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Conserved domains on  [gi|50510835|dbj|BAD32403|]
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mKIAA1184 protein, partial [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GSH_gloB super family cl30131
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 124-383 1.20e-93

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]


The actual alignment was detected with superfamily member TIGR03413:

Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 280.58  E-value: 1.20e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835   124 VLPIPVLSDNYSYLIIDTQaGLAVAVDPSDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQDG 203
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPD-GQAAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAEL-LEAFPAPVYGPAEER 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835   204 IPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTFEGTAETMLSSLDTVLD 283
Cdd:TIGR03413  79 IPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPA-----LFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835   284 LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRMERKSTCPSTLGEERAYNPFLRTHCLELQEALGPgpgp 363
Cdd:TIGR03413 154 LPDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAALGS---- 229

                         250       260
                  ....*....|....*....|
gi 50510835   364 tsdDGCSRAQLLEELRRLKD 383
Cdd:TIGR03413 230 ---QGADPVEVFAALRAWKD 246
 
Name Accession Description Interval E-value
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 124-383 1.20e-93

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: 280.58  E-value: 1.20e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835   124 VLPIPVLSDNYSYLIIDTQaGLAVAVDPSDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQDG 203
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPD-GQAAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAEL-LEAFPAPVYGPAEER 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835   204 IPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTFEGTAETMLSSLDTVLD 283
Cdd:TIGR03413  79 IPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPA-----LFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835   284 LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRMERKSTCPSTLGEERAYNPFLRTHCLELQEALGPgpgp 363
Cdd:TIGR03413 154 LPDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAALGS---- 229

                         250       260
                  ....*....|....*....|
gi 50510835   364 tsdDGCSRAQLLEELRRLKD 383
Cdd:TIGR03413 230 ---QGADPVEVFAALRAWKD 246
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 126-294 8.42e-88

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: 262.78  E-value: 8.42e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 126 PIPVLSDNYSYLIIDTQAGLAVAVDPSDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQDGIP 205
Cdd:cd07723   2 PIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAEDRIP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 206 YLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGDLLFLSGCGRTFEGTAETMLSSLDTVLDLG 285
Cdd:cd07723  82 GLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEP-----ALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLALP 156


                ....*....
gi 50510835 286 DDTLLWPGH 294
Cdd:cd07723 157 DDTLVYCGH 165
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 123-383 4.86e-86

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 261.62  E-value: 4.86e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835  123 KVLPIPVLSDNYSYLIIDTQAGLAVAVDPSDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQD 202
Cdd:PLN02469   2 KIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835  203 GIPYLTHPLCHQDVVSVGR-LQIRALATPGHTQGHLVYLLDGEPYKGPScLFSGDLLFLSGCGRTFEGTAETMLSSLDTV 281
Cdd:PLN02469  82 NVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDPA-VFTGDTLFIAGCGKFFEGTAEQMYQSLCVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835  282 L-DLGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRMERKSTCPSTLGEERAYNPFLRTHCLELQEALgpg 360
Cdd:PLN02469 161 LgSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKV--- 237

                        250       260
                 ....*....|....*....|....
gi 50510835  361 pgptsddGC-SRAQLLEELRRLKD 383
Cdd:PLN02469 238 -------GCeSPVEALREVRKMKD 254
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 128-346 5.98e-39

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: 138.67  E-value: 5.98e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 128 PVLSDNYSYLIIDTqaGLAVAVDP----SDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQDg 203
Cdd:COG0491  10 GAGLGVNSYLIVGG--DGAVLIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAAL-AEAFGAPVYAHAAE- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 204 IPYLT----------------HPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRT- 266
Cdd:COG0491  86 AEALEapaagalfgrepvppdRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKV-----LFTGDALFSGGVGRPd 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 267 -FEGTAETMLSSLDTVLDLGDDtLLWPGHEYAeenlgfagvvepenlarerkmqwVQRQRMERKSTCPSTLGEERayNPF 345
Cdd:COG0491 161 lPDGDLAQWLASLERLLALPPD-LVIPGHGPP-----------------------TTAEAIDYLEELLAALGERA--NPF 214


                .
gi 50510835 346 L 346
Cdd:COG0491 215 L 215
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 134-294 1.81e-28

