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Conserved domains on  [gi|116642887|ref|NP_056303|]
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probable hydrolase PNKD isoform 1 precursor [Homo sapiens]

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 ...
 121-380 1.05e-92

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: 278.27  E-value: 1.05e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887  121 VLPIPVLSDNYSYLIIDTQAQlAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDG 200
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAF-PAPVYGPAEER 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887  201 IPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLG 280
Cdd:TIGR03413  79 IPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPA-----LFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887  281 LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALgpgpGP 360
Cdd:TIGR03413 154 LPDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAAL----GS 229

                         250       260
                  ....*....|....*....|
gi 116642887  361 TGDDDysrAQLLEELRRLKD 380
Cdd:TIGR03413 230 QGADP---VEVFAALRAWKD 246
 
Name Accession Description Interval E-value
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 121-380 1.05e-92

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: 278.27  E-value: 1.05e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887  121 VLPIPVLSDNYSYLIIDTQAQlAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDG 200
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAF-PAPVYGPAEER 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887  201 IPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLG 280
Cdd:TIGR03413  79 IPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPA-----LFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887  281 LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALgpgpGP 360
Cdd:TIGR03413 154 LPDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAAL----GS 229

                         250       260
                  ....*....|....*....|
gi 116642887  361 TGDDDysrAQLLEELRRLKD 380
Cdd:TIGR03413 230 QGADP---VEVFAALRAWKD 246
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 123-291 3.20e-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: 263.55  E-value: 3.20e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 123 PIPVLSDNYSYLIIDTQAQLAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQDGIP 202
Cdd:cd07723    2 PIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAEDRIP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 203 YLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLGLG 282
Cdd:cd07723   82 GLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEP-----ALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLALP 156


                 ....*....
gi 116642887 283 DDTLLWPGH 291
Cdd:cd07723  157 DDTLVYCGH 165
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 120-380 1.49e-86

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 262.78  E-value: 1.49e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 120 KVLPIPVLSDNYSYLIIDTQAQLAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQD 199
Cdd:PLN02469   2 KIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 200 GIPYLTHPLCHQDVVSVGR-LQIRALATPGHTQGHLVYLLDGEPYKGPScLFSGDLLFLSGCGRTFEGNAETMLSSLDTV 278
Cdd:PLN02469  82 NVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDPA-VFTGDTLFIAGCGKFFEGTAEQMYQSLCVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 279 LG-LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALGpg 357
Cdd:PLN02469 161 LGsLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVG-- 238

                        250       260
                 ....*....|....*....|...
gi 116642887 358 pgptgddDYSRAQLLEELRRLKD 380
Cdd:PLN02469 239 -------CESPVEALREVRKMKD 254
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 125-343 2.80e-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: 139.44  E-value: 2.80e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 125 PVLSDNYSYLIIDTQAqlAVAVDP----SDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQDg 200
Cdd:COG0491   10 GAGLGVNSYLIVGGDG--AVLIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAAL-AEAFGAPVYAHAAE- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 201 IPYLT----------------HPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRT- 263
Cdd:COG0491   86 AEALEapaagalfgrepvppdRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKV-----LFTGDALFSGGVGRPd 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 264 -FEGNAETMLSSLDTVLGLGDDtLLWPGHEYAeenlgfagvvepenlarerkmqwVQRQRLERKGTCPSTLGEERsyNPF 342
Cdd:COG0491  161 lPDGDLAQWLASLERLLALPPD-LVIPGHGPP-----------------------TTAEAIDYLEELLAALGERA--NPF 214


                 .
gi 116642887 343 L 343
Cdd:COG0491  215 L 215
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 131-291 1.63e-27

