGRTDFQG---GCS 202
Cdd:cd07724   78 IGEGAPaSFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGD------PDAVFTGDTLFVGDVGRPDLPGeaeGLA 151
                        170       180
                 ....*....|....*....|....*.
gi 731409215 203 HQLYNSVHSQIFTLPKDTLIYPAHDY 228
Cdd:cd07724  152 RQLYDSLQRKLLLLPDETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
47-228 6.32e-34

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: 122.88  E-value: 6.32e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  47 LFRQLFEQESSTYTYLLADvshpDKPALLIDPV--DKKVERDLSLVKELGLKLIYAMNTHVHADHVTGTGLIKTKVpGVK 124
Cdd:COG0491    4 LPGGTPGAGLGVNSYLIVG----GDGAVLIDTGlgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 125 SIISK----------------MSKSKADLLVENGDKIYFGDLYLEVRATPGHTIGCVTYVTgdapdqPEPRMAFTGDALL 188
Cdd:COG0491   79 VYAHAaeaealeapaagalfgREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV------PDEKVLFTGDALF 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 731409215 189 IRGCGRTDFQGGCSHQLYNSVHsQIFTLPkDTLIYPAHDY 228
Cdd:COG0491  153 SGGVGRPDLPDGDLAQWLASLE-RLLALP-PDLVIPGHGP 190
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
59-226 1.17e-23

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: 94.54  E-value: 1.17e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215    59 YTYLLADvshpDKPALLIDPVDKKVERDLSLVKELGL-KLIYAMNTHVHADHVTGTGLIKtKVPGVKSIISKMSK----- 132
Cdd:smart00849   1 NSYLVRD----DGGAILIDTGPGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELL-EAPGAPVYAPEGTAellkd 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215   133 --------------SKADLLVENGDKIYFGDLYLEVRATPGHTIGCVTYVTgdapdqPEPRMAFTGDALLIRGCGRTDFQ 198
Cdd:smart00849  76 llallgelgaeaepAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL------PEGKILFTGDLLFAGGDGRTLVD 149
                          170       180
                   ....*....|....*....|....*....
gi 731409215   199 GGcSHQLYNSVHSQI-FTLPKDTLIYPAH 226
Cdd:smart00849 150 GG-DAAASDALESLLkLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
57-226 1.83e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 73.17  E-value: 1.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215   57 STYTYLLADvshpDKPALLIDP---VDKKVERDLSLVKELGLKLIYAMNTHVHADHVTGTGLIK--TKVPGV-------- 123
Cdd:pfam00753   5 QVNSYLIEG----GGGAVLIDTggsAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAeaTDVPVIvvaeeare 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  124 -------------KSIISKMSKSKADLLVENGDKIYFGDLYLEVRATPGHTIGCVTYVTGDApdqpepRMAFTGDALLIR 190
Cdd:pfam00753  81 lldeelglaasrlGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGG------KVLFTGDLLFAG 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 731409215  191 GCGRTDFQGGCSHQLYNSVHSQ------IFTLPKDTLIYPAH 226
Cdd:pfam00753 155 EIGRLDLPLGGLLVLHPSSAESslesllKLAKLKAAVIVPGH 196
 
Name Accession Description Interval E-value
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
36-286 0e+00

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 544.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  36 STSFGQSSKKLLFRQLFEQESSTYTYLLADVSHPDKPALLIDPVDKKVERDLSLVKELGLKLIYAMNTHVHADHVTGTGL 115
Cdd:PLN02962   1 SSSSSSSSSKLLFRQLFEKESSTYTYLLADVSHPDKPALLIDPVDKTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 116 IKTKVPGVKSIISKMSKSKADLLVENGDKIYFGDLYLEVRATPGHTIGCVTYVTGDAPDQPEPRMAFTGDALLIRGCGRT 195
Cdd:PLN02962  81 LKTKLPGVKSIISKASGSKADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPDQPQPRMAFTGDALLIRGCGRT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 196 DFQGGCSHQLYNSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKDIMENLNLSYPKMIDLAVPAN 275
Cdd:PLN02962 161 DFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDYKGFTVSTVGEEMLYNPRLTKDEETFKTIMENLNLPYPKMIDVAVPAN 240
                        250
                 ....*....|.
gi 731409215 276 MVCGLQDLSAK 286
Cdd:PLN02962 241 MVCGLQDPPAK 251
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
47-228 4.67e-76

