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Conserved domains on  [gi|19114358|ref|NP_593446|]
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hydroxyacylglutathione hydrolase Glo2 [Schizosaccharomyces pombe]

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 ...
 17-178 4.32e-81

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: 240.44  E-value: 4.32e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  17 NYAYLLTCDKTKITAIVDPAEPESVIPVIKektaKKEIDLQYILTTHHHYDHAGGNEDILSYFPSLKVYGGKN--ASGVT 94
Cdd:cd07723   9 NYIYLIVDEATGEAAVVDPGEAEPVLAALE----KNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAEdrIPGLD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  95 YTPKDKEIFKVGEVQVEALHTPCHTQDSICYYVssPSKRAVFTGDTLFTSGCGRFFEGDAKQMDYALNHvLAALPDDTVT 174
Cdd:cd07723  85 HPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV--PDEPALFTGDTLFSGGCGRFFEGTAEQMYASLQK-LLALPDDTLV 161


                ....
gi 19114358 175 YPGH 178
Cdd:cd07723 162 YCGH 165
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 179-254 1.03e-26

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: 99.05  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   179 EYTKSNAKFSSTIF-STPELTKLVDFCKNHES---TTGHFTIGDEKKFNPFMCLGLESVQKAVGSSDPITVMKKLRDMKN 254
Cdd:pfam16123   1 EYTLSNLKFALSVEpDNEALQKRLAWVEALRAagePTVPSTLGDEKATNPFLRVDDPAVQKATGETDPVEVFAALRELKD 80
 
Name Accession Description Interval E-value
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 17-178 4.32e-81

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: 240.44  E-value: 4.32e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  17 NYAYLLTCDKTKITAIVDPAEPESVIPVIKektaKKEIDLQYILTTHHHYDHAGGNEDILSYFPSLKVYGGKN--ASGVT 94
Cdd:cd07723   9 NYIYLIVDEATGEAAVVDPGEAEPVLAALE----KNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAEdrIPGLD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  95 YTPKDKEIFKVGEVQVEALHTPCHTQDSICYYVssPSKRAVFTGDTLFTSGCGRFFEGDAKQMDYALNHvLAALPDDTVT 174
Cdd:cd07723  85 HPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV--PDEPALFTGDTLFSGGCGRFFEGTAEQMYASLQK-LLALPDDTLV 161


                ....
gi 19114358 175 YPGH 178
Cdd:cd07723 162 YCGH 165
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 16-254 4.09e-73

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 223.87  E-value: 4.09e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   16 NNYAYLLTCDKTKITAIVDPAEPESVIPVIKEKTAKkeidLQYILTTHHHYDHAGGNEDILSYFPSLKVYGG--KNASGV 93
Cdd:PLN02469  11 DNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAK----IKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGslDNVKGC 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   94 TYTPKDKEIFKVG-EVQVEALHTPCHTQDSICYYVSSPS--KRAVFTGDTLFTSGCGRFFEGDAKQMDYALNHVLAALPD 170
Cdd:PLN02469  87 THPVENGDKLSLGkDVNILALHTPCHTKGHISYYVTGKEgeDPAVFTGDTLFIAGCGKFFEGTAEQMYQSLCVTLGSLPK 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  171 DTVTYPGHEYTKSNAKFSSTIfsTPELTKL------VDFCKNHESTTGHFTIGDEKKFNPFMCLGLESVQKAVGSSDPIT 244
Cdd:PLN02469 167 PTQVYCGHEYTVKNLKFALTV--EPDNEKLkqklewAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVGCESPVE 244

                        250
                 ....*....|
gi 19114358  245 VMKKLRDMKN 254
Cdd:PLN02469 245 ALREVRKMKD 254
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 17-254 7.92e-68

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: 209.70  E-value: 7.92e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358    17 NYAYLLTCDKTKiTAIVDPAEPESVIPVIKEKTAKkeidLQYILTTHHHYDHAGGNEDILSYFPsLKVYGGKNA--SGVT 94
Cdd:TIGR03413  10 NYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLT----LTAILLTHHHHDHVGGVAELLEAFP-APVYGPAEEriPGIT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358    95 YTPKDKEIFKVGEVQVEALHTPCHTQDSICYYvsSPSKRAVFTGDTLFTSGCGRFFEGDAKQMDYALNHvLAALPDDTVT 174
Cdd:TIGR03413  84 HPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYY--LPDSPALFCGDTLFSAGCGRLFEGTPEQMYDSLQR-LAALPDDTLV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   175 YPGHEYTKSNAKFSSTIFST-PELTKLVDFC----KNHEST--TghfTIGDEKKFNPFMCLGLESVQKAVGSS--DPITV 245
Cdd:TIGR03413 161 YCAHEYTLSNLRFALTVEPDnPALQERLKEVealrAQGQPTlpS---TLGLERATNPFLRADDPAVRAALGSQgaDPVEV 237


                  ....*....
gi 19114358   246 MKKLRDMKN 254
Cdd:TIGR03413 238 FAALRAWKD 246
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 3-181 2.11e-34

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 122.88  E-value: 2.11e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   3 FHITPIWMWKGTGNNyAYLLTCDKTkiTAIVDPAEPESVIPVIKEKTAKKEIDLQYILTTHHHYDHAGGNEDILSYF--- 79
Cdd:COG0491   2 YVLPGGTPGAGLGVN-SYLIVGGDG--AVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFgap 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  80 -------------PSLKVYGGKNASGVTYTPKDKEIFKVGEVQVEALHTPCHTQDSICYYVssPSKRAVFTGDTLFTSGC 146
Cdd:COG0491  79 vyahaaeaealeaPAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV--PDEKVLFTGDALFSGGV 156

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19114358 147 GR--FFEGDAKQMDYALNHvLAALPDDTVtYPGHEYT 181
Cdd:COG0491 157 GRpdLPDGDLAQWLASLER-LLALPPDLV-IPGHGPP 191
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 18-178 2.46e-30

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: 111.49  E-value: 2.46e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358     18 YAYLLTCDKTKItaIVDPAEPESViPVIKEKTAKKEIDLQYILTTHHHYDHAGGNEDILSYfPSLKVYGGKN-------- 89
Cdd:smart00849   1 NSYLVRDDGGAI--LIDTGPGEAE-DLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEA-PGAPVYAPEGtaellkdl 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358     90 ------------ASGVTYTPKDKEIFKVGEVQVEALHTPCHTQDSICYYVssPSKRAVFTGDTLFTSGCGR-FFEGDAKQ 156
Cdd:smart00849  77 lallgelgaeaePAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL--PEGKILFTGDLLFAGGDGRtLVDGGDAA 154