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: 109.57  E-value: 1.81e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835    134 YSYLIIDTqaGLAVAVDP--SDPRAVQASIEKERV-NLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQD-------- 202
Cdd:smart00849   1 NSYLVRDD--GGAILIDTgpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAP-GAPVYAPEGTaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835    203 ----------GIPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpSCLFSGDLLFLSGCGRTF-EGTA 271
Cdd:smart00849  78 allgelgaeaEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEG-----KILFTGDLLFAGGDGRTLvDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 50510835    272 ETMLSSLDTVLDL--GDDTLLWPGH 294
Cdd:smart00849 153 AAASDALESLLKLlkLLPKLVVPGH 177
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 295-383 1.03e-27

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: 104.44  E-value: 1.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835   295 EYAEENLGFAGVVEPENLARERKMQWVQRQRMERKSTCPSTLGEERAYNPFLRTHCLELQEALGpgpgptsddGCSRAQL 374
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATG---------ETDPVEV 71


                  ....*....
gi 50510835   375 LEELRRLKD 383
Cdd:pfam16123  72 FAALRELKD 80
 
Name Accession Description Interval E-value
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 124-383 1.20e-93

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: 280.58  E-value: 1.20e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835   124 VLPIPVLSDNYSYLIIDTQaGLAVAVDPSDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQDG 203
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPD-GQAAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAEL-LEAFPAPVYGPAEER 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835   204 IPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTFEGTAETMLSSLDTVLD 283
Cdd:TIGR03413  79 IPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPA-----LFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835   284 LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRMERKSTCPSTLGEERAYNPFLRTHCLELQEALGPgpgp 363
Cdd:TIGR03413 154 LPDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAALGS---- 229

                         250       260
                  ....*....|....*....|
gi 50510835   364 tsdDGCSRAQLLEELRRLKD 383
Cdd:TIGR03413 230 ---QGADPVEVFAALRAWKD 246
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 126-294 8.42e-88

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: 262.78  E-value: 8.42e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 126 PIPVLSDNYSYLIIDTQAGLAVAVDPSDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQDGIP 205
Cdd:cd07723   2 PIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAEDRIP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 206 YLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGDLLFLSGCGRTFEGTAETMLSSLDTVLDLG 285
Cdd:cd07723  82 GLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEP-----ALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLALP 156


                ....*....
gi 50510835 286 DDTLLWPGH 294
Cdd:cd07723 157 DDTLVYCGH 165
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 123-383 4.86e-86

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 261.62  E-value: 4.86e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835  123 KVLPIPVLSDNYSYLIIDTQAGLAVAVDPSDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQD 202
Cdd:PLN02469   2 KIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835  203 GIPYLTHPLCHQDVVSVGR-LQIRALATPGHTQGHLVYLLDGEPYKGPScLFSGDLLFLSGCGRTFEGTAETMLSSLDTV 281
Cdd:PLN02469  82 NVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDPA-VFTGDTLFIAGCGKFFEGTAEQMYQSLCVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835  282 L-DLGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRMERKSTCPSTLGEERAYNPFLRTHCLELQEALgpg 360
Cdd:PLN02469 161 LgSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKV--- 237

                        250       260
                 ....*....|....*....|....
gi 50510835  361 pgptsddGC-SRAQLLEELRRLKD 383
Cdd:PLN02469 238 -------GCeSPVEALREVRKMKD 254
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 127-383 2.01e-52

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 177.34  E-value: 2.01e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835  127 IPVLSDNYSYLIIDTQAGLAVAVDPSDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSP--QDGI 204
Cdd:PLN02398  81 VPCLKDNYAYLLHDEDTGTVGVVDPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARY-GAKVIGSAvdKDRI 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835  205 PYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLldgepYKGPSCLFSGDLLFLSGCGRTFEGTAETMLSSLDTVLDL 284
Cdd:PLN02398 160 PGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFY-----FPGSGAIFTGDTLFSLSCGKLFEGTPEQMLSSLQKIISL 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835  285 GDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRMERKSTCPSTLGEERAYNPFLRTHCLELQEALG-PGpgp 363
Cdd:PLN02398 235 PDDTNIYCGHEYTLSNSKFALSIEPNNEVLQSYAAHVAHLRSKGLPTIPTTVKMEKACNPFLRTSSTDIRKSLSiPD--- 311