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 106.87  E-value: 1.63e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887   131 YSYLIIDTQAqlAVAVDP--SDPRAVQASIEKEGV-TLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQD-------- 199
Cdd:smart00849   1 NSYLVRDDGG--AILIDTgpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAP-GAPVYAPEGTaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887   200 ----------GIPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTF-EGNA 268
Cdd:smart00849  78 allgelgaeaEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKI-----LFTGDLLFAGGDGRTLvDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 116642887   269 ETMLSSLDTVLGL--GDDTLLWPGH 291
Cdd:smart00849 153 AAASDALESLLKLlkLLPKLVVPGH 177
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 292-380 9.68e-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: 101.75  E-value: 9.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887  292 EYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALGPGpgptgdddySRAQL 371
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGET---------DPVEV 71


                  ....*....
gi 116642887  372 LEELRRLKD 380
Cdd:pfam16123  72 FAALRELKD 80
 
Name Accession Description Interval E-value
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 121-380 1.05e-92

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: 278.27  E-value: 1.05e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887  121 VLPIPVLSDNYSYLIIDTQAQlAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDG 200
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAF-PAPVYGPAEER 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887  201 IPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLG 280
Cdd:TIGR03413  79 IPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPA-----LFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887  281 LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALgpgpGP 360
Cdd:TIGR03413 154 LPDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAAL----GS 229

                         250       260
                  ....*....|....*....|
gi 116642887  361 TGDDDysrAQLLEELRRLKD 380
Cdd:TIGR03413 230 QGADP---VEVFAALRAWKD 246
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 123-291 3.20e-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: 263.55  E-value: 3.20e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 123 PIPVLSDNYSYLIIDTQAQLAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQDGIP 202
Cdd:cd07723    2 PIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAEDRIP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 203 YLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLGLG 282
Cdd:cd07723   82 GLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEP-----ALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLALP 156


                 ....*....
gi 116642887 283 DDTLLWPGH 291
Cdd:cd07723  157 DDTLVYCGH 165
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 120-380 1.49e-86

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 262.78  E-value: 1.49e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 120 KVLPIPVLSDNYSYLIIDTQAQLAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQD 199
Cdd:PLN02469   2 KIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 200 GIPYLTHPLCHQDVVSVGR-LQIRALATPGHTQGHLVYLLDGEPYKGPScLFSGDLLFLSGCGRTFEGNAETMLSSLDTV 278
Cdd:PLN02469  82 NVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDPA-VFTGDTLFIAGCGKFFEGTAEQMYQSLCVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 279 LG-LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALGpg 357
Cdd:PLN02469 161 LGsLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVG-- 238

                        250       260
                 ....*....|....*....|...
gi 116642887 358 pgptgddDYSRAQLLEELRRLKD 380
Cdd:PLN02469 239 -------CESPVEALREVRKMKD 254
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 124-380 3.85e-48

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 166.17  E-value: 3.85e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 124 IPVLSDNYSYLIIDTQAQLAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSP--QDGI 201
Cdd:PLN02398  81 VPCLKDNYAYLLHDEDTGTVGVVDPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARY-GAKVIGSAvdKDRI 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 202 PYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLldgepYKGPSCLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLGL 281
Cdd:PLN02398 160 PGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFY-----FPGSGAIFTGDTLFSLSCGKLFEGTPEQMLSSLQKIISL 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 282 GDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALGPgpgPT 361
Cdd:PLN02398 235 PDDTNIYCGHEYTLSNSKFALSIEPNNEVLQSYAAHVAHLRSKGLPTIPTTVKMEKACNPFLRTSSTDIRKSLSI---PD 311

                        250
                 ....*....|....*....
gi 116642887 362 GDDDysrAQLLEELRRLKD 380
Cdd:PLN02398 312 TADE---AEALGIIRRAKD 327
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 129-291 5.70e-45

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: 152.69  E-value: 5.70e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 129 DNYSYLIIDTQAQLAVAVDPS-DPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDgIPYLT-- 205
Cdd:cd16275   11 INYSYIIIDKATREAAVVDPAwDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKY-DAPVYMSKEE-IDYYGfr 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 206 ----HPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGepykgpsCLFSGDLLFLSGCGRT--FEGNAETMLSSLDTVL 279
Cdd:cd16275   89 cpnlIPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGD-------SLFTGDTLFIEGCGRCdlPGGDPEEMYESLQRLK 161

