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Conserved domains on  [gi|21703352|ref|NP_072094|]
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probable hydrolase PNKD isoform 2 [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 ...
 97-356 5.38e-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: 277.88  E-value: 5.38e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352    97 VLPIPVLSDNYSYLIIDTQAQlAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDG 176
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAF-PAPVYGPAEER 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352   177 IPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLG 256
Cdd:TIGR03413  79 IPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPA-----LFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352   257 LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALgpgpGP 336
Cdd:TIGR03413 154 LPDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAAL----GS 229

                         250       260
                  ....*....|....*....|
gi 21703352   337 TGDDDysrAQLLEELRRLKD 356
Cdd:TIGR03413 230 QGADP---VEVFAALRAWKD 246
 
Name Accession Description Interval E-value
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 97-356 5.38e-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: 277.88  E-value: 5.38e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352    97 VLPIPVLSDNYSYLIIDTQAQlAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDG 176
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAF-PAPVYGPAEER 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352   177 IPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLG 256
Cdd:TIGR03413  79 IPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPA-----LFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352   257 LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALgpgpGP 336
Cdd:TIGR03413 154 LPDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAAL----GS 229

                         250       260
                  ....*....|....*....|
gi 21703352   337 TGDDDysrAQLLEELRRLKD 356
Cdd:TIGR03413 230 QGADP---VEVFAALRAWKD 246
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 99-267 1.59e-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: 1.59e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352  99 PIPVLSDNYSYLIIDTQAQLAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQDGIP 178
Cdd:cd07723   2 PIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAEDRIP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 179 YLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLGLG 258
Cdd:cd07723  82 GLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEP-----ALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLALP 156


                ....*....
gi 21703352 259 DDTLLWPGH 267
Cdd:cd07723 157 DDTLVYCGH 165
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 96-356 6.80e-87

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 262.78  E-value: 6.80e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352   96 KVLPIPVLSDNYSYLIIDTQAQLAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQD 175
Cdd:PLN02469   2 KIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352  176 GIPYLTHPLCHQDVVSVGR-LQIRALATPGHTQGHLVYLLDGEPYKGPScLFSGDLLFLSGCGRTFEGNAETMLSSLDTV 254
Cdd:PLN02469  82 NVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDPA-VFTGDTLFIAGCGKFFEGTAEQMYQSLCVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352  255 LG-LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALGpg 333
Cdd:PLN02469 161 LGsLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVG-- 238

                        250       260
                 ....*....|....*....|...
gi 21703352  334 pgptgddDYSRAQLLEELRRLKD 356
Cdd:PLN02469 239 -------CESPVEALREVRKMKD 254
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 101-319 3.72e-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: 138.28  E-value: 3.72e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 101 PVLSDNYSYLIIDTQAqlAVAVDP----SDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQDg 176
Cdd:COG0491  10 GAGLGVNSYLIVGGDG--AVLIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAAL-AEAFGAPVYAHAAE- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 177 IPYLT----------------HPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRT- 239
Cdd:COG0491  86 AEALEapaagalfgrepvppdRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKV-----LFTGDALFSGGVGRPd 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 240 -FEGNAETMLSSLDTVLGLGDDtLLWPGHEYAeenlgfagvvepenlarerkmqwVQRQRLERKGTCPSTLGEERsyNPF 318
Cdd:COG0491 161 lPDGDLAQWLASLERLLALPPD-LVIPGHGPP-----------------------TTAEAIDYLEELLAALGERA--NPF 214


                .
gi 21703352 319 L 319
Cdd:COG0491 215 L 215
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 107-267 8.20e-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: 107.25  E-value: 8.20e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352    107 YSYLIIDTQAqlAVAVDP--SDPRAVQASIEKEGV-TLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQD-------- 175
Cdd:smart00849   1 NSYLVRDDGG--AILIDTgpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAP-GAPVYAPEGTaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352    176 ----------GIPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTF-EGNA 244
Cdd:smart00849  78 allgelgaeaEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKI-----LFTGDLLFAGGDGRTLvDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 21703352    245 ETMLSSLDTVLGL--GDDTLLWPGH 267
Cdd:smart00849 153 AAASDALESLLKLlkLLPKLVVPGH 177
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 268-356 6.83e-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: 6.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352   268 EYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALGPGpgptgdddySRAQL 347
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGET---------DPVEV 71


