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Conserved domains on  [gi|18406237|ref|NP_565999|]
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glyoxalase 2-1 [Arabidopsis thaliana]

Protein Classification

PLN02398 family protein( domain architecture ID 11476741)

PLN02398 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 1-331 0e+00

hydroxyacylglutathione hydrolase


:

Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 675.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237    1 MPVISKASSTttNSSIPSCSRIGGQLCVWPGLRQLCLRKSLLYGVMWLLSMPLKTLRGARKTLKITHFCSISNMPSSLKI 80
Cdd:PLN02398   1 MQMISKASSA--MSSFRCSRRIRGQLCVRPGVRQLCLRKSLLYGVMKLLSMPLKTLRGAGRTLKVAQFCSVSNVSSSLQI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237   81 ELVPCSKDNYAYLLHDEDTGTVGVVDPSEAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDKDR 160
Cdd:PLN02398  79 ELVPCLKDNYAYLLHDEDTGTVGVVDPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVDKDR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  161 IPGIDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLSCGTLSEGTPEQMLSSLQKIVSLPDDT 240
Cdd:PLN02398 159 IPGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGKLFEGTPEQMLSSLQKIISLPDDT 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  241 NIYCGRENTAGNLKFALSVEPKNETLQSYATRVAHLRSQGLPSIPTTVKVEKACNPFLRISSKDIRKSLSIPDSATEAEA 320
Cdd:PLN02398 239 NIYCGHEYTLSNSKFALSIEPNNEVLQSYAAHVAHLRSKGLPTIPTTVKMEKACNPFLRTSSTDIRKSLSIPDTADEAEA 318

                        330
                 ....*....|.
gi 18406237  321 LRRIQRARDRF 331
Cdd:PLN02398 319 LGIIRRAKDNF 329
 
Name Accession Description Interval E-value
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 1-331 0e+00

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 675.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237    1 MPVISKASSTttNSSIPSCSRIGGQLCVWPGLRQLCLRKSLLYGVMWLLSMPLKTLRGARKTLKITHFCSISNMPSSLKI 80
Cdd:PLN02398   1 MQMISKASSA--MSSFRCSRRIRGQLCVRPGVRQLCLRKSLLYGVMKLLSMPLKTLRGAGRTLKVAQFCSVSNVSSSLQI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237   81 ELVPCSKDNYAYLLHDEDTGTVGVVDPSEAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDKDR 160
Cdd:PLN02398  79 ELVPCLKDNYAYLLHDEDTGTVGVVDPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVDKDR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  161 IPGIDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLSCGTLSEGTPEQMLSSLQKIVSLPDDT 240
Cdd:PLN02398 159 IPGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGKLFEGTPEQMLSSLQKIISLPDDT 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  241 NIYCGRENTAGNLKFALSVEPKNETLQSYATRVAHLRSQGLPSIPTTVKVEKACNPFLRISSKDIRKSLSIPDSATEAEA 320
Cdd:PLN02398 239 NIYCGHEYTLSNSKFALSIEPNNEVLQSYAAHVAHLRSKGLPTIPTTVKMEKACNPFLRTSSTDIRKSLSIPDTADEAEA 318

                        330
                 ....*....|.
gi 18406237  321 LRRIQRARDRF 331
Cdd:PLN02398 319 LGIIRRAKDNF 329
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 80-331 2.30e-119

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: 343.75  E-value: 2.30e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237    80 IELVPCSKDNYAYLLHDEDTGTVgVVDPSEAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAvdKD 159
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPDGQAA-VVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAFPAPVYGPA--EE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237   160 RIPGIDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLSCGTLSEGTPEQMLSSLQKIVSLPDD 239
Cdd:TIGR03413  78 RIPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAALPDD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237   240 TNIYCGRENTAGNLKFALSVEPKNETLQSYATRVAHLRSQGLPSIPTTVKVEKACNPFLRISSKDIRKSLSIPDsATEAE 319
Cdd:TIGR03413 158 TLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAALGSQG-ADPVE 236

                         250
                  ....*....|..
gi 18406237   320 ALRRIQRARDRF 331
Cdd:TIGR03413 237 VFAALRAWKDNF 248
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 83-245 1.32e-86

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: 257.39  E-value: 1.32e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  83 VPCSKDNYAYLLHDEDTGTVGVVDPSEAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYG-AKVIGSAvdKDRI 161
Cdd:cd07723   3 IPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPdAPVYGPA--EDRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 162 PGIDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLSCGTLSEGTPEQMLSSLQKIVSLPDDTN 241
Cdd:cd07723  81 PGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLALPDDTL 160


                ....
gi 18406237 242 IYCG 245
Cdd:cd07723 161 VYCG 164
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 78-245 2.95e-50

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: 166.40  E-value: 2.95e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  78 LKIELVPCSKDNYAYLLHDEDtGTVgVVDP----SEAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIG 153
Cdd:COG0491   4 LPGGTPGAGLGVNSYLIVGGD-GAV-LIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 154 SAVDKDRI-------------PGIDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLSCG--TL 218
Cdd:COG0491  82 HAAEAEALeapaagalfgrepVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGrpDL 161

                       170       180
                ....*....|....*....|....*..
gi 18406237 219 SEGTPEQMLSSLQKIVSLPDDTnIYCG 245
Cdd:COG0491 162 PDGDLAQWLASLERLLALPPDL-VIPG 187
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 90-245 3.54e-37

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: 131.14  E-value: 3.54e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237     90 YAYLLHDEDtGTVgVVDP--SEAAPVIEALSRKNW-NLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDKD------- 159
Cdd:smart00849   1 NSYLVRDDG-GAI-LIDTgpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAEllkdlla 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237    160 ---------RIPGIDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLSCG-TLSEGTPEQMLSS 229
Cdd:smart00849  79 llgelgaeaEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGrTLVDGGDAAASDA 158

                          170
                   ....*....|....*...
gi 18406237    230 LQKIVSL--PDDTNIYCG 245
Cdd:smart00849 159 LESLLKLlkLLPKLVVPG 176
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 247-331 5.67e-29

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: 106.75  E-value: 5.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237   247 ENTAGNLKFALSVEPKNETLQSYATRVAHLRSQGLPSIPTTVKVEKACNPFLRISSKDIRKSLSIPDsatEAEALRRIQR 326
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGETD---PVEVFAALRE 77