                        170
                 ....*....|...
gi 116642887 280 GL-GDDTLLWPGH 291
Cdd:cd16275  162 KLpPPNTRVYPGH 174
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 124-345 5.56e-42

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 147.66  E-value: 5.56e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 124 IPVLSDNYSYLIIDTQAQlAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQDGIPY 203
Cdd:PRK10241   6 IPAFDDNYIWVLNDEAGR-CLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQETQDKG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 204 LTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLldGEPYkgpscLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLGLGD 283
Cdd:PRK10241  85 TTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF--SKPY-----LFCGDTLFSGGCGRLFEGTASQMYQSLKKINALPD 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116642887 284 DTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRT 345
Cdd:PRK10241 158 DTLICCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINLFLRT 219
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 131-293 2.04e-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: 141.00  E-value: 2.04e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 131 YSYLIIDTQAQLAVAVDPSDPRA--VQASIEKEGVTLVAILCTHKHWDH-SGGnRDLSRRHrDCRVYGSPQDGIPYLTHP 207
Cdd:cd07724   13 LSYLVGDPETGEAAVIDPVRDSVdrYLDLAAELGLKITYVLETHVHADHvSGA-RELAERT-GAPIVIGEGAPASFFDRL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 208 LCHQDVVSVGRLQIRALATPGHTQGHLVYLLDgepykGPSCLFSGDLLFLSGCGRT-----FEGNAETMLSSL-DTVLGL 281
Cdd:cd07724   91 LKDGDVLELGNLTLEVLHTPGHTPESVSYLVG-----DPDAVFTGDTLFVGDVGRPdlpgeAEGLARQLYDSLqRKLLLL 165

                        170
                 ....*....|..
gi 116642887 282 GDDTLLWPGHEY 293
Cdd:cd07724  166 PDETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 125-343 2.80e-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: 139.44  E-value: 2.80e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 125 PVLSDNYSYLIIDTQAqlAVAVDP----SDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQDg 200
Cdd:COG0491   10 GAGLGVNSYLIVGGDG--AVLIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAAL-AEAFGAPVYAHAAE- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 201 IPYLT----------------HPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRT- 263
Cdd:COG0491   86 AEALEapaagalfgrepvppdRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKV-----LFTGDALFSGGVGRPd 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 264 -FEGNAETMLSSLDTVLGLGDDtLLWPGHEYAeenlgfagvvepenlarerkmqwVQRQRLERKGTCPSTLGEERsyNPF 342
Cdd:COG0491  161 lPDGDLAQWLASLERLLALPPD-LVIPGHGPP-----------------------TTAEAIDYLEELLAALGERA--NPF 214


                 .
gi 116642887 343 L 343
Cdd:COG0491  215 L 215
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 120-291 1.61e-35

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


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 128.56  E-value: 1.61e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 120 KVLPIPVLSDNySYLIIDTQAQlAVAVDPSDP--RAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSP 197
Cdd:cd06262    1 KRLPVGPLQTN-CYLVSDEEGE-AILIDPGAGalEKILEAIEELGLKIKAILLTHGHFDHIGGLAEL-KEAPGAPVYIHE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 198 QDgIPYLTHPLCHQ--------------------DVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGDLLFL 257
Cdd:cd06262   78 AD-AELLEDPELNLaffgggplpppepdilledgDTIELGGLELEVIHTPGHTPGSVCFYIEEEG-----VLFTGDTLFA 151

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 116642887 258 SGCGRT--FEGNAETMLSSLDTVLG-LGDDTLLWPGH 291
Cdd:cd06262  152 GSIGRTdlPGGDPEQLIESIKKLLLlLPDDTVVYPGH 188
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 119-343 8.10e-33

