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Conserved domains on  [gi|6324614|ref|NP_014683|]
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hydroxyacylglutathione hydrolase GLO4 [Saccharomyces cerevisiae S288C]

Protein Classification

hydroxyacylglutathione hydrolase( domain architecture ID 10869960)

hydroxyacylglutathione hydrolase is a type II glyoxalase that catalyzes the hydrolysis of (R)-S-lactoylglutathione to (R)-lactate and glutathione

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 18-198 2.12e-64

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: 199.22  E-value: 2.12e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   18 MRWLTGGVNYSYLLSTEDRRNSWLIDPAEPLEVSPKLsAEEKKSIDAIVNTHHHYDHSGGNLALYSILcqensgHDIKII 97
Cdd:cd07723   1 VPIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAAL-EKNGLTLTAILTTHHHWDHTGGNAELKALF------PDAPVY 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   98 GGSKSS-PGVTEVPDNLQQYHLGNLRVTCIRTPCHTKDSICYYIKDletgEQCIFTGDTLFIAGCGRFFEGTGRDMDMAL 176
Cdd:cd07723  74 GPAEDRiPGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPD----EPALFTGDTLFSGGCGRFFEGTAEQMYASL 149

                       170       180
                ....*....|....*....|...
gi 6324614  177 NQIM-LravgetnWNKVKIYPGH 198
Cdd:cd07723 150 QKLLaL-------PDDTLVYCGH 165
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 199-285 3.96e-20

Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of hydroxyacylglutathione hydrolase enzymes. Substrate binding occurs at the interface between this domain and the catalytic domain (pfam00753).


:

Pssm-ID: 465030 [Multi-domain]  Cd Length: 82  Bit Score: 82.10  E-value: 3.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614    199 EYTKGNVSFIRAKIysdiGQNKEFDALEQYCK---SNECTTGHFTLRDELGYNPFMRLDDRAVRLAVGDTagtyPRSVVM 275
Cdd:pfam16123   1 EYTLSNLKFALSVE----PDNEALQKRLAWVEalrAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGET----DPVEVF 72

                          90
                  ....*....|
gi 6324614    276 QELRKLKNAM 285
Cdd:pfam16123  73 AALRELKDNF 82
 
Name Accession Description Interval E-value
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 18-198 2.12e-64

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: 199.22  E-value: 2.12e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   18 MRWLTGGVNYSYLLSTEDRRNSWLIDPAEPLEVSPKLsAEEKKSIDAIVNTHHHYDHSGGNLALYSILcqensgHDIKII 97
Cdd:cd07723   1 VPIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAAL-EKNGLTLTAILTTHHHWDHTGGNAELKALF------PDAPVY 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   98 GGSKSS-PGVTEVPDNLQQYHLGNLRVTCIRTPCHTKDSICYYIKDletgEQCIFTGDTLFIAGCGRFFEGTGRDMDMAL 176
Cdd:cd07723  74 GPAEDRiPGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPD----EPALFTGDTLFSGGCGRFFEGTAEQMYASL 149

                       170       180
                ....*....|....*....|...
gi 6324614  177 NQIM-LravgetnWNKVKIYPGH 198
Cdd:cd07723 150 QKLLaL-------PDDTLVYCGH 165
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 26-283 3.65e-53

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 173.79  E-value: 3.65e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614    26 NYSYLLSTEDRRNSWLIDPAEPLEVSpKLSAEEKKSIDAIVNTHHHYDHSGGNLALYSILcqensgHDIKIIGGSKSS-P 104
Cdd:PLN02469  12 NYAYLIIDESTKDAAVVDPVDPEKVL-QAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLV------PGIKVYGGSLDNvK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   105 GVTEVPDNLQQYHLGN-LRVTCIRTPCHTKDSICYYIKDLETGEQCIFTGDTLFIAGCGRFFEGTGRDMDMALNQIMLRA 183
Cdd:PLN02469  85 GCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDPAVFTGDTLFIAGCGKFFEGTAEQMYQSLCVTLGSL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   184 VGETNwnkvkIYPGHEYTKGNVSFIRA--KIYSDIGQNKEFdALEQycKSNECTTGHFTLRDELGYNPFMRLDDRAVRLA 261
Cdd:PLN02469 165 PKPTQ-----VYCGHEYTVKNLKFALTvePDNEKLKQKLEW-AEKQ--RQAGLPTVPSTIEEELETNPFMRVDLPEIQEK 236

                        250       260
                 ....*....|....*....|..
gi 6324614   262 VGDTAgtypRSVVMQELRKLKN 283
Cdd:PLN02469 237 VGCES----PVEALREVRKMKD 254
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 26-283 5.90e-46

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


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 155.00  E-value: 5.90e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614     26 NYSYLLSTEDRRnSWLIDPAEPLEVSPKLsAEEKKSIDAIVNTHHHYDHSGGNLALysilcQEnsGHDIKIIGGSKS-SP 104
Cdd:TIGR03413  10 NYIWLLHDPDGQ-AAVVDPGEAEPVLDAL-EARGLTLTAILLTHHHHDHVGGVAEL-----LE--AFPAPVYGPAEErIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614    105 GVTEVPDNLQQYHLGNLRVTCIRTPCHTKDSICYYIKDletgEQCIFTGDTLFIAGCGRFFEGTGRDMDMALNQimLRAV 184
Cdd:TIGR03413  81 GITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPD----SPALFCGDTLFSAGCGRLFEGTPEQMYDSLQR--LAAL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614    185 -GETnwnkvKIYPGHEYTKGNVSFIRAkiysdI-GQNkefDALEQYCKS-------NECT--TghfTLRDELGYNPFMRL 253
Cdd:TIGR03413 155 pDDT-----LVYCAHEYTLSNLRFALT-----VePDN---PALQERLKEvealraqGQPTlpS---TLGLERATNPFLRA 218

