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Conserved domains on  [gi|593429537|gb|EXQ19213|]
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metallo-beta-lactamase [Staphylococcus aureus H68996]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869984)

MBL fold metallo-hydrolase containing a rhodanese homology domain (RHOD)

Gene Ontology:  GO:0016787|GO:0046872
PubMed:  11513844|17597585

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 1-171 2.43e-51

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: 167.96  E-value: 2.43e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537   1 MIIDPICD-LSSYIRVADEESLTITHAAETHIHANFVSGIRDVAIKLNASIYVSGESDDMLGYknmpnhtHFVQHNDDIY 79
Cdd:cd07724   26 AVIDPVRDsVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGEGAPASFFD-------RLLKDGDVLE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  80 VGNIKLKVLHTPGHTPESISFLLTDEGAgaqvpmgLFSGDFIFVGDIGRPDLLekavkveGLSEIGAKQMFKSIES-IKD 158
Cdd:cd07724   99 LGNLTLEVLHTPGHTPESVSYLVGDPDA-------VFTGDTLFVGDVGRPDLP-------GEAEGLARQLYDSLQRkLLL 164

                        170
                 ....*....|...
gi 593429537 159 LPDYIQIWPGHGA 171
Cdd:cd07724  165 LPDETLVYPGHDY 177
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 251-289 1.20e-03

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


:

Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 37.28  E-value: 1.20e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 593429537 251 DLRSKEAYHGGHIEGTINIPYDKNFINQIGWYLNYNQEI 289
Cdd:cd00158   15 DVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPI 53
 
Name Accession Description Interval E-value
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 1-171 2.43e-51

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: 167.96  E-value: 2.43e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537   1 MIIDPICD-LSSYIRVADEESLTITHAAETHIHANFVSGIRDVAIKLNASIYVSGESDDMLGYknmpnhtHFVQHNDDIY 79
Cdd:cd07724   26 AVIDPVRDsVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGEGAPASFFD-------RLLKDGDVLE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  80 VGNIKLKVLHTPGHTPESISFLLTDEGAgaqvpmgLFSGDFIFVGDIGRPDLLekavkveGLSEIGAKQMFKSIES-IKD 158
Cdd:cd07724   99 LGNLTLEVLHTPGHTPESVSYLVGDPDA-------VFTGDTLFVGDVGRPDLP-------GEAEGLARQLYDSLQRkLLL 164

                        170
                 ....*....|...
gi 593429537 159 LPDYIQIWPGHGA 171
Cdd:cd07724  165 LPDETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 1-171 9.01e-31

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: 115.56  E-value: 9.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537   1 MIIDP---ICDLSSYIRVADEESLTITHAAETHIHANFVSGIRDVAIKLNASIYVS---------GESDDMLGYKNMPnH 68
Cdd:COG0491   27 VLIDTglgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHaaeaealeaPAAGALFGREPVP-P 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  69 THFVQHNDDIYVGNIKLKVLHTPGHTPESISFLLTDEGAgaqvpmgLFSGDFIFVGDIGRPDLLEKAvkveglseigAKQ 148
Cdd:COG0491  106 DRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKV-------LFTGDALFSGGVGRPDLPDGD----------LAQ 168

                        170       180
                 ....*....|....*....|...
gi 593429537 149 MFKSIESIKDLPDYIqIWPGHGA 171
Cdd:COG0491  169 WLASLERLLALPPDL-VIPGHGP 190
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 23-169 8.84e-16

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: 74.13  E-value: 8.84e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537    23 ITHAAETHIHANFVSGIRDVAIKLNASIYVSGESDDML-----------GYKNMPNHTHFVQHNDDIYVGNIKLKVLHTP 91
Cdd:smart00849  36 IDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLkdllallgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTP 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537    92 GHTPESISFLLTDEGAgaqvpmgLFSGDFIFVGDIGRPDLlekavkveglsEIGAKQMFKSIESIKDL--PDYIQIWPGH 169
Cdd:smart00849 116 GHTPGSIVLYLPEGKI-------LFTGDLLFAGGDGRTLV-----------DGGDAAASDALESLLKLlkLLPKLVVPGH 177
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 2-169 1.92e-13