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: 122.07  E-value: 8.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 119 VKVLPIPVLSDNySYLIIDTQAQLAVAVDPSDPR-AVQASIEKEGVTLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSP 197
Cdd:cd16322    1 VRPFTLGPLQEN-TYLVADEGGGEAVLVDPGDESeKLLARFGTTGLTLLYILLTHAHFDHVGGVADL-RRHPGAPVYLHP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 198 QD----------------GIPYLT---HPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpSCLFSGDLLFLS 258
Cdd:cd16322   79 DDlplyeaadlgakafglGIEPLPppdRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEE-----GLLFSGDLLFQG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 259 GCGRT--FEGNAETMLSSLDTVLGLGDDTLLWPGHeyaeenlgfaGVvepenlarerkmqwvqrqrlerkgtcPSTLGEE 336
Cdd:cd16322  154 SIGRTdlPGGDPKAMAASLRRLLTLPDETRVFPGH----------GP--------------------------PTTLGEE 197


                 ....*..
gi 116642887 337 RSYNPFL 343
Cdd:cd16322  198 RRTNPFL 204
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 131-291 1.63e-27

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 106.87  E-value: 1.63e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887   131 YSYLIIDTQAqlAVAVDP--SDPRAVQASIEKEGV-TLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQD-------- 199
Cdd:smart00849   1 NSYLVRDDGG--AILIDTgpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAP-GAPVYAPEGTaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887   200 ----------GIPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTF-EGNA 268
Cdd:smart00849  78 allgelgaeaEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKI-----LFTGDLLFAGGDGRTLvDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 116642887   269 ETMLSSLDTVLGL--GDDTLLWPGH 291
Cdd:smart00849 153 AAASDALESLLKLlkLLPKLVVPGH 177
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 292-380 9.68e-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: 101.75  E-value: 9.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887  292 EYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALGPGpgptgdddySRAQL 371
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGET---------DPVEV 71


                  ....*....
gi 116642887  372 LEELRRLKD 380
Cdd:pfam16123  72 FAALRELKD 80
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 124-291 1.68e-25

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: 101.86  E-value: 1.68e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 124 IPV--LSDNySYLIIDTQAQLAVAVDP-SDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQD- 199
Cdd:cd07737    4 IPVtpFQQN-CSLIWCEETKEAAVIDPgGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAEL-AEHYGVPIIGPHKEd 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 200 --------------GIPYL-----THPLCHQDVVSVGRLQIRALATPGHTQGHLVYLldGEPYKgpsCLFSGDLLFLSGC 260
Cdd:cd07737   82 kfllenlpeqsqmfGFPPAeaftpDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFF--NRESK---LAIVGDVLFKGSI 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 116642887 261 GRT-F-EGNAETMLSSL-DTVLGLGDDTLLWPGH 291
Cdd:cd07737  157 GRTdFpGGNHAQLIASIkEKLLPLGDDVTFIPGH 190
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 132-291 7.31e-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: 99.87  E-value: 7.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 132 SYlIIDTQAQLAVaVDP--SDPRAVQASIEK-EGVTLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDGIPYL---- 204
Cdd:cd16278   20 TY-LLGAPDGVVV-IDPgpDDPAHLDALLAAlGGGRVSAILVTHTHRDHSPGAARLAERT-GAPVRAFGPHRAGGQdtdf 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 205 --THPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGDLLFlsGCGRTF----EGNAETMLSSLDTV 278
Cdd:cd16278   97 apDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEG-----ALFTGDHVM--GWSTTViappDGDLGDYLASLERL 169

                        170
                 ....*....|...
gi 116642887 279 LGLgDDTLLWPGH 291
Cdd:cd16278  170 LAL-DDRLLLPGH 181
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 128-343 1.44e-18