                         250       260       270
                  ....*....|....*....|....*....|
gi 6324614    254 DDRAVRLAVGDTAGTypRSVVMQELRKLKN 283
Cdd:TIGR03413 219 DDPAVRAALGSQGAD--PVEVFAALRAWKD 246
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 27-198 1.53e-27

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 104.94  E-value: 1.53e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614      27 YSYLLSTEDRRnsWLIDP--AEPLEVSPKLSAEEKKSIDAIVNTHHHYDHSGGNLALYS-----ILCQE-------NSGH 92
Cdd:smart00849   1 NSYLVRDDGGA--ILIDTgpGEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEapgapVYAPEgtaellkDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614      93 DIKIIGGSKSSPGVTEVPDNLQQYHLGNLRVTCIRTPCHTKDSICYYIKDletgEQCIFTGDTLFIAGCGR-FFEGTGRD 171
Cdd:smart00849  79 LLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPE----GKILFTGDLLFAGGDGRtLVDGGDAA 154

                          170       180
                   ....*....|....*....|....*..
gi 6324614     172 MDMALNQIMLRAVGEtnwnKVKIYPGH 198
Cdd:smart00849 155 ASDALESLLKLLKLL----PKLVVPGH 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 26-201 2.02e-25

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: 100.15  E-value: 2.02e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   26 NYSYLLSTEDRrnSWLIDPAEPLEVSPKLSA---EEKKSIDAIVNTHHHYDHSGGNLALYS-----ILCQENSGHDIKII 97
Cdd:COG0491  15 VNSYLIVGGDG--AVLIDTGLGPADAEALLAalaALGLDIKAVLLTHLHPDHVGGLAALAEafgapVYAHAAEAEALEAP 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   98 GGSKSSPGVTEVPDNL----QQYHLGNLRVTCIRTPCHTKDSICYYIKDletgEQCIFTGDTLFIAGCGRFFEGTGrDMD 173
Cdd:COG0491  93 AAGALFGREPVPPDRTledgDTLELGGPGLEVIHTPGHTPGHVSFYVPD----EKVLFTGDALFSGGVGRPDLPDG-DLA 167

                       170       180
                ....*....|....*....|....*....
gi 6324614  174 MALNQI-MLRAVGETnwnkvKIYPGHEYT 201
Cdd:COG0491 168 QWLASLeRLLALPPD-----LVIPGHGPP 191
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 199-285 3.96e-20

Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of hydroxyacylglutathione hydrolase enzymes. Substrate binding occurs at the interface between this domain and the catalytic domain (pfam00753).


Pssm-ID: 465030 [Multi-domain]  Cd Length: 82  Bit Score: 82.10  E-value: 3.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614    199 EYTKGNVSFIRAKIysdiGQNKEFDALEQYCK---SNECTTGHFTLRDELGYNPFMRLDDRAVRLAVGDTagtyPRSVVM 275
Cdd:pfam16123   1 EYTLSNLKFALSVE----PDNEALQKRLAWVEalrAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGET----DPVEVF 72

                          90
                  ....*....|
gi 6324614    276 QELRKLKNAM 285
Cdd:pfam16123  73 AALRELKDNF 82
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
21-198 5.92e-16

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 74.33  E-value: 5.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614     21 LTGGVNYSYLLSTEDRrnsW-LIDP----AEPLEVSPKLSAEEKKSIDAIVNTHHHYDHSGGNLAL-------------- 81
Cdd:pfam00753   1 LGPGQVNSYLIEGGGG---AvLIDTggsaEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELaeatdvpvivvaee 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614     82 -----YSILCQENSGHDIKIIGGSKSSPGVteVPDNLQQYHLGNLRVTCIRTPCHTKDSICYYIKDletgEQCIFTGDTL 156
Cdd:pfam00753  78 arellDEELGLAASRLGLPGPPVVPLPPDV--VLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGG----GKVLFTGDLL 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 6324614    157 FIAGCGR--FFEGTGRDMDMALNQIMLRAVGE-TNWNKVKIYPGH 198
Cdd:pfam00753 152 FAGEIGRldLPLGGLLVLHPSSAESSLESLLKlAKLKAAVIVPGH 196
 
Name Accession Description Interval E-value
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 18-198 2.12e-64

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: 199.22  E-value: 2.12e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   18 MRWLTGGVNYSYLLSTEDRRNSWLIDPAEPLEVSPKLsAEEKKSIDAIVNTHHHYDHSGGNLALYSILcqensgHDIKII 97
Cdd:cd07723   1 VPIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAAL-EKNGLTLTAILTTHHHWDHTGGNAELKALF------PDAPVY 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   98 GGSKSS-PGVTEVPDNLQQYHLGNLRVTCIRTPCHTKDSICYYIKDletgEQCIFTGDTLFIAGCGRFFEGTGRDMDMAL 176
Cdd:cd07723  74 GPAEDRiPGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPD----EPALFTGDTLFSGGCGRFFEGTAEQMYASL 149