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 69.02  E-value: 1.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537   2 IIDPIcDLSSYIRVADEESLTITHAAETHIHANFVSGIRDVAiKLNASIYVSGESDDmlgykNMPNHTHFVQHNDDIYVG 81
Cdd:PLN02469  27 VVDPV-DPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIK-KLVPGIKVYGGSLD-----NVKGCTHPVENGDKLSLG 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  82 N-IKLKVLHTPGHTPESISFLLTdeGAGAQVPmGLFSGDFIFVGDIGRpdllekavkvegLSEIGAKQMFKSI-ESIKDL 159
Cdd:PLN02469 100 KdVNILALHTPCHTKGHISYYVT--GKEGEDP-AVFTGDTLFIAGCGK------------FFEGTAEQMYQSLcVTLGSL 164

                        170
                 ....*....|
gi 593429537 160 PDYIQIWPGH 169
Cdd:PLN02469 165 PKPTQVYCGH 174
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
1-169 4.91e-06

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 46.59  E-value: 4.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537    1 MIIDPICDLSS----YIRVADEESLTITHAAETHIHANFVSGIRDVAIKLNASIYVSGESDDMLGYK------------- 63
Cdd:pfam00753  18 VLIDTGGSAEAalllLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEelglaasrlglpg 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537   64 ---NMPNHTHFVQHNDDIYVGNIKLKVLHTPGHTPESISFLLTDEGAgaqvpmgLFSGDFIFVGDIGRPDLLEKAVKVEG 140
Cdd:pfam00753  98 ppvVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKV-------LFTGDLLFAGEIGRLDLPLGGLLVLH 170

                         170       180
                  ....*....|....*....|....*....
gi 593429537  141 LSeiGAKQMFKSIESIKDLpDYIQIWPGH 169
Cdd:pfam00753 171 PS--SAESSLESLLKLAKL-KAAVIVPGH 196
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 251-289 1.20e-03

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 37.28  E-value: 1.20e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 593429537 251 DLRSKEAYHGGHIEGTINIPYDKNFINQIGWYLNYNQEI 289
Cdd:cd00158   15 DVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPI 53
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 251-273 2.27e-03

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 37.25  E-value: 2.27e-03
                         10        20
                 ....*....|....*....|...
gi 593429537 251 DLRSKEAYHGGHIEGTINIPYDK 273
Cdd:COG0607   24 DVREPEEFAAGHIPGAINIPLGE 46
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 251-274 3.99e-03

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 36.28  E-value: 3.99e-03
                           10        20
                   ....*....|....*....|....
gi 593429537   251 DLRSKEAYHGGHIEGTINIPYDKN 274
Cdd:smart00450   9 DVRSPEEYEGGHIPGAVNIPLSEL 32
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 250-272 7.73e-03

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 35.15  E-value: 7.73e-03
                          10        20
                  ....*....|....*....|...
gi 593429537  250 FDLRSKEAYHGGHIEGTINIPYD 272
Cdd:pfam00581   9 IDVRPPEEYAKGHIPGAVNVPLS 31
 
Name Accession Description Interval E-value
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 1-171 2.43e-51

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: 167.96  E-value: 2.43e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537   1 MIIDPICD-LSSYIRVADEESLTITHAAETHIHANFVSGIRDVAIKLNASIYVSGESDDMLGYknmpnhtHFVQHNDDIY 79
Cdd:cd07724   26 AVIDPVRDsVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGEGAPASFFD-------RLLKDGDVLE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  80 VGNIKLKVLHTPGHTPESISFLLTDEGAgaqvpmgLFSGDFIFVGDIGRPDLLekavkveGLSEIGAKQMFKSIES-IKD 158
Cdd:cd07724   99 LGNLTLEVLHTPGHTPESVSYLVGDPDA-------VFTGDTLFVGDVGRPDLP-------GEAEGLARQLYDSLQRkLLL 164