                  ....*
gi 18406237   327 ARDRF 331
Cdd:pfam16123  78 LKDNF 82
 
Name Accession Description Interval E-value
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 1-331 0e+00

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 675.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237    1 MPVISKASSTttNSSIPSCSRIGGQLCVWPGLRQLCLRKSLLYGVMWLLSMPLKTLRGARKTLKITHFCSISNMPSSLKI 80
Cdd:PLN02398   1 MQMISKASSA--MSSFRCSRRIRGQLCVRPGVRQLCLRKSLLYGVMKLLSMPLKTLRGAGRTLKVAQFCSVSNVSSSLQI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237   81 ELVPCSKDNYAYLLHDEDTGTVGVVDPSEAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDKDR 160
Cdd:PLN02398  79 ELVPCLKDNYAYLLHDEDTGTVGVVDPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVDKDR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  161 IPGIDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLSCGTLSEGTPEQMLSSLQKIVSLPDDT 240
Cdd:PLN02398 159 IPGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGKLFEGTPEQMLSSLQKIISLPDDT 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  241 NIYCGRENTAGNLKFALSVEPKNETLQSYATRVAHLRSQGLPSIPTTVKVEKACNPFLRISSKDIRKSLSIPDSATEAEA 320
Cdd:PLN02398 239 NIYCGHEYTLSNSKFALSIEPNNEVLQSYAAHVAHLRSKGLPTIPTTVKMEKACNPFLRTSSTDIRKSLSIPDTADEAEA 318

                        330
                 ....*....|.
gi 18406237  321 LRRIQRARDRF 331
Cdd:PLN02398 319 LGIIRRAKDNF 329
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 80-331 2.30e-119

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: 343.75  E-value: 2.30e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237    80 IELVPCSKDNYAYLLHDEDTGTVgVVDPSEAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAvdKD 159
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPDGQAA-VVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAFPAPVYGPA--EE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237   160 RIPGIDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLSCGTLSEGTPEQMLSSLQKIVSLPDD 239
Cdd:TIGR03413  78 RIPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAALPDD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237   240 TNIYCGRENTAGNLKFALSVEPKNETLQSYATRVAHLRSQGLPSIPTTVKVEKACNPFLRISSKDIRKSLSIPDsATEAE 319
Cdd:TIGR03413 158 TLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAALGSQG-ADPVE 236

                         250
                  ....*....|..
gi 18406237   320 ALRRIQRARDRF 331
Cdd:TIGR03413 237 VFAALRAWKDNF 248
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 83-245 1.32e-86

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: 257.39  E-value: 1.32e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  83 VPCSKDNYAYLLHDEDTGTVGVVDPSEAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYG-AKVIGSAvdKDRI 161
Cdd:cd07723   3 IPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPdAPVYGPA--EDRI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 162 PGIDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLSCGTLSEGTPEQMLSSLQKIVSLPDDTN 241
Cdd:cd07723  81 PGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLALPDDTL 160


                ....
gi 18406237 242 IYCG 245
Cdd:cd07723 161 VYCG 164
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 78-331 1.39e-71

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 222.71  E-value: 1.39e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237   78 LKIELVPCSKDNYAYLLHDEDTGTVGVVDPSEAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERY-GAKVIGSAV 156
Cdd:PLN02469   1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVpGIKVYGGSL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  157 DKdrIPGIDILLKDSDKWMFAGH-EVRILDTPGHTQGHISFYFPGS----ATIFTGDLIYSLSCGTLSEGTPEQMLSSLQ 231
Cdd:PLN02469  81 DN--VKGCTHPVENGDKLSLGKDvNILALHTPCHTKGHISYYVTGKegedPAVFTGDTLFIAGCGKFFEGTAEQMYQSLC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  232 KIV-SLPDDTNIYCGRENTAGNLKFALSVEPKNETLQSYATRVAHLRSQGLPSIPTTVKVEKACNPFLRISSKDIRKSLS 310
Cdd:PLN02469 159 VTLgSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVG 238

                        250       260
                 ....*....|....*....|.
gi 18406237  311 IPDSateAEALRRIQRARDRF 331
Cdd:PLN02469 239 CESP---VEALREVRKMKDNW 256
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 83-305 8.21e-63

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 200.05  E-value: 8.21e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237   83 VPCSKDNYAYLLHDeDTGTVGVVDPSEAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVI-GSAVDKDRi 161
Cdd:PRK10241   6 IPAFDDNYIWVLND-EAGRCLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVyGPQETQDK- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  162 pGIDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYfpGSATIFTGDLIYSLSCGTLSEGTPEQMLSSLQKIVSLPDDTN 241
Cdd:PRK10241  84 -GTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF--SKPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKINALPDDTL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18406237  242 IYCGRENTAGNLKFALSVEPKNETLQSYATRVAHLRSQGLPSIPTTVKVEKACNPFLRISSKDI 305
Cdd:PRK10241 161 ICCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINLFLRTEDIDL 224
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 78-245 2.95e-50

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: 166.40  E-value: 2.95e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  78 LKIELVPCSKDNYAYLLHDEDtGTVgVVDP----SEAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIG 153
Cdd:COG0491   4 LPGGTPGAGLGVNSYLIVGGD-GAV-LIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 154 SAVDKDRI-------------PGIDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLSCG--TL 218
Cdd:COG0491  82 HAAEAEALeapaagalfgrepVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGrpDL 161

                       170       180
                ....*....|....*....|....*..
gi 18406237 219 SEGTPEQMLSSLQKIVSLPDDTnIYCG 245
Cdd:COG0491 162 PDGDLAQWLASLERLLALPPDL-VIPG 187
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 91-245 6.96e-48

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: 159.37  E-value: 6.96e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  91 AYLLHDEDTGTVgVVDP--SEAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDKDRI------- 161
Cdd:cd06262  12 CYLVSDEEGEAI-LIDPgaGALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAELLedpelnl 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 162 ----------PGIDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLSCG--TLSEGTPEQMLSS 229
Cdd:cd06262  91 affgggplppPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGrtDLPGGDPEQLIES 170

                       170
                ....*....|....*..
gi 18406237 230 LQKIVS-LPDDTNIYCG 245
Cdd:cd06262 171 IKKLLLlLPDDTVVYPG 187
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 88-298 1.96e-37

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: 132.86  E-value: 1.96e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  88 DNYAYLLHDEDTGTVGVVDPSEAAP-VIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDK-------- 158
Cdd:cd16322  10 QENTYLVADEGGGEAVLVDPGDESEkLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDLplyeaadl 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 159 ---------DRIPGIDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLSCG--TLSEGTPEQML 227
Cdd:cd16322  90 gakafglgiEPLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGrtDLPGGDPKAMA 169

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18406237 228 SSLQKIVSLPDDTNIYCGrentagnlkfalsvepknetlqsyatrvaHlrsqglpSIPTTVKVEKACNPFL 298
Cdd:cd16322 170 ASLRRLLTLPDETRVFPG-----------------------------H-------GPPTTLGEERRTNPFL 204
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 90-245 3.54e-37

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: 131.14  E-value: 3.54e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237     90 YAYLLHDEDtGTVgVVDP--SEAAPVIEALSRKNW-NLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDKD------- 159
Cdd:smart00849   1 NSYLVRDDG-GAI-LIDTgpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAEllkdlla 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237    160 ---------RIPGIDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLSCG-TLSEGTPEQMLSS 229
Cdd:smart00849  79 llgelgaeaEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGrTLVDGGDAAASDA 158

                          170
                   ....*....|....*...
gi 18406237    230 LQKIVSL--PDDTNIYCG 245
Cdd:smart00849 159 LESLLKLlkLLPKLVVPG 176
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 90-243 1.41e-36

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: 129.44  E-value: 1.41e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  90 YAYLLHDEDTGTVGVVDPS--EAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAvdKDRIPGIDIL 167
Cdd:cd07724  13 LSYLVGDPETGEAAVIDPVrdSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGE--GAPASFFDRL 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 168 LKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLSCG-----TLSEGTPEQMLSSLQ-KIVSLPDDTN 241
Cdd:cd07724  91 LKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGrpdlpGEAEGLARQLYDSLQrKLLLLPDETL 170


                ..
gi 18406237 242 IY 243
Cdd:cd07724 171 VY 172
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 88-245 5.04e-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: 125.34  E-value: 5.04e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  88 DNYAYLLHDEDTGTVGVVDPS-EAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDKD----RIP 162
Cdd:cd16275  11 INYSYIIIDKATREAAVVDPAwDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDyygfRCP 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 163 GIdILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSatIFTGDLIYSLSCG--TLSEGTPEQMLSSLQKIVSL-PDD 239
Cdd:cd16275  91 NL-IPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGDS--LFTGDTLFIEGCGrcDLPGGDPEEMYESLQRLKKLpPPN 167


                ....*.
gi 18406237 240 TNIYCG 245
Cdd:cd16275 168 TRVYPG 173
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 247-331 5.67e-29

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: 106.75  E-value: 5.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237   247 ENTAGNLKFALSVEPKNETLQSYATRVAHLRSQGLPSIPTTVKVEKACNPFLRISSKDIRKSLSIPDsatEAEALRRIQR 326
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGETD---PVEVFAALRE 77


                  ....*
gi 18406237   327 ARDRF 331
Cdd:pfam16123  78 LKDNF 82
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 90-245 1.55e-27

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: 106.54  E-value: 1.55e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  90 YAYLLHDEDTGTVgvVD---PSEAAPVIEALSRKNWN---LTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDK----- 158
Cdd:cd07721  12 NAYLIEDDDGLTL--IDtglPGSAKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEREApyleg 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 159 ---------------------DRIPGIDILLKDSDKwMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLscGT 217
Cdd:cd07721  90 ekpypppvrlgllgllspllpVKPVPVDRTLEDGDT-LDLAGGLRVIHTPGHTPGHISLYLEEDGVLIAGDALVTV--GG 166

                       170       180       190
                ....*....|....*....|....*....|....*
gi 18406237 218 LSEGTP-------EQMLSSLQKIVSLPDDTnIYCG 245
Cdd:cd07721 167 ELVPPPppftwdmEEALESLRKLAELDPEV-LAPG 200
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 92-245 2.24e-26

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: 103.02  E-value: 2.24e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  92 YLLHDEDTGTVGVVDP-SEAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAV-DK---DRIP---- 162
Cdd:cd07737  14 SLIWCEETKEAAVIDPgGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKeDKfllENLPeqsq 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 163 --GI--------DILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLSCG--TLSEGTPEQMLSSL 230
Cdd:cd07737  94 mfGFppaeaftpDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGrtDFPGGNHAQLIASI 173

                       170
                ....*....|....*.
gi 18406237 231 Q-KIVSLPDDTNIYCG 245
Cdd:cd07737 174 KeKLLPLGDDVTFIPG 189
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 92-240 3.05e-23

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: 94.48  E-value: 3.05e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  92 YLLHDEDTgtVGVVDPSEAAP-----VIEALSRKNwnLTYILNTHHHDDHIGGNAELKERYGAKVIG------SAVDKDR 160
Cdd:cd16278  21 YLLGAPDG--VVVIDPGPDDPahldaLLAALGGGR--VSAILVTHTHRDHSPGAARLAERTGAPVRAfgphraGGQDTDF 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 161 IPgiDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIysLSCGT--LS--EGTPEQMLSSLQKIVSL 236
Cdd:cd16278  97 AP--DRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHV--MGWSTtvIAppDGDLGDYLASLERLLAL 172


                ....
gi 18406237 237 PDDT 240
Cdd:cd16278 173 DDRL 176
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 98-240 1.65e-20

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: 88.01  E-value: 1.65e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  98 DTGTVgVVD----PSEAAPVIEALSRknwnLT-----YILNTHHHDDHIGGNAELKERyGAKVIGSA------------- 155
Cdd:cd16282  23 DDGVV-VIDtgasPRLARALLAAIRK----VTdkpvrYVVNTHYHGDHTLGNAAFADA-GAPIIAHEntreelaargeay 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 156 ------VDKDRIPGI-----DILLKDSDKWMFAGHEVRILDT-PGHTQGHISFYFPGSATIFTGDLIYSLSCGTLSEGTP 223
Cdd:cd16282  97 lelmrrLGGDAMAGTelvlpDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEGVLFAGDLVFNGRIPFLPDGSL 176