                  ....*....
gi 21703352   348 LEELRRLKD 356
Cdd:pfam16123  72 FAALRELKD 80
 
Name Accession Description Interval E-value
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 97-356 5.38e-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: 277.88  E-value: 5.38e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352    97 VLPIPVLSDNYSYLIIDTQAQlAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDG 176
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAF-PAPVYGPAEER 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352   177 IPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLG 256
Cdd:TIGR03413  79 IPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPA-----LFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352   257 LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALgpgpGP 336
Cdd:TIGR03413 154 LPDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAAL----GS 229

                         250       260
                  ....*....|....*....|
gi 21703352   337 TGDDDysrAQLLEELRRLKD 356
Cdd:TIGR03413 230 QGADP---VEVFAALRAWKD 246
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 99-267 1.59e-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: 1.59e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352  99 PIPVLSDNYSYLIIDTQAQLAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQDGIP 178
Cdd:cd07723   2 PIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAEDRIP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 179 YLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLGLG 258
Cdd:cd07723  82 GLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEP-----ALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLALP 156


                ....*....
gi 21703352 259 DDTLLWPGH 267
Cdd:cd07723 157 DDTLVYCGH 165
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 96-356 6.80e-87

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 262.78  E-value: 6.80e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352   96 KVLPIPVLSDNYSYLIIDTQAQLAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQD 175
Cdd:PLN02469   2 KIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352  176 GIPYLTHPLCHQDVVSVGR-LQIRALATPGHTQGHLVYLLDGEPYKGPScLFSGDLLFLSGCGRTFEGNAETMLSSLDTV 254
Cdd:PLN02469  82 NVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDPA-VFTGDTLFIAGCGKFFEGTAEQMYQSLCVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352  255 LG-LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALGpg 333
Cdd:PLN02469 161 LGsLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVG-- 238

                        250       260
                 ....*....|....*....|...
gi 21703352  334 pgptgddDYSRAQLLEELRRLKD 356
Cdd:PLN02469 239 -------CESPVEALREVRKMKD 254
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 29-356 3.93e-49

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 168.10  E-value: 3.93e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352   29 SPRGCRARRGLRGLLMAHSQrLLFRIGYsLYTRTWLGYLFYRQqLRRARNRYPKGHSKTQPRLFNGVKVLPIPVLSDNYS 108
Cdd:PLN02398  13 SFRCSRRIRGQLCVRPGVRQ-LCLRKSL-LYGVMKLLSMPLKT-LRGAGRTLKVAQFCSVSNVSSSLQIELVPCLKDNYA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352  109 YLIIDTQAQLAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSP--QDGIPYLTHPLCH 186
Cdd:PLN02398  90 YLLHDEDTGTVGVVDPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARY-GAKVIGSAvdKDRIPGIDIVLKD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352  187 QDVVSVGRLQIRALATPGHTQGHLVYLldgepYKGPSCLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLGLGDDTLLWPG 266
Cdd:PLN02398 169 GDKWMFAGHEVLVMETPGHTRGHISFY-----FPGSGAIFTGDTLFSLSCGKLFEGTPEQMLSSLQKIISLPDDTNIYCG 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352  267 HEYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALGPgpgPTGDDDysrAQ 346
Cdd:PLN02398 244 HEYTLSNSKFALSIEPNNEVLQSYAAHVAHLRSKGLPTIPTTVKMEKACNPFLRTSSTDIRKSLSI---PDTADE---AE 317

                        330
                 ....*....|
gi 21703352  347 LLEELRRLKD 356
Cdd:PLN02398 318 ALGIIRRAKD 327
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 105-267 4.40e-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: 152.31  E-value: 4.40e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 105 DNYSYLIIDTQAQLAVAVDPS-DPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDgIPYLT-- 181
Cdd:cd16275  11 INYSYIIIDKATREAAVVDPAwDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKY-DAPVYMSKEE-IDYYGfr 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 182 ----HPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGepykgpsCLFSGDLLFLSGCGRT--FEGNAETMLSSLDTVL 255
Cdd:cd16275  89 cpnlIPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGD-------SLFTGDTLFIEGCGRCdlPGGDPEEMYESLQRLK 161

                       170
                ....*....|...
gi 21703352 256 GL-GDDTLLWPGH 267
Cdd:cd16275 162 KLpPPNTRVYPGH 174
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 100-321 3.17e-42