                       170       180
                ....*....|....*....|...
gi 6324614  177 NQIM-LravgetnWNKVKIYPGH 198
Cdd:cd07723 150 QKLLaL-------PDDTLVYCGH 165
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 26-283 3.65e-53

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 173.79  E-value: 3.65e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614    26 NYSYLLSTEDRRNSWLIDPAEPLEVSpKLSAEEKKSIDAIVNTHHHYDHSGGNLALYSILcqensgHDIKIIGGSKSS-P 104
Cdd:PLN02469  12 NYAYLIIDESTKDAAVVDPVDPEKVL-QAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLV------PGIKVYGGSLDNvK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   105 GVTEVPDNLQQYHLGN-LRVTCIRTPCHTKDSICYYIKDLETGEQCIFTGDTLFIAGCGRFFEGTGRDMDMALNQIMLRA 183
Cdd:PLN02469  85 GCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDPAVFTGDTLFIAGCGKFFEGTAEQMYQSLCVTLGSL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   184 VGETNwnkvkIYPGHEYTKGNVSFIRA--KIYSDIGQNKEFdALEQycKSNECTTGHFTLRDELGYNPFMRLDDRAVRLA 261
Cdd:PLN02469 165 PKPTQ-----VYCGHEYTVKNLKFALTvePDNEKLKQKLEW-AEKQ--RQAGLPTVPSTIEEELETNPFMRVDLPEIQEK 236

                        250       260
                 ....*....|....*....|..
gi 6324614   262 VGDTAgtypRSVVMQELRKLKN 283
Cdd:PLN02469 237 VGCES----PVEALREVRKMKD 254
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 26-283 5.90e-46

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


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 155.00  E-value: 5.90e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614     26 NYSYLLSTEDRRnSWLIDPAEPLEVSPKLsAEEKKSIDAIVNTHHHYDHSGGNLALysilcQEnsGHDIKIIGGSKS-SP 104
Cdd:TIGR03413  10 NYIWLLHDPDGQ-AAVVDPGEAEPVLDAL-EARGLTLTAILLTHHHHDHVGGVAEL-----LE--AFPAPVYGPAEErIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614    105 GVTEVPDNLQQYHLGNLRVTCIRTPCHTKDSICYYIKDletgEQCIFTGDTLFIAGCGRFFEGTGRDMDMALNQimLRAV 184
Cdd:TIGR03413  81 GITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPD----SPALFCGDTLFSAGCGRLFEGTPEQMYDSLQR--LAAL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614    185 -GETnwnkvKIYPGHEYTKGNVSFIRAkiysdI-GQNkefDALEQYCKS-------NECT--TghfTLRDELGYNPFMRL 253
Cdd:TIGR03413 155 pDDT-----LVYCAHEYTLSNLRFALT-----VePDN---PALQERLKEvealraqGQPTlpS---TLGLERATNPFLRA 218

                         250       260       270
                  ....*....|....*....|....*....|
gi 6324614    254 DDRAVRLAVGDTAGTypRSVVMQELRKLKN 283
Cdd:TIGR03413 219 DDPAVRAALGSQGAD--PVEVFAALRAWKD 246
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 26-266 7.74e-35

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 128.04  E-value: 7.74e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614    26 NYSYLLSTEDRRNSWLIDPAEpleVSPKLSAEEKKS--IDAIVNTHHHYDHSGGNLALysilcqeNSGHDIKIIGGSKSS 103
Cdd:PLN02398  87 NYAYLLHDEDTGTVGVVDPSE---AVPVIDALSRKNrnLTYILNTHHHYDHTGGNLEL-------KARYGAKVIGSAVDK 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   104 ---PGVTEVPDNLQQYHLGNLRVTCIRTPCHTKDSICYYIkdleTGEQCIFTGDTLFIAGCGRFFEGTGRDMDMALNQIM 180
Cdd:PLN02398 157 driPGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYF----PGSGAIFTGDTLFSLSCGKLFEGTPEQMLSSLQKII 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   181 lRAVGETNwnkvkIYPGHEYTKGNVSFIRAkiysdIGQNKEfdALEQYC------KSNECTTGHFTLRDELGYNPFMRLD 254
Cdd:PLN02398 233 -SLPDDTN-----IYCGHEYTLSNSKFALS-----IEPNNE--VLQSYAahvahlRSKGLPTIPTTVKMEKACNPFLRTS 299

                        250
                 ....*....|....
gi 6324614   255 DRAVR--LAVGDTA 266
Cdd:PLN02398 300 STDIRksLSIPDTA 313
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 24-198 3.12e-28

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: 106.99  E-value: 3.12e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   24 GVNySYLLSTEDRRNsWLIDPAepLEVSPKLSA---EEKKSIDAIVNTHHHYDHSGGNLALYS-----ILCQENSGHDIK 95
Cdd:cd06262   9 QTN-CYLVSDEEGEA-ILIDPG--AGALEKILEaieELGLKIKAILLTHGHFDHIGGLAELKEapgapVYIHEADAELLE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   96 IIGGSKSS----PGVTEVPDNL----QQYHLGNLRVTCIRTPCHTKDSICYYIKDletgEQCIFTGDTLFIAGCGRFFEG 167
Cdd:cd06262  85 DPELNLAFfgggPLPPPEPDILledgDTIELGGLELEVIHTPGHTPGSVCFYIEE----EGVLFTGDTLFAGSIGRTDLP 160