                          170       180
                   ....*....|....*....|...
gi 19114358    157 MDYALNHVLAAL-PDDTVTYPGH 178
Cdd:smart00849 155 ASDALESLLKLLkLLPKLVVPGH 177
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 179-254 1.03e-26

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: 99.05  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   179 EYTKSNAKFSSTIF-STPELTKLVDFCKNHES---TTGHFTIGDEKKFNPFMCLGLESVQKAVGSSDPITVMKKLRDMKN 254
Cdd:pfam16123   1 EYTLSNLKFALSVEpDNEALQKRLAWVEALRAagePTVPSTLGDEKATNPFLRVDDPAVQKATGETDPVEVFAALRELKD 80
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
13-178 1.88e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 69.70  E-value: 1.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358    13 GTGNNYAYLLTCDKTKItaIVDPAEPESVIPVIKEKTAKKEI-DLQYILTTHHHYDHAGGNEDILSYF-------PSLKV 84
Cdd:pfam00753   2 GPGQVNSYLIEGGGGAV--LIDTGGSAEAALLLLLAALGLGPkDIDAVILTHGHFDHIGGLGELAEATdvpvivvAEEAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358    85 YGGKNASGVTYTPK-----------------DKEIFKVGEVQVEALHTPCHTQDSICYYVssPSKRAVFTGDTLFTSGCG 147
Cdd:pfam00753  80 ELLDEELGLAASRLglpgppvvplppdvvleEGDGILGGGLGLLVTHGPGHGPGHVVVYY--GGGKVLFTGDLLFAGEIG 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 19114358   148 RF-FEGDAKQMDYALNH-------VLAALPDDTVTYPGH 178
Cdd:pfam00753 158 RLdLPLGGLLVLHPSSAessleslLKLAKLKAAVIVPGH 196
 
Name Accession Description Interval E-value
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 17-178 4.32e-81

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: 240.44  E-value: 4.32e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  17 NYAYLLTCDKTKITAIVDPAEPESVIPVIKektaKKEIDLQYILTTHHHYDHAGGNEDILSYFPSLKVYGGKN--ASGVT 94
Cdd:cd07723   9 NYIYLIVDEATGEAAVVDPGEAEPVLAALE----KNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAEdrIPGLD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  95 YTPKDKEIFKVGEVQVEALHTPCHTQDSICYYVssPSKRAVFTGDTLFTSGCGRFFEGDAKQMDYALNHvLAALPDDTVT 174
Cdd:cd07723  85 HPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV--PDEPALFTGDTLFSGGCGRFFEGTAEQMYASLQK-LLALPDDTLV 161


                ....
gi 19114358 175 YPGH 178
Cdd:cd07723 162 YCGH 165
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 16-254 4.09e-73

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 223.87  E-value: 4.09e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   16 NNYAYLLTCDKTKITAIVDPAEPESVIPVIKEKTAKkeidLQYILTTHHHYDHAGGNEDILSYFPSLKVYGG--KNASGV 93
Cdd:PLN02469  11 DNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAK----IKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGslDNVKGC 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   94 TYTPKDKEIFKVG-EVQVEALHTPCHTQDSICYYVSSPS--KRAVFTGDTLFTSGCGRFFEGDAKQMDYALNHVLAALPD 170
Cdd:PLN02469  87 THPVENGDKLSLGkDVNILALHTPCHTKGHISYYVTGKEgeDPAVFTGDTLFIAGCGKFFEGTAEQMYQSLCVTLGSLPK 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  171 DTVTYPGHEYTKSNAKFSSTIfsTPELTKL------VDFCKNHESTTGHFTIGDEKKFNPFMCLGLESVQKAVGSSDPIT 244
Cdd:PLN02469 167 PTQVYCGHEYTVKNLKFALTV--EPDNEKLkqklewAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVGCESPVE 244

                        250
                 ....*....|
gi 19114358  245 VMKKLRDMKN 254
Cdd:PLN02469 245 ALREVRKMKD 254
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 17-254 7.92e-68

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: 209.70  E-value: 7.92e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358    17 NYAYLLTCDKTKiTAIVDPAEPESVIPVIKEKTAKkeidLQYILTTHHHYDHAGGNEDILSYFPsLKVYGGKNA--SGVT 94
Cdd:TIGR03413  10 NYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLT----LTAILLTHHHHDHVGGVAELLEAFP-APVYGPAEEriPGIT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358    95 YTPKDKEIFKVGEVQVEALHTPCHTQDSICYYvsSPSKRAVFTGDTLFTSGCGRFFEGDAKQMDYALNHvLAALPDDTVT 174
Cdd:TIGR03413  84 HPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYY--LPDSPALFCGDTLFSAGCGRLFEGTPEQMYDSLQR-LAALPDDTLV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   175 YPGHEYTKSNAKFSSTIFST-PELTKLVDFC----KNHEST--TghfTIGDEKKFNPFMCLGLESVQKAVGSS--DPITV 245
Cdd:TIGR03413 161 YCAHEYTLSNLRFALTVEPDnPALQERLKEVealrAQGQPTlpS---TLGLERATNPFLRADDPAVRAALGSQgaDPVEV 237


                  ....*....
gi 19114358   246 MKKLRDMKN 254
Cdd:TIGR03413 238 FAALRAWKD 246
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 16-255 6.92e-45

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 153.46  E-value: 6.92e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   16 NNYAYLLTCDKTKITAIVDPAEPESVIPVIKektaKKEIDLQYILTTHHHYDHAGGNEDILSYFPSlKVYG-GKNAS--- 91
Cdd:PLN02398  86 DNYAYLLHDEDTGTVGVVDPSEAVPVIDALS----RKNRNLTYILNTHHHYDHTGGNLELKARYGA-KVIGsAVDKDrip 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   92 GVTYTPKDKEIFKVGEVQVEALHTPCHTQDSICYYVssPSKRAVFTGDTLFTSGCGRFFEGDAKQMDYALNHVLaALPDD 171
Cdd:PLN02398 161 GIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYF--PGSGAIFTGDTLFSLSCGKLFEGTPEQMLSSLQKII-SLPDD 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  172 TVTYPGHEYTKSNAKFSSTIFSTPELTKL----VDFCKNHESTTGHFTIGDEKKFNPFMCLGLESVQKAVGSSDPITVMK 247
Cdd:PLN02398 238 TNIYCGHEYTLSNSKFALSIEPNNEVLQSyaahVAHLRSKGLPTIPTTVKMEKACNPFLRTSSTDIRKSLSIPDTADEAE 317


