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Conserved domains on  [gi|17536925|ref|NP_496556|]
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hydroxyacylglutathione hydrolase [Caenorhabditis elegans]

Protein Classification

hydroxyacylglutathione hydrolase( domain architecture ID 1004484)

hydroxyacylglutathione hydrolase catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid

CATH:  3.60.15.10
EC:  3.1.2.6
Gene Ontology:  GO:0004416|GO:0019243|GO:0046872
SCOP:  4002292

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02469 super family cl31885
hydroxyacylglutathione hydrolase
 12-260 1.17e-89

hydroxyacylglutathione hydrolase


The actual alignment was detected with superfamily member PLN02469:

Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 265.86  E-value: 1.17e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925   12 DNFMYIVKKSSEARAALlVDLVNEEDYKELADKENIDITAVLTTHHHYDHCGGNEGFRRQFPNVMILGGD-SRIPAMDRH 90
Cdd:PLN02469  11 DNYAYLIIDESTKDAAV-VDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSlDNVKGCTHP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925   91 VKHGDMAEF-AGLQIKCLSTPCHTSGHICYHITNPAADSTSpgvVFTGDTLFIAGCGRFFEGTAPQMDVALNEILKNLPV 169
Cdd:PLN02469  90 VENGDKLSLgKDVNILALHTPCHTKGHISYYVTGKEGEDPA---VFTGDTLFIAGCGKFFEGTAEQMYQSLCVTLGSLPK 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  170 ETQIFPGHEYTVANLKFACHVEPGNEKAAQKLEWAQRQIEQGGFTVPSTVAEEKATNPFMRVREsEEIQKSIGTCDAVVG 249
Cdd:PLN02469 167 PTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDL-PEIQEKVGCESPVEA 245

                        250
                 ....*....|.
gi 17536925  250 MAKLREMKNKF 260
Cdd:PLN02469 246 LREVRKMKDNW 256
 
Name Accession Description Interval E-value
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 12-260 1.17e-89

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 265.86  E-value: 1.17e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925   12 DNFMYIVKKSSEARAALlVDLVNEEDYKELADKENIDITAVLTTHHHYDHCGGNEGFRRQFPNVMILGGD-SRIPAMDRH 90
Cdd:PLN02469  11 DNYAYLIIDESTKDAAV-VDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSlDNVKGCTHP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925   91 VKHGDMAEF-AGLQIKCLSTPCHTSGHICYHITNPAADSTSpgvVFTGDTLFIAGCGRFFEGTAPQMDVALNEILKNLPV 169
Cdd:PLN02469  90 VENGDKLSLgKDVNILALHTPCHTKGHISYYVTGKEGEDPA---VFTGDTLFIAGCGKFFEGTAEQMYQSLCVTLGSLPK 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  170 ETQIFPGHEYTVANLKFACHVEPGNEKAAQKLEWAQRQIEQGGFTVPSTVAEEKATNPFMRVREsEEIQKSIGTCDAVVG 249
Cdd:PLN02469 167 PTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDL-PEIQEKVGCESPVEA 245

                        250
                 ....*....|.
gi 17536925  250 MAKLREMKNKF 260
Cdd:PLN02469 246 LREVRKMKDNW 256
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 12-260 1.55e-85

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: 255.15  E-value: 1.55e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925    12 DNFMYIVKKssEARAALLVDLVNEEDYKELADKENIDITAVLTTHHHYDHCGGNEGFRRQFPNVMILGGDSRIPAMDRHV 91
Cdd:TIGR03413   9 DNYIWLLHD--PDGQAAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAFPAPVYGPAEERIPGITHPV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925    92 KHGDMAEFAGLQIKCLSTPCHTSGHICYHItnpaADStspGVVFTGDTLFIAGCGRFFEGTAPQMDVALnEILKNLPVET 171
Cdd:TIGR03413  87 KDGDTVTLGGLEFEVLAVPGHTLGHIAYYL----PDS---PALFCGDTLFSAGCGRLFEGTPEQMYDSL-QRLAALPDDT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925   172 QIFPGHEYTVANLKFACHVEPGNEKAAQKLEWAQRQIEQGGFTVPSTVAEEKATNPFMRVrESEEIQKSIG--TCDAVVG 249
Cdd:TIGR03413 159 LVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRA-DDPAVRAALGsqGADPVEV 237

                         250
                  ....*....|.
gi 17536925   250 MAKLREMKNKF 260
Cdd:TIGR03413 238 FAALRAWKDNF 248
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 12-177 2.32e-72