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: 229.59  E-value: 4.67e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  47 LFRQLFEQESSTYTYLLADVShpDKPALLIDPVDKKVERDLSLVKELGLKLIYAMNTHVHADHVTGTGLIKTKvPGVKSI 126
Cdd:cd07724    1 IFRQFFDPGLGTLSYLVGDPE--TGEAAVIDPVRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAER-TGAPIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 127 ISKMSK-SKADLLVENGDKIYFGDLYLEVRATPGHTIGCVTYVTGDapdqpePRMAFTGDALLIRGCGRTDFQG---GCS 202
Cdd:cd07724   78 IGEGAPaSFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGD------PDAVFTGDTLFVGDVGRPDLPGeaeGLA 151
                        170       180
                 ....*....|....*....|....*.
gi 731409215 203 HQLYNSVHSQIFTLPKDTLIYPAHDY 228
Cdd:cd07724  152 RQLYDSLQRKLLLLPDETLVYPGHDY 177
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
59-226 3.51e-39

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: 134.90  E-value: 3.51e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  59 YTYLLADvsHPDKPALLIDPVD-KKVerdLSLVKELGLKLIYAMNTHVHADHVTGTGLIKTKVPGVKSIISKMSK-SKAD 136
Cdd:cd07723   10 YIYLIVD--EATGEAAVVDPGEaEPV---LAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAEDRiPGLD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 137 LLVENGDKIYFGDLYLEVRATPGHTIGCVTYVTGDAPdqpeprMAFTGDALLIRGCGRTdFQGGCShQLYNSvHSQIFTL 216
Cdd:cd07723   85 HPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEP------ALFTGDTLFSGGCGRF-FEGTAE-QMYAS-LQKLLAL 155
                        170
                 ....*....|
gi 731409215 217 PKDTLIYPAH 226
Cdd:cd07723  156 PDDTLVYCGH 165
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
57-226 3.78e-38

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: 132.79  E-value: 3.78e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  57 STYTYLLADvshPDKPALLIDPVDKKVERDLSLVKELGLKLIYAMNTHVHADHVTGTGLIKtKVPGVKSIISK------- 129
Cdd:cd06262    9 QTNCYLVSD---EEGEAILIDPGAGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELK-EAPGAPVYIHEadaelle 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 130 -------------MSKSKADLLVENGDKIYFGDLYLEVRATPGHTIGCVTYVTgdapdqPEPRMAFTGDALLIRGCGRTD 196
Cdd:cd06262   85 dpelnlaffgggpLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYI------EEEGVLFTGDTLFAGSIGRTD 158
                        170       180       190
                 ....*....|....*....|....*....|
gi 731409215 197 FQGGCSHQLYNSVHSQIFTLPKDTLIYPAH 226
Cdd:cd06262  159 LPGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
47-228 6.32e-34

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: 122.88  E-value: 6.32e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  47 LFRQLFEQESSTYTYLLADvshpDKPALLIDPV--DKKVERDLSLVKELGLKLIYAMNTHVHADHVTGTGLIKTKVpGVK 124
Cdd:COG0491    4 LPGGTPGAGLGVNSYLIVG----GDGAVLIDTGlgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 125 SIISK----------------MSKSKADLLVENGDKIYFGDLYLEVRATPGHTIGCVTYVTgdapdqPEPRMAFTGDALL 188
Cdd:COG0491   79 VYAHAaeaealeapaagalfgREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV------PDEKVLFTGDALF 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 731409215 189 IRGCGRTDFQGGCSHQLYNSVHsQIFTLPkDTLIYPAHDY 228
Cdd:COG0491  153 SGGVGRPDLPDGDLAQWLASLE-RLLALP-PDLVIPGHGP 190
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
59-226 2.68e-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: 106.85  E-value: 2.68e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  59 YTYLLADVShpDKPALLIDPV-DkkVERDLSLVKELGLKLIYAMNTHVHADHVTGtgliktkvpgVKSIISK------MS 131
Cdd:cd16275   13 YSYIIIDKA--TREAAVVDPAwD--IEKILAKLNELGLTLTGILLTHSHFDHVNL----------VEPLLAKydapvyMS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 132 KSKADL---------LVENGDKIYFGDLYLEVRATPGHTIGCVTYVTGDApdqpeprmAFTGDALLIRGCGRTDFQGGCS 202
Cdd:cd16275   79 KEEIDYygfrcpnliPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGDS--------LFTGDTLFIEGCGRCDLPGGDP 150
                        170       180
                 ....*....|....*....|....
gi 731409215 203 HQLYNSVHSQIFTLPKDTLIYPAH 226
Cdd:cd16275  151 EEMYESLQRLKKLPPPNTRVYPGH 174
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
60-246 1.18e-27