                 ....*...
gi 19114358  248 KLRDMKNA 255
Cdd:PLN02398 318 ALGIIRRA 325
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 16-191 3.06e-40

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 139.19  E-value: 3.06e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   16 NNYAYLLTCDKTKiTAIVDPAEPESVIPVIKEKTAKKEIdlqyILTTHHHYDHAGGNEDILSYFPSLKVYGGKNA--SGV 93
Cdd:PRK10241  11 DNYIWVLNDEAGR-CLIVDPGEAEPVLNAIAENNWQPEA----IFLTHHHHDHVGGVKELVEKFPQIVVYGPQETqdKGT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   94 TYTPKDKEIFKVGEVQVEALHTPCHTQDSICYYvsspSKRAVFTGDTLFTSGCGRFFEGDAKQMDYALNHVlAALPDDTV 173
Cdd:PRK10241  86 TQVVKDGETAFVLGHEFSVFATPGHTLGHICYF----SKPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKI-NALPDDTL 160

                        170
                 ....*....|....*...
gi 19114358  174 TYPGHEYTKSNAKFSSTI 191
Cdd:PRK10241 161 ICCAHEYTLSNMKFALSI 178
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 18-180 4.90e-38

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: 131.37  E-value: 4.90e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  18 YAYLLTCDKTKITAIVDPAEpeSVIPVIKEKTAKKEIDLQYILTTHHHYDHA-GGNEdiLSYFPSLKVYGGKNASGV-TY 95
Cdd:cd07724  13 LSYLVGDPETGEAAVIDPVR--DSVDRYLDLAAELGLKITYVLETHVHADHVsGARE--LAERTGAPIVIGEGAPASfFD 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  96 TP-KDKEIFKVGEVQVEALHTPCHTQDSICYYVSSPskRAVFTGDTLFTSGCGR-----FFEGDAKQMdYA-LNHVLAAL 168
Cdd:cd07724  89 RLlKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDP--DAVFTGDTLFVGDVGRpdlpgEAEGLARQL-YDsLQRKLLLL 165

                       170
                ....*....|..
gi 19114358 169 PDDTVTYPGHEY 180
Cdd:cd07724 166 PDETLVYPGHDY 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 13-178 1.02e-36

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: 128.17  E-value: 1.02e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  13 GTGNNYAYLLTCDKTKiTAIVDPAEPEsvIPVIKEKTAKKEIDLQYILTTHHHYDHAGGNEDILSYFPsLKVYGGK---- 88
Cdd:cd06262   6 GPLQTNCYLVSDEEGE-AILIDPGAGA--LEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPG-APVYIHEadae 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  89 -------NASGVTYTP----------KDKEIFKVGEVQVEALHTPCHTQDSICYYVssPSKRAVFTGDTLFTSGCGR--F 149
Cdd:cd06262  82 lledpelNLAFFGGGPlpppepdillEDGDTIELGGLELEVIHTPGHTPGSVCFYI--EEEGVLFTGDTLFAGSIGRtdL 159

                       170       180
                ....*....|....*....|....*....
gi 19114358 150 FEGDAKQMDYALNHVLAALPDDTVTYPGH 178
Cdd:cd06262 160 PGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 17-178 1.81e-35

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: 124.57  E-value: 1.81e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  17 NYAYLLTCDKTKITAIVDPA-EPESVIpvikEKTAKKEIDLQYILTTHHHYDHAGGNEDiLSYFPSLKVYGGKN---ASG 92
Cdd:cd16275  12 NYSYIIIDKATREAAVVDPAwDIEKIL----AKLNELGLTLTGILLTHSHFDHVNLVEP-LLAKYDAPVYMSKEeidYYG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  93 VTYTP----KDKEIFKVGEVQVEALHTPCHTQDSICYYVSSpskrAVFTGDTLFTSGCGR--FFEGDAKQMDYALNHVLA 166
Cdd:cd16275  87 FRCPNliplEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGD----SLFTGDTLFIEGCGRcdLPGGDPEEMYESLQRLKK 162

                       170
                ....*....|..
gi 19114358 167 ALPDDTVTYPGH 178
Cdd:cd16275 163 LPPPNTRVYPGH 174
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 3-181 2.11e-34

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 122.88  E-value: 2.11e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   3 FHITPIWMWKGTGNNyAYLLTCDKTkiTAIVDPAEPESVIPVIKEKTAKKEIDLQYILTTHHHYDHAGGNEDILSYF--- 79
Cdd:COG0491   2 YVLPGGTPGAGLGVN-SYLIVGGDG--AVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFgap 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  80 -------------PSLKVYGGKNASGVTYTPKDKEIFKVGEVQVEALHTPCHTQDSICYYVssPSKRAVFTGDTLFTSGC 146
Cdd:COG0491  79 vyahaaeaealeaPAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV--PDEKVLFTGDALFSGGV 156

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19114358 147 GR--FFEGDAKQMDYALNHvLAALPDDTVtYPGHEYT 181
Cdd:COG0491 157 GRpdLPDGDLAQWLASLER-LLALPPDLV-IPGHGPP 191
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 19-226 4.16e-31

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: 113.98  E-value: 4.16e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  19 AYLLTCDKTKITAIVDPA-EPESVIPVIKEKtakkEIDLQYILTTHHHYDHAGGNEDILS------YFPS--LKVYGGKN 89
Cdd:cd16322  13 TYLVADEGGGEAVLVDPGdESEKLLARFGTT----GLTLLYILLTHAHFDHVGGVADLRRhpgapvYLHPddLPLYEAAD 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  90 ASGVT--------YTP----KDKEIFKVGEVQVEALHTPCHTQDSICYYVssPSKRAVFTGDTLFTSGCGR--FFEGDAK 155
Cdd:cd16322  89 LGAKAfglgieplPPPdrllEDGQTLTLGGLEFKVLHTPGHSPGHVCFYV--EEEGLLFSGDLLFQGSIGRtdLPGGDPK 166

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114358 156 QMDYALNHVLaALPDDTVTYPGHeytksnakfsstifstpeltklvdfcknHESTtghfTIGDEKKFNPFM 226
Cdd:cd16322 167 AMAASLRRLL-TLPDETRVFPGH----------------------------GPPT----TLGEERRTNPFL 204
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 18-178 2.46e-30