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: 218.48  E-value: 2.32e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  12 DNFMYIVKKSsEARAALLVDLVNEEDYKELADKENIDITAVLTTHHHYDHCGGNEGFRRQFPNVMILGG-DSRIPAMDRH 90
Cdd:cd07723   8 DNYIYLIVDE-ATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPaEDRIPGLDHP 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  91 VKHGDMAEFAGLQIKCLSTPCHTSGHICYHITNpaadstsPGVVFTGDTLFIAGCGRFFEGTAPQMDVALNEILKnLPVE 170
Cdd:cd07723  87 VKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPD-------EPALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLA-LPDD 158


                ....*..
gi 17536925 171 TQIFPGH 177
Cdd:cd07723 159 TLVYCGH 165
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 178-260 4.77e-38

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: 128.33  E-value: 4.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925   178 EYTVANLKFACHVEPGNEKAAQKLEWAQRQIEQGGFTVPSTVAEEKATNPFMRVREsEEIQKSIGTCDAVVGMAKLREMK 257
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDD-PAVQKATGETDPVEVFAALRELK 79


                  ...
gi 17536925   258 NKF 260
Cdd:pfam16123  80 DNF 82
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 12-181 4.38e-30

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: 112.09  E-value: 4.38e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  12 DNFMYIVKKSSEAraaLLVD----LVNEEDYKELADKENIDITAVLTTHHHYDHCGGNEGFRRQFpNVMILGGDSRIPAM 87
Cdd:COG0491  14 GVNSYLIVGGDGA---VLIDtglgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAPVYAHAAEAEAL 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  88 ----------------DRHVKHGDMAEFAGLQIKCLSTPCHTSGHICYHItnpaadsTSPGVVFTGDTLFIAGCGR--FF 149
Cdd:COG0491  90 eapaagalfgrepvppDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV-------PDEKVLFTGDALFSGGVGRpdLP 162

                       170       180       190
                ....*....|....*....|....*....|..
gi 17536925 150 EGTAPQMDVALNEILKnLPVETqIFPGHEYTV 181
Cdd:COG0491 163 DGDLAQWLASLERLLA-LPPDL-VIPGHGPPT 192
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 15-177 1.64e-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: 104.17  E-value: 1.64e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925     15 MYIVKKSSEAraaLLVDLVNEEDY---KELADKENIDITAVLTTHHHYDHCGGNEGFRRQfPNVMILG------------ 79
Cdd:smart00849   2 SYLVRDDGGA---ILIDTGPGEAEdllAELKKLGPKKIDAIILTHGHPDHIGGLPELLEA-PGAPVYApegtaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925     80 -------GDSRIPAMDRHVKHGDMAEFAGLQIKCLSTPCHTSGHICYHItnpaadsTSPGVVFTGDTLFIAGCGR-FFEG 151
Cdd:smart00849  78 allgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL-------PEGKILFTGDLLFAGGDGRtLVDG 150

                          170       180
                   ....*....|....*....|....*..
gi 17536925    152 TAPQMDVALNEILKNL-PVETQIFPGH 177
Cdd:smart00849 151 GDAAASDALESLLKLLkLLPKLVVPGH 177
 
Name Accession Description Interval E-value
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 12-260 1.17e-89

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 265.86  E-value: 1.17e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925   12 DNFMYIVKKSSEARAALlVDLVNEEDYKELADKENIDITAVLTTHHHYDHCGGNEGFRRQFPNVMILGGD-SRIPAMDRH 90
Cdd:PLN02469  11 DNYAYLIIDESTKDAAV-VDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSlDNVKGCTHP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925   91 VKHGDMAEF-AGLQIKCLSTPCHTSGHICYHITNPAADSTSpgvVFTGDTLFIAGCGRFFEGTAPQMDVALNEILKNLPV 169
Cdd:PLN02469  90 VENGDKLSLgKDVNILALHTPCHTKGHISYYVTGKEGEDPA---VFTGDTLFIAGCGKFFEGTAEQMYQSLCVTLGSLPK 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  170 ETQIFPGHEYTVANLKFACHVEPGNEKAAQKLEWAQRQIEQGGFTVPSTVAEEKATNPFMRVREsEEIQKSIGTCDAVVG 249
Cdd:PLN02469 167 PTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDL-PEIQEKVGCESPVEA 245

                        250
                 ....*....|.
gi 17536925  250 MAKLREMKNKF 260
Cdd:PLN02469 246 LREVRKMKDNW 256
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 12-260 1.55e-85

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: 255.15  E-value: 1.55e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925    12 DNFMYIVKKssEARAALLVDLVNEEDYKELADKENIDITAVLTTHHHYDHCGGNEGFRRQFPNVMILGGDSRIPAMDRHV 91
Cdd:TIGR03413   9 DNYIWLLHD--PDGQAAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAFPAPVYGPAEERIPGITHPV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925    92 KHGDMAEFAGLQIKCLSTPCHTSGHICYHItnpaADStspGVVFTGDTLFIAGCGRFFEGTAPQMDVALnEILKNLPVET 171
Cdd:TIGR03413  87 KDGDTVTLGGLEFEVLAVPGHTLGHIAYYL----PDS---PALFCGDTLFSAGCGRLFEGTPEQMYDSL-QRLAALPDDT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925   172 QIFPGHEYTVANLKFACHVEPGNEKAAQKLEWAQRQIEQGGFTVPSTVAEEKATNPFMRVrESEEIQKSIG--TCDAVVG 249
Cdd:TIGR03413 159 LVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRA-DDPAVRAALGsqGADPVEV 237