                       170
                ....*....|....*..
gi 18406237 224 EQMLSSLQKIVSLPDDT 240
Cdd:cd16282 177 AGWIAALDRLLALDATV 193
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
90-245 1.95e-20

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 87.42  E-value: 1.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237    90 YAYLLHDEDtGTVgVVDP--SEAAPVIE---ALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVD------- 157
Cdd:pfam00753   7 NSYLIEGGG-GAV-LIDTggSAEAALLLllaALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEarellde 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237   158 ---------KDRIPGIDILLKDSDKWM-----FAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLSCGTLSEGTP 223
Cdd:pfam00753  85 elglaasrlGLPGPPVVPLPPDVVLEEgdgilGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDLPLG 164

                         170       180       190
                  ....*....|....*....|....*....|..
gi 18406237   224 ----------EQMLSSLQKIVSLPDDTnIYCG 245
Cdd:pfam00753 165 gllvlhpssaESSLESLLKLAKLKAAV-IVPG 195
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 87-239 2.05e-20

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: 86.97  E-value: 2.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  87 KDNYAYLLHDEDTGTVgvVDP----SEAAPVIEA----LSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDK 158
Cdd:cd07725  13 GHVNVYLLRDGDETTL--IDTglatEEDAEALWEglkeLGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGATVYILDVTP 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 159 dripgidilLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGD--LIYSLSCGTLSEGTPE----QMLSSLQK 232
Cdd:cd07725  91 ---------VKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDavLPKITPNVSLWAVRVEdplgAYLESLDK 161


                ....*..
gi 18406237 233 IVSLPDD 239
Cdd:cd07725 162 LEKLDVD 168
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 91-237 2.27e-20

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: 87.55  E-value: 2.27e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  91 AYLLHDE------DTGTVGVVDPSEAApvIEALSRKNWNLTYILNTHHHDDHIGGNAELKERY-GAKVI----------- 152
Cdd:cd07726  18 SYLLDGEgrpaliDTGPSSSVPRLLAA--LEALGIAPEDVDYIILTHIHLDHAGGAGLLAEALpNAKVYvhprgarhlid 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 153 ------GSA----------------VDKDRIpgidILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGD-- 208
Cdd:cd07726  96 psklwaSARavygdeadrlggeilpVPEERV----IVLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDaa 171

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 18406237 209 --LIYSLSCGTLSEGTP-----EQMLSSLQKIVSLP 237
Cdd:cd07726 172 gvRYPELDVVGPPSTPPpdfdpEAWLESLDRLLSLK 207
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 87-239 3.09e-20

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: 86.82  E-value: 3.09e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  87 KDNYAYLLhdeDTGTvgvvDPSEAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDKDRI----- 161
Cdd:cd07743  16 GDKEALLI---DSGL----DEDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAFIenpll 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 162 ---------PGIDILLK-------------DSDKWMFAGHEVRILDTPGHTQGHISFYFPGSaTIFTGDLIYslscgtlS 219
Cdd:cd07743  89 epsylggayPPKELRNKflmakpskvddiiEEGELELGGVGLEIIPLPGHSFGQIGILTPDG-VLFAGDALF-------G 160

                       170       180       190
                ....*....|....*....|....*....|.
gi 18406237 220 EGT-----------PEQMLSSLQKIVSLPDD 239
Cdd:cd07743 161 EEVlekygipflydVEEQLETLEKLEELDAD 191
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 98-199 1.06e-17

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: 81.09  E-value: 1.06e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  98 DTGtvgvvDPSEAAPVI----EALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDKDRI------------ 161
Cdd:cd16280  37 DAL-----NNNEAADLIvdglEKLGLDPADIKYILITHGHGDHYGGAAYLKDLYGAKVVMSEADWDMMeeppeegdnprw 111

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 18406237 162 ---PGIDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFP 199
Cdd:cd16280 112 gppPERDIVIKDGDTLTLGDTTITVYLTPGHTPGTLSLIFP 152
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 128-245 2.69e-15

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: 72.66  E-value: 2.69e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 128 LNTHHHDDHIGGNAELKERYG--------------AKVIGSAVDKDRIPGIDIL-LKDSDKWMFAGHEVRILDTPGHTQG 192
Cdd:cd07712  47 VATHGHFDHIGGLHEFEEVYVhpadaeilaapdnfETLTWDAATYSVPPAGPTLpLRDGDVIDLGDRQLEVIHTPGHTPG 126

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 18406237 193 HISFYFPGSATIFTGDLIYSLSCGTLSEGTP-EQMLSSLQKIVSLPDDTN-IYCG 245
Cdd:cd07712 127 SIALLDRANRLLFSGDVVYDGPLIMDLPHSDlDDYLASLEKLSKLPDEFDkVLPG 181
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 124-245 4.92e-15

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: 72.18  E-value: 4.92e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 124 LTYILNTHHHDDHIGGNAELKERYGA------KVIGSAVDKDRIPGIDIL--LKDSDKWMFAGHEVRILDTPGHTQGHIS 195
Cdd:cd07722  57 ISDILLTHWHHDHVGGLPDVLDLLRGpsprvyKFPRPEEDEDPDEDGGDIhdLQDGQVFKVEGATLRVIHTPGHTTDHVC 136

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18406237 196 FYFPGSATIFTGDLIyslscgtLSEGT------PEQMlSSLQKIVSLPDDTnIYCG 245
Cdd:cd07722 137 FLLEEENALFTGDCV-------LGHGTavfedlAAYM-ASLKKLLSLGPGR-IYPG 183
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 90-243 4.45e-13

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 67.90  E-value: 4.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237   90 YAYLLHDedtgtvgVVDPSEAAPVIEALSRK-----------NWNLTYILNTHHHDDHIGGNAELKERY-GAKVIGSAVD 157
Cdd:PLN02962  24 YTYLLAD-------VSHPDKPALLIDPVDKTvdrdlslvkelGLKLIYAMNTHVHADHVTGTGLLKTKLpGVKSIISKAS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  158 KDRipgIDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYF------PGSATIFTGDLIYSLSCG--TLSEGTPEQMLSS 229
Cdd:PLN02962  97 GSK---ADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTgegpdqPQPRMAFTGDALLIRGCGrtDFQGGSSDQLYKS 173