                        170
                 ....*....|...
gi 593429537 159 LPDYIQIWPGHGA 171
Cdd:cd07724  165 LPDETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 1-171 9.01e-31

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: 115.56  E-value: 9.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537   1 MIIDP---ICDLSSYIRVADEESLTITHAAETHIHANFVSGIRDVAIKLNASIYVS---------GESDDMLGYKNMPnH 68
Cdd:COG0491   27 VLIDTglgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHaaeaealeaPAAGALFGREPVP-P 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  69 THFVQHNDDIYVGNIKLKVLHTPGHTPESISFLLTDEGAgaqvpmgLFSGDFIFVGDIGRPDLLEKAvkveglseigAKQ 148
Cdd:COG0491  106 DRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKV-------LFTGDALFSGGVGRPDLPDGD----------LAQ 168

                        170       180
                 ....*....|....*....|...
gi 593429537 149 MFKSIESIKDLPDYIqIWPGHGA 171
Cdd:COG0491  169 WLASLERLLALPPDL-VIPGHGP 190
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 1-169 2.00e-30

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: 113.40  E-value: 2.00e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537   1 MIIDPICDLSSYIRVADEESLTITHAAETHIHANFVSGIRDVAIKLNASIYVSGESDDMLGYKnmPNHTHFVQHNDDIYV 80
Cdd:cd16275   26 AVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDYYGFR--CPNLIPLEDGDTIKI 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  81 GNIKLKVLHTPGHTPESISFLLTDEgagaqvpmgLFSGDFIFVGDIGRPDLLEKAvkveglseigAKQMFKSIESIKDL- 159
Cdd:cd16275  104 GDTEITCLLTPGHTPGSMCYLLGDS---------LFTGDTLFIEGCGRCDLPGGD----------PEEMYESLQRLKKLp 164

                        170
                 ....*....|
gi 593429537 160 PDYIQIWPGH 169
Cdd:cd16275  165 PPNTRVYPGH 174
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 2-169 4.43e-30

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: 112.17  E-value: 4.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537   2 IIDPiCDLSSYIRVADEESLTITHAAETHIHANFVSGIRDVAIKL-NASIYVSGESddmlgykNMPNHTHFVQHNDDIYV 80
Cdd:cd07723   24 VVDP-GEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFpDAPVYGPAED-------RIPGLDHPVKDGDEIKL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  81 GNIKLKVLHTPGHTPESISFLLTDEGAgaqvpmgLFSGDFIFVGDIGRPDllekavkvEGlseiGAKQMFKSIESIKDLP 160
Cdd:cd07723   96 GGLEVKVLHTPGHTLGHICYYVPDEPA-------LFTGDTLFSGGCGRFF--------EG----TAEQMYASLQKLLALP 156


                 ....*....
gi 593429537 161 DYIQIWPGH 169
Cdd:cd07723  157 DDTLVYCGH 165
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 2-194 5.64e-28

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: 107.82  E-value: 5.64e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537   2 IIDPICDLSSYIRVADEESLTITHAAETHIHANFVSGIRDVAIKLNASIYVsgESDDMLGYKN--------------MPN 67
Cdd:cd16322   26 LVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYL--HPDDLPLYEAadlgakafglgiepLPP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  68 HTHFVQHNDDIYVGNIKLKVLHTPGHTPESISFLLTDEGAgaqvpmgLFSGDFIFVGDIGRPDLlekavkveglseIGA- 146
Cdd:cd16322  104 PDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGL-------LFSGDLLFQGSIGRTDL------------PGGd 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 593429537 147 -KQMFKSIESIKDLPDYIQIWPGHGagspcgkslgaiPTSTLGYEKQTN 194
Cdd:cd16322  165 pKAMAASLRRLLTLPDETRVFPGHG------------PPTTLGEERRTN 201
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 2-169 7.68e-22