                         250
                  ....*....|.
gi 17536925   250 MAKLREMKNKF 260
Cdd:TIGR03413 238 FAALRAWKDNF 248
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 12-177 2.32e-72

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: 218.48  E-value: 2.32e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  12 DNFMYIVKKSsEARAALLVDLVNEEDYKELADKENIDITAVLTTHHHYDHCGGNEGFRRQFPNVMILGG-DSRIPAMDRH 90
Cdd:cd07723   8 DNYIYLIVDE-ATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPaEDRIPGLDHP 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  91 VKHGDMAEFAGLQIKCLSTPCHTSGHICYHITNpaadstsPGVVFTGDTLFIAGCGRFFEGTAPQMDVALNEILKnLPVE 170
Cdd:cd07723  87 VKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPD-------EPALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLA-LPDD 158


                ....*..
gi 17536925 171 TQIFPGH 177
Cdd:cd07723 159 TLVYCGH 165
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 12-260 7.64e-54

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 176.96  E-value: 7.64e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925   12 DNFMYIVKKSSEARAALlVDLVNEEDYKELADKENIDITAVLTTHHHYDHCGGNEGFRRQFPNVMILGG--DSRIPAMDR 89
Cdd:PLN02398  86 DNYAYLLHDEDTGTVGV-VDPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAvdKDRIPGIDI 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925   90 HVKHGDMAEFAGLQIKCLSTPCHTSGHICYHItnPAAdstspGVVFTGDTLFIAGCGRFFEGTAPQMDVALNEILkNLPV 169
Cdd:PLN02398 165 VLKDGDKWMFAGHEVLVMETPGHTRGHISFYF--PGS-----GAIFTGDTLFSLSCGKLFEGTPEQMLSSLQKII-SLPD 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  170 ETQIFPGHEYTVANLKFACHVEPGNEkAAQklEWAQRQIE---QGGFTVPSTVAEEKATNPFMRVrESEEIQKSIG---T 243
Cdd:PLN02398 237 DTNIYCGHEYTLSNSKFALSIEPNNE-VLQ--SYAAHVAHlrsKGLPTIPTTVKMEKACNPFLRT-SSTDIRKSLSipdT 312

                        250
                 ....*....|....*..
gi 17536925  244 CDAVVGMAKLREMKNKF 260
Cdd:PLN02398 313 ADEAEALGIIRRAKDNF 329
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 178-260 4.77e-38

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: 128.33  E-value: 4.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925   178 EYTVANLKFACHVEPGNEKAAQKLEWAQRQIEQGGFTVPSTVAEEKATNPFMRVREsEEIQKSIGTCDAVVGMAKLREMK 257
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDD-PAVQKATGETDPVEVFAALRELK 79


                  ...
gi 17536925   258 NKF 260
Cdd:pfam16123  80 DNF 82
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 12-239 5.52e-37

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 131.10  E-value: 5.52e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925   12 DNFMYIVkkSSEARAALLVDLVNEEDYKELADKENIDITAVLTTHHHYDHCGGNEGFRRQFPNVMILG-GDSRIPAMDRH 90
Cdd:PRK10241  11 DNYIWVL--NDEAGRCLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGpQETQDKGTTQV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925   91 VKHGDMAEFAGLQIKCLSTPCHTSGHICYHitnpaadstSPGVVFTGDTLFIAGCGRFFEGTAPQMDVALNEIlKNLPVE 170
Cdd:PRK10241  89 VKDGETAFVLGHEFSVFATPGHTLGHICYF---------SKPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKI-NALPDD 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17536925  171 TQIFPGHEYTVANLKFACHVEPGNEKAAQKLEWAQRQIEQGGFTVPSTVAEEKATNPFMRVRESEEIQK 239
Cdd:PRK10241 159 TLICCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINLFLRTEDIDLINV 227
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 16-177 3.45e-34

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: 121.62  E-value: 3.45e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  16 YIVkkSSEARAALLVD--LVNEEDYKELADKENIDITAVLTTHHHYDHCGGNEGFRRQFP-------------------N 74
Cdd:cd06262  13 YLV--SDEEGEAILIDpgAGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGapvyiheadaelledpelnL 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  75 VMILGGDSRIPAMDRHVKHGDMAEFAGLQIKCLSTPCHTSGHICYHItnpaadsTSPGVVFTGDTLFIAGCGR--FFEGT 152
Cdd:cd06262  91 AFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYI-------EEEGVLFTGDTLFAGSIGRtdLPGGD 163