                        250       260
                 ....*....|....*....|
gi 50510835  364 TSDDgcsrAQLLEELRRLKD 383
Cdd:PLN02398 312 TADE----AEALGIIRRAKD 327
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 132-294 1.09e-43

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: 149.61  E-value: 1.09e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 132 DNYSYLIIDTQAGLAVAVDPS-DPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDgIPYLT-- 208
Cdd:cd16275  11 INYSYIIIDKATREAAVVDPAwDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKY-DAPVYMSKEE-IDYYGfr 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 209 ----HPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGepykgpsCLFSGDLLFLSGCGRT--FEGTAETMLSSLDTVL 282
Cdd:cd16275  89 cpnlIPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGD-------SLFTGDTLFIEGCGRCdlPGGDPEEMYESLQRLK 161

                       170
                ....*....|...
gi 50510835 283 DL-GDDTLLWPGH 294
Cdd:cd16275 162 KLpPPNTRVYPGH 174
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 127-353 2.26e-43

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 151.52  E-value: 2.26e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835  127 IPVLSDNYSYLIIDtQAGLAVAVDPSDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQDGIPY 206
Cdd:PRK10241   6 IPAFDDNYIWVLND-EAGRCLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQETQDKG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835  207 LTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLldGEPYkgpscLFSGDLLFLSGCGRTFEGTAETMLSSLDTVLDLGD 286
Cdd:PRK10241  85 TTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF--SKPY-----LFCGDTLFSGGCGRLFEGTASQMYQSLKKINALPD 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50510835  287 DTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRMERKSTCPSTLGEERAYNPFLRTHCLEL 353
Cdd:PRK10241 158 DTLICCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINLFLRTEDIDL 224
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 134-296 5.39e-40

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: 139.84  E-value: 5.39e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 134 YSYLIIDTQAGLAVAVDPSDPRA--VQASIEKERVNLVAILCTHKHWDH-SGGnRDLSRRHrDCRVYGSPQDGIPYLTHP 210
Cdd:cd07724  13 LSYLVGDPETGEAAVIDPVRDSVdrYLDLAAELGLKITYVLETHVHADHvSGA-RELAERT-GAPIVIGEGAPASFFDRL 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 211 LCHQDVVSVGRLQIRALATPGHTQGHLVYLLDgepykGPSCLFSGDLLFLSGCGRT-----FEGTAETMLSSL-DTVLDL 284
Cdd:cd07724  91 LKDGDVLELGNLTLEVLHTPGHTPESVSYLVG-----DPDAVFTGDTLFVGDVGRPdlpgeAEGLARQLYDSLqRKLLLL 165

                       170
                ....*....|..
gi 50510835 285 GDDTLLWPGHEY 296
Cdd:cd07724 166 PDETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 128-346 5.98e-39

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: 138.67  E-value: 5.98e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 128 PVLSDNYSYLIIDTqaGLAVAVDP----SDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQDg 203
Cdd:COG0491  10 GAGLGVNSYLIVGG--DGAVLIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAAL-AEAFGAPVYAHAAE- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 204 IPYLT----------------HPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRT- 266
Cdd:COG0491  86 AEALEapaagalfgrepvppdRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKV-----LFTGDALFSGGVGRPd 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 267 -FEGTAETMLSSLDTVLDLGDDtLLWPGHEYAeenlgfagvvepenlarerkmqwVQRQRMERKSTCPSTLGEERayNPF 345
Cdd:COG0491 161 lPDGDLAQWLASLERLLALPPD-LVIPGHGPP-----------------------TTAEAIDYLEELLAALGERA--NPF 214


                .
gi 50510835 346 L 346
Cdd:COG0491 215 L 215
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 123-294 3.01e-34

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 125.09  E-value: 3.01e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 123 KVLPIPVLSDNySYLIIDtQAGLAVAVDPSDP--RAVQASIEKERVNLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSP 200
Cdd:cd06262   1 KRLPVGPLQTN-CYLVSD-EEGEAILIDPGAGalEKILEAIEELGLKIKAILLTHGHFDHIGGLAEL-KEAPGAPVYIHE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 201 QDgIPYLTHPLCHQ--------------------DVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGDLLFL 260
Cdd:cd06262  78 AD-AELLEDPELNLaffgggplpppepdilledgDTIELGGLELEVIHTPGHTPGSVCFYIEEEG-----VLFTGDTLFA 151