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: 111.49  E-value: 2.46e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358     18 YAYLLTCDKTKItaIVDPAEPESViPVIKEKTAKKEIDLQYILTTHHHYDHAGGNEDILSYfPSLKVYGGKN-------- 89
Cdd:smart00849   1 NSYLVRDDGGAI--LIDTGPGEAE-DLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEA-PGAPVYAPEGtaellkdl 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358     90 ------------ASGVTYTPKDKEIFKVGEVQVEALHTPCHTQDSICYYVssPSKRAVFTGDTLFTSGCGR-FFEGDAKQ 156
Cdd:smart00849  77 lallgelgaeaePAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL--PEGKILFTGDLLFAGGDGRtLVDGGDAA 154

                          170       180
                   ....*....|....*....|...
gi 19114358    157 MDYALNHVLAAL-PDDTVTYPGH 178
Cdd:smart00849 155 ASDALESLLKLLkLLPKLVVPGH 177
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 179-254 1.03e-26

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: 99.05  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   179 EYTKSNAKFSSTIF-STPELTKLVDFCKNHES---TTGHFTIGDEKKFNPFMCLGLESVQKAVGSSDPITVMKKLRDMKN 254
Cdd:pfam16123   1 EYTLSNLKFALSVEpDNEALQKRLAWVEALRAagePTVPSTLGDEKATNPFLRVDDPAVQKATGETDPVEVFAALRELKD 80
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 20-178 7.66e-23

Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Salmonella enterica serovar typhimurium YcbL which has type II hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as glyoxalase II) activity, and has a single metal ion binding site, and Thermus thermophilus TTHA1623 which does not have GLX2 activity and has two metal ion binding sites with a glyoxalase II-type metal coordination. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 92.23  E-value: 7.66e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  20 YLLTCDKTKITAIVDP-AEPESVIPVIKEKTAKkeidLQYILTTHHHYDHAGGNEDILSYF------PSL---------- 82
Cdd:cd07737  14 SLIWCEETKEAAVIDPgGDADKILQAIEDLGLT----LKKILLTHGHLDHVGGAAELAEHYgvpiigPHKedkfllenlp 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  83 ---KVYGGKNASGVTytP----KDKEIFKVGEVQVEALHTPCHTQDSICYYvsSPSKRAVFTGDTLFTSGCGR--FFEGD 153
Cdd:cd07737  90 eqsQMFGFPPAEAFT--PdrwlEEGDTVTVGNLTLEVLHCPGHTPGHVVFF--NRESKLAIVGDVLFKGSIGRtdFPGGN 165

                       170       180
                ....*....|....*....|....*
gi 19114358 154 AKQMDYALNHVLAALPDDTVTYPGH 178
Cdd:cd07737 166 HAQLIASIKEKLLPLGDDVTFIPGH 190
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 20-178 7.31e-19

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: 81.43  E-value: 7.31e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  20 YLLTCDKTKItaIVDPAEPE-SVIPVIKEK-TAKKEIDLQYILTTHHHYDHAGGNEDILSYF--PSLKVY--------GG 87
Cdd:cd07722  21 YLVGTGKRRI--LIDTGEGRpSYIPLLKSVlDSEGNATISDILLTHWHHDHVGGLPDVLDLLrgPSPRVYkfprpeedED 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  88 KNASGVTYTP-KDKEIFKVGEVQVEALHTPCHTQDSICYYVssPSKRAVFTGDTLFtsGCGR-FFEGDAKQMDyALNHVL 165
Cdd:cd07722  99 PDEDGGDIHDlQDGQVFKVEGATLRVIHTPGHTTDHVCFLL--EEENALFTGDCVL--GHGTaVFEDLAAYMA-SLKKLL 173

                       170
                ....*....|...
gi 19114358 166 AALPddTVTYPGH 178
Cdd:cd07722 174 SLGP--GRIYPGH 184
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 18-180 5.87e-17

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 77.53  E-value: 5.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   18 YAYLL--TCDKTKITAIVDPAEP--ESVIPVIKEKTAKkeidLQYILTTHHHYDHAGGNEDILSYFPSLKVYGGKnASG- 92
Cdd:PLN02962  24 YTYLLadVSHPDKPALLIDPVDKtvDRDLSLVKELGLK----LIYAMNTHVHADHVTGTGLLKTKLPGVKSIISK-ASGs 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   93 ---VTYTPKDKEIFkvGEVQVEALHTPCHTQDSICYYV----SSPSKRAVFTGDTLFTSGCGR--FFEGDAKQMDYALNH 163
Cdd:PLN02962  99 kadLFVEPGDKIYF--GDLYLEVRATPGHTAGCVTYVTgegpDQPQPRMAFTGDALLIRGCGRtdFQGGSSDQLYKSVHS 176

                        170
                 ....*....|....*..
gi 19114358  164 VLAALPDDTVTYPGHEY 180
Cdd:PLN02962 177 QIFTLPKDTLIYPAHDY 193
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 19-140 1.83e-16

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: 75.61  E-value: 1.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  19 AYLLTCDKTkiTAIVDPAePESVIPVIKEKTAKKEI---DLQYILTTHHHYDHAGGNEDILSYFPSLKVY---------- 85
Cdd:cd07726  18 SYLLDGEGR--PALIDTG-PSSSVPRLLAALEALGIapeDVDYIILTHIHLDHAGGAGLLAEALPNAKVYvhprgarhli 94

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114358  86 -------GGKNASG---VTY-------------TPKDKEIFKVGEVQVEALHTPCHTQDSICYYVssPSKRAVFTGDT 140
Cdd:cd07726  95 dpsklwaSARAVYGdeaDRLggeilpvpeerviVLEDGETLDLGGRTLEVIDTPGHAPHHLSFLD--EESDGLFTGDA 170
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
13-178 1.88e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 69.70  E-value: 1.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358    13 GTGNNYAYLLTCDKTKItaIVDPAEPESVIPVIKEKTAKKEI-DLQYILTTHHHYDHAGGNEDILSYF-------PSLKV 84
Cdd:pfam00753   2 GPGQVNSYLIEGGGGAV--LIDTGGSAEAALLLLLAALGLGPkDIDAVILTHGHFDHIGGLGELAEATdvpvivvAEEAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358    85 YGGKNASGVTYTPK-----------------DKEIFKVGEVQVEALHTPCHTQDSICYYVssPSKRAVFTGDTLFTSGCG 147
Cdd:pfam00753  80 ELLDEELGLAASRLglpgppvvplppdvvleEGDGILGGGLGLLVTHGPGHGPGHVVVYY--GGGKVLFTGDLLFAGEIG 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 19114358   148 RF-FEGDAKQMDYALNH-------VLAALPDDTVTYPGH 178
Cdd:pfam00753 158 RLdLPLGGLLVLHPSSAessleslLKLAKLKAAVIVPGH 196
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 15-141 6.05e-14