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 84.46  E-value: 1.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 128 SDNYSYLIIDTQ--AQLAVAVDPSDpRAVQ---ASIEKEGVTLVAILCTHKHWDHSGG-----NRDLSRRHRDCRVYGSP 197
Cdd:PLN02962  21 SSTYTYLLADVShpDKPALLIDPVD-KTVDrdlSLVKELGLKLIYAMNTHVHADHVTGtgllkTKLPGVKSIISKASGSK 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 198 QDgipyltHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLL-DGEPYKGPSCLFSGDLLFLSGCGRT-FE-GNAETMLSS 274
Cdd:PLN02962 100 AD------LFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTgEGPDQPQPRMAFTGDALLIRGCGRTdFQgGSSDQLYKS 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 275 LDT-VLGLGDDTLLWPGHEYaeenlgfagvvepenlarerkmqwvqrqrlerKGTCPSTLGEERSYNPFL 343
Cdd:PLN02962 174 VHSqIFTLPKDTLIYPAHDY--------------------------------KGFTVSTVGEEMLYNPRL 211
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 132-291 9.27e-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: 80.27  E-value: 9.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 132 SYLIIDTqAQLAVAVDPSDPRAVQASiekEGVTLVAILCTHKHWDHSGGNRDLSRRHRD--CRVYGSP---------QDG 200
Cdd:cd07722   28 RRILIDT-GEGRPSYIPLLKSVLDSE---GNATISDILLTHWHHDHVGGLPDVLDLLRGpsPRVYKFPrpeededpdEDG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 201 IPYltHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGD-LLflsGCGRT-FEGNAETMlSSLDTV 278
Cdd:cd07722  104 GDI--HDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEEN-----ALFTGDcVL---GHGTAvFEDLAAYM-ASLKKL 172

                        170
                 ....*....|...
gi 116642887 279 LGLGDDTlLWPGH 291
Cdd:cd07722  173 LSLGPGR-IYPGH 184
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 119-291 2.87e-15

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: 73.49  E-value: 2.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 119 VKVLPIPVLSDNYSYLIIDTqaqlAVAVdPSDPRAVQASIEKEGVTLVAI---LCTHKHWDHSGGNRDLSRRhRDCRVYG 195
Cdd:cd07725   12 LGHVNVYLLRDGDETTLIDT----GLAT-EEDAEALWEGLKELGLKPSDIdrvLLTHHHPDHIGLAGKLQEK-SGATVYI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 196 SPqdgipylTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpSCLFSGD--LLFLSGCG----RTFEGNAE 269
Cdd:cd07725   86 LD-------VTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDR-----RELFVGDavLPKITPNVslwaVRVEDPLG 153

                        170       180
                 ....*....|....*....|..
gi 116642887 270 TMLSSLDTVLGLGDDtLLWPGH 291
Cdd:cd07725  154 AYLESLDKLEKLDVD-LAYPGH 174
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
131-291 1.24e-13