                        170
                 ....*....|....*
gi 18406237  230 LQ-KIVSLPDDTNIY 243
Cdd:PLN02962 174 VHsQIFTLPKDTLIY 188
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 114-192 3.05e-11

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


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 62.50  E-value: 3.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 114 IEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDKDRIPG-----------------IDILLKDSDKWMF 176
Cdd:cd16309  51 IKKLGFDVKDVKYLLNTHAHFDHAGGLAELKKATGAQLVASAADKPLLESgyvgsgdtknlqfppvrVDRVIGDGDKVTL 130

                        90
                ....*....|....*.
gi 18406237 177 AGHEVRILDTPGHTQG 192
Cdd:cd16309 131 GGTTLTAHLTPGHSPG 146
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 91-237 8.83e-11

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: 59.90  E-value: 8.83e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  91 AYLLHDEDtGTVGVVDPSEAAPV---IEALSRknwnLTYILNTHHHD--DHiggnAELKERYGAKVIGSAVDKDRIPGID 165
Cdd:cd07727  17 SYLILRPE-GNILVDSPRYSPPLakrIEALGG----IRYIFLTHRDDvaDH----AKWAERFGAKRIIHEDDVNAVTRPD 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 166 --ILLKDSDKWMFAGhEVRILDTPGHTQGHISFYFPGSATIFTGD-LIYSLSCGTLSEGT-------PEQmLSSLQKIVS 235
Cdd:cd07727  88 evIVLWGGDPWELDP-DLTLIPVPGHTRGSVVLLYKEKGVLFTGDhLAWSRRRGWLSAFRyvcwyswPEQ-AESVERLAD 165


                ..
gi 18406237 236 LP 237
Cdd:cd07727 166 LD 167
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 98-204 1.70e-10

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: 60.41  E-value: 1.70e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  98 DTGtvgvvdPSEAAPVIEA----LSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDKDRIPG---------- 163
Cdd:cd16288  37 DTG------LESSAPMIKAnirkLGFKPSDIKILLNSHAHLDHAGGLAALKKLTGAKLMASAEDAALLASggksdfhygd 110

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18406237 164 ---------IDILLKDSDKWMFAGHEVRILDTPGHTQGHIS-------------FYFPGSATI 204
Cdd:cd16288 111 dslafppvkVDRVLKDGDRVTLGGTTLTAHLTPGHTRGCTTwtmtvkddgkvyqVVFADSLTV 173
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 90-236 2.45e-10

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: 59.92  E-value: 2.45e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  90 YAYLL-HDE-----DTG-------------TVGVVDPSEAAPVIEALSRKNWN---LTYILNTHHHDDHIGGNAELKery 147
Cdd:cd07729  33 YAYLIeHPEgtilvDTGfhpdaaddpggleLAFPPGVTEEQTLEEQLARLGLDpedIDYVILSHLHFDHAGGLDLFP--- 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 148 GAKVI-----------GSAVDKDRIPGIDIL--LKDSDKWMFAGHE------VRILDTPGHTQGHISFYF--PGSATIFT 206
Cdd:cd07729 110 NATIIvqraeleyatgPDPLAAGYYEDVLALddDLPGGRVRLVDGDydlfpgVTLIPTPGHTPGHQSVLVrlPEGTVLLA 189

                       170       180       190
                ....*....|....*....|....*....|....*
gi 18406237 207 GDLIY---SLSCGTLSE--GTPEQMLSSLQKIVSL 236
Cdd:cd07729 190 GDAAYtyeNLEEGRPPGinYDPEAALASLERLKAL 224
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 114-199 2.80e-10

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: 59.79  E-value: 2.80e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 114 IEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDKDRIPG-------------------IDILLKDSDKW 174
Cdd:cd16308  51 IQALGFKFKDIKILLTTQAHYDHVGAMAAIKQQTGAKMMVDEKDAKVLADggksdyemggygstfapvkADKLLHDGDTI 130

                        90       100
                ....*....|....*....|....*
gi 18406237 175 MFAGHEVRILDTPGHTQGHISFYFP 199
Cdd:cd16308 131 KLGGTKLTLLHHPGHTKGSCSFLFD 155
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 97-238 3.11e-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: 55.67  E-value: 3.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  97 EDTGTVGVVDPSEAA---PVIEALSRKNWNL---TYILNTHHHDDHIGgNAELKERygAKVI-GSAVDKDRipGIDILLK 169
Cdd:cd07711  28 KDGGKNILVDTGTPWdrdLLLKALAEHGLSPediDYVVLTHGHPDHIG-NLNLFPN--ATVIvGWDICGDS--YDDHSLE 102

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18406237 170 DSDKwMFAGHEVRILDTPGHTQGHISFYFPGSAT---IFTGDLI-------YSLSCGTLSEgTPEQMLSSLQKIVSLPD 238
Cdd:cd07711 103 EGDG-YEIDENVEVIPTPGHTPEDVSVLVETEKKgtvAVAGDLFereedleDPILWDPLSE-DPELQEESRKRILALAD 179
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 114-196 4.71e-09

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


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 56.01  E-value: 4.71e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 114 IEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDKDRIPG--------------------IDILLKDSDK 173
Cdd:cd07708  51 IKKLGFKFSDTKLILISHAHFDHAGGSAEIKKQTGAKVMAGAEDVSLLLSggssdfhyandsstyfpqstVDRAVHDGER 130

                        90       100
                ....*....|....*....|...
gi 18406237 174 WMFAGHEVRILDTPGHTQGHISF 196
Cdd:cd07708 131 VTLGGTVLTAHATPGHTPGCTTW 153
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 107-192 2.44e-08

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: 53.99  E-value: 2.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 107 PSEAAPVIE----ALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDK----------DRIPG--------I 164
Cdd:cd16310  40 LEENAALIEqnikALGFKLSDIKIIINTHAHYDHAGGLAQLKADTGAKLWASRGDRpaleagkhigDNITQpapfpavkV 119