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: 91.19  E-value: 7.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537   2 IIDP-ICDLSSYIRVADEESLTITHAAETHIHanF--VSGIRDVAIKLNASIYVSGESDDML------------GYKNMP 66
Cdd:cd06262   24 LIDPgAGALEKILEAIEELGLKIKAILLTHGH--FdhIGGLAELKEAPGAPVYIHEADAELLedpelnlaffggGPLPPP 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  67 NHTHFVQHNDDIYVGNIKLKVLHTPGHTPESISFLLTDEGAgaqvpmgLFSGDFIFVGDIGRPDLlekavkvEGLSEiga 146
Cdd:cd06262  102 EPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGV-------LFTGDTLFAGSIGRTDL-------PGGDP--- 164

                        170       180
                 ....*....|....*....|....
gi 593429537 147 KQMFKSIES-IKDLPDYIQIWPGH 169
Cdd:cd06262  165 EQLIESIKKlLLLLPDDTVVYPGH 188
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 2-169 3.49e-18

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: 81.06  E-value: 3.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537   2 IIDPICDLSSYIRVADEESLTITHAAETHIHANFVSGIRDVAIKLNASIYVSGESDD-----------MLGYKNMPNHT- 69
Cdd:cd07737   26 VIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKEDKfllenlpeqsqMFGFPPAEAFTp 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  70 -HFVQHNDDIYVGNIKLKVLHTPGHTPESISFLltDEGAGAqvpmgLFSGDFIFVGDIGRPDLLEKavkveglseiGAKQ 148
Cdd:cd07737  106 dRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFF--NRESKL-----AIVGDVLFKGSIGRTDFPGG----------NHAQ 168

                        170       180
                 ....*....|....*....|..
gi 593429537 149 MFKSI-ESIKDLPDYIQIWPGH 169
Cdd:cd07737  169 LIASIkEKLLPLGDDVTFIPGH 190
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 23-169 8.84e-16

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: 74.13  E-value: 8.84e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537    23 ITHAAETHIHANFVSGIRDVAIKLNASIYVSGESDDML-----------GYKNMPNHTHFVQHNDDIYVGNIKLKVLHTP 91
Cdd:smart00849  36 IDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLkdllallgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTP 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537    92 GHTPESISFLLTDEGAgaqvpmgLFSGDFIFVGDIGRPDLlekavkveglsEIGAKQMFKSIESIKDL--PDYIQIWPGH 169
Cdd:smart00849 116 GHTPGSIVLYLPEGKI-------LFTGDLLFAGGDGRTLV-----------DGGDAAASDALESLLKLlkLLPKLVVPGH 177
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 2-169 1.92e-13

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 69.02  E-value: 1.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537   2 IIDPIcDLSSYIRVADEESLTITHAAETHIHANFVSGIRDVAiKLNASIYVSGESDDmlgykNMPNHTHFVQHNDDIYVG 81
Cdd:PLN02469  27 VVDPV-DPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIK-KLVPGIKVYGGSLD-----NVKGCTHPVENGDKLSLG 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  82 N-IKLKVLHTPGHTPESISFLLTdeGAGAQVPmGLFSGDFIFVGDIGRpdllekavkvegLSEIGAKQMFKSI-ESIKDL 159
Cdd:PLN02469 100 KdVNILALHTPCHTKGHISYYVT--GKEGEDP-AVFTGDTLFIAGCGK------------FFEGTAEQMYQSLcVTLGSL 164

                        170
                 ....*....|
gi 593429537 160 PDYIQIWPGH 169
Cdd:PLN02469 165 PKPTQVYCGH 174
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 15-171 3.49e-13