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: 105.89  E-value: 1.18e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  60 TYLLADVShpDKPALLIDPVDKKvERDLSLVKELGLKLIYAMNTHVHADHVTGTGLIK--TKVP---------------- 121
Cdd:cd16322   13 TYLVADEG--GGEAVLVDPGDES-EKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRrhPGAPvylhpddlplyeaadl 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 122 GVKSIISKMSKS-KADLLVENGDKIYFGDLYLEVRATPGHTIGCVTYVTgdapdqPEPRMAFTGDALLIRGCGRTDFQGG 200
Cdd:cd16322   90 GAKAFGLGIEPLpPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYV------EEEGLLFSGDLLFQGSIGRTDLPGG 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 731409215 201 CSHQLYNSvHSQIFTLPKDTLIYPAHDykgfTVSTVGEEMLYNPRL 246
Cdd:cd16322  164 DPKAMAAS-LRRLLTLPDETRVFPGHG----PPTTLGEERRTNPFL 204
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
59-265 1.58e-24

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 99.07  E-value: 1.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  59 YTYLLADVShpDKPALLIDPVDkkVERDLSLVKELGLKLIYAMNTHVHADHVTGTGLIKTKVPGVKSIISKMSKSKA-DL 137
Cdd:PLN02469  13 YAYLIIDES--TKDAAVVDPVD--PEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSLDNVKGcTH 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 138 LVENGDKIYFG-DLYLEVRATPGHTIGCVTY-VTGDAPDQPEprmAFTGDALLIRGCGRtdFQGGCSHQLYNSVHSQIFT 215
Cdd:PLN02469  89 PVENGDKLSLGkDVNILALHTPCHTKGHISYyVTGKEGEDPA---VFTGDTLFIAGCGK--FFEGTAEQMYQSLCVTLGS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 216 LPKDTLIYPAHDY--------------------------------KGFTVSTVGEEMLYNPRLTKDEetfKDIMENLNLS 263
Cdd:PLN02469 164 LPKPTQVYCGHEYtvknlkfaltvepdneklkqklewaekqrqagLPTVPSTIEEELETNPFMRVDL---PEIQEKVGCE 240

                 ..
gi 731409215 264 YP 265
Cdd:PLN02469 241 SP 242
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
59-226 1.17e-23

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: 94.54  E-value: 1.17e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215    59 YTYLLADvshpDKPALLIDPVDKKVERDLSLVKELGL-KLIYAMNTHVHADHVTGTGLIKtKVPGVKSIISKMSK----- 132
Cdd:smart00849   1 NSYLVRD----DGGAILIDTGPGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELL-EAPGAPVYAPEGTAellkd 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215   133 --------------SKADLLVENGDKIYFGDLYLEVRATPGHTIGCVTYVTgdapdqPEPRMAFTGDALLIRGCGRTDFQ 198
Cdd:smart00849  76 llallgelgaeaepAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL------PEGKILFTGDLLFAGGDGRTLVD 149
                          170       180
                   ....*....|....*....|....*....
gi 731409215   199 GGcSHQLYNSVHSQI-FTLPKDTLIYPAH 226
Cdd:smart00849 150 GG-DAAASDALESLLkLLKLLPKLVVPGH 177
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
71-226 1.24e-22

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: 92.23  E-value: 1.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  71 KPALLIDPVDKkVERDLSLVKELGLKLIYAMNTHVHADHVTGTGLIK--TKVPgvksII----------------SKM-- 130
Cdd:cd07737   22 KEAAVIDPGGD-ADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAehYGVP----IIgphkedkfllenlpeqSQMfg 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 131 -SKSKA---DLLVENGDKIYFGDLYLEVRATPGHTIGCVTYVtgdapdQPEPRMAFTGDALLIRGCGRTDFQGGCSHQLY 206
Cdd:cd07737   97 fPPAEAftpDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFF------NRESKLAIVGDVLFKGSIGRTDFPGGNHAQLI 170
                        170       180
                 ....*....|....*....|
gi 731409215 207 NSVHSQIFTLPKDTLIYPAH 226
Cdd:cd07737  171 ASIKEKLLPLGDDVTFIPGH 190
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
59-228 4.16e-17