                        90       100
                ....*....|....*....|....*...
gi 18406237 165 DILLKDSDKWMFAGHEVRILDTPGHTQG 192
Cdd:cd16310 120 DRILGDGEKIKLGDITLTATLTPGHTKG 147
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 125-211 3.22e-08

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: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 52.59  E-value: 3.22e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 125 TYILNTHHHDDHIGGNAELKERyGAKVIGSAVDKDRI--------PGIDILLKDSDKWMFAGheVRI-LDTPG--HTQGH 193
Cdd:cd16276  47 THVVYSHNHADHIGGASIFKDE-GATIIAHEATAELLkrnpdpkrPVPTVTFDDEYTLEVGG--QTLeLSYFGpnHGPGN 123

                        90
                ....*....|....*...
gi 18406237 194 ISFYFPGSATIFTGDLIY 211
Cdd:cd16276 124 IVIYLPKQKVLMAVDLIN 141
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 98-195 6.06e-08

Erythrobacter vulgaris EVM-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 EVM-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: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 52.74  E-value: 6.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  98 DTGTvgvvdpSEAAPV----IEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDK--------------- 158
Cdd:cd16315  37 DSGT------EEAAPLvlanIRKLGFDPKDVRWLLSSHEHFDHVGGLAALQRATGARVAASAAAApvlesgkpapddpqa 110

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 18406237 159 ---DRIPG--IDILLKDSDKWMFAGHEVRILDTPGHTQGHIS 195
Cdd:cd16315 111 glhEPFPPvrVDRIVEDGDTVALGSLRLTAHATPGHTPGALS 152
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 105-236 7.50e-08

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: 51.73  E-value: 7.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 105 VDP----SEAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERY-GAKVIGSA--VD-----------------KDR 160
Cdd:cd07739  30 VDAqftrADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAFpDAKVVATPavVAhikaqlepklafwgpllGGN 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 161 IPGIDILLK--DSDKWMFAGHEVRILDTPGHTQGHISF-YFPGSATIFTGDLIYSlscGT----LSEGTPEQM---LSSL 230
Cdd:cd07739 110 APARLVVPEplDGDTLTLEGHPLEIVGVGGGDTDDTTYlWIPSLKTVVAGDVVYN---GVhvwlADATTPELRaawLAAL 186


                ....*.
gi 18406237 231 QKIVSL 236
Cdd:cd07739 187 DKIEAL 192
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 ...
 109-195 2.37e-07

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: 51.19  E-value: 2.37e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 109 EAAPVIEA----LSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSA----------VDKD--------RIPGI-- 164
Cdd:cd16290  42 QSAPQIEAniraLGFRLEDVKLILNSHAHFDHAGGIAALQRDSGATVAASPagaaalrsggVDPDdpqagaadPFPPVak 121

                        90       100       110
                ....*....|....*....|....*....|.
gi 18406237 165 DILLKDSDKWMFAGHEVRILDTPGHTQGHIS 195
Cdd:cd16290 122 VRVVADGEVVKLGPLAVTAHATPGHTPGGTS 152
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 98-233 2.54e-07

metallo-beta-lactamases; subclasses B1 and B2 and related proteins; 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 B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B1 MBls include chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1. B2 MBLs have a narrow substrate profile that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis. B2 MBLs include Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I.


Pssm-ID: 293793 [Multi-domain]  Cd Length: 219  Bit Score: 50.62  E-value: 2.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  98 DTGTVGVVD----PSEAAPVIEALSRK-NWNLTYILNTHHHDDHIGGNAELKERyGAKVIGSAVDKD------------- 159
Cdd:cd07707  28 GSKGLVLVDstwtPKTTKELIKEIEKVsQKPVTEVINTHFHTDRAGGNAYLKER-GAKTVSTALTRDlaksewaeivaft 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 160 -----RIPGIDILLKDSD------------KWMFAGhevrildtPGHTQGHISFYFPGSATIFTGDLIYSLSCGTLSEGT 222
Cdd:cd07707 107 rkglpEYPDLGYELPDGVldgdfnlqfgkvEAFYPG--------PAHTPDNIVVYFPQENVLYGGCIIKETDLGNVADAD 178

                       170
                ....*....|.
gi 18406237 223 PEQMLSSLQKI 233
Cdd:cd07707 179 VKEWPTSIERL 189
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 107-239 5.53e-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: 49.86  E-value: 5.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 107 PSEAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAV----------DKD--------RIPGIDIL- 167
Cdd:cd16313  44 PEQIAASIRQLGFKLEDVKYILSSHDHWDHAGGIAALQKLTGAQVLASPAtvavlrsgsmGKDdpqfggltPMPPVASVr 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 168 -LKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGS-----ATIFTGDLIYSLSCGTLS-EGTPE---QMLSSLQKIVSLP 237
Cdd:cd16313 124 aVRDGEVVKLGPLAVTAHATPGHTTGGTSWTWQSCeqgrcANMVFADSLTAVSADGYRfSAHPAvlaDVEQSIAAVEKLA 203


                ..
gi 18406237 238 DD 239
Cdd:cd16313 204 CD 205
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 80-233 2.96e-06

Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; 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 MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293860  Cd Length: 212  Bit Score: 47.24  E-value: 2.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  80 IELVPCSKDNYAY--LLHDEDTGTVG-----VVDPSEAA----PVIEALSRK--NW-------NLTYILNTHHHDDHIGG 139
Cdd:cd16302   1 LEIIKLSDHVYVHvsYLETETFGKVPcngmiVINGGEAVvfdtPTNDSQSEEliDWienslkaKVKAVVPTHFHDDCLGG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 140 NAELKER----YG-AKVIGSAvDKDRIPGIDILLKDSDKWMFAGHEVRILDT-PGHTQGHISFYFPGSATIFTGDLIYSL 213
Cdd:cd16302  81 LKAFHRRgipsYAnQKTIALA-KEKGLPVPQHGFSDSLTLKLGGKKIVCRYFgEGHTKDNIVVYFPSEKVLFGGCMVKSL 159