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: 68.09  E-value: 6.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  15 GNNYAYLLTCDKTkiTAIVD--PAEPESVIPV---IKEKTAKK-EIDlqYILTTHHHYDHAGGnediLSYFPSL---KVY 85
Cdd:cd07725  13 GHVNVYLLRDGDE--TTLIDtgLATEEDAEALwegLKELGLKPsDID--RVLLTHHHPDHIGL----AGKLQEKsgaTVY 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19114358  86 GgknasgVTYTP-KDKEIFKVGEVQVEALHTPCHTQDSICYYVSspSKRAVFTGDTL 141
Cdd:cd07725  85 I------LDVTPvKDGDKIDLGGLRLKVIETPGHTPGHIVLYDE--DRRELFVGDAV 133
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 58-178 4.70e-13

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: 65.59  E-value: 4.70e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  58 YILTTHHHYDHAGGnedilsyFPSLK------VYGG--KNASGVTYTPK------DKEIFKVGEVQVEALHTPCHTQDSI 123
Cdd:cd16278  56 AILVTHTHRDHSPG-------AARLAertgapVRAFgpHRAGGQDTDFApdrplaDGEVIEGGGLRLTVLHTPGHTSDHL 128

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19114358 124 CYYVssPSKRAVFTGDTLFtsGCGRFF----EGDAKqmDY--ALnHVLAALPDDTVtYPGH 178
Cdd:cd16278 129 CFAL--EDEGALFTGDHVM--GWSTTViappDGDLG--DYlaSL-ERLLALDDRLL-LPGH 181
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 45-178 1.04e-11

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 62.20  E-value: 1.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  45 IKEKTAKKeidLQYILTTHHHYDHAGGN---------------------EDILSYFPSLKVYGGKNASGVTYTP-----K 98
Cdd:cd16282  45 IRKVTDKP---VRYVVNTHYHGDHTLGNaafadagapiiahentreelaARGEAYLELMRRLGGDAMAGTELVLpdrtfD 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  99 DKEIFKVGEVQVEALHT-PCHTQDSICYYVssPSKRAVFTGDTLFTSGCGRFFEGDAKQMDYALNHvLAALPDDTVTyPG 177
Cdd:cd16282 122 DGLTLDLGGRTVELIHLgPAHTPGDLVVWL--PEEGVLFAGDLVFNGRIPFLPDGSLAGWIAALDR-LLALDATVVV-PG 197


                .
gi 19114358 178 H 178
Cdd:cd16282 198 H 198
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 8-178 3.35e-11

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: 60.70  E-value: 3.35e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   8 IWMWKGTGNNYAYLLTCDKTKItaIVD---PAEPESVIPVIKEKTAKKEiDLQYILTTHHHYDHAGGNEDILSYfPSLKV 84
Cdd:cd07721   2 VYQLPLLPPVNAYLIEDDDGLT--LIDtglPGSAKRILKALRELGLSPK-DIRRILLTHGHIDHIGSLAALKEA-PGAPV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  85 Y----------GGKNASGVTYTPKDKEIFKV--------------GEV-----QVEALHTPCHTQDSICYYVssPSKRAV 135
Cdd:cd07721  78 YahereapyleGEKPYPPPVRLGLLGLLSPLlpvkpvpvdrtledGDTldlagGLRVIHTPGHTPGHISLYL--EEDGVL 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 19114358 136 FTGDTLFTSGcGR------FFEGDAKQmdyALN--HVLAALPDDTVtYPGH 178
Cdd:cd07721 156 IAGDALVTVG-GElvppppPFTWDMEE---ALEslRKLAELDPEVL-APGH 201
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 21-158 1.01e-09

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: 56.44  E-value: 1.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  21 LLTCDKTKItaIVDPAEPESViPVIKEKTAKKEI---DLQYILTTHHHYDHAGGNedilSYFPSLKVYGGKNASGVTYTP 97
Cdd:cd07711  26 LIKDGGKNI--LVDTGTPWDR-DLLLKALAEHGLspeDIDYVVLTHGHPDHIGNL----NLFPNATVIVGWDICGDSYDD 98

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19114358  98 KDkeIFKVGEVQ----VEALHTPCHTQDSICYYVSSPSK-RAVFTGDtLFTSgcgrffEGDAKQMD 158
Cdd:cd07711  99 HS--LEEGDGYEidenVEVIPTPGHTPEDVSVLVETEKKgTVAVAGD-LFER------EEDLEDPI 155
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 62-178 5.85e-09

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: 54.17  E-value: 5.85e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  62 THHHYDHAGGNedilSYFPslKVY----------GGKNASGVTYTP--------------KDKEIFKVGEVQVEALHTPC 117
Cdd:cd07712  49 THGHFDHIGGL----HEFE--EVYvhpadaeilaAPDNFETLTWDAatysvppagptlplRDGDVIDLGDRQLEVIHTPG 122

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19114358 118 HTQDSICYYvsSPSKRAVFTGDTLFTSGCgrFFEGDAKQMDYALNHV--LAALPD--DTVtYPGH 178
Cdd:cd07712 123 HTPGSIALL--DRANRLLFSGDVVYDGPL--IMDLPHSDLDDYLASLekLSKLPDefDKV-LPGH 182
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 55-179 3.93e-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: 52.60  E-value: 3.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  55 DLQYILTTHHHYDHAGGNEdilsYFPSLKVY----------GGKNASGVTYTPKDKEIFKVGEVQ-------------VE 111
Cdd:cd07729  88 DIDYVILSHLHFDHAGGLD----LFPNATIIvqraeleyatGPDPLAAGYYEDVLALDDDLPGGRvrlvdgdydlfpgVT 163

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19114358 112 ALHTPCHTQDSICYYVSSPSKRAVFTGDTLFT-----SGCGRFFEGDAKQMDYALNHV--LAALPDDTVtYPGHE 179
Cdd:cd07729 164 LIPTPGHTPGHQSVLVRLPEGTVLLAGDAAYTyenleEGRPPGINYDPEAALASLERLkaLAEREGARV-IPGHD 237
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 39-139 5.06e-08

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: 51.37  E-value: 5.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  39 ESVIPVIKEKTAKKeIDlqYILTTHHHYDHAGGNEDILSYFPSLKVY-GGKNASGVTY---------------TPKDKEI 102
Cdd:cd07731  35 DVVVPYLKARGIKK-LD--YLILTHPDADHIGGLDAVLKNFPVKEVYmPGVTHTTKTYedlldaikekgipvtPCKAGDR 111