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 79.89  E-value: 4.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  59 YTYLLAD-------VSHPDKPALLIDPVDKKverdlslvkelGLKLIYAMNTHVHADHVTGTGLIKTKVpGVKSIISKMS 131
Cdd:PLN02398  88 YAYLLHDedtgtvgVVDPSEAVPVIDALSRK-----------NRNLTYILNTHHHYDHTGGNLELKARY-GAKVIGSAVD 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 132 KSKA---DLLVENGDKIYFGDLYLEVRATPGHTIGCVTYVTgdapdqPEPRMAFTGDALLIRGCGRTdFQgGCSHQLYNS 208
Cdd:PLN02398 156 KDRIpgiDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYF------PGSGAIFTGDTLFSLSCGKL-FE-GTPEQMLSS 227
                        170       180
                 ....*....|....*....|
gi 731409215 209 VhSQIFTLPKDTLIYPAHDY 228
Cdd:PLN02398 228 L-QKIISLPDDTNIYCGHEY 246
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
57-226 1.83e-15

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 73.17  E-value: 1.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215   57 STYTYLLADvshpDKPALLIDP---VDKKVERDLSLVKELGLKLIYAMNTHVHADHVTGTGLIK--TKVPGV-------- 123
Cdd:pfam00753   5 QVNSYLIEG----GGGAVLIDTggsAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAeaTDVPVIvvaeeare 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  124 -------------KSIISKMSKSKADLLVENGDKIYFGDLYLEVRATPGHTIGCVTYVTGDApdqpepRMAFTGDALLIR 190
Cdd:pfam00753  81 lldeelglaasrlGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGG------KVLFTGDLLFAG 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 731409215  191 GCGRTDFQGGCSHQLYNSVHSQ------IFTLPKDTLIYPAH 226
Cdd:pfam00753 155 EIGRLDLPLGGLLVLHPSSAESslesllKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
70-187 2.41e-14

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: 69.87  E-value: 2.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  70 DKPALLIDP-----VDKKVERDLslvKELGLKLIYAMNTHVHADHVTGTGLIKtKVPGVKSIISKMSK------------ 132
Cdd:cd07743   17 DKEALLIDSgldedAGRKIRKIL---EELGWKLKAIINTHSHADHIGGNAYLQ-KKTGCKVYAPKIEKafienpllepsy 92
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 731409215 133 -------------------SKADLLVENGdKIYFGDLYLEVRATPGHTIGCVTYVTGDapdqpepRMAFTGDAL 187
Cdd:cd07743   93 lggayppkelrnkflmakpSKVDDIIEEG-ELELGGVGLEIIPLPGHSFGQIGILTPD-------GVLFAGDAL 158
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
103-228 2.84e-14

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 71.01  E-value: 2.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 103 THVHADHVTGTGLIKTKVPGVKSIISKMSKSK-ADLLVENGDKIYFGDLYLEVRATPGHTIGCVTYVTgdapdqpEPRMa 181
Cdd:PRK10241  52 THHHHDHVGGVKELVEKFPQIVVYGPQETQDKgTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYFS-------KPYL- 123
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 731409215 182 FTGDALLIRGCGRTdFQGGCShQLYNSVHsQIFTLPKDTLIYPAHDY 228
Cdd:PRK10241 124 FCGDTLFSGGCGRL-FEGTAS-QMYQSLK-KINALPDDTLICCAHEY 167
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
61-182 6.38e-11

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: 61.35  E-value: 6.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  61 YLLADVSHPDKPALLIDPVdKKVERDLSLVKelglkliYAMNTHVHADHVTGTGLIKtKVPGVKSIISKMSKS------- 133
Cdd:cd16309   33 HILIDGAMPQSTPLIKDNI-KKLGFDVKDVK-------YLLNTHAHFDHAGGLAELK-KATGAQLVASAADKPllesgyv 103
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 731409215 134 -------------KADLLVENGDKIYFGDLYLEVRATPGHTIGCVTYVTGDAPDQPEPRMAF 182
Cdd:cd16309  104 gsgdtknlqfppvRVDRVIGDGDKVTLGGTTLTAHLTPGHSPGCTSWTTTVKDTAGPPREVL 165
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
60-169 2.11e-10