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 147.66  E-value: 3.17e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352  100 IPVLSDNYSYLIIDTQAQlAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQDGIPY 179
Cdd:PRK10241   6 IPAFDDNYIWVLNDEAGR-CLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQETQDKG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352  180 LTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLldGEPYkgpscLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLGLGD 259
Cdd:PRK10241  85 TTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF--SKPY-----LFCGDTLFSGGCGRLFEGTASQMYQSLKKINALPD 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21703352  260 DTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRT 321
Cdd:PRK10241 158 DTLICCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINLFLRT 219
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 107-269 1.67e-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: 140.61  E-value: 1.67e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 107 YSYLIIDTQAQLAVAVDPSDPRA--VQASIEKEGVTLVAILCTHKHWDH-SGGnRDLSRRHrDCRVYGSPQDGIPYLTHP 183
Cdd:cd07724  13 LSYLVGDPETGEAAVIDPVRDSVdrYLDLAAELGLKITYVLETHVHADHvSGA-RELAERT-GAPIVIGEGAPASFFDRL 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 184 LCHQDVVSVGRLQIRALATPGHTQGHLVYLLDgepykGPSCLFSGDLLFLSGCGRT-----FEGNAETMLSSL-DTVLGL 257
Cdd:cd07724  91 LKDGDVLELGNLTLEVLHTPGHTPESVSYLVG-----DPDAVFTGDTLFVGDVGRPdlpgeAEGLARQLYDSLqRKLLLL 165

                       170
                ....*....|..
gi 21703352 258 GDDTLLWPGHEY 269
Cdd:cd07724 166 PDETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 101-319 3.72e-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: 138.28  E-value: 3.72e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 101 PVLSDNYSYLIIDTQAqlAVAVDP----SDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQDg 176
Cdd:COG0491  10 GAGLGVNSYLIVGGDG--AVLIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAAL-AEAFGAPVYAHAAE- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 177 IPYLT----------------HPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRT- 239
Cdd:COG0491  86 AEALEapaagalfgrepvppdRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKV-----LFTGDALFSGGVGRPd 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 240 -FEGNAETMLSSLDTVLGLGDDtLLWPGHEYAeenlgfagvvepenlarerkmqwVQRQRLERKGTCPSTLGEERsyNPF 318
Cdd:COG0491 161 lPDGDLAQWLASLERLLALPPD-LVIPGHGPP-----------------------TTAEAIDYLEELLAALGERA--NPF 214


                .
gi 21703352 319 L 319
Cdd:COG0491 215 L 215
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 96-267 1.21e-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: 128.17  E-value: 1.21e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352  96 KVLPIPVLSDNySYLIIDTQAQlAVAVDPSDP--RAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSP 173
Cdd:cd06262   1 KRLPVGPLQTN-CYLVSDEEGE-AILIDPGAGalEKILEAIEELGLKIKAILLTHGHFDHIGGLAEL-KEAPGAPVYIHE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 174 QDgIPYLTHPLCHQ--------------------DVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGDLLFL 233
Cdd:cd06262  78 AD-AELLEDPELNLaffgggplpppepdilledgDTIELGGLELEVIHTPGHTPGSVCFYIEEEG-----VLFTGDTLFA 151

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 21703352 234 SGCGRT--FEGNAETMLSSLDTVLG-LGDDTLLWPGH 267
Cdd:cd06262 152 GSIGRTdlPGGDPEQLIESIKKLLLlLPDDTVVYPGH 188
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 95-319 2.43e-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: 122.84  E-value: 2.43e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352  95 VKVLPIPVLSDNySYLIIDTQAQLAVAVDPSDPR-AVQASIEKEGVTLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSP 173
Cdd:cd16322   1 VRPFTLGPLQEN-TYLVADEGGGEAVLVDPGDESeKLLARFGTTGLTLLYILLTHAHFDHVGGVADL-RRHPGAPVYLHP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 174 QD----------------GIPYLT---HPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpSCLFSGDLLFLS 234
Cdd:cd16322  79 DDlplyeaadlgakafglGIEPLPppdRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEE-----GLLFSGDLLFQG 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 235 GCGRT--FEGNAETMLSSLDTVLGLGDDTLLWPGHeyaeenlgfaGVvepenlarerkmqwvqrqrlerkgtcPSTLGEE 312
Cdd:cd16322 154 SIGRTdlPGGDPKAMAASLRRLLTLPDETRVFPGH----------GP--------------------------PTTLGEE 197