                       170       180       190
                ....*....|....*....|....*....|...
gi 6324614  168 TGRDMDM--ALNQIMLRAVGETnwnkvKIYPGH 198
Cdd:cd06262 161 GGDPEQLieSIKKLLLLLPDDT-----VVYPGH 188
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 27-198 1.53e-27

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 104.94  E-value: 1.53e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614      27 YSYLLSTEDRRnsWLIDP--AEPLEVSPKLSAEEKKSIDAIVNTHHHYDHSGGNLALYS-----ILCQE-------NSGH 92
Cdd:smart00849   1 NSYLVRDDGGA--ILIDTgpGEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEapgapVYAPEgtaellkDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614      93 DIKIIGGSKSSPGVTEVPDNLQQYHLGNLRVTCIRTPCHTKDSICYYIKDletgEQCIFTGDTLFIAGCGR-FFEGTGRD 171
Cdd:smart00849  79 LLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPE----GKILFTGDLLFAGGDGRtLVDGGDAA 154

                          170       180
                   ....*....|....*....|....*..
gi 6324614     172 MDMALNQIMLRAVGEtnwnKVKIYPGH 198
Cdd:smart00849 155 ASDALESLLKLLKLL----PKLVVPGH 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 26-201 2.02e-25

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: 100.15  E-value: 2.02e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   26 NYSYLLSTEDRrnSWLIDPAEPLEVSPKLSA---EEKKSIDAIVNTHHHYDHSGGNLALYS-----ILCQENSGHDIKII 97
Cdd:COG0491  15 VNSYLIVGGDG--AVLIDTGLGPADAEALLAalaALGLDIKAVLLTHLHPDHVGGLAALAEafgapVYAHAAEAEALEAP 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   98 GGSKSSPGVTEVPDNL----QQYHLGNLRVTCIRTPCHTKDSICYYIKDletgEQCIFTGDTLFIAGCGRFFEGTGrDMD 173
Cdd:COG0491  93 AAGALFGREPVPPDRTledgDTLELGGPGLEVIHTPGHTPGHVSFYVPD----EKVLFTGDALFSGGVGRPDLPDG-DLA 167

                       170       180
                ....*....|....*....|....*....
gi 6324614  174 MALNQI-MLRAVGETnwnkvKIYPGHEYT 201
Cdd:COG0491 168 QWLASLeRLLALPPD-----LVIPGHGPP 191
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 26-198 8.88e-25

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: 97.61  E-value: 8.88e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   26 NYSYLLSTEDRRNSWLIDPAEPLEVSPKLSAEEKKSIDAIVNTHHHYDHSGGNLALYSIlcqensgHDIKI------IGG 99
Cdd:cd16275  12 NYSYIIIDKATREAAVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAK-------YDAPVymskeeIDY 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614  100 SK-SSPGVTEVpDNLQQYHLGNLRVTCIRTPCHTKDSICYYIkdletgEQCIFTGDTLFIAGCGR--FFEGTGRDMDMAL 176
Cdd:cd16275  85 YGfRCPNLIPL-EDGDTIKIGDTEITCLLTPGHTPGSMCYLL------GDSLFTGDTLFIEGCGRcdLPGGDPEEMYESL 157

                       170       180
                ....*....|....*....|..
gi 6324614  177 NqiMLRAVGETNwnkVKIYPGH 198
Cdd:cd16275 158 Q--RLKKLPPPN---TRVYPGH 174
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 26-255 2.17e-21

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 90.27  E-value: 2.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614    26 NYSYLLSTEDRRnSWLIDPAEpleVSPKLSA--EEKKSIDAIVNTHHHYDHSGGNLALYSILCQensghdIKIIGGSKS- 102
Cdd:PRK10241  12 NYIWVLNDEAGR-CLIVDPGE---AEPVLNAiaENNWQPEAIFLTHHHHDHVGGVKELVEKFPQ------IVVYGPQETq 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   103 SPGVTEVPDNLQQYHLGNLRVTCIRTPCHTKDSICYYikdletGEQCIFTGDTLFIAGCGRFFEGTGRDMDMALNQImlR 182
Cdd:PRK10241  82 DKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF------SKPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKI--N 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324614   183 AVGEtnwnKVKIYPGHEYTKGNVSFIRAKIYSDIGQNkefdalEQYCKSNEC-----TTGHFTLRDELGYNPFMRLDD 255
Cdd:PRK10241 154 ALPD----DTLICCAHEYTLSNMKFALSILPHDLSIN------DYYRKVKELraknqITLPVILKNERQINLFLRTED 221
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 27-200 1.59e-20

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: 86.30  E-value: 1.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   27 YSYLLSTEDRRNSWLIDPA-EPLEVSPKLSAEEKKSIDAIVNTHHHYDH-SGgnlALYsiLCQEnsgHDIKIIGGSKSSP 104
Cdd:cd07724  13 LSYLVGDPETGEAAVIDPVrDSVDRYLDLAAELGLKITYVLETHVHADHvSG---ARE--LAER---TGAPIVIGEGAPA 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614  105 GVTEVP--DNlQQYHLGNLRVTCIRTPCHTKDSICYYIKDletgEQCIFTGDTLFIAGCGR--FFegtGRDMDMA----- 175
Cdd:cd07724  85 SFFDRLlkDG-DVLELGNLTLEVLHTPGHTPESVSYLVGD----PDAVFTGDTLFVGDVGRpdLP---GEAEGLArqlyd 156

                       170       180
                ....*....|....*....|....*.
gi 6324614  176 -LNQIMLRAVGETnwnkvKIYPGHEY 200
Cdd:cd07724 157 sLQRKLLLLPDET-----LVYPGHDY 177
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 199-285 3.96e-20

Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of hydroxyacylglutathione hydrolase enzymes. Substrate binding occurs at the interface between this domain and the catalytic domain (pfam00753).