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: 67.17  E-value: 3.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  15 VADEESLTITHAAETHIHANFVSGIRDV---AIKLNASIYVSGESDDMLGYKNMPNHTHFVQHNDDIYVGNIKLKVLHTP 91
Cdd:cd07722   49 LDSEGNATISDILLTHWHHDHVGGLPDVldlLRGPSPRVYKFPRPEEDEDPDEDGGDIHDLQDGQVFKVEGATLRVIHTP 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  92 GHTPESISFLLTDEGAgaqvpmgLFSGDFIfvgdigrpdLLEKAVKVEGLSEigakQMfKSIESIKDLPdYIQIWPGHGA 171
Cdd:cd07722  129 GHTTDHVCFLLEEENA-------LFTGDCV---------LGHGTAVFEDLAA----YM-ASLKKLLSLG-PGRIYPGHGP 186
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 1-207 1.13e-12

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 66.74  E-value: 1.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537   1 MIIDPI-----CDLSsyirVADEESLTITHAAETHIHANFVSGIRDVAIKLNA--SIY--VSGESDDmlgyknmpnhtHF 71
Cdd:PLN02962  39 LLIDPVdktvdRDLS----LVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGvkSIIskASGSKAD-----------LF 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  72 VQHNDDIYVGNIKLKVLHTPGHTPESISFlLTDEGAGAQVPMGLFSGDFIFVGDIGRPDLlekavkvEGLSeigAKQMFK 151
Cdd:PLN02962 104 VEPGDKIYFGDLYLEVRATPGHTAGCVTY-VTGEGPDQPQPRMAFTGDALLIRGCGRTDF-------QGGS---SDQLYK 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 593429537 152 SIES-IKDLPDYIQIWPGHgagspcgkSLGAIPTSTLGYEKQTNWAFSENNEaTFID 207
Cdd:PLN02962 173 SVHSqIFTLPKDTLIYPAH--------DYKGFTVSTVGEEMLYNPRLTKDEE-TFKT 220
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 1-169 1.76e-11

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: 62.26  E-value: 1.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537   1 MIID---PICDLSSYIRVADEESLTithAAETHIHANFVSGI----------RDVAIkLNASIYVSGESDDMLGYKNMP- 66
Cdd:cd07712   21 LLIDtglGIGDLKEYVRTLTDLPLL---VVATHGHFDHIGGLhefeevyvhpADAEI-LAAPDNFETLTWDAATYSVPPa 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  67 NHTHFVQHNDDIYVGNIKLKVLHTPGHTPESISFLltDEGAGAqvpmgLFSGDFIFVGDI-----GRPdllekavkvegl 141
Cdd:cd07712   97 GPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALL--DRANRL-----LFSGDVVYDGPLimdlpHSD------------ 157

                        170       180
                 ....*....|....*....|....*....
gi 593429537 142 seigAKQMFKSIESIKDLPDYI-QIWPGH 169
Cdd:cd07712  158 ----LDDYLASLEKLSKLPDEFdKVLPGH 182
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 2-171 2.49e-11

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 61.74  E-value: 2.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537   2 IIDPICDLSSYI-RVADE-ESLTITHAAETHIHANFVSGIRDVAIKLNASIYVSGESDDMLGYKNMPNHtHFVQHNDDIY 79
Cdd:cd16278   31 VIDPGPDDPAHLdALLAAlGGGRVSAILVTHTHRDHSPGAARLAERTGAPVRAFGPHRAGGQDTDFAPD-RPLADGEVIE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  80 VGNIKLKVLHTPGHTPESISFLLTDEGAgaqvpmgLFSGDFIFVGD---IGRPDllekavkveglseiGA-KQMFKSIES 155
Cdd:cd16278  110 GGGLRLTVLHTPGHTSDHLCFALEDEGA-------LFTGDHVMGWSttvIAPPD--------------GDlGDYLASLER 168