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: 59.77  E-value: 2.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  60 TYLLADvshpDKPALLID--PVD--KKVERDlslVKELGLKLI---YAMNTHVHADHVTGTGLIKtKVPGVKSIISKMSK 132
Cdd:cd16310   24 SYLITS----NHGAILLDggLEEnaALIEQN---IKALGFKLSdikIIINTHAHYDHAGGLAQLK-ADTGAKLWASRGDR 95
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 731409215 133 S---------------------KADLLVENGDKIYFGDLYLEVRATPGHTIGCVTYVT 169
Cdd:cd16310   96 PaleagkhigdnitqpapfpavKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTWST 153
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
90-169 1.48e-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: 57.33  E-value: 1.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  90 VKELGLK---LIYAMNTHVHADHVTGTGLIKtKVPGVKSIISKMSKS----------------------KADLLVENGDK 144
Cdd:cd16288   51 IRKLGFKpsdIKILLNSHAHLDHAGGLAALK-KLTGAKLMASAEDAAllasggksdfhygddslafppvKVDRVLKDGDR 129
                         90       100
                 ....*....|....*....|....*
gi 731409215 145 IYFGDLYLEVRATPGHTIGCVTYVT 169
Cdd:cd16288  130 VTLGGTTLTAHLTPGHTRGCTTWTM 154
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
103-168 1.48e-09

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: 57.21  E-value: 1.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 103 THVHADHVTGTGLIKTKvPGVKSIISK----MSKSKA--------------DLLVENGDKIYFGDLYLEVRATPGHTIGC 164
Cdd:cd16280   68 THGHGDHYGGAAYLKDL-YGAKVVMSEadwdMMEEPPeegdnprwgppperDIVIKDGDTLTLGDTTITVYLTPGHTPGT 146

                 ....
gi 731409215 165 VTYV 168
Cdd:cd16280  147 LSLI 150
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
61-190 1.70e-09

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: 56.15  E-value: 1.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  61 YLLADvshpDKPALLIDP-VDKKVERDL--SLVKELGLKLI---YAMNTHVHADHVTGTGLIKtkvpgvksiiskmSKSK 134
Cdd:cd07725   18 YLLRD----GDETTLIDTgLATEEDAEAlwEGLKELGLKPSdidRVLLTHHHPDHIGLAGKLQ-------------EKSG 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 731409215 135 ADLLVEN------GDKIYFGDLYLEVRATPGHTIGCVTYVTGDApdqpepRMAFTGDALLIR 190
Cdd:cd07725   81 ATVYILDvtpvkdGDKIDLGGLRLKVIETPGHTPGHIVLYDEDR------RELFVGDAVLPK 136
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
66-187 9.87e-09

metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B3 MBLs include Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Stenotrophomonas Maltophilia L1, and Bradyrhizobium diazoefficiens BJP-1, Serratia marcescens SMB-1, and Pseudomonas Aeruginosa AIM-1. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 54.86  E-value: 9.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  66 VSHPDKPALLIDPVDKKVERDLSLVKELGLKLI---YAMNTHVHADHVTGTGLIKTKV---------------------- 120
Cdd:cd07708   27 IVTPQGNILIDGDMEQNAPMIKANIKKLGFKFSdtkLILISHAHFDHAGGSAEIKKQTgakvmagaedvslllsggssdf 106
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 731409215 121 PGVKSIISKMSKSKADLLVENGDKIYFGDLYLEVRATPGHTIGCVTYvTGDAPDQPEPRMAFTGDAL 187
Cdd:cd07708  107 HYANDSSTYFPQSTVDRAVHDGERVTLGGTVLTAHATPGHTPGCTTW-TMTLKDHGKQYQVVFADSL 172
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
73-187 1.60e-07