Pssm-ID: 465030 [Multi-domain]  Cd Length: 82  Bit Score: 82.10  E-value: 3.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614    199 EYTKGNVSFIRAKIysdiGQNKEFDALEQYCK---SNECTTGHFTLRDELGYNPFMRLDDRAVRLAVGDTagtyPRSVVM 275
Cdd:pfam16123   1 EYTLSNLKFALSVE----PDNEALQKRLAWVEalrAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGET----DPVEVF 72

                          90
                  ....*....|
gi 6324614    276 QELRKLKNAM 285
Cdd:pfam16123  73 AALRELKDNF 82
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 24-198 3.82e-17

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: 77.19  E-value: 3.82e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   24 GVNySYLLSTEDRRnsWLIDPAEPLEVSPK-----LSAEEKKSIDAIVNTHHHYDHSGGnlaLYSILcQENSGHDIKI-- 96
Cdd:cd07722  17 GTN-TYLVGTGKRR--ILIDTGEGRPSYIPllksvLDSEGNATISDILLTHWHHDHVGG---LPDVL-DLLRGPSPRVyk 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   97 -------IGGSKSSPGVTEVPDNlQQYHLGNLRVTCIRTPCHTKDSICYYIKDletgEQCIFTGDTlfIAGCGR-FFEgt 168
Cdd:cd07722  90 fprpeedEDPDEDGGDIHDLQDG-QVFKVEGATLRVIHTPGHTTDHVCFLLEE----ENALFTGDC--VLGHGTaVFE-- 160

                       170       180       190
                ....*....|....*....|....*....|....
gi 6324614  169 grdmD----MALNQIMLRAvgetnwNKVKIYPGH 198
Cdd:cd07722 161 ----DlaayMASLKKLLSL------GPGRIYPGH 184
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
21-198 5.92e-16

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 74.33  E-value: 5.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614     21 LTGGVNYSYLLSTEDRrnsW-LIDP----AEPLEVSPKLSAEEKKSIDAIVNTHHHYDHSGGNLAL-------------- 81
Cdd:pfam00753   1 LGPGQVNSYLIEGGGG---AvLIDTggsaEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELaeatdvpvivvaee 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614     82 -----YSILCQENSGHDIKIIGGSKSSPGVteVPDNLQQYHLGNLRVTCIRTPCHTKDSICYYIKDletgEQCIFTGDTL 156
Cdd:pfam00753  78 arellDEELGLAASRLGLPGPPVVPLPPDV--VLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGG----GKVLFTGDLL 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 6324614    157 FIAGCGR--FFEGTGRDMDMALNQIMLRAVGE-TNWNKVKIYPGH 198
Cdd:pfam00753 152 FAGEIGRldLPLGGLLVLHPSSAESSLESLLKlAKLKAAVIVPGH 196
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 29-198 7.16e-14

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: 68.91  E-value: 7.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   29 YLLSTEDRRNSWLIDPAEPLEVSPKLSAEEKKSIDAIVNTHHHYDHSGGNLALYS-----ILCQE---------NSGHDI 94
Cdd:cd16322  14 YLVADEGGGEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRhpgapVYLHPddlplyeaaDLGAKA 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   95 KIIGGSKSSPgvtevPDNL----QQYHLGNLRVTCIRTPCHTKDSICYYIKDletgEQCIFTGDTLFIAGCGR--FFEGT 168
Cdd:cd16322  94 FGLGIEPLPP-----PDRLledgQTLTLGGLEFKVLHTPGHSPGHVCFYVEE----EGLLFSGDLLFQGSIGRtdLPGGD 164

                       170       180       190
                ....*....|....*....|....*....|
gi 6324614  169 GRDMDMALNQIMlRAVGETnwnkvKIYPGH 198
Cdd:cd16322 165 PKAMAASLRRLL-TLPDET-----RVFPGH 188
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 24-155 4.03e-12

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: 63.28  E-value: 4.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   24 GVNySYLLSTEDRRnsWLIDP--AEPLEVSPKLSAEEKKSIDAIVNTHHHYDHSGGNLALYSILCQENSGHDIKIIGGSK 101
Cdd:cd16278  17 GTN-TYLLGAPDGV--VVIDPgpDDPAHLDALLAALGGGRVSAILVTHTHRDHSPGAARLAERTGAPVRAFGPHRAGGQD 93