                       170       180
                ....*....|....*....|....*
gi 17536925 153 APQMDVALNEILKNLPVETQIFPGH 177
Cdd:cd06262 164 PEQLIESIKKLLLLLPDDTVVYPGH 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 12-181 4.38e-30

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: 112.09  E-value: 4.38e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  12 DNFMYIVKKSSEAraaLLVD----LVNEEDYKELADKENIDITAVLTTHHHYDHCGGNEGFRRQFpNVMILGGDSRIPAM 87
Cdd:COG0491  14 GVNSYLIVGGDGA---VLIDtglgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAF-GAPVYAHAAEAEAL 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  88 ----------------DRHVKHGDMAEFAGLQIKCLSTPCHTSGHICYHItnpaadsTSPGVVFTGDTLFIAGCGR--FF 149
Cdd:COG0491  90 eapaagalfgrepvppDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV-------PDEKVLFTGDALFSGGVGRpdLP 162

                       170       180       190
                ....*....|....*....|....*....|..
gi 17536925 150 EGTAPQMDVALNEILKnLPVETqIFPGHEYTV 181
Cdd:COG0491 163 DGDLAQWLASLERLLA-LPPDL-VIPGHGPPT 192
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 12-177 5.60e-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: 110.32  E-value: 5.60e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  12 DNFMYIV--KKSSEAraaLLVDLVNE-EDYKELADKENIDITAVLTTHHHYDHCGGNEGFRRQF-PNVMILGGD---SRI 84
Cdd:cd16275  11 INYSYIIidKATREA---AVVDPAWDiEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYdAPVYMSKEEidyYGF 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  85 PAMDRH-VKHGDMAEFAGLQIKCLSTPCHTSGHICYHITNPaadstspgvVFTGDTLFIAGCGR--FFEGTAPQMDVALN 161
Cdd:cd16275  88 RCPNLIpLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGDS---------LFTGDTLFIEGCGRcdLPGGDPEEMYESLQ 158

                       170
                ....*....|....*.
gi 17536925 162 EILKNLPVETQIFPGH 177
Cdd:cd16275 159 RLKKLPPPNTRVYPGH 174
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 21-179 1.78e-29

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: 109.03  E-value: 1.78e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  21 SSEARAALLVD--LVNEEDYKELADKENIDITAVLTTHHHYDHCGGnEGFRRQFPNVMI-LGGDSRIPAMDRHVKHGDMA 97
Cdd:cd07724  19 DPETGEAAVIDpvRDSVDRYLDLAAELGLKITYVLETHVHADHVSG-ARELAERTGAPIvIGEGAPASFFDRLLKDGDVL 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  98 EFAGLQIKCLSTPCHTSGHICYHITNPAAdstspgvVFTGDTLFIAGCGR-----FFEGTAPQMDVALNEILKNLPVETQ 172
Cdd:cd07724  98 ELGNLTLEVLHTPGHTPESVSYLVGDPDA-------VFTGDTLFVGDVGRpdlpgEAEGLARQLYDSLQRKLLLLPDETL 170


                ....*..
gi 17536925 173 IFPGHEY 179
Cdd:cd07724 171 VYPGHDY 177
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 15-177 1.64e-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: 104.17  E-value: 1.64e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925     15 MYIVKKSSEAraaLLVDLVNEEDY---KELADKENIDITAVLTTHHHYDHCGGNEGFRRQfPNVMILG------------ 79
Cdd:smart00849   2 SYLVRDDGGA---ILIDTGPGEAEdllAELKKLGPKKIDAIILTHGHPDHIGGLPELLEA-PGAPVYApegtaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925     80 -------GDSRIPAMDRHVKHGDMAEFAGLQIKCLSTPCHTSGHICYHItnpaadsTSPGVVFTGDTLFIAGCGR-FFEG 151
Cdd:smart00849  78 allgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL-------PEGKILFTGDLLFAGGDGRtLVDG 150

                          170       180
                   ....*....|....*....|....*..
gi 17536925    152 TAPQMDVALNEILKNL-PVETQIFPGH 177
Cdd:smart00849 151 GDAAASDALESLLKLLkLLPKLVVPGH 177
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 25-241 1.39e-23

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 95.63  E-value: 1.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925   25 RAALLVDLVNEEDYKELA--DKENIDITAVLTTHHHYDHCGGNEGFRRQFPNVM-ILGGDSRIPAmDRHVKHGDMAEFAG 101
Cdd:PLN02962  36 KPALLIDPVDKTVDRDLSlvKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVKsIISKASGSKA-DLFVEPGDKIYFGD 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  102 LQIKCLSTPCHTSGHICYhITNPAADSTSPGVVFTGDTLFIAGCGR--FFEGTAPQMDVALNEILKNLPVETQIFPGHEY 179
Cdd:PLN02962 115 LYLEVRATPGHTAGCVTY-VTGEGPDQPQPRMAFTGDALLIRGCGRtdFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDY 193