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: 50.32  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  73 ALLIDPVDKkvERDL-SLVKELGLKLIYAMNTHVHADHVTG-------------TGLIKTKVPGVKSIISKMSKSK---- 134
Cdd:cd07712   20 ALLIDTGLG--IGDLkEYVRTLTDLPLLVVATHGHFDHIGGlhefeevyvhpadAEILAAPDNFETLTWDAATYSVppag 97
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 731409215 135 ADLLVENGDKIYFGDLYLEVRATPGHTIGCVTYVtgdapdQPEPRMAFTGDAL 187
Cdd:cd07712   98 PTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALL------DRANRLLFSGDVV 144
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
58-193 3.11e-06

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: 47.10  E-value: 3.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  58 TYTYLLADvshPDKPALlIDP-VDKKVERDLSLVKELGL---KLIYAMNTHVHADHVTGTGLIKTKVP---------GVK 124
Cdd:cd07726   16 IASYLLDG---EGRPAL-IDTgPSSSVPRLLAALEALGIapeDVDYIILTHIHLDHAGGAGLLAEALPnakvyvhprGAR 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 125 SII--SKMSKS-------KADLL--------------VENGDKIYFGDLYLEVRATPGHtigcvtyvtgdAPDQ-----P 176
Cdd:cd07726   92 HLIdpSKLWASaravygdEADRLggeilpvpeervivLEDGETLDLGGRTLEVIDTPGH-----------APHHlsfldE 160
                        170
                 ....*....|....*..
gi 731409215 177 EPRMAFTGDALLIRGCG 193
Cdd:cd07726  161 ESDGLFTGDAAGVRYPE 177
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
58-191 5.51e-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: 42.86  E-value: 5.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  58 TYTYLLADvshpDKPALLIDP-----------VDKKVERDLSLVkelglkLIyamnTHVHADHVTGTGLIK--TKVP--- 121
Cdd:cd16278   18 TNTYLLGA----PDGVVVIDPgpddpahldalLAALGGGRVSAI------LV----THTHRDHSPGAARLAerTGAPvra 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 731409215 122 -GVKSIISKMSKSKADLLVENGDKIYFGDLYLEVRATPGHTIGCVTYVTgdapdqPEPRMAFTGDALLIRG 191
Cdd:cd16278   84 fGPHRAGGQDTDFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFAL------EDEGALFTGDHVMGWS 148
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
90-168 6.99e-05

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


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 43.23  E-value: 6.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  90 VKELGLK---LIYAMNTHVHADHVTGTGLIKTKVpGVKSIISK---------------MSKS-------KADLLVENGDK 144
Cdd:cd16308   51 IQALGFKfkdIKILLTTQAHYDHVGAMAAIKQQT-GAKMMVDEkdakvladggksdyeMGGYgstfapvKADKLLHDGDT 129
                         90       100
                 ....*....|....*....|....
gi 731409215 145 IYFGDLYLEVRATPGHTIGCVTYV 168
Cdd:cd16308  130 IKLGGTKLTLLHHPGHTKGSCSFL 153
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
58-226 1.04e-04

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: 42.14  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  58 TYTYLLadvsHPDKPALLID---PVDKKVERDLSLVKELGLKLI-YAMNTHVHADHVTGTGLIKTKVPGVKSIISKMSKS 133
Cdd:cd07722   18 TNTYLV----GTGKRRILIDtgeGRPSYIPLLKSVLDSEGNATIsDILLTHWHHDHVGGLPDVLDLLRGPSPRVYKFPRP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 134 KADLL----------VENGDKIYFGDLYLEVRATPGHTigcvtyvtgdaPDQ-----PEPRMAFTGDALLirGCGRTDFQ 198
Cdd:cd07722   94 EEDEDpdedggdihdLQDGQVFKVEGATLRVIHTPGHT-----------TDHvcfllEEENALFTGDCVL--GHGTAVFE 160
                        170       180
                 ....*....|....*....|....*...
gi 731409215 199 ggCSHQLYNSVHSqIFTLPKDTlIYPAH 226
Cdd:cd07722  161 --DLAAYMASLKK-LLSLGPGR-IYPGH 184
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
87-186 1.29e-04

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 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: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 41.80  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  87 LSLVKELGLKL--I-YAMNTHVHADHVTGTGLIktkvPGVKSIISKMSKSKADLLVENGDKIYFG-DLYLEVRATPGHTI 162
Cdd:cd07711   48 LKALAEHGLSPedIdYVVLTHGHPDHIGNLNLF----PNATVIVGWDICGDSYDDHSLEEGDGYEiDENVEVIPTPGHTP 123
                         90       100
                 ....*....|....*....|....
gi 731409215 163 GCVTYVTGDAPDQpepRMAFTGDA 186
Cdd:cd07711  124 EDVSVLVETEKKG---TVAVAGDL 144
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
90-167 2.16e-04