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 50510835 261 SGCGRT--FEGTAETMLSSLDTVLD-LGDDTLLWPGH 294
Cdd:cd06262 152 GSIGRTdlPGGDPEQLIESIKKLLLlLPDDTVVYPGH 188
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 122-346 3.48e-34

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: 125.54  E-value: 3.48e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 122 VKVLPIPVLSDNySYLIIDTQAGLAVAVDPSDPR-AVQASIEKERVNLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSP 200
Cdd:cd16322   1 VRPFTLGPLQEN-TYLVADEGGGEAVLVDPGDESeKLLARFGTTGLTLLYILLTHAHFDHVGGVADL-RRHPGAPVYLHP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 201 QD----------------GIPYLT---HPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpSCLFSGDLLFLS 261
Cdd:cd16322  79 DDlplyeaadlgakafglGIEPLPppdRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEE-----GLLFSGDLLFQG 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 262 GCGRT-FEGTA-ETMLSSLDTVLDLGDDTLLWPGHeyaeenlgfagvvepenlarerkmqwvqrqrMErkstcPSTLGEE 339
Cdd:cd16322 154 SIGRTdLPGGDpKAMAASLRRLLTLPDETRVFPGH-------------------------------GP-----PTTLGEE 197


                ....*..
gi 50510835 340 RAYNPFL 346
Cdd:cd16322 198 RRTNPFL 204
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 134-294 1.81e-28

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: 109.57  E-value: 1.81e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835    134 YSYLIIDTqaGLAVAVDP--SDPRAVQASIEKERV-NLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQD-------- 202
Cdd:smart00849   1 NSYLVRDD--GGAILIDTgpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAP-GAPVYAPEGTaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835    203 ----------GIPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpSCLFSGDLLFLSGCGRTF-EGTA 271
Cdd:smart00849  78 allgelgaeaEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEG-----KILFTGDLLFAGGDGRTLvDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 50510835    272 ETMLSSLDTVLDL--GDDTLLWPGH 294
Cdd:smart00849 153 AAASDALESLLKLlkLLPKLVVPGH 177
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 295-383 1.03e-27

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: 104.44  E-value: 1.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835   295 EYAEENLGFAGVVEPENLARERKMQWVQRQRMERKSTCPSTLGEERAYNPFLRTHCLELQEALGpgpgptsddGCSRAQL 374
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATG---------ETDPVEV 71


                  ....*....
gi 50510835   375 LEELRRLKD 383
Cdd:pfam16123  72 FAALRELKD 80
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 135-294 4.48e-25

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: 100.64  E-value: 4.48e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 135 SYlIIDTQAGLAVaVDP--SDP---RAVQASIEKERVnlVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDGIPYL-- 207
Cdd:cd16278  20 TY-LLGAPDGVVV-IDPgpDDPahlDALLAALGGGRV--SAILVTHTHRDHSPGAARLAERT-GAPVRAFGPHRAGGQdt 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 208 ----THPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGDLLFlsGCGRTF----EGTAETMLSSLD 279
Cdd:cd16278  95 dfapDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEG-----ALFTGDHVM--GWSTTViappDGDLGDYLASLE 167

                       170
                ....*....|....*
gi 50510835 280 TVLDLgDDTLLWPGH 294
Cdd:cd16278 168 RLLAL-DDRLLLPGH 181
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 127-294 1.81e-23

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


Pssm-ID: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 96.47  E-value: 1.81e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 127 IPV--LSDNySYLIIDTQAGLAVAVDP-SDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQD- 202
Cdd:cd07737   4 IPVtpFQQN-CSLIWCEETKEAAVIDPgGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAEL-AEHYGVPIIGPHKEd 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 203 --------------GIPYL-----THPLCHQDVVSVGRLQIRALATPGHTQGHLVYLldGEPYKgpsCLFSGDLLFLSGC 263
Cdd:cd07737  82 kfllenlpeqsqmfGFPPAeaftpDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFF--NRESK---LAIVGDVLFKGSI 156