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 68.93  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887  131 YSYLIIDTQAqlAVAVDP--SDPRAVQASIEKEGV---TLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGS--------- 196
Cdd:pfam00753   7 NSYLIEGGGG--AVLIDTggSAEAALLLLLAALGLgpkDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAeearellde 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887  197 -------------PQDGIPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLldgepYKGPSCLFSGDLLFLSGCGRT 263
Cdd:pfam00753  85 elglaasrlglpgPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVY-----YGGGKVLFTGDLLFAGEIGRL 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 116642887  264 ----------FEGNAETMLSSLDTVLGLgDDTLLWPGH 291
Cdd:pfam00753 160 dlplggllvlHPSSAESSLESLLKLAKL-KAAVIVPGH 196
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 118-291 1.38e-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: 68.79  E-value: 1.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 118 GVKVLPIPVLSdnYSYLIIDtqAQLAVAVD---PSDPRAVQASIEKEGVT---LVAILCTHKHWDHSGGNRDLsRRHRDC 191
Cdd:cd07721    1 GVYQLPLLPPV--NAYLIED--DDGLTLIDtglPGSAKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAAL-KEAPGA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 192 RVYGSPQDgIPYLTH---PLCHQDVVSVGRLQ-------------------------IRALATPGHTQGHLVYLLDGEpy 243
Cdd:cd07721   76 PVYAHERE-APYLEGekpYPPPVRLGLLGLLSpllpvkpvpvdrtledgdtldlaggLRVIHTPGHTPGHISLYLEED-- 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 116642887 244 kgpSCLFSGDLLFLSGcGRTFEGNA------ETMLSSLDTVLGLGDDTLLwPGH 291
Cdd:cd07721  153 ---GVLIAGDALVTVG-GELVPPPPpftwdmEEALESLRKLAELDPEVLA-PGH 201
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 126-291 1.48e-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: 68.71  E-value: 1.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 126 VLSDNYSYLIIDTqaqlavAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQDgIPYLT 205
Cdd:cd07743   13 YVFGDKEALLIDS------GLDEDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYL-QKKTGCKVYAPKIE-KAFIE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 206 HPL------------------------------CHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpsCLFSGDLL 255
Cdd:cd07743   85 NPLlepsylggayppkelrnkflmakpskvddiIEEGELELGGVGLEIIPLPGHSFGQIGILTPDG------VLFAGDAL 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 116642887 256 F----LSGCGRTFEGNAETMLSSLDTVLGLGDDTLLwPGH 291
Cdd:cd07743  159 FgeevLEKYGIPFLYDVEEQLETLEKLEELDADYYV-PGH 197
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 134-291 1.61e-12

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 66.05  E-value: 1.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 134 LIIDTQAQLAVAvdpsdpRAVQASIEKEG---VTLVAIlcTHKHWDHSGGN-----------------RDLSRRHRDCRV 193
Cdd:cd16282   27 VVIDTGASPRLA------RALLAAIRKVTdkpVRYVVN--THYHGDHTLGNaafadagapiiahentrEELAARGEAYLE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 194 YGSPQDG-------IPYLTHPLCHQDVVSVGRLQIRALAT-PGHTQGHLVYLLDGEpykgpSCLFSGDLLFLSGCGRTFE 265
Cdd:cd16282   99 LMRRLGGdamagteLVLPDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEE-----GVLFAGDLVFNGRIPFLPD 173

                        170       180
                 ....*....|....*....|....*.
gi 116642887 266 GNAETMLSSLDTVLGLGDDTLLwPGH 291
Cdd:cd16282  174 GSLAGWIAALDRLLALDATVVV-PGH 198
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 97-292 1.39e-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: 63.77  E-value: 1.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887  97 LRRARNRYPKGHSKTQPRLFNGVKVLPIpvlsdnYSYLI--------IDTQAQLAVAVDPSDPRAVQASIEKEGVTLVAI 168
Cdd:cd07729    5 LDYGTVTVDKSSLFYYGRGPGEPIDLPV------YAYLIehpegtilVDTGFHPDAADDPGGLELAFPPGVTEEQTLEEQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 169 L--------------CTHKHWDHSGGNRDL-------SRR-----HRDCRVYGSPQDGIPYLTHPLCHQDVVSV-GRLQ- 220
Cdd:cd07729   79 LarlgldpedidyviLSHLHFDHAGGLDLFpnatiivQRAeleyaTGPDPLAAGYYEDVLALDDDLPGGRVRLVdGDYDl 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 221 ---IRALATPGHTQGHLVYLLDGEpyKGPsCLFSGDL-----LFLSGCGRTFEGNAETMLSSLDTVLGL--GDDTLLWPG 290
Cdd:cd07729  159 fpgVTLIPTPGHTPGHQSVLVRLP--EGT-VLLAGDAaytyeNLEEGRPPGINYDPEAALASLERLKALaeREGARVIPG 235