                        170
                 ....*....|....*.
gi 593429537 156 IKDLPDyIQIWPGHGA 171
Cdd:cd16278  169 LLALDD-RLLLPGHGP 183
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 29-170 1.31e-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: 48.06  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  29 THIHANFVSGIRDVAIKLNASIYVSGesddmlgyknmpnhTHFVQHNDDIYVGNIKLKVLHTPGHTPESISFLLTDEGag 108
Cdd:cd07725   62 THHHPDHIGLAGKLQEKSGATVYILD--------------VTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRR-- 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 593429537 109 aqvpmGLFSGDFIfVGDI-----GRPDLLEKAVkveglseigaKQMFKSIESIKDLpDYIQIWPGHG 170
Cdd:cd07725  126 -----ELFVGDAV-LPKItpnvsLWAVRVEDPL----------GAYLESLDKLEKL-DVDLAYPGHG 175
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 45-119 2.03e-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: 47.87  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  45 KLNAS---IYvsGESDDMLGYKNMP---NHTHFVQHNDDIYVGNIKLKVLHTPGHTPESISFLLTDEGagaqvpmGLFSG 118
Cdd:cd07726   98 KLWASaraVY--GDEADRLGGEILPvpeERVIVLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESD-------GLFTG 168


                 .
gi 593429537 119 D 119
Cdd:cd07726  169 D 169
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 85-170 3.32e-06

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: 47.22  E-value: 3.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  85 LKVLHTPGHTPESISFLLTDEGAgaqvpmgLFSGDFIFVGDigrpdllekavkveGLSEIGAKQMF----KSIESIKDLP 160
Cdd:cd07721  132 LRVIHTPGHTPGHISLYLEEDGV-------LIAGDALVTVG--------------GELVPPPPPFTwdmeEALESLRKLA 190

                         90
                 ....*....|..
gi 593429537 161 DYI--QIWPGHG 170
Cdd:cd07721  191 ELDpeVLAPGHG 202
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 86-171 3.52e-06

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: 46.81  E-value: 3.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  86 KVLHTPGHTPESISFLLTDEGAgaqvpmglfsGDFIFVGD-IGRPDLLEKAVKVEGLSEIGAKQMfKSIESIKDLPDYIq 164
Cdd:cd07711  114 EVIPTPGHTPEDVSVLVETEKK----------GTVAVAGDlFEREEDLEDPILWDPLSEDPELQE-ESRKRILALADWI- 181


                 ....*..
gi 593429537 165 IwPGHGA 171
Cdd:cd07711  182 I-PGHGP 187
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
1-169 4.91e-06

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 46.59  E-value: 4.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537    1 MIIDPICDLSS----YIRVADEESLTITHAAETHIHANFVSGIRDVAIKLNASIYVSGESDDMLGYK------------- 63
Cdd:pfam00753  18 VLIDTGGSAEAalllLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEelglaasrlglpg 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537   64 ---NMPNHTHFVQHNDDIYVGNIKLKVLHTPGHTPESISFLLTDEGAgaqvpmgLFSGDFIFVGDIGRPDLLEKAVKVEG 140
Cdd:pfam00753  98 ppvVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKV-------LFTGDLLFAGEIGRLDLPLGGLLVLH 170

                         170       180
                  ....*....|....*....|....*....
gi 593429537  141 LSeiGAKQMFKSIESIKDLpDYIQIWPGH 169
Cdd:pfam00753 171 PS--SAESSLESLLKLAKL-KAAVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 23-169 1.23e-05

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 46.37  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  23 ITHAAETHIHANFVSGIRDVAIKLNASIYVSGESDDmlgykNMPNHTHFVQHNDDIYVGNIKLKVLHTPGHTPESISFLL 102
Cdd:PLN02398 122 LTYILNTHHHYDHTGGNLELKARYGAKVIGSAVDKD-----RIPGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYF 196

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 593429537 103 TdeGAGAqvpmgLFSGDFIFVGDIGRpdllekavkvegLSEIGAKQMFKSIESIKDLPDYIQIWPGH 169
Cdd:PLN02398 197 P--GSGA-----IFTGDTLFSLSCGK------------LFEGTPEQMLSSLQKIISLPDDTNIYCGH 244
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 65-171 2.17e-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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 44.86  E-value: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  65 MPNHThfVQHNDDIYVGNIKLKVLHT-PGHTPESISFLLTDEGAgaqvpmgLFSGDFIFVgdiGRPDLLEKAvkveglse 143
Cdd:cd16282  115 LPDRT--FDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEGV-------LFAGDLVFN---GRIPFLPDG-------- 174