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17536925  180 TvanlkfachvepgnekaaqklewaqrqieqgGFTVpSTVAEEKATNPfmRVRESEEIQKSI 241
Cdd:PLN02962 194 K-------------------------------GFTV-STVGEEMLYNP--RLTKDEETFKTI 221
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 21-229 4.71e-22

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


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 90.49  E-value: 4.71e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  21 SSEARAALLVDLVNE-EDYKELADKENIDITAVLTTHHHYDHCGGNEGFRRQ-----------------FPNVMILGGDS 82
Cdd:cd16322  18 DEGGGEAVLVDPGDEsEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHpgapvylhpddlplyeaADLGAKAFGLG 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  83 --RIPAMDRHVKHGDMAEFAGLQIKCLSTPCHTSGHICYHItnpaadsTSPGVVFTGDTLFIAGCGRF-FEGTAP-QMDV 158
Cdd:cd16322  98 iePLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYV-------EEEGLLFSGDLLFQGSIGRTdLPGGDPkAMAA 170

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17536925 159 ALNEILkNLPVETQIFPGHeytvanlkfachvepgnekaaqklewaqrqieqggfTVPSTVAEEKATNPFM 229
Cdd:cd16322 171 SLRRLL-TLPDETRVFPGH------------------------------------GPPTTLGEERRTNPFL 204
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 22-177 5.49e-17

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: 76.44  E-value: 5.49e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  22 SEARAALLVDLVNE-EDYKELADKENIDITAVLTTHHHYDHCGGNEGFRRQFpNVMILG---GDS----RIPAM------ 87
Cdd:cd07737  19 EETKEAAVIDPGGDaDKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHY-GVPIIGphkEDKflleNLPEQsqmfgf 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  88 --------DRHVKHGDMAEFAGLQIKCLSTPCHTSGHICYHitNPAAdstspGVVFTGDTLFIAGCGR--FFEGTAPQMD 157
Cdd:cd07737  98 ppaeaftpDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFF--NRES-----KLAIVGDVLFKGSIGRtdFPGGNHAQLI 170

                       170       180
                ....*....|....*....|
gi 17536925 158 VALNEILKNLPVETQIFPGH 177
Cdd:cd07737 171 ASIKEKLLPLGDDVTFIPGH 190
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 49-139 1.84e-15

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: 72.14  E-value: 1.84e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  49 ITAVLTTHHHYDHCGGNEGFRRQFpNVMILGGDSRIPAM-------DRHVKHGDMAEFAGLQIKCLSTPCHTSGHICYHI 121
Cdd:cd16278  54 VSAILVTHTHRDHSPGAARLAERT-GAPVRAFGPHRAGGqdtdfapDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFAL 132

                        90
                ....*....|....*...
gi 17536925 122 TNpaadstsPGVVFTGDT 139
Cdd:cd16278 133 ED-------EGALFTGDH 143
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
27-177 2.42e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 69.70  E-value: 2.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925    27 ALLVDLVNEEDYKELA-----DKENIDITAVLTTHHHYDHCGGNEGFRRQFPNV---------MILGGDSRIPAM----- 87
Cdd:pfam00753  17 AVLIDTGGSAEAALLLllaalGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPvivvaeearELLDEELGLAASrlglp 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925    88 --------DRHVKHGDMAEFAGLQIKcLSTPCHTSGHICYHITNPAADstspgVVFTGDTLFIAGCGR--FFEGTAPQMD 157
Cdd:pfam00753  97 gppvvplpPDVVLEEGDGILGGGLGL-LVTHGPGHGPGHVVVYYGGGK-----VLFTGDLLFAGEIGRldLPLGGLLVLH 170

                         170       180
                  ....*....|....*....|....*..
gi 17536925   158 -------VALNEILKNLPVETqIFPGH 177
Cdd:pfam00753 171 pssaessLESLLKLAKLKAAV-IVPGH 196
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 16-140 5.45e-13

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: 65.40  E-value: 5.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  16 YIVKKSSEAraaLLVD--LVNEEDYKELAD--KENI----DITAVLTTHHHYDHCGGNEGFRRQF-PNVMILGgdsripa 86
Cdd:cd07725  18 YLLRDGDET---TLIDtgLATEEDAEALWEglKELGlkpsDIDRVLLTHHHPDHIGLAGKLQEKSgATVYILD------- 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 17536925  87 mDRHVKHGDMAEFAGLQIKCLSTPCHTSGHICYHitnpaadSTSPGVVFTGDTL 140
Cdd:cd07725  88 -VTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLY-------DEDRRELFVGDAV 133
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 48-177 1.45e-12