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 19114358 103 FKVGEVQVEALHTPCHTQD-----SICYYVSSPSKRAVFTGD 139
Cdd:cd07731 112 WQLGGVSFEVLSPPKDDYDdlnnnSCVLRLTYGGTSFLLTGD 153
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 3-120 9.58e-08

BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Bradyrhizobium diazoefficiens BJP-1, Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Caulobacter crescentus Mbl1b. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 51.55  E-value: 9.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   3 FHIT-PIWmWKGTGNNYAYLLTCDKTKItaIVDPAEPESViPVIKEKTAK---KEIDLQYILTTHHHYDHAGGnediLSY 78
Cdd:cd16288   8 FRIAgNVY-YVGTSGLASYLITTPQGLI--LIDTGLESSA-PMIKANIRKlgfKPSDIKILLNSHAHLDHAGG----LAA 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114358  79 FPSL---KVY-----------GGK-----NASGVTYTP-------KDKEIFKVGEVQVEALHTPCHTQ 120
Cdd:cd16288  80 LKKLtgaKLMasaedaallasGGKsdfhyGDDSLAFPPvkvdrvlKDGDRVTLGGTTLTAHLTPGHTR 147
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
55-152 1.72e-07

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 50.58  E-value: 1.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  55 DLQYILTTHHHYDHAGGNEDILSYF------PSLKVYGGK----------NASG------VTYTP-KDKEIFKVGEVQVE 111
Cdd:COG1234  52 DIDAIFITHLHGDHIAGLPGLLSTRslagreKPLTIYGPPgtkefleallKASGtdldfpLEFHEiEPGEVFEIGGFTVT 131

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 19114358 112 ALHTpCHTQDSICYYVSSPSKRAVFTGDTLFTSGCGRFFEG 152
Cdd:COG1234 132 AFPL-DHPVPAYGYRFEEPGRSLVYSGDTRPCEALVELAKG 171
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 13-168 2.66e-07

SMB-1, THIN-B 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 SMB-1- and THIN-B-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 50.25  E-value: 2.66e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  13 GTGNNYAYLLTCDKTKItaIVD---PAEPESVIPVIKEKTAKKEiDLQYILTTHHHYDHAGG-----------------N 72
Cdd:cd16313  18 GTGGISAVLITSPQGHI--LIDggfPKSPEQIAASIRQLGFKLE-DVKYILSSHDHWDHAGGiaalqkltgaqvlaspaT 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  73 EDILS---------YFPSLKVYGGknaSGVTYTPKDKEIFKVGEVQVEALHTPCHTQDSICY-YVSSPSKRA---VFtGD 139
Cdd:cd16313  95 VAVLRsgsmgkddpQFGGLTPMPP---VASVRAVRDGEVVKLGPLAVTAHATPGHTTGGTSWtWQSCEQGRCanmVF-AD 170

                       170       180       190
                ....*....|....*....|....*....|.
gi 19114358 140 TL--FTSGCGRFFEGDAKQMDYalNHVLAAL 168
Cdd:cd16313 171 SLtaVSADGYRFSAHPAVLADV--EQSIAAV 199
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 13-125 4.32e-07

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: 49.47  E-value: 4.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  13 GTGNNYAYLLTCDKTKItaIVDPAEPESViPVIKEKTAK---KEIDLQYILTTHHHYDHAGGNEDI----------LSYF 79
Cdd:cd07708  18 GTDDLAAYLIVTPQGNI--LIDGDMEQNA-PMIKANIKKlgfKFSDTKLILISHAHFDHAGGSAEIkkqtgakvmaGAED 94

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19114358  80 PSLKVYGGK------NASGVTYTP-------KDKEIFKVGEVQVEALHTPCHTQDSICY 125
Cdd:cd07708  95 VSLLLSGGSsdfhyaNDSSTYFPQstvdravHDGERVTLGGTVLTAHATPGHTPGCTTW 153
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 13-125 5.85e-07

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: 49.39  E-value: 5.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  13 GTGNNYAYLLTCDKTKItaIVDPAEPESViPVIKEKTAK---KEIDLQYILTTHHHYDHAGGNEDIlSYFPSLKVY---- 85
Cdd:cd16308  18 GTYDLACYLIVTPKGNI--LINTGLAESV-PLIKKNIQAlgfKFKDIKILLTTQAHYDHVGAMAAI-KQQTGAKMMvdek 93

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19114358  86 -------GGKN-----ASGVTYTP-------KDKEIFKVGEVQVEALHTPCHTQDSICY 125
Cdd:cd16308  94 dakvladGGKSdyemgGYGSTFAPvkadkllHDGDTIKLGGTKLTLLHHPGHTKGSCSF 152
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 41-139 1.11e-06

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: 48.32  E-value: 1.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  41 VIPVIKEKtAKKEIDlqYILTTHHHYDHAGGNEDILSYFPSLKVYGGK---------------NASGVTYTP-KDKEIFK 104
Cdd:COG2333  41 VLPYLRAL-GIRRLD--LLVLTHPDADHIGGLAAVLEAFPVGRVLVSGppdtsetyerllealKEKGIPVRPcRAGDTWQ 117

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 19114358 105 VGEVQVEALHtPCHTQ--------DSICYYVSSPSKRAVFTGD 139
Cdd:COG2333 118 LGGVRFEVLW-PPEDLlegsdennNSLVLRLTYGGFSFLLTGD 159
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 32-143 1.81e-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) 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: 47.14  E-value: 1.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  32 IVDPAEPESVIPVIKEKTAKKEIDLQYILTTHHHYDHAGGNEDILSYFPsLKVYGGKNASGVT-------------YTPK 98
Cdd:cd07743  22 LIDSGLDEDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTG-CKVYAPKIEKAFIenpllepsylggaYPPK 100

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19114358  99 --------------DKEI----FKVGEVQVEALHTPCHTQDSICYYVSSpskRAVFTGDTLFT 143
Cdd:cd07743 101 elrnkflmakpskvDDIIeegeLELGGVGLEIIPLPGHSFGQIGILTPD---GVLFAGDALFG 160
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 13-178 4.63e-06

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


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 46.57  E-value: 4.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  13 GTGNNYAYLLTCDKTKItaIVDPAEPESViPVIKEKTAK---KEIDLQYILTTHHHYDHAGGNEDI--LSYFPSLKVYGG 87
Cdd:cd16290  18 GTGGLSAVLITSPQGLI--LIDGALPQSA-PQIEANIRAlgfRLEDVKLILNSHAHFDHAGGIAALqrDSGATVAASPAG 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  88 KNA--SGVT------------YTP-------KDKEIFKVGEVQVEALHTPCHTQDSICY-YVSSPSKRA---VFtGDTLF 142
Cdd:cd16290  95 AAAlrSGGVdpddpqagaadpFPPvakvrvvADGEVVKLGPLAVTAHATPGHTPGGTSWtWRSCEGGRCldiVY-ADSLT 173