                       170       180       190
                ....*....|....*....|....*....|....
gi 50510835 264 GRT-F-EGTAETMLSSL-DTVLDLGDDTLLWPGH 294
Cdd:cd07737 157 GRTdFpGGNHAQLIASIkEKLLPLGDDVTFIPGH 190
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 135-294 2.87e-18

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 81.81  E-value: 2.87e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 135 SYLIIDTQAGLaVAVDPSDPRAVQASIEKErvnLVAILCTHKHWDHSGGNRDLSRRHRD--CRVYGSP---------QDG 203
Cdd:cd07722  28 RRILIDTGEGR-PSYIPLLKSVLDSEGNAT---ISDILLTHWHHDHVGGLPDVLDLLRGpsPRVYKFPrpeededpdEDG 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 204 IPYltHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGD-LLflsGCGRT-FEGTAETMlSSLDTV 281
Cdd:cd07722 104 GDI--HDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEEN-----ALFTGDcVL---GHGTAvFEDLAAYM-ASLKKL 172

                       170
                ....*....|...
gi 50510835 282 LDLGDDTlLWPGH 294
Cdd:cd07722 173 LSLGPGR-IYPGH 184
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 122-294 6.86e-17

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: 78.11  E-value: 6.86e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 122 VKVLPIPVLSDNYSYLIIDTqaGLAVavdPSDPRAVQASIEKERVNLVAI---LCTHKHWDHSGGNRDLSRRhRDCRVYG 198
Cdd:cd07725  12 LGHVNVYLLRDGDETTLIDT--GLAT---EEDAEALWEGLKELGLKPSDIdrvLLTHHHPDHIGLAGKLQEK-SGATVYI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 199 SPqdgipylTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpSCLFSGD--LLFLSGCG----RTFEGTAE 272
Cdd:cd07725  86 LD-------VTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDR-----RELFVGDavLPKITPNVslwaVRVEDPLG 153

                       170       180
                ....*....|....*....|..
gi 50510835 273 TMLSSLDTVLDLGDDtLLWPGH 294
Cdd:cd07725 154 AYLESLDKLEKLDVD-LAYPGH 174
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 131-346 3.80e-16

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 77.53  E-value: 3.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835  131 SDNYSYLIIDTQ--AGLAVAVDPSDpRAVQ---ASIEKERVNLVAILCTHKHWDHSGG-----NRDLSRRHRDCRVYGSP 200
Cdd:PLN02962  21 SSTYTYLLADVShpDKPALLIDPVD-KTVDrdlSLVKELGLKLIYAMNTHVHADHVTGtgllkTKLPGVKSIISKASGSK 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835  201 QDgipyltHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLL-DGEPYKGPSCLFSGDLLFLSGCGRT-FE-GTAETMLSS 277
Cdd:PLN02962 100 AD------LFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTgEGPDQPQPRMAFTGDALLIRGCGRTdFQgGSSDQLYKS 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835  278 LDT-VLDLGDDTLLWPGHEYaeenlgfagvvepenlarerkmqwvqrqrmerKSTCPSTLGEERAYNPFL 346
Cdd:PLN02962 174 VHSqIFTLPKDTLIYPAHDY--------------------------------KGFTVSTVGEEMLYNPRL 211
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
134-294 3.54e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 70.48  E-value: 3.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835   134 YSYLIIDTqaGLAVAVDP--SDPRAVQASIEKERVN---LVAILCTHKHWDHSGGNRDLSRRHRDCRVYGS--------- 199
Cdd:pfam00753   7 NSYLIEGG--GGAVLIDTggSAEAALLLLLAALGLGpkdIDAVILTHGHFDHIGGLGELAEATDVPVIVVAeearellde 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835   200 -------------PQDGIPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLldgepYKGPSCLFSGDLLFLSGCGRT 266
Cdd:pfam00753  85 elglaasrlglpgPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVY-----YGGGKVLFTGDLLFAGEIGRL 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 50510835   267 ----------FEGTAETMLSSLDTVLDLgDDTLLWPGH 294
Cdd:pfam00753 160 dlplggllvlHPSSAESSLESLLKLAKL-KAAVIVPGH 196
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 121-294 2.70e-13