                         90       100
                 ....*....|....*....|....*...
gi 593429537 144 iGAKQMFKSIESIKDLPDYIqIWPGHGA 171
Cdd:cd16282  175 -SLAGWIAALDRLLALDATV-VVPGHGP 200
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 29-103 4.74e-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: 44.00  E-value: 4.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  29 THIHANFVSGIRDVAIKLNASIYVS----------GESD-DMLGYKNM--PNHTHFVQHNDD-IYVGNIKLKVLHTPGHT 94
Cdd:cd16308   67 TQAHYDHVGAMAAIKQQTGAKMMVDekdakvladgGKSDyEMGGYGSTfaPVKADKLLHDGDtIKLGGTKLTLLHHPGHT 146


                 ....*....
gi 593429537  95 PESISFLLT 103
Cdd:cd16308  147 KGSCSFLFD 155
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 29-169 9.71e-05

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 43.27  E-value: 9.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  29 THIHANFVSGIRDVAIKL-NASIYVSGESDDmlgyknmPNHTHFVQHNDDIYVGNIKLKVLHTPGHTPESISFLltdega 107
Cdd:PRK10241  52 THHHHDHVGGVKELVEKFpQIVVYGPQETQD-------KGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF------ 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 593429537 108 gaQVPMgLFSGDFIFVGDIGRpdllekavkvegLSEIGAKQMFKSIESIKDLPDYIQIWPGH 169
Cdd:PRK10241 119 --SKPY-LFCGDTLFSGGCGR------------LFEGTASQMYQSLKKINALPDDTLICCAH 165
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 1-133 9.60e-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: 40.22  E-value: 9.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537   1 MIIDPICDLSsyIRVADEESLTITHAaethiHANFVSGIRDVAIKLNASIYVSGESDDML--GYKNMPNH-----THFVQ 73
Cdd:cd07708   46 MIKANIKKLG--FKFSDTKLILISHA-----HFDHAGGSAEIKKQTGAKVMAGAEDVSLLlsGGSSDFHYandssTYFPQ 118

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 593429537  74 HNDD--------IYVGNIKLKVLHTPGHTPESISFLLTDEGAGAQVPMGLF-----SGDFIFVGDIGRPDLLE 133
Cdd:cd07708  119 STVDravhdgerVTLGGTVLTAHATPGHTPGCTTWTMTLKDHGKQYQVVFAdsltvNPGYRLVDNPTYPKIVE 191
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 29-106 9.68e-04

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 40.26  E-value: 9.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  29 THIHANFVSGIRDVAIKLNASIYVSGESDDML----------GYKNMPNHTHFVQHNDDIYVGNIKLKVLHTPGHTPESI 98
Cdd:cd16280   68 THGHGDHYGGAAYLKDLYGAKVVMSEADWDMMeeppeegdnpRWGPPPERDIVIKDGDTLTLGDTTITVYLTPGHTPGTL 147

                         90
                 ....*....|
gi 593429537  99 SFL--LTDEG 106
Cdd:cd16280  148 SLIfpVKDGG 157
RHOD cd00158
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 251-289 1.20e-03

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


Pssm-ID: 238089 [Multi-domain]  Cd Length: 89  Bit Score: 37.28  E-value: 1.20e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 593429537 251 DLRSKEAYHGGHIEGTINIPYDKNFINQIGWYLNYNQEI 289
Cdd:cd00158   15 DVREPEEYAAGHIPGAINIPLSELEERAALLELDKDKPI 53
PspE COG0607
Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; ...
 251-273 2.27e-03

Rhodanese-related sulfurtransferase [Inorganic ion transport and metabolism]; Rhodanese-related sulfurtransferase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440372 [Multi-domain]  Cd Length: 106  Bit Score: 37.25  E-value: 2.27e-03
                         10        20
                 ....*....|....*....|...
gi 593429537 251 DLRSKEAYHGGHIEGTINIPYDK 273
Cdd:COG0607   24 DVREPEEFAAGHIPGAINIPLGE 46
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 1-169 3.00e-03