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 19114358 143 TSGCGRF-FEGDAKQmdyalNHV---------LAALPDDTV--TYPGH 178
Cdd:cd16290 174 AVSADGFrFSDDAHP-----ARVaafrrsiatVAALPCDILisAHPDA 216
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 3-136 5.47e-06

Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of Mbl1b-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293868  Cd Length: 252  Bit Score: 46.29  E-value: 5.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   3 FHITPIWMWKGTGNNYAYLLTCDKTkitAIVDPAEPESVIPVIKEKTAKKEIDL---QYILTTHHHYDHAG--------- 70
Cdd:cd16310   8 FRIVDNIYYVGTKGIGSYLITSNHG---AILLDGGLEENAALIEQNIKALGFKLsdiKIIINTHAHYDHAGglaqlkadt 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  71 GNEDILSY--FPSL---KVYGGKNASGVTYTP-------KDKEIFKVGEVQVEALHTPCHTQDSICYYVSSPSK----RA 134
Cdd:cd16310  85 GAKLWASRgdRPALeagKHIGDNITQPAPFPAvkvdrilGDGEKIKLGDITLTATLTPGHTKGCTTWSTTVKENgrplRV 164


                ..
gi 19114358 135 VF 136
Cdd:cd16310 165 VF 166
NorV COG0426
Flavorubredoxin [Energy production and conversion];
19-139 1.50e-04

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 42.51  E-value: 1.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  19 AYLLTCDKTkitAIVDPAEP---ESVIPVIKEKTAKKEIDlqYILTTHHHYDHAGGNEDILSYFPSLKVYGGKNAS---- 91
Cdd:COG0426  36 SYLIVDEKT---ALIDTVGEsffEEFLENLSKVIDPKKID--YIIVNHQEPDHSGSLPELLELAPNAKIVCSKKAArflp 110

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  92 -----------GVtytpKDKEIFKVGEVQVEALHTP-CHTQDSICYYVssPSKRAVFTGD 139
Cdd:COG0426 111 hfygipdfrfiVV----KEGDTLDLGGHTLQFIPAPmLHWPDTMFTYD--PEDKILFSGD 164
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 6-140 1.76e-04

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: 41.09  E-value: 1.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358   6 TPIWMWKGTGNNYAYLLTCDKTKItaIVDPaePESVIPVIkEKTAKKEIDLQYILTTHHHYDHAGGnediLSYFP----- 80
Cdd:cd16272   6 TGGAVPSLTRNTSSYLLETGGTRI--LLDC--GEGTVYRL-LKAGVDPDKLDAIFLSHFHLDHIGG----LPTLLfarry 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  81 -----SLKVYGGK---------NASGVTYTPK-----------DKEIFKVGEVQVEALHTpCHTQDSICYYVSSPSKRAV 135
Cdd:cd16272  77 ggrkkPLTIYGPKgikefleklLNFPVEILPLgfpleieeleeGGEVLELGDLKVEAFPV-KHSVESLGYRIEAEGKSIV 155


                ....*
gi 19114358 136 FTGDT 140
Cdd:cd16272 156 YSGDT 160
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 54-101 2.64e-04

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: 41.45  E-value: 2.64e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 19114358  54 IDL---QYILTTHHHYDHAGGNEDILSYFPSLKVYGGKNASGVTYTPKDKE 101
Cdd:cd07713  51 IDLsdiDAVVLSHGHYDHTGGLKALLELNPKAPVYAHPDAFEPRYSKRGGG 101
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 13-71 2.77e-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: 41.32  E-value: 2.77e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114358  13 GTGNNYAYLLTCDKTKItaIVDPAEPESViPVIKEKTAK---KEIDLQYILTTHHHYDHAGG 71
Cdd:cd16309  18 GTAGLGVFLITTPEGHI--LIDGAMPQST-PLIKDNIKKlgfDVKDVKYLLNTHAHFDHAGG 76
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
54-103 3.73e-04

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 41.02  E-value: 3.73e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 19114358  54 IDLQ---YILTTHHHYDHAGGNEDILSYFPSLKVYGGKNASGVTYTPKDKEIF 103
Cdd:COG1237  53 IDLSdidAVVLSHGHYDHTGGLPALLELNPKAPVYAHPDAFEKRYSKRPGGKY 105
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 19-139 4.65e-04

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. 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. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 40.55  E-value: 4.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  19 AYLLTCDKTkitAIVDPAEP---ESVIPVIKEKTAKKEIDlqYILTTHHHYDHAGGNEDILSYFPSLKVYGgkNASGVTY 95
Cdd:cd07709  34 SYLIKDEKT---ALIDTVKEpffDEFLENLEEVIDPRKID--YIVVNHQEPDHSGSLPELLELAPNAKIVC--SKKAARF 106

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 19114358  96 TP-------------KDKEIFKVGEVQVEALHTP-CHTQDSICYYVssPSKRAVFTGD 139
Cdd:cd07709 107 LKhfypgiderfvvvKDGDTLDLGKHTLKFIPAPmLHWPDTMVTYD--PEDKILFSGD 162
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 59-139 7.35e-04

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. 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: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 39.70  E-value: 7.35e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  59 ILTTHHHYDHAGGNEDILSYFPsLKVYGGKNASGV---------------TYTPKDKEIFKVGEVQVEALHTpCH-TQDS 122
Cdd:cd07714  59 IFITHGHEDHIGALPYLLPELN-VPIYATPLTLALikkkleefklikkvkLNEIKPGERIKLGDFEVEFFRV-THsIPDS 136

                        90
                ....*....|....*..
gi 19114358 123 ICYYVSSPSKRAVFTGD 139
Cdd:cd07714 137 VGLAIKTPEGTIVHTGD 153
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 19-145 9.30e-04

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 39.52  E-value: 9.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  19 AYLLTCDKTKItaIVDP--AEPESVIPVIKEKTAK-KEIDlqYILTTHHHYDHAG---------------GNEDILSYFP 80
Cdd:COG2220  13 TFLIETGGKRI--LIDPvfSGRASPVNPLPLDPEDlPKID--AVLVTHDHYDHLDdatlralkrtgatvvAPLGVAAWLR 88