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: 68.02  E-value: 2.70e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 121 GVKVLPIPVLSdnYSYLI--------IDTqaGLavavdPSDPRAVQASIEKERVN---LVAILCTHKHWDHSGGNRDLsR 189
Cdd:cd07721   1 GVYQLPLLPPV--NAYLIedddgltlIDT--GL-----PGSAKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAAL-K 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 190 RHRDCRVYGSPQDgIPYLTH---PLCHQDVVSVGRLQ-------------------------IRALATPGHTQGHLVYLL 241
Cdd:cd07721  71 EAPGAPVYAHERE-APYLEGekpYPPPVRLGLLGLLSpllpvkpvpvdrtledgdtldlaggLRVIHTPGHTPGHISLYL 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 50510835 242 DGEpykgpSCLFSGDLLFLSGcGRTFEGTA------ETMLSSLDTVLDLGDDTLLwPGH 294
Cdd:cd07721 150 EED-----GVLIAGDALVTVG-GELVPPPPpftwdmEEALESLRKLAELDPEVLA-PGH 201
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 137-294 4.92e-13

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 67.59  E-value: 4.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 137 LIIDTQAGLAVAvdpsdpRAVQASIEK---ERVNLVAIlcTHKHWDHSGGN-----------------RDLSRRHRDCRV 196
Cdd:cd16282  27 VVIDTGASPRLA------RALLAAIRKvtdKPVRYVVN--THYHGDHTLGNaafadagapiiahentrEELAARGEAYLE 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 197 YGSPQDG-------IPYLTHPLCHQDVVSVGRLQIRALAT-PGHTQGHLVYLLDGEpykgpSCLFSGDLLFLSGCGRTFE 268
Cdd:cd16282  99 LMRRLGGdamagteLVLPDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEE-----GVLFAGDLVFNGRIPFLPD 173

                       170       180
                ....*....|....*....|....*.
gi 50510835 269 GTAETMLSSLDTVLDLGDDTLLwPGH 294
Cdd:cd16282 174 GSLAGWIAALDRLLALDATVVV-PGH 198
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 129-294 7.80e-13

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 66.79  E-value: 7.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 129 VLSDNYSYLIIDTqaGLavavDPSDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQDgIPYLT 208
Cdd:cd07743  13 YVFGDKEALLIDS--GL----DEDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYL-QKKTGCKVYAPKIE-KAFIE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 209 HPL------------------------------CHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpsCLFSGDLL 258
Cdd:cd07743  85 NPLlepsylggayppkelrnkflmakpskvddiIEEGELELGGVGLEIIPLPGHSFGQIGILTPDG------VLFAGDAL 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 50510835 259 FlsgcgrtfegTAETM--------------LSSLDTVLDLGDDTLLwPGH 294
Cdd:cd07743 159 F----------GEEVLekygipflydveeqLETLEKLEELDADYYV-PGH 197
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 100-295 1.04e-11

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: 64.16  E-value: 1.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 100 LRRARNRYPKGHSKTQPRLFNGVKVLPIpvlsdnYSYLI--------IDTqaGL--AVAVDPSDPRAVQASIEKERVNLV 169
Cdd:cd07729   5 LDYGTVTVDKSSLFYYGRGPGEPIDLPV------YAYLIehpegtilVDT--GFhpDAADDPGGLELAFPPGVTEEQTLE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 170 AIL--------------CTHKHWDHSGGNRDL-------SRR-----HRDCRVYGSPQDGIPYLTHPLCHQDVVSV-GRL 222
Cdd:cd07729  77 EQLarlgldpedidyviLSHLHFDHAGGLDLFpnatiivQRAeleyaTGPDPLAAGYYEDVLALDDDLPGGRVRLVdGDY 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 223 Q----IRALATPGHTQGHLVYLLDGEpyKGPsCLFSGDL-----LFLSGCGRTFEGTAETMLSSLDTVLDL--GDDTLLW 291
Cdd:cd07729 157 DlfpgVTLIPTPGHTPGHQSVLVRLP--EGT-VLLAGDAaytyeNLEEGRPPGINYDPEAALASLERLKALaeREGARVI 233