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 6324614  102 SSPGVTEVPDNLQQYHLGNLRVTCIRTPCHTKDSICYYIKDletgEQCIFTGDT 155
Cdd:cd16278  94 TDFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALED----EGALFTGDH 143
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 24-156 1.59e-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: 1.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   24 GVNYSYLLSTEDRRNswLIDPAEPLEVSPKLSAEEKK-------SIDAIVNTHHHYDHSGgnLALYsilCQENSGHDIKI 96
Cdd:cd07725  13 GHVNVYLLRDGDETT--LIDTGLATEEDAEALWEGLKelglkpsDIDRVLLTHHHPDHIG--LAGK---LQEKSGATVYI 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   97 iggskssPGVTEVPDnLQQYHLGNLRVTCIRTPCHTKDSICYYikDLETGEqcIFTGDTL 156
Cdd:cd07725  86 -------LDVTPVKD-GDKIDLGGLRLKVIETPGHTPGHIVLY--DEDRRE--LFVGDAV 133
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
15-167 1.81e-08

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 54.05  E-value: 1.81e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   15 PIKMRWLTggvnySYLLSTEDRRnsWLIDPAEP-------LEVSPKlsaeekkSIDAIVNTHHHYDHSGGNLALYSILCQ 87
Cdd:COG1234  13 PTPGRATS-----SYLLEAGGER--LLIDCGEGtqrqllrAGLDPR-------DIDAIFITHLHGDHIAGLPGLLSTRSL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   88 ENSGHDIKIIG-------------GSKSSPG----VTEVPDNlQQYHLGNLRVTCIRTpCHTKDSICYYIkdlETGEQCI 150
Cdd:COG1234  79 AGREKPLTIYGppgtkefleallkASGTDLDfpleFHEIEPG-EVFEIGGFTVTAFPL-DHPVPAYGYRF---EEPGRSL 153

                       170
                ....*....|....*...
gi 6324614  151 -FTGDTLFIAGCGRFFEG 167
Cdd:COG1234 154 vYSGDTRPCEALVELAKG 171
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 60-198 3.77e-08

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: 52.61  E-value: 3.77e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   60 KSIDAIVNTHHHYDHSGGnLAlysILCQEN------SGHDIKIIGGSKSSPGVTE----------VPDNLQQYH------ 117
Cdd:cd07721  48 KDIRRILLTHGHIDHIGS-LA---ALKEAPgapvyaHEREAPYLEGEKPYPPPVRlgllgllsplLPVKPVPVDrtledg 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614  118 -----LGNLRVtcIRTPCHTKDSICYYIKDLETgeqcIFTGDTLFIAGcGRFFEGTGR---DMDMALNQImlRAVGETNW 189
Cdd:cd07721 124 dtldlAGGLRV--IHTPGHTPGHISLYLEEDGV----LIAGDALVTVG-GELVPPPPPftwDMEEALESL--RKLAELDP 194


                ....*....
gi 6324614  190 NkvKIYPGH 198
Cdd:cd07721 195 E--VLAPGH 201
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 27-206 1.06e-07

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 51.72  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614    27 YSYLLS--TEDRRNSWLIDPAEPlEVSPKLSAEEKKSIDAI--VNTHHHYDHSGGNLALYSILCQENSGhdIKIIGGSKS 102
Cdd:PLN02962  24 YTYLLAdvSHPDKPALLIDPVDK-TVDRDLSLVKELGLKLIyaMNTHVHADHVTGTGLLKTKLPGVKSI--ISKASGSKA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   103 SPGVtevpDNLQQYHLGNLRVTCIRTPCHTKDSICYYikdleTGE-------QCIFTGDTLFIAGCGR--FFEGTGRDMD 173
Cdd:PLN02962 101 DLFV----EPGDKIYFGDLYLEVRATPGHTAGCVTYV-----TGEgpdqpqpRMAFTGDALLIRGCGRtdFQGGSSDQLY 171

                        170       180       190
                 ....*....|....*....|....*....|...
gi 6324614   174 MALNQIMLRAVGETnwnkvKIYPGHEYTKGNVS 206
Cdd:PLN02962 172 KSVHSQIFTLPKDT-----LIYPAHDYKGFTVS 199
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 59-198 1.03e-06

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 48.33  E-value: 1.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   59 KKSIDAIVNTHHHYDHSGGNLALYS----ILCQENSGHDIKIIGGSKSS----------PGVTEVP-----DNLQQYHLG 119
Cdd:cd16282  50 DKPVRYVVNTHYHGDHTLGNAAFADagapIIAHENTREELAARGEAYLElmrrlggdamAGTELVLpdrtfDDGLTLDLG 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614  120 NLRVTCIRT-PCHTKDSICYYIKDletgEQCIFTGDTLFIAGCGRFFEGTGRDMDMALNQimLRAVGETnwnkvKIYPGH 198
Cdd:cd16282 130 GRTVELIHLgPAHTPGDLVVWLPE----EGVLFAGDLVFNGRIPFLPDGSLAGWIAALDR--LLALDAT-----VVVPGH 198
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 15-176 1.83e-06

L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 47.60  E-value: 1.83e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   15 PIKMRWLTGGvnySYLLSTEDRRnsWLIDP-----AEPLEVSPkLSAEEKKSIDAIVNTHHHYDHSG--------GNLAL 81
Cdd:COG2220   3 GMKITWLGHA---TFLIETGGKR--ILIDPvfsgrASPVNPLP-LDPEDLPKIDAVLVTHDHYDHLDdatlralkRTGAT 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   82 ysILCQENSGHDIKIIGGSKsspgVTEVpDNLQQYHLGNLRVTCirTPCH--------TKDSICYYIkdLETGEQCIF-T 152
Cdd:COG2220  77 --VVAPLGVAAWLRAWGFPR----VTEL-DWGESVELGGLTVTA--VPARhssgrpdrNGGLWVGFV--IETDGKTIYhA 145