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 38.28  E-value: 3.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537   1 MIIDPICDLSSYIRVA---DEESLTITHAAETHIHANFVSGIRDVAIKLNASIYVSGESDDML------------GYKNM 65
Cdd:cd07743   21 LLIDSGLDEDAGRKIRkilEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAFIenpllepsylggAYPPK 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  66 PNHTHF----------VQHNDDIYVGNIKLKVLHTPGHTPESISFlLTDEGAgaqvpmgLFSGDFIFvgdigRPDLLEKa 135
Cdd:cd07743  101 ELRNKFlmakpskvddIIEEGELELGGVGLEIIPLPGHSFGQIGI-LTPDGV-------LFAGDALF-----GEEVLEK- 166

                        170       180       190
                 ....*....|....*....|....*....|....
gi 593429537 136 VKVEGLSEIgaKQMFKSIESIKDLpDYIQIWPGH 169
Cdd:cd07743  167 YGIPFLYDV--EEQLETLEKLEEL-DADYYVPGH 197
RHOD smart00450
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ...
 251-274 3.99e-03

Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.


Pssm-ID: 197731 [Multi-domain]  Cd Length: 100  Bit Score: 36.28  E-value: 3.99e-03
                           10        20
                   ....*....|....*....|....
gi 593429537   251 DLRSKEAYHGGHIEGTINIPYDKN 274
Cdd:smart00450   9 DVRSPEEYEGGHIPGAVNIPLSEL 32
RHOD_HSP67B2 cd01519
Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein ...
 234-273 4.37e-03

Member of the Rhodanese Homology Domain superfamily. This CD includes the heat shock protein 67B2 of Drosophila melanogaster and other similar proteins, many of which are uncharacterized.


Pssm-ID: 238777 [Multi-domain]  Cd Length: 106  Bit Score: 36.48  E-value: 4.37e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 593429537 234 YQPYTVYPATSTNRLTFDLRSKEAYHGGHIEGTINIPYDK 273
Cdd:cd01519    3 FEEVKNLPNPHPNKVLIDVREPEELKTGKIPGAINIPLSS 42
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 85-123 5.69e-03

uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YmaE and Nostoc all1228 proteins.Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 37.17  E-value: 5.69e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 593429537  85 LKVLHTPGHTPESISFLLTDEGAgaqvpmgLFSGDFIFV 123
Cdd:cd07727  104 LTLIPVPGHTRGSVVLLYKEKGV-------LFTGDHLAW 135
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 23-169 6.06e-03

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 37.58  E-value: 6.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  23 ITHAAETHIHANFVSGIRDVAiklNASIYVS-GESDDMLGYKNMPNHTHFVQHNDDIYVGNIK-------------LKVL 88
Cdd:cd07729   89 IDYVILSHLHFDHAGGLDLFP---NATIIVQrAELEYATGPDPLAAGYYEDVLALDDDLPGGRvrlvdgdydlfpgVTLI 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 593429537  89 HTPGHTPESISFLLTDEGagaqvpmglfsGDFIFVGDIG--RPDLLEKAVKVEGLSEIGAKQMFKSIESIKDLPDyIQIW 166
Cdd:cd07729  166 PTPGHTPGHQSVLVRLPE-----------GTVLLAGDAAytYENLEEGRPPGINYDPEAALASLERLKALAEREG-ARVI 233


                 ...
gi 593429537 167 PGH 169
Cdd:cd07729  234 PGH 236
Rhodanese pfam00581
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ...
 250-272 7.73e-03

Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.


Pssm-ID: 425764 [Multi-domain]  Cd Length: 92  Bit Score: 35.15  E-value: 7.73e-03
                          10        20
                  ....*....|....*....|...
gi 593429537  250 FDLRSKEAYHGGHIEGTINIPYD 272
Cdd:pfam00581   9 IDVRPPEEYAKGHIPGAVNVPLS 31
 
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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