                ....
gi 50510835 292 PGHE 295
Cdd:cd07729 234 PGHD 237
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 137-294 2.57e-09

uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 56.10  E-value: 2.57e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 137 LIIDTQAGLAvavdpSDPRAVQASIEKErvnLVAILcTHKHWDHSGGN----------RDLSRRHRDCRVYGSPQDGIPY 206
Cdd:cd07712  21 LLIDTGLGIG-----DLKEYVRTLTDLP---LLVVA-THGHFDHIGGLhefeevyvhpADAEILAAPDNFETLTWDAATY 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 207 ------LTHPLCHQDVVSVGRLQIRALATPGHTQGHLVyLLDgepyKGPSCLFSGDL-----LFLSGCGRTFegtaETML 275
Cdd:cd07712  92 svppagPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIA-LLD----RANRLLFSGDVvydgpLIMDLPHSDL----DDYL 162

                       170       180
                ....*....|....*....|
gi 50510835 276 SSLDTVLDLGDD-TLLWPGH 294
Cdd:cd07712 163 ASLEKLSKLPDEfDKVLPGH 182
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 135-294 3.42e-09

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 56.35  E-value: 3.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 135 SYLIiDTQAGLAVaVDP----SDPRAVQASIEK--ERVNLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQdGIPYLT 208
Cdd:cd07726  18 SYLL-DGEGRPAL-IDTgpssSVPRLLAALEALgiAPEDVDYIILTHIHLDHAGGAGLLAEALPNAKVYVHPR-GARHLI 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 209 HP--------------------------------LCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpSCLFSGD 256
Cdd:cd07726  95 DPsklwasaravygdeadrlggeilpvpeervivLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEES-----DGLFTGD 169

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 50510835 257 LLFLSGCGRTFEGTAET---------MLSSLDTVLDLGDDTLLwPGH 294
Cdd:cd07726 170 AAGVRYPELDVVGPPSTpppdfdpeaWLESLDRLLSLKPERIY-LTH 215
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 135-235 3.85e-06

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


Pssm-ID: 293868  Cd Length: 252  Bit Score: 47.83  E-value: 3.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 135 SYLIIDTQAGLAVAVDPSDPRA-VQASIEKERVNLV---AILCTHKHWDHSGGnrdLSRRHRD--CRVYGSPQD------ 202
Cdd:cd16310  24 SYLITSNHGAILLDGGLEENAAlIEQNIKALGFKLSdikIIINTHAHYDHAGG---LAQLKADtgAKLWASRGDrpalea 100

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 50510835 203 ----------GIPY----LTHPLCHQDVVSVGRLQIRALATPGHTQG 235
Cdd:cd16310 101 gkhigdnitqPAPFpavkVDRILGDGEKIKLGDITLTATLTPGHTKG 147
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 138-246 6.92e-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: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 46.81  E-value: 6.92e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 138 IIDTQAGLAV--AVDPSDPRAV-QASIEKERVN---LVAILCTHKHWDHSGGNRDLsRRHRDCRVYGS----------PQ 201
Cdd:cd16280  26 AIDTGDGLILidALNNNEAADLiVDGLEKLGLDpadIKYILITHGHGDHYGGAAYL-KDLYGAKVVMSeadwdmmeepPE 104

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 50510835 202 DGIPYLTHPLCHQDVV-------SVGRLQIRALATPGHTQGHLVYLLD----GEPY 246
Cdd:cd16280 105 EGDNPRWGPPPERDIVikdgdtlTLGDTTITVYLTPGHTPGTLSLIFPvkdgGKTH 160
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 224-261 1.22e-04

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


Pssm-ID: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 42.57  E-value: 1.22e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 50510835 224 IRALATPGHTQGHLVYLldgepYKGPSCLFSGDLLFLS 261
Cdd:cd07727 104 LTLIPVPGHTRGSVVLL-----YKEKGVLFTGDHLAWS 136
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 151-235 1.39e-04

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: 43.05  E-value: 1.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 151 PSDPRAVQASIEK-----ERVNLvaILCTHKHWDHSGGNRDLsRRHRDCRVYGSP------QDGIP------YLTHPLCH 213
Cdd:cd16312  41 PQSAPLIIANIEAlgfriEDVKL--ILNSHAHWDHAGGIAAL-QKASGATVAASAhgaqvlQSGTNgkddpqYQAKPVVH 117