                 ..
gi 116642887 291 HE 292
Cdd:cd07729  236 HD 237
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 151-291 1.69e-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: 56.87  E-value: 1.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 151 PRAVQASIEKEgVTLVAilcTHKHWDHSGGN----------RDLSRRHRDCRVYGSPQDGIPY------LTHPLCHQDVV 214
Cdd:cd07712   33 KEYVRTLTDLP-LLVVA---THGHFDHIGGLhefeevyvhpADAEILAAPDNFETLTWDAATYsvppagPTLPLRDGDVI 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 215 SVGRLQIRALATPGHTQGHLVyLLDgepyKGPSCLFSGD------LLFLSGCgrtfeGNAETMLSSLDTVLGLGDD-TLL 287
Cdd:cd07712  109 DLGDRQLEVIHTPGHTPGSIA-LLD----RANRLLFSGDvvydgpLIMDLPH-----SDLDDYLASLEKLSKLPDEfDKV 178


                 ....
gi 116642887 288 WPGH 291
Cdd:cd07712  179 LPGH 182
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 132-291 5.72e-09

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


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 55.58  E-value: 5.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 132 SYLIiDTQAQLAVaVDP---SDPRAVQASIEKEGVTLV---AILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQdGIPYLT 205
Cdd:cd07726   18 SYLL-DGEGRPAL-IDTgpsSSVPRLLAALEALGIAPEdvdYIILTHIHLDHAGGAGLLAEALPNAKVYVHPR-GARHLI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 206 HP--------------------------------LCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpSCLFSGD 253
Cdd:cd07726   95 DPsklwasaravygdeadrlggeilpvpeervivLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEES-----DGLFTGD 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 116642887 254 LLFLSGCGRTFEG---------NAETMLSSLDTVLGLGDDTLLwPGH 291
Cdd:cd07726  170 AAGVRYPELDVVGppstpppdfDPEAWLESLDRLLSLKPERIY-LTH 215
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 132-232 8.31e-07

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: 49.76  E-value: 8.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 132 SYLII-DTQAQLAVAVDPSDPRAVQASIEKEGVTLV---AILCTHKHWDHSGGnrdLSRRHRD--CRVYGSPQD------ 199
Cdd:cd16310   24 SYLITsNHGAILLDGGLEENAALIEQNIKALGFKLSdikIIINTHAHYDHAGG---LAQLKADtgAKLWASRGDrpalea 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 116642887 200 ----------GIPY----LTHPLCHQDVVSVGRLQIRALATPGHTQG 232
Cdd:cd16310  101 gkhigdnitqPAPFpavkVDRILGDGEKIKLGDITLTATLTPGHTKG 147
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 156-243 7.02e-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: 7.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 156 ASIEKEGV---TLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGS----------PQDGIPYLTHPLCHQDVV-------S 215
Cdd:cd16280   50 DGLEKLGLdpaDIKYILITHGHGDHYGGAAYL-KDLYGAKVVMSeadwdmmeepPEEGDNPRWGPPPERDIVikdgdtlT 128

                         90       100       110
                 ....*....|....*....|....*....|..
gi 116642887 216 VGRLQIRALATPGHTQGHLVYLLD----GEPY 243
Cdd:cd16280  129 LGDTTITVYLTPGHTPGTLSLIFPvkdgGKTH 160
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 138-232 4.67e-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: 44.59  E-value: 4.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 138 TQAQLAVAVDPSDPRA---VQASIEKEGVTL---VAILCTHKHWDHSGGNRDLsRRHRDCRVYGSP------QDGIP--- 202
Cdd:cd16312   28 TSPQGHVLLDGALPQSaplIIANIEALGFRIedvKLILNSHAHWDHAGGIAAL-QKASGATVAASAhgaqvlQSGTNgkd 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 116642887 203 ---YLTHPLCH------------QDVVSVGRLQIRALATPGHTQG 232
Cdd:cd16312  107 dpqYQAKPVVHvakvakvkevgeGDTLKVGPLRLTAHMTPGHTPG 151
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 146-254 9.08e-05

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: 42.96  E-value: 9.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 146 VDPSDPRAVQA---SIEKEG-----VTLVaiLCTHKHWDHSGGNRDLSR-RHrdcrVYGSPQDGIPYLTHPLCHQDVVSV 216
Cdd:cd07711   36 VDTGTPWDRDLllkALAEHGlspedIDYV--VLTHGHPDHIGNLNLFPNaTV----IVGWDICGDSYDDHSLEEGDGYEI 109