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: 64.55  E-value: 1.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  48 DITAVLTTHHHYDHCGGNEGFRRQfPNV----------MILGGDSRIPAM-------------------DRHVKHGDMAE 98
Cdd:cd07721  49 DIRRILLTHGHIDHIGSLAALKEA-PGApvyahereapYLEGEKPYPPPVrlgllgllspllpvkpvpvDRTLEDGDTLD 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  99 FAGlQIKCLSTPCHTSGHICYHItnpaadsTSPGVVFTGDTLFIAGcGRFFEGTAPQ---MDVALN--EILKNLPVETqI 173
Cdd:cd07721 128 LAG-GLRVIHTPGHTPGHISLYL-------EEDGVLIAGDALVTVG-GELVPPPPPFtwdMEEALEslRKLAELDPEV-L 197


                ....
gi 17536925 174 FPGH 177
Cdd:cd07721 198 APGH 201
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 41-177 3.78e-12

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: 63.32  E-value: 3.78e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  41 LADKENIDITAVLTTHHHYDHCGGNEGFRRQF--PNV----MILGGDSRIPAMDRHVKHG--DMAEFA--GLQIKCLSTP 110
Cdd:cd07722  49 LDSEGNATISDILLTHWHHDHVGGLPDVLDLLrgPSPrvykFPRPEEDEDPDEDGGDIHDlqDGQVFKveGATLRVIHTP 128

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17536925 111 CHTSGHICYHItnpaadsTSPGVVFTGDTlfIAGCGR-FFEGTAPQMDvALNEILKNLPveTQIFPGH 177
Cdd:cd07722 129 GHTTDHVCFLL-------EEENALFTGDC--VLGHGTaVFEDLAAYMA-SLKKLLSLGP--GRIYPGH 184
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 21-177 1.51e-10

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: 59.12  E-value: 1.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  21 SSEARAALLVDLVneedyKELADKeniDITAVLTTHHHYDHCGGNEGFRRQFP---------------------NVMILG 79
Cdd:cd16282  33 ASPRLARALLAAI-----RKVTDK---PVRYVVNTHYHGDHTLGNAAFADAGApiiahentreelaargeayleLMRRLG 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  80 GD----SRIPAMDRHVKHGDMAEFAGLQIKCLST-PCHTSGHICYHItnPAAdstspGVVFTGDTLFIAGCGRFFEGTAP 154
Cdd:cd16282 105 GDamagTELVLPDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWL--PEE-----GVLFAGDLVFNGRIPFLPDGSLA 177

                       170       180
                ....*....|....*....|...
gi 17536925 155 QMDVALNEILKNLPveTQIFPGH 177
Cdd:cd16282 178 GWIAALDRLLALDA--TVVVPGH 198
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 16-141 2.49e-09

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 55.61  E-value: 2.49e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  16 YIVKKSSEAraaLLVDLVNEEDY----KELADKENIDITAVLTTHHHYDHCGGNEGFRRQFP------------------ 73
Cdd:cd07743  12 VYVFGDKEA---LLIDSGLDEDAgrkiRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGckvyapkiekafienpll 88

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17536925  74 NVMILGGDSRIPAMDRHVKHG-----------DMAEFAGLQIKCLSTPCHTSGHICYhitnpaadSTSPGVVFTGDTLF 141
Cdd:cd07743  89 EPSYLGGAYPPKELRNKFLMAkpskvddiieeGELELGGVGLEIIPLPGHSFGQIGI--------LTPDGVLFAGDALF 159
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 48-177 3.48e-09

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: 55.19  E-value: 3.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  48 DITAVLTTHHHYDHCGGNEGFRRQFPN------------------------------VMILGGDSR-IPAmDR--HVKHG 94
Cdd:cd07726  54 DVDYIILTHIHLDHAGGAGLLAEALPNakvyvhprgarhlidpsklwasaravygdeADRLGGEILpVPE-ERviVLEDG 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  95 DMAEFAGLQIKCLSTPCHTSGHICYHitnpaaDSTSpGVVFTGDTLFIAGCGRFFEG----TAPQMDVALN----EILKN 166
Cdd:cd07726 133 ETLDLGGRTLEVIDTPGHAPHHLSFL------DEES-DGLFTGDAAGVRYPELDVVGppstPPPDFDPEAWleslDRLLS 205

                       170
                ....*....|.
gi 17536925 167 LPVEtQIFPGH 177
Cdd:cd07726 206 LKPE-RIYLTH 215
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 48-178 1.45e-08