                        90       100       110
                ....*....|....*....|....*....|....
gi 50510835 214 ------------QDVVSVGRLQIRALATPGHTQG 235
Cdd:cd16312 118 vakvakvkevgeGDTLKVGPLRLTAHMTPGHTPG 151
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 224-259 1.48e-04

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 42.92  E-value: 1.48e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 50510835 224 IRALATPGHTQGHLVYLLDGepyKGPSCLFSGDLLF 259
Cdd:cd07720 175 ITAVPAPGHTPGHTGYRIES---GGERLLIWGDIVH 207
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 171-257 1.67e-04

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 42.19  E-value: 1.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 171 ILCTHKHWDHSGGNRDLSR-RHrdcrVYGSPQDGIPYLTHPLCHQDVVSVGrLQIRALATPGHTQGHLVYLLDGEPYKgp 249
Cdd:cd07711  64 VVLTHGHPDHIGNLNLFPNaTV----IVGWDICGDSYDDHSLEEGDGYEID-ENVEVIPTPGHTPEDVSVLVETEKKG-- 136


                ....*...
gi 50510835 250 SCLFSGDL 257
Cdd:cd07711 137 TVAVAGDL 144
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
170-256 1.70e-04

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 42.87  E-value: 1.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 170 AILCTHKHWDHSGG------NRDLSRRHRDCRVYGsPQDGIPYLT----------------HPLCHQDVVSVGRLQIRAL 227
Cdd:COG1234  55 AIFITHLHGDHIAGlpgllsTRSLAGREKPLTIYG-PPGTKEFLEallkasgtdldfplefHEIEPGEVFEIGGFTVTAF 133

                        90       100
                ....*....|....*....|....*....
gi 50510835 228 ATPgHTQGHLVYLLDgepYKGPSCLFSGD 256
Cdd:COG1234 134 PLD-HPVPAYGYRFE---EPGRSLVYSGD 158
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 135-235 2.69e-04

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: 42.31  E-value: 2.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 135 SYLIiDTQAGLaVAVDPSDPRAV---QASIEK---ERVNLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQD------ 202
Cdd:cd16288  24 SYLI-TTPQGL-ILIDTGLESSApmiKANIRKlgfKPSDIKILLNSHAHLDHAGGLAAL-KKLTGAKLMASAEDaallas 100

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 50510835 203 --------GIPYLTHP-------LCHQDVVSVGRLQIRALATPGHTQG 235
Cdd:cd16288 101 ggksdfhyGDDSLAFPpvkvdrvLKDGDRVTLGGTTLTAHLTPGHTRG 148
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 164-258 4.47e-04

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 41.35  E-value: 4.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 164 ERVNLVaiLCTHKHWDHSGGN---------------------RDLSRRHRDCRVYGSPQDGIPYLTHPlchqdVVSVGRL 222
Cdd:cd16277  62 EDVDYV--LCTHLHVDHVGWNtrlvdgrwvptfpnarylfsrAEYDHWSSPDAGGPPNRGVFEDSVLP-----VIEAGLA 134

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 50510835 223 Q-----------IRALATPGHTQGHLVYLLDGEpykGPSCLFSGDLL 258
Cdd:cd16277 135 DlvdddheildgIRLEPTPGHTPGHVSVELESG---GERALFTGDVM 178
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 135-235 1.17e-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: 40.12  E-value: 1.17e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50510835 135 SYLIIDTQAGLAVAVD-PSDPRAVQASIEKE--RVNLVAI-LCTHKHWDHSGGNRDLSRR--------HRDCRV------ 196
Cdd:cd16307  24 SYLITTPRGNILINSNlESSVPQIKASIEKLgfKFSDTKIlLISHAHFDHAAGSALIKREthakymvmDGDVDVvesggk 103

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 50510835 197 ----YGSPqdgiPYLTHPLCHQD-------VVSVGRLQIRALATPGHTQG 235
Cdd:cd16307 104 sdffYGND----PSTYFPPAHVDkvlhdgeQVELGGTVLTAHLTAGHTKG 149
 
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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