                       170       180
                ....*....|....*....|..
gi 18406237 214 SC--GTLSEGTPEQMLSSLQKI 233
Cdd:cd16302 160 GAgkGNLEDANVEAWPKTVEKV 181
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 125-212 3.62e-06

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 47.13  E-value: 3.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 125 TYILNTHHHDDHIGGNAELKE----------RYgakVIG----------SAVDKDRIPGIDillkDS---------DKWM 175
Cdd:cd16277  65 DYVLCTHLHVDHVGWNTRLVDgrwvptfpnaRY---LFSraeydhwsspDAGGPPNRGVFE----DSvlpvieaglADLV 137

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 18406237 176 FAGHE----VRILDTPGHTQGHISFYF--PGSATIFTGDLIYS 212
Cdd:cd16277 138 DDDHEildgIRLEPTPGHTPGHVSVELesGGERALFTGDVMHH 180
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 109-239 1.06e-05

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: 46.13  E-value: 1.06e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 109 EAAPVI----EALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSA----VDKDRIPGIDILLKDSD-------- 172
Cdd:cd16312  42 QSAPLIianiEALGFRIEDVKLILNSHAHWDHAGGIAALQKASGATVAASAhgaqVLQSGTNGKDDPQYQAKpvvhvakv 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 173 ---KWMFAGHEVRILD-------TPGHTQGHISFYFPGSATIFTGDLIYSLSCGTLSEG---------TPEQMLS---SL 230
Cdd:cd16312 122 akvKEVGEGDTLKVGPlrltahmTPGHTPGGTTWTWTSCEGQRCLDVVYADSLNPYSSGdfyytgkggYPDISASfraSI 201


                ....*....
gi 18406237 231 QKIVSLPDD 239
Cdd:cd16312 202 AKVAALPCD 210
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 123-233 1.16e-05

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: 45.74  E-value: 1.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 123 NLTYILNTHHHDDHIGGNAELKERyGAKVIGSAVDKDR-----IPGIDILLKDSDKWMFAGHEVRIL-DTPGHTQGHISF 196
Cdd:cd16304  63 PVTLAIVTHAHDDRIGGIKALQKR-GIPVYSTKLTAQLakkqgYPSPDGILKDDTTLKFGNTKIETFyPGEGHTADNIVV 141

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 18406237 197 YFPGSATIFTGDLIYSL---SCGTLSEGTPEQMLSSLQKI 233
Cdd:cd16304 142 WLPQSKILFGGCLVKSLeakDLGNTADANLKEWPTSIRNV 181
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 126-208 1.57e-05

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


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 45.72  E-value: 1.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 126 YILNTHHHDDHIGG-----NAEL-----------KERYGAKVIGSAVDKDRIPGIDILLKDSDKWM-----FAGH----- 179
Cdd:cd07730  86 AVILSHLHWDHIGGlsdfpNARLivgpgakealrPPGYPSGFLPELLPSDFEGRLVRWEEDDFLWVplgpfPRALdlfgd 165

                        90       100       110
                ....*....|....*....|....*....|...
gi 18406237 180 -EVRILDTPGHTQGHISFYF---PGSATIFTGD 208
Cdd:cd07730 166 gSLYLVDLPGHAPGHLGLLArttSGTWVFLAGD 198
SoxH_rel_PQQ_2 TIGR04559
quinoprotein relay system zinc metallohydrolase 2; By homology, members are Zn ...
 102-211 2.83e-05

quinoprotein relay system zinc metallohydrolase 2; By homology, members are Zn metallohydrolases in the same family as the SoxH protein associated with sulfate metabolism, Bacillus cereus beta-lactamase II (see PDB:1bc2), and, more distantly, hydroxyacylglutathione hydrolase (glyoxalase II). All members occur in genomes with both PQQ biosynthesis and a PQQ-dependent (quinoprotein) dehydrogenase that has a motif of two consecutive Cys residues (see TIGR03075). The Cys-Cys motif is associated with electron transfer by specialized cytochromes such as c551. All these genomes also include a fusion protein (TIGR04557) whose domains resemble SoxY and SoxZ from thiosulfate oxidation. A conserved Cys in this fusion protein aligns to the Cys residue in SoxY that carries sulfur cycle intermediates. In many genomes, the genes for PQQ biosynthesis enzymes, PQQ-dependent enzymes, their associated cytochromes, and members of this family are clustered. Note that one to three closely related Zn metallohydrolases may occur; this family represents a specific clade among them. Some members of this family have a short additional N-terminal domain with four conserved Cys residues. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275352  Cd Length: 283  Bit Score: 44.88  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237   102 VGVVDPSEAAPVIEALSRKNWNLT-----YILNTHHHDDHIGGNAELKE-----------------------RYGAKVIG 153
Cdd:TIGR04559  41 VAVIDTGGSRAEGEALLAAIRQRTdlpirYVINTHVHPDHIFGNAAFREdgaefvghaklpralaargefylASFARLLG 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18406237   154 SAVDKDRIPGIDILLKDSDKWMFAGhevRILD----TPGHTQGHISFYFPGSATIFTGDLIY 211
Cdd:TIGR04559 121 EAFLGTEIVPPTRLVADPLELDLGG---RVLEltawPTAHTDNDLTVFDEKTGTLFTGDLLF 179
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 98-196 5.20e-05

Pseudomonas Aeruginosa AIM-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 AIM-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: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 44.11  E-value: 5.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  98 DTGTVgvvdpsEAAPVIEA----LSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGsavdkdRIPGIDIL---LKD 170
Cdd:cd16314  37 DGGTD------KAAPLIEAniraLGFRPEDVRYIVSSHEHFDHAGGIARLQRATGAPVVA------REPAATTLergRSD 104

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 18406237 171 SDKWMFAGHE--------VRILD---------------TPGHTQGHISF 196
Cdd:cd16314 105 RSDPQFLVVEkfppvasvQRIGDgevlrvgplaltahaTPGHTPGGTSW 153
NorV COG0426
Flavorubredoxin [Energy production and conversion];
91-209 9.32e-05