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: 53.76  E-value: 1.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  48 DITAVLTTHHHYDHCGGNegfrRQFPNVMIL-----------------GGDSRIPAMDRHVKHGDM------AEFAGLqI 104
Cdd:cd07729  88 DIDYVILSHLHFDHAGGL----DLFPNATIIvqraeleyatgpdplaaGYYEDVLALDDDLPGGRVrlvdgdYDLFPG-V 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925 105 KCLSTPCHTSGHICYHITNPaadstSPGVVFTGDTLFIAgcgRFFEGTAPQ---MDVA--------LNEILKNLPVEtqI 173
Cdd:cd07729 163 TLIPTPGHTPGHQSVLVRLP-----EGTVLLAGDAAYTY---ENLEEGRPPginYDPEaalaslerLKALAEREGAR--V 232


                ....*
gi 17536925 174 FPGHE 178
Cdd:cd07729 233 IPGHD 237
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 15-177 4.65e-08

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: 51.48  E-value: 4.65e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  15 MYIVKKSSEAraaLLVD----LVNEEDY-KELADKEnidITAVLTtHHHYDHCGGNEgfrrQFPNVMILGGDS-RIPAMD 88
Cdd:cd07712  11 IYLLRGRDRA---LLIDtglgIGDLKEYvRTLTDLP---LLVVAT-HGHFDHIGGLH----EFEEVYVHPADAeILAAPD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  89 RH--------------------VKHGDMAEFAGLQIKCLSTPCHTSGHICYHitnpaaDSTSpGVVFTGDTLFIAGCGRF 148
Cdd:cd07712  80 NFetltwdaatysvppagptlpLRDGDVIDLGDRQLEVIHTPGHTPGSIALL------DRAN-RLLFSGDVVYDGPLIMD 152

                       170       180       190
                ....*....|....*....|....*....|
gi 17536925 149 FEGTAPQMDVALNEILKNLPVE-TQIFPGH 177
Cdd:cd07712 153 LPHSDLDDYLASLEKLSKLPDEfDKVLPGH 182
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 29-117 1.66e-07

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: 50.28  E-value: 1.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  29 LVDLVNEEDYKELAD---KENI---DITAVLTTHHHYDHCGGNegfrRQFPN-VMILGGDSRIPAMDRHV--KHGDMAEF 99
Cdd:cd07711  35 LVDTGTPWDRDLLLKalaEHGLspeDIDYVVLTHGHPDHIGNL----NLFPNaTVIVGWDICGDSYDDHSleEGDGYEID 110

                        90
                ....*....|....*...
gi 17536925 100 AGLQIkcLSTPCHTSGHI 117
Cdd:cd07711 111 ENVEV--IPTPGHTPEDV 126
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 48-143 2.08e-06

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. 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: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 47.54  E-value: 2.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  48 DITAVLTTHHHYDHCGG--NEGFRRQFPNVMIL------------GGDSRIPAMDRHV---------------KHGDMAE 98
Cdd:cd07720  91 DIDDVLLTHLHPDHIGGlvDAGGKPVFPNAEVHvseaewdfwlddANAAKAPEGAKRFfdaardrlrpyaaagRFEDGDE 170

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 17536925  99 FAGlQIKCLSTPCHTSGHICYHItnpaaDSTSPGVVFTGDTLFIA 143
Cdd:cd07720 171 VLP-GITAVPAPGHTPGHTGYRI-----ESGGERLLIWGDIVHHP 209
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 48-144 1.52e-05

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 44.91  E-value: 1.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  48 DITAVLTTHHHYDHCGGN--EGFRRQFPNVM-ILGGDSRIPAMDRH----VKHGDMAEFAGLQIKClsTPC-HTSGHICY 119
Cdd:COG2220  48 KIDAVLVTHDHYDHLDDAtlRALKRTGATVVaPLGVAAWLRAWGFPrvteLDWGESVELGGLTVTA--VPArHSSGRPDR 125

                        90       100
                ....*....|....*....|....*..
gi 17536925 120 HITNPAadstspGVVFTGD--TLFIAG 144
Cdd:COG2220 126 NGGLWV------GFVIETDgkTIYHAG 146
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 48-122 5.78e-05

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


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 43.23  E-value: 5.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  48 DITAVLTTHHHYDHCGGNEGFRRQF-PNVMILGGDSRIPA--------------------MDRHVKHGDMAEFAGLQIKC 106
Cdd:cd16308  60 DIKILLTTQAHYDHVGAMAAIKQQTgAKMMVDEKDAKVLAdggksdyemggygstfapvkADKLLHDGDTIKLGGTKLTL 139

                        90
                ....*....|....*.
gi 17536925 107 LSTPCHTSGHICYHIT 122
Cdd:cd16308 140 LHHPGHTKGSCSFLFD 155
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 29-119 8.20e-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: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 42.96  E-value: 8.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  29 LVD-LVNEEDYKELADkeNI--------DITAVLTTHHHYDHCGGNEGFRRQF----------------PNVMILGG-DS 82
Cdd:cd16280  35 LIDaLNNNEAADLIVD--GLeklgldpaDIKYILITHGHGDHYGGAAYLKDLYgakvvmseadwdmmeePPEEGDNPrWG 112