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: 41.66  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  90 VKELGLKLI---YAMNTHVHADHVTGTGLIKTK-----------VPGVKS-----------IISKMSKSKADLLVENGDK 144
Cdd:cd16307   51 IEKLGFKFSdtkILLISHAHFDHAAGSALIKREthakymvmdgdVDVVESggksdffygndPSTYFPPAHVDKVLHDGEQ 130
                         90       100
                 ....*....|....*....|...
gi 731409215 145 IYFGDLYLEVRATPGHTIGCVTY 167
Cdd:cd16307  131 VELGGTVLTAHLTAGHTKGCTTW 153
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 ...
75-167 3.97e-04

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: 41.18  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  75 LID-PVDKKVERDLSLVKELG-----LKLIyaMNTHVHADHVTG-------TG-LIKTKVPGVKSI-------------- 126
Cdd:cd16290   35 LIDgALPQSAPQIEANIRALGfrledVKLI--LNSHAHFDHAGGiaalqrdSGaTVAASPAGAAALrsggvdpddpqaga 112
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 731409215 127 ISKMSKSKADLLVENGDKIYFGDLYLEVRATPGHTIGCVTY 167
Cdd:cd16290  113 ADPFPPVAKVRVVADGEVVKLGPLAVTAHATPGHTPGGTSW 153
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
59-191 1.08e-03

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: 39.51  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  59 YTYLLADvshpDKPALLID---PVD-KKVERDLslvKELGLK-------LIyamnTHVHADHV---------TG------ 112
Cdd:cd07721   12 NAYLIED----DDGLTLIDtglPGSaKRILKAL---RELGLSpkdirriLL----THGHIDHIgslaalkeaPGapvyah 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 113 -------TGLIKTKVPGVKSIISKMSKSK------ADLLVENGDKI-YFGDLylEVRATPGHTIGCVTYVtgdapdQPEP 178
Cdd:cd07721   81 ereapylEGEKPYPPPVRLGLLGLLSPLLpvkpvpVDRTLEDGDTLdLAGGL--RVIHTPGHTPGHISLY------LEED 152
                        170
                 ....*....|...
gi 731409215 179 RMAFTGDALLIRG 191
Cdd:cd07721  153 GVLIAGDALVTVG 165
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
66-186 2.20e-03

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 38.27  E-value: 2.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  66 VSHPDKpALLID--PVDKKVERD-LSLVKELG-LKLIYAMNTHVHADHVTGTGLIKTKVPgVKSII-------SKMSKSK 134
Cdd:cd07731   15 IQTPGK-TILIDtgPRDSFGEDVvVPYLKARGiKKLDYLILTHPDADHIGGLDAVLKNFP-VKEVYmpgvthtTKTYEDL 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 731409215 135 ADLLVEN---------GDKIYFGDLYLEVRATPGHTIG------CVTYVT-GDApdqpepRMAFTGDA 186
Cdd:cd07731   93 LDAIKEKgipvtpckaGDRWQLGGVSFEVLSPPKDDYDdlnnnsCVLRLTyGGT------SFLLTGDA 154
NorV COG0426
Flavorubredoxin [Energy production and conversion];
49-186 8.56e-03

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 37.12  E-value: 8.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215  49 RQLFE-----QESSTY-TYLLADvshpDKPALlIDPVDKKVERDL--SLVKELGLKLI-YAMNTHVHADHVTGTGLIKTK 119
Cdd:COG0426   19 RRLFEgeyptPRGTTYnSYLIVD----EKTAL-IDTVGESFFEEFleNLSKVIDPKKIdYIIVNHQEPDHSGSLPELLEL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 731409215 120 VPGVKSIISKMSKskaDLL-------------VENGDKIYFGDLYLEVRATPG-H---TIgcVTYVTGDapdqpepRMAF 182
Cdd:COG0426   94 APNAKIVCSKKAA---RFLphfygipdfrfivVKEGDTLDLGGHTLQFIPAPMlHwpdTM--FTYDPED-------KILF 161

                 ....
gi 731409215 183 TGDA 186
Cdd:COG0426  162 SGDA 165
 
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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