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 43.67  E-value: 9.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  91 AYLLHDE-----DTgtvgvVDPSEAAPVIEALSR----KNwnLTYILnTHHHD-DHIGGNAELKERY-GAKVIGSA---- 155
Cdd:COG0426  36 SYLIVDEktaliDT-----VGESFFEEFLENLSKvidpKK--IDYII-VNHQEpDHSGSLPELLELApNAKIVCSKkaar 107

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18406237 156 -------VDKDRIpgidILLKDSDKWMFAGHEVRILDTPG-HTQGHISFYFPGSATIFTGDL 209
Cdd:COG0426 108 flphfygIPDFRF----IVVKEGDTLDLGGHTLQFIPAPMlHWPDTMFTYDPEDKILFSGDA 165
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 123-196 1.01e-04

Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-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 L1- and Pom-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: 293847  Cd Length: 239  Bit Score: 42.88  E-value: 1.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 123 NLTYILNTHHHDDHIGGNAELKERYGAKVIG---SAVDKDRIPGIDILLKDS--------DKWMFAGHEVRILD------ 185
Cdd:cd16289  60 DLKLILHSHAHADHAGPLAALKRATGARVAAnaeSAVLLARGGSDDIHFGDGitfppvqaDRIVMDGEVVTLGGvtftah 139

                        90
                ....*....|..
gi 18406237 186 -TPGHTQGHISF 196
Cdd:cd16289 140 fTPGHTPGSTSW 151
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 97-155 1.54e-04

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 42.49  E-value: 1.54e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18406237   97 EDTGTVGVVDP----SEAAPViealSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSA 155
Cdd:PRK00685  14 ETGGKKILIDPfitgNPLADL----KPEDVKVDYILLTHGHGDHLGDTVEIAKRTGATVIANA 72
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 109-154 4.05e-04

Janthinobacterium lividum THIN-B2 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-B2-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: 293869  Cd Length: 257  Bit Score: 41.51  E-value: 4.05e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 18406237 109 EAAPVI----EALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGS 154
Cdd:cd16311  42 ESAPKIianiEALGFRIEDVKLILNSHGHIDHAGGLAELQRRSGALVAAS 91
Lactamase_B_5 pfam14597
Metallo-beta-lactamase superfamily; This is a small family of putative metal-dependent ...
 116-236 5.31e-04

Metallo-beta-lactamase superfamily; This is a small family of putative metal-dependent hydrolases.


Pssm-ID: 373150  Cd Length: 199  Bit Score: 40.60  E-value: 5.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237   116 ALSRKNWN-------LTYILNTHhhDDHIGGNAELKERYGAKVIGSAVDKDRIPgidILlkdSDKWMFAGHEV----RIL 184
Cdd:pfam14597  41 ALSNHDWNhleslggVAWIVLTN--SDHIRAAKEIAHQTYAKIAGPAGEKETFP---IA---CDRWLSDGDELvpglQVL 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 18406237   185 DTPG-HTQGHISFYFPGSaTIFTGDLIYSLSCGTLSEGTPEQMLSSLQKIVSL 236
Cdd:pfam14597 113 ELQGsKTPGELALLLEET-TLITGDLVRAPKAGSLTILPDEKLLNRAAAVASV 164
Sfh-1-like_MBL-B2 cd16305
Serratia fonticola Sfh-I and related metallo-beta-lactamases, subclass B2; MBL-fold ...
 87-238 9.25e-04

Serratia fonticola Sfh-I and related metallo-beta-lactamases, subclass B2; 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. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis.


Pssm-ID: 293863  Cd Length: 226  Bit Score: 39.98  E-value: 9.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237  87 KDNYAYLLHDEDTGTVGVVDPSEAAPVIEALSRKNWNLTY--ILNTHHHDDHIGGNAELKErYGAKVI------------ 152
Cdd:cd16305  20 QENSMVYIGTDGITIIGATWTPETAETLEKEIRKVSPLPIkeVINTNYHTDRAGGNAYWKT-LGASIVstqmtydleksq 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 153 -GSAVD-----KDRIPGIDILLKDS----DKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFtGDLIYSLSCGTLSEGT 222
Cdd:cd16305  99 wGSIVDftrqgNNKYPNLEKSLPDTvypgDFNLQNGSVRALYLGEAHTEDGIFVYFPAERVLY-GNCILKEKLGNMSFAN 177

                       170
                ....*....|....*.
gi 18406237 223 PEQMLSSLQKIVSLPD 238
Cdd:cd16305 178 RTEYPKTLKKLKGLIE 193
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 124-209 2.89e-03

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 37.88  E-value: 2.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 124 LTYILNTHHHDDHIGGNAELKERY-GAKVIGSAVDKDRIPGIDIL------------LKDSDKWMFAGHEVRILDTPGHT 190
Cdd:cd07731  49 LDYLILTHPDADHIGGLDAVLKNFpVKEVYMPGVTHTTKTYEDLLdaikekgipvtpCKAGDRWQLGGVSFEVLSPPKDD 128

                        90       100       110
                ....*....|....*....|....*....|...
gi 18406237 191 Q--------------GHISFyfpgsatIFTGDL 209
Cdd:cd07731 129 YddlnnnscvlrltyGGTSF-------LLTGDA 154
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 112-192 4.25e-03

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


Pssm-ID: 293865  Cd Length: 255  Bit Score: 38.20  E-value: 4.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18406237 112 PVIEALSRK---NWNLTYI-LNTHHHDDHIGGNAELKERYGAK---------VIGSAVDKDRIPG-----------IDIL 167
Cdd:cd16307  45 PQIKASIEKlgfKFSDTKIlLISHAHFDHAAGSALIKRETHAKymvmdgdvdVVESGGKSDFFYGndpstyfppahVDKV 124

                        90       100
                ....*....|....*....|....*
gi 18406237 168 LKDSDKWMFAGHEVRILDTPGHTQG 192
Cdd:cd16307 125 LHDGEQVELGGTVLTAHLTAGHTKG 149
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 98-152 5.31e-03

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 37.91  E-value: 5.31e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18406237  98 DTGTVGVVDPSEAApVIEALSRKN-WNLTYILNTHHHDDHIGGNAELKERYGAKVI 152
Cdd:COG2333  27 DTGPRPSFDAGERV-VLPYLRALGiRRLDLLVLTHPDADHIGGLAAVLEAFPVGRV 81
 
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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