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19114358  81 SLkvyGGKNASGVTYTpkdkEIFKVGEVQVEAL---HTPCHTQDSIC----YYVSSPSKRAVFTGDTLFTSG 145
Cdd:COG2220  89 AW---GFPRVTELDWG----ESVELGGLTVTAVparHSSGRPDRNGGlwvgFVIETDGKTIYHAGDTGYFPE 153
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 13-85 9.54e-04

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: 39.55  E-value: 9.54e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19114358  13 GTGNNyayLLTcDKTKITAIVDpaEPESVIPVIKEKTAKKEiDLQYILTTHHHYDHAGG-----NEDILSYFPSLKVY 85
Cdd:cd07728  60 GIGNG---KLT-EKQKRNFGVT--EESSIEESLAELGLTPE-DIDYVLMTHLHFDHASGltkvkGEQLVSVFPNATIY 130
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 13-172 1.23e-03

Janthinobacterium lividum THIN-B 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 THIN-B-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 39.20  E-value: 1.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  13 GTGNNYAYLLTCDKTKItaIVDPAEPESVIPVIK--EKTAKKEIDLQYILTTHHHYDHAGGNEDI---------LSYFPS 81
Cdd:cd16312  18 GTAGLSAVLVTSPQGHV--LLDGALPQSAPLIIAniEALGFRIEDVKLILNSHAHWDHAGGIAALqkasgatvaASAHGA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  82 LKVYGGKN--------ASGVTYTPK--------DKEIFKVGEVQVEALHTPCHTQDSICY------------YVSSPSKR 133
Cdd:cd16312  96 QVLQSGTNgkddpqyqAKPVVHVAKvakvkevgEGDTLKVGPLRLTAHMTPGHTPGGTTWtwtscegqrcldVVYADSLN 175

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 19114358 134 AVFTGDTLFTSGCG------RFFEGDAKQMDYALNHVLAALPDDT 172
Cdd:cd16312 176 PYSSGDFYYTGKGGypdisaSFRASIAKVAALPCDIIIAVHPGFT 220
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 33-142 1.40e-03

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


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 38.64  E-value: 1.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  33 VDP----AEPESVIPVIKEkTAKKeidLQYILTTHHHYDHAGGNEDILSYFPSLKVY----------------------- 85
Cdd:cd07739  30 VDAqftrADAERLADWIKA-SGKT---LTTIYITHGHPDHYFGLEVLLEAFPDAKVVatpavvahikaqlepklafwgpl 105

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  86 GGKNA--SGVTYTPKDKEIFKVGEVQVEALHTPCHTQDSICY-YVssPSKRAVFTGDTLF 142
Cdd:cd07739 106 LGGNApaRLVVPEPLDGDTLTLEGHPLEIVGVGGGDTDDTTYlWI--PSLKTVVAGDVVY 163
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 55-147 3.63e-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: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 37.95  E-value: 3.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  55 DLQYILTTHHHYDHAGGNEdilsYFPSL---KVY---------------GGKNASGVTYTP----KDKEIFKVGEVQVEA 112
Cdd:cd16280  61 DIKYILITHGHGDHYGGAA----YLKDLygaKVVmseadwdmmeeppeeGDNPRWGPPPERdiviKDGDTLTLGDTTITV 136

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 19114358 113 LHTPCHTQDSICYY--VSSPSK--RAVFTGDTLFTSGCG 147
Cdd:cd16280 137 YLTPGHTPGTLSLIfpVKDGGKthRAGLWGGTGLNTGPN 175
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 33-90 4.11e-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: 37.63  E-value: 4.11e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 19114358  33 VDPAEPESVIPVIKEKTAKKEiDLQYILTTHHHYDHAGGnediLSYFPSLKVYGGKNA 90
Cdd:cd07730  62 VPLEVEEDVAEQLAAGGIDPE-DIDAVILSHLHWDHIGG----LSDFPNARLIVGPGA 114
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 55-84 4.92e-03

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


Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 37.22  E-value: 4.92e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 19114358  55 DLQYILTTHHHYDHAGGnediLSYFPSLKV 84
Cdd:cd07742  80 DVRHIVLTHLDLDHAGG----LADFPHATV 105
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 110-141 5.63e-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: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 37.12  E-value: 5.63e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 19114358 110 VEALHTPCHTQDSICYYVSSPSKRAVFTGDTL 141
Cdd:cd16277 147 IRLEPTPGHTPGHVSVELESGGERALFTGDVM 178
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 110-144 6.43e-03

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


Pssm-ID: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 36.40  E-value: 6.43e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 19114358 110 VEALHTPCHTQDSICYYVssPSKRAVFTGDTLFTS 144
Cdd:cd07727 104 LTLIPVPGHTRGSVVLLY--KEKGVLFTGDHLAWS 136
PRK05452 PRK05452
anaerobic nitric oxide reductase flavorubredoxin; Provisional
 3-90 7.93e-03

anaerobic nitric oxide reductase flavorubredoxin; Provisional


Pssm-ID: 235475 [Multi-domain]  Cd Length: 479  Bit Score: 37.05  E-value: 7.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358    3 FHITPIWMWKGTGNNyAYLLTCDKTKITAIVDPAEPESVIpvikeKTAKKEIDLQ---YILTTHHHYDHAGGNEDILSYF 79
Cdd:PRK05452  22 FHGTEYKTLRGSSYN-SYLIREEKNVLIDTVDHKFSREFV-----QNLRNEIDLAdidYIVINHAEEDHAGALTELMAQI 95

                         90
                 ....*....|.
gi 19114358   80 PSLKVYGGKNA 90
Cdd:PRK05452  96 PDTPIYCTANA 106
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 39-179 9.13e-03

Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Bacillus cereus Beta-lactamase 2, also called BcII. MBLs (class B of the Ambler beta-lactamase classification) 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. BcII is a chromosome-encoded B1 MBL. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293862 [Multi-domain]  Cd Length: 212  Bit Score: 36.49  E-value: 9.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114358  39 ESVIPVIKEKTaKKEIdlQYILTTHHHYDHAGGNEDILSYfpSLKVYGG--------KNASGVT-YTPKDKEIFKVGEVQ 109
Cdd:cd16304  50 EELLDWIKKKL-KKPV--TLAIVTHAHDDRIGGIKALQKR--GIPVYSTkltaqlakKQGYPSPdGILKDDTTLKFGNTK 124

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19114358 110 VEALHT-PCHTQDSICYYVssPSKRAVFTG---DTLFTSGCGRFFEGDAKQMDYALNHVLAALPDDTVTYPGHE 179
Cdd:cd16304 125 IETFYPgEGHTADNIVVWL--PQSKILFGGclvKSLEAKDLGNTADANLKEWPTSIRNVLKRYPNAEIVVPGHG 196
 
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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