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 17536925  83 RIPAMDRHVKHGDMAEFAGLQIKCLSTPCHTSGHICY 119
Cdd:cd16280 113 PPPERDIVIKDGDTLTLGDTTITVYLTPGHTPGTLSL 149
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 8-122 2.03e-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: 41.76  E-value: 2.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925   8 LRRADNFMYI------VKKSSEARAALLVDLVNEEDYKELADkeNI--------DITAVLTTHHHYDHCGGNEGFRRQF- 72
Cdd:cd07708   8 FQIAGNTYYVgtddlaAYLIVTPQGNILIDGDMEQNAPMIKA--NIkklgfkfsDTKLILISHAHFDHAGGSAEIKKQTg 85

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17536925  73 --------PNVMILGGDSRIP-------------AMDRHVKHGDMAEFAGLQIKCLSTPCHTSGHICYHIT 122
Cdd:cd07708  86 akvmagaeDVSLLLSGGSSDFhyandsstyfpqsTVDRAVHDGERVTLGGTVLTAHATPGHTPGCTTWTMT 156
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 24-68 4.04e-04

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: 40.56  E-value: 4.04e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 17536925  24 ARAALlvdlvnEEDYKELADKEnidITAVLTTHHHYDHCGGNEGF 68
Cdd:cd07710  41 AKAAL------ELFRKHTGDKP---VKAIIYTHSHPDHFGGAGGF 76
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 44-131 7.34e-04

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


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 40.16  E-value: 7.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  44 KENI--------DITAVLTTHHHYDHCGGNEGFRRQFPNVMILGGDSR-----------------IPA--MDRHVKHGDM 96
Cdd:cd16309  48 KDNIkklgfdvkDVKYLLNTHAHFDHAGGLAELKKATGAQLVASAADKpllesgyvgsgdtknlqFPPvrVDRVIGDGDK 127

                        90       100       110
                ....*....|....*....|....*....|....*
gi 17536925  97 AEFAGLQIKCLSTPCHTSGhiCYHITNPAADSTSP 131
Cdd:cd16309 128 VTLGGTTLTAHLTPGHSPG--CTSWTTTVKDTAGP 160
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 35-77 1.26e-03

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. 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: 293814  Cd Length: 249  Bit Score: 39.16  E-value: 1.26e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 17536925  35 EEDYKELADKENiDITAVLTTHHHYDHCGG-----NEGFRRQFPNVMI 77
Cdd:cd07728  83 EESLAELGLTPE-DIDYVLMTHLHFDHASGltkvkGEQLVSVFPNATI 129
BDS1 COG2015
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary ...
 24-68 2.75e-03

Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441618 [Multi-domain]  Cd Length: 629  Bit Score: 38.67  E-value: 2.75e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 17536925  24 ARAALlvDLVNeedyKELADKeniDITAVLTTHHHYDHCGGNEGF 68
Cdd:COG2015 126 AAAAL--ALYR----KHLGDR---PVKAVIYTHSHVDHFGGVRGV 161
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-64 2.87e-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) 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: 293839  Cd Length: 252  Bit Score: 38.24  E-value: 2.87e-03
                        10
                ....*....|....*..
gi 17536925  48 DITAVLTTHHHYDHCGG 64
Cdd:cd16281  94 DITDVILTHLHFDHCGG 110
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
42-77 6.82e-03

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 37.17  E-value: 6.82e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 17536925  42 ADKENID---ITAVLTTHHHYDHCGGNEGFRRQFPNVMI 77
Cdd:COG1237  48 AEKLGIDlsdIDAVVLSHGHYDHTGGLPALLELNPKAPV 86
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-83 7.10e-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) 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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 36.86  E-value: 7.10e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 17536925  48 DITAVLTTHHHYDHCGGnegfRRQFPNV-MILGGDSR 83
Cdd:cd07730  83 DIDAVILSHLHWDHIGG----LSDFPNArLIVGPGAK 115
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 48-139 8.03e-03

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: 36.47  E-value: 8.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17536925  48 DITAVLTTHHHYDHCGG------------------------NEGFRRQFPNVMILGGDSRIPAMDRHVKH-GDMAEFAGL 102
Cdd:cd16272  50 KLDAIFLSHFHLDHIGGlptllfarryggrkkpltiygpkgIKEFLEKLLNFPVEILPLGFPLEIEELEEgGEVLELGDL 129

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 17536925 103 QIKCLSTpCHTSGHICYHITnpaadSTSPGVVFTGDT 139
Cdd:cd16272 130 KVEAFPV-KHSVESLGYRIE-----AEGKSIVYSGDT 160
 
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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