                       170       180
                ....*....|....*....|....*.
gi 6324614  153 GDTLFIAGcgrfFEGTGR--DMDMAL 176
Cdd:COG2220 146 GDTGYFPE----MKEIGErfPIDVAL 167
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 28-198 1.14e-05

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: 44.85  E-value: 1.14e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   28 SYLLSTEDRRNSWLIDPAEPLEVSPKLSAEEKKSIDAIVNTHHHYDHSGGNLALysilcqeNSGHDIKIIGGSKS-SPGV 106
Cdd:cd07737  13 CSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAEL-------AEHYGVPIIGPHKEdKFLL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614  107 TEVPDNLQQYHL--------------------GNLRVTCIRTPCHTKDSICYYIKDletgEQCIFTGDTLFIAGCGR--F 164
Cdd:cd07737  86 ENLPEQSQMFGFppaeaftpdrwleegdtvtvGNLTLEVLHCPGHTPGHVVFFNRE----SKLAIVGDVLFKGSIGRtdF 161

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 6324614  165 FEGTGRDmdmalnqiMLRAVGETNW---NKVKIYPGH 198
Cdd:cd07737 162 PGGNHAQ--------LIASIKEKLLplgDDVTFIPGH 190
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 28-155 4.32e-05

Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. 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: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 43.02  E-value: 4.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   28 SYLLSTEDRRnsWLIDPAEPleVSPKLSAEEKK--SIDAIVNTHHHYDHSGGNLALYSILCQENSGHDIKIIGG------ 99
Cdd:cd16272  19 SYLLETGGTR--ILLDCGEG--TVYRLLKAGVDpdKLDAIFLSHFHLDHIGGLPTLLFARRYGGRKKPLTIYGPkgikef 94

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614  100 -------------SKSSPGVTEVPDNLQQYHLGNLRVTCIRTpCHTKDSICYYIkdlETGEQCI-FTGDT 155
Cdd:cd16272  95 lekllnfpveilpLGFPLEIEELEEGGEVLELGDLKVEAFPV-KHSVESLGYRI---EAEGKSIvYSGDT 160
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 15-167 9.98e-05

Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme; this subgroup includes the short form (ELAC1). Only the short form exists in bacteria. 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: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 42.82  E-value: 9.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   15 PIKMRWLTggvnySYLLSTEDRRnsWLIDPAE----PLEVSpKLSAeekKSIDAIVNTHHHYDHSGGNLALYSILCQENS 90
Cdd:cd07717  11 PTPERNLS-----SIALRLEGEL--WLFDCGEgtqrQLLRA-GLSP---SKIDRIFITHLHGDHILGLPGLLSTMSLLGR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   91 GHDIKIIG-------------GSKSSPG----VTEVPDNLQQ-YHLGNLRVTCIRTpCHTKDSICYYIkdlETGEQCIFT 152
Cdd:cd07717  80 TEPLTIYGpkglkefletllrLSASRLPypieVHELEPDPGLvFEDDGFTVTAFPL-DHRVPCFGYRF---EEGRKIAYL 155

                       170
                ....*....|....*
gi 6324614  153 GDTLFIAGCGRFFEG 167
Cdd:cd07717 156 GDTRPCEGLVELAKG 170
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 61-155 1.37e-04

Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 41.73  E-value: 1.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   61 SIDAIVNTHHHYDHSGGNLALYSILCQENSGHDIKIIG---------------------------GSKSSPG----VTEV 109
Cdd:cd07719  51 DLDAVFLTHLHSDHVADLPALLLTAWLAGRKTPLPVYGppgtralvdgllaayaldidyrarigdEGRPDPGalveVHEI 130

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 6324614  110 PDNLQQYHLGNLRVTCIRTPcH--TKDSICYYIkdlETGEQCI-FTGDT 155
Cdd:cd07719 131 AAGGVVYEDDGVKVTAFLVD-HgpVPPALAYRF---DTPGRSVvFSGDT 175
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 54-198 2.14e-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: 41.42  E-value: 2.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   54 LSAEEkksIDAIVNTHHHYDHSgGNLAL---------YSILCQENSGHDIKIIGGSKSSPGVtEVpdnlqqyhlgnlrvt 124
Cdd:cd07711  56 LSPED---IDYVVLTHGHPDHI-GNLNLfpnatvivgWDICGDSYDDHSLEEGDGYEIDENV-EV--------------- 115

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6324614  125 cIRTPCHTKDSICYYIKDLETGEqCIFTGDtLFI----AGCGRFFEGTGRDMDmALNQIMLRAVGETNWnkvkIYPGH 198
Cdd:cd07711 116 -IPTPGHTPEDVSVLVETEKKGT-VAVAGD-LFEreedLEDPILWDPLSEDPE-LQEESRKRILALADW----IIPGH 185
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 28-76 4.30e-04

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. 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: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 40.52  E-value: 4.30e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324614   28 SYLLSTEDRRnsWLID-------------PAEPLEVSPKlsaeekkSIDAIVNTHHHYDHSG 76
Cdd:cd16295  14 CYLLETGGKR--ILLDcglfqggkeleelNNEPFPFDPK-------EIDAVILTHAHLDHSG 66
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-78 7.57e-04