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 116642887 217 GrLQIRALATPGHTQGHLVYLLDGEPYKgpSCLFSGDL 254
Cdd:cd07711  110 D-ENVEVIPTPGHTPEDVSVLVETEKKG--TVAVAGDL 144
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
133-253 1.30e-04

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 43.26  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 133 YLIID----TQAQLAVA-VDPSDPRAvqasiekegvtlvaILCTHKHWDHSGG------NRDLSRRHRDCRVYGsPQDGI 201
Cdd:COG1234   30 RLLIDcgegTQRQLLRAgLDPRDIDA--------------IFITHLHGDHIAGlpgllsTRSLAGREKPLTIYG-PPGTK 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116642887 202 PYLT----------------HPLCHQDVVSVGRLQIRALATPgHTQGHLVYLLDgepYKGPSCLFSGD 253
Cdd:COG1234   95 EFLEallkasgtdldfplefHEIEPGEVFEIGGFTVTAFPLD-HPVPAYGYRFE---EPGRSLVYSGD 158
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 221-258 1.60e-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: 42.18  E-value: 1.60e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 116642887 221 IRALATPGHTQGHLVYLldgepYKGPSCLFSGDLLFLS 258
Cdd:cd07727  104 LTLIPVPGHTRGSVVLL-----YKEKGVLFTGDHLAWS 136
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 221-256 2.13e-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: 42.54  E-value: 2.13e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 116642887 221 IRALATPGHTQGHLVYLLDGepyKGPSCLFSGDLLF 256
Cdd:cd07720  175 ITAVPAPGHTPGHTGYRIES---GGERLLIWGDIVH 207
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 132-232 2.79e-04

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: 42.05  E-value: 2.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 132 SYLIIDTQAQLAVAVD-PSDPRAVQASIEKEGVTLV---AILCTHKHWDHSGGNRDLSRR--------HRDCRV------ 193
Cdd:cd16307   24 SYLITTPRGNILINSNlESSVPQIKASIEKLGFKFSdtkILLISHAHFDHAAGSALIKREthakymvmDGDVDVvesggk 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 116642887 194 ----YGSPqdgiPYLTHPLCHQD-------VVSVGRLQIRALATPGHTQG 232
Cdd:cd16307  104 sdffYGND----PSTYFPPAHVDkvlhdgeQVELGGTVLTAHLTAGHTKG 149
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 161-255 3.36e-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: 41.74  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 161 EGVTLVaiLCTHKHWDHSGGN---------------------RDLSRRHRDCRVYGSPQDGIPYLTHPlchqdVVSVGRL 219
Cdd:cd16277   62 EDVDYV--LCTHLHVDHVGWNtrlvdgrwvptfpnarylfsrAEYDHWSSPDAGGPPNRGVFEDSVLP-----VIEAGLA 134

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 116642887 220 Q-----------IRALATPGHTQGHLVYLLDGEpykGPSCLFSGDLL 255
Cdd:cd16277  135 DlvdddheildgIRLEPTPGHTPGHVSVELESG---GERALFTGDVM 178
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 132-232 3.76e-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: 41.54  E-value: 3.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116642887 132 SYLIIDTQAqlAVAVDPSDPRAV---QASIEKEGVT---LVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQD------ 199
Cdd:cd16288   24 SYLITTPQG--LILIDTGLESSApmiKANIRKLGFKpsdIKILLNSHAHLDHAGGLAAL-KKLTGAKLMASAEDaallas 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 116642887 200 --------GIPYLTHP-------LCHQDVVSVGRLQIRALATPGHTQG 232
Cdd:cd16288  101 ggksdfhyGDDSLAFPpvkvdrvLKDGDRVTLGGTTLTAHLTPGHTRG 148
 
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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