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 39.82  E-value: 7.57e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 6324614   35 DRRNSWLIDPAEPLEVSPKLSA---EEKKSIDAIVNTHHHYDHSGGN 78
Cdd:cd07743  16 GDKEALLIDSGLDEDAGRKIRKileELGWKLKAIINTHSHADHIGGN 62
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 28-159 9.98e-04

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: 39.10  E-value: 9.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   28 SYLLSTEDrrNSWLIDPAEPlevSPKLSA--EEKKSIDAIVNTHHHY--DHS------GGNLALYSILCQENSGHDIKII 97
Cdd:cd07727  17 SYLILRPE--GNILVDSPRY---SPPLAKriEALGGIRYIFLTHRDDvaDHAkwaerfGAKRIIHEDDVNAVTRPDEVIV 91

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324614   98 GGSksSPGVTEVPDnlqqyhlgnlrVTCIRTPCHTKDSICYYIKDletgEQCIFTGDTLFIA 159
Cdd:cd07727  92 LWG--GDPWELDPD-----------LTLIPVPGHTRGSVVLLYKE----KGVLFTGDHLAWS 136
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 41-179 1.13e-03

Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. 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: 293841  Cd Length: 181  Bit Score: 39.18  E-value: 1.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   41 LIDPAEPLEVSPK------------LSAEEKKSIDAIVNTHHHYDHsggnLALYSILCQENSGHDIKIIGG-----SKSS 103
Cdd:cd16283  17 LTDPVFSERASPVsfggpkrltppgLPLEELPPIDAVLISHNHYDH----LDLPTVKRLGGRPPYLVPLGLkkwflKKGI 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614  104 PGVTEVpDNLQQYHLGNLRVTCI-------RTPCHTKDSI-CYYIkdLETGEQCI-FTGDTlfiaGCGRFFEGTGR---D 171
Cdd:cd16283  93 TNVVEL-DWWQSTEIGGVRITFVpaqhwsrRTLFDTNESLwGGWV--IEGEGFRIyFAGDT----GYFPGFREIGRrfgP 165


                ....*...
gi 6324614  172 MDMALNQI 179
Cdd:cd16283 166 IDLALLPI 173
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 60-199 1.35e-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: 39.12  E-value: 1.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   60 KSIDAIVNTHHHYDHSgGNLALYS---ILCQENsghDIKIIGGSKSSPGVTEVPDNLQQYHLGNLR-------------V 123
Cdd:cd07729  87 EDIDYVILSHLHFDHA-GGLDLFPnatIIVQRA---ELEYATGPDPLAAGYYEDVLALDDDLPGGRvrlvdgdydlfpgV 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614  124 TCIRTPCHTKDSICYYIkDLETGeQCIFTGDTLFIAgcgRFFE-----GTGRDMDMALNQI-MLRAVGETnwNKVKIYPG 197
Cdd:cd07729 163 TLIPTPGHTPGHQSVLV-RLPEG-TVLLAGDAAYTY---ENLEegrppGINYDPEAALASLeRLKALAER--EGARVIPG 235


                ..
gi 6324614  198 HE 199
Cdd:cd07729 236 HD 237
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 30-77 2.02e-03

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 38.69  E-value: 2.02e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6324614   30 LLSTEDRRNsWLID--PAEPLE-----VSPKLSAEEKKSIDAIVNTHHHYDHSGG 77
Cdd:COG2333  15 LIRTPDGKT-ILIDtgPRPSFDagervVLPYLRALGIRRLDLLVLTHPDADHIGG 68
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 38-98 2.20e-03

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. 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: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 38.64  E-value: 2.20e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324614   38 NSW-LIDPAEPLEvspklSAEE----------KKSIDAIVNTHHHYDHSGGNLAlysILCQENSGhDIKIIG 98
Cdd:cd07710  27 TGLiIIDTLESAE-----AAKAalelfrkhtgDKPVKAIIYTHSHPDHFGGAGG---FVEEEDSG-KVPIIA 89
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 28-85 2.86e-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: 37.88  E-value: 2.86e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324614   28 SYLLSTEDRrnSWLID--PAEPLE---VSPKLSAEEKKSIDAIVNTHHHYDHSGGnlaLYSIL 85
Cdd:cd07731  12 AILIQTPGK--TILIDtgPRDSFGedvVVPYLKARGIKKLDYLILTHPDADHIGG---LDAVL 69
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
27-77 3.59e-03

Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440850  Cd Length: 273  Bit Score: 38.33  E-value: 3.59e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6324614   27 YSYLLSTEDRR-------NSWLIDPAEPLEVSPKlsaeekkSIDAIVNTHHHYDHSGG 77
Cdd:COG1237  23 LSALIETEGKRilfdtgqSDVLLKNAEKLGIDLS-------DIDAVVLSHGHYDHTGG 73
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 27-77 5.59e-03

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. 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: 293799  Cd Length: 269  Bit Score: 37.60  E-value: 5.59e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324614   27 YSYLLSTEDRRnsWLID--P-------AEPLEVSPKlsaeekkSIDAIVNTHHHYDHSGG 77
Cdd:cd07713  21 LSLLIETEGKK--ILFDtgQsgvllhnAKKLGIDLS-------DIDAVVLSHGHYDHTGG 71
 
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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