                ....*..
gi 21703352 313 RSYNPFL 319
Cdd:cd16322 198 RRTNPFL 204
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 107-267 8.20e-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: 107.25  E-value: 8.20e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352    107 YSYLIIDTQAqlAVAVDP--SDPRAVQASIEKEGV-TLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQD-------- 175
Cdd:smart00849   1 NSYLVRDDGG--AILIDTgpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAP-GAPVYAPEGTaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352    176 ----------GIPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTF-EGNA 244
Cdd:smart00849  78 allgelgaeaEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKI-----LFTGDLLFAGGDGRTLvDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 21703352    245 ETMLSSLDTVLGL--GDDTLLWPGH 267
Cdd:smart00849 153 AAASDALESLLKLlkLLPKLVVPGH 177
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 268-356 6.83e-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: 6.83e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352   268 EYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALGPGpgptgdddySRAQL 347
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGET---------DPVEV 71


                  ....*....
gi 21703352   348 LEELRRLKD 356
Cdd:pfam16123  72 FAALRELKD 80
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 100-267 2.17e-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: 101.09  E-value: 2.17e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 100 IPV--LSDNySYLIIDTQAQLAVAVDP-SDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQD- 175
Cdd:cd07737   4 IPVtpFQQN-CSLIWCEETKEAAVIDPgGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAEL-AEHYGVPIIGPHKEd 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 176 --------------GIPYL-----THPLCHQDVVSVGRLQIRALATPGHTQGHLVYLldGEPYKgpsCLFSGDLLFLSGC 236
Cdd:cd07737  82 kfllenlpeqsqmfGFPPAeaftpDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFF--NRESK---LAIVGDVLFKGSI 156

                       170       180       190
                ....*....|....*....|....*....|....
gi 21703352 237 GRT-F-EGNAETMLSSL-DTVLGLGDDTLLWPGH 267
Cdd:cd07737 157 GRTdFpGGNHAQLIASIkEKLLPLGDDVTFIPGH 190
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 108-267 5.37e-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: 5.37e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 108 SYlIIDTQAQLAVaVDP--SDPRAVQASIEK-EGVTLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDGIPYL---- 180
Cdd:cd16278  20 TY-LLGAPDGVVV-IDPgpDDPAHLDALLAAlGGGRVSAILVTHTHRDHSPGAARLAERT-GAPVRAFGPHRAGGQdtdf 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 181 --THPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGDLLFlsGCGRTF----EGNAETMLSSLDTV 254
Cdd:cd16278  97 apDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEG-----ALFTGDHVM--GWSTTViappDGDLGDYLASLERL 169

                       170
                ....*....|...
gi 21703352 255 LGLgDDTLLWPGH 267
Cdd:cd16278 170 LAL-DDRLLLPGH 181
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 104-319 2.98e-19

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 86.00  E-value: 2.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352  104 SDNYSYLIIDTQ--AQLAVAVDPSDpRAVQ---ASIEKEGVTLVAILCTHKHWDHSGG-----NRDLSRRHRDCRVYGSP 173
Cdd:PLN02962  21 SSTYTYLLADVShpDKPALLIDPVD-KTVDrdlSLVKELGLKLIYAMNTHVHADHVTGtgllkTKLPGVKSIISKASGSK 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352  174 QDgipyltHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLL-DGEPYKGPSCLFSGDLLFLSGCGRT-FE-GNAETMLSS 250
Cdd:PLN02962 100 AD------LFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTgEGPDQPQPRMAFTGDALLIRGCGRTdFQgGSSDQLYKS 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352  251 LDT-VLGLGDDTLLWPGHEYaeenlgfagvvepenlarerkmqwvqrqrlerKGTCPSTLGEERSYNPFL 319
Cdd:PLN02962 174 VHSqIFTLPKDTLIYPAHDY--------------------------------KGFTVSTVGEEMLYNPRL 211
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 108-267 1.13e-17

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: 79.88  E-value: 1.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 108 SYLIIDTqAQLAVAVDPSDPRAVQASiekEGVTLVAILCTHKHWDHSGGNRDLSRRHRD--CRVYGSP---------QDG 176
Cdd:cd07722  28 RRILIDT-GEGRPSYIPLLKSVLDSE---GNATISDILLTHWHHDHVGGLPDVLDLLRGpsPRVYKFPrpeededpdEDG 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 177 IPYltHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGD-LLflsGCGRT-FEGNAETMlSSLDTV 254
Cdd:cd07722 104 GDI--HDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEEN-----ALFTGDcVL---GHGTAvFEDLAAYM-ASLKKL 172

                       170
                ....*....|...
gi 21703352 255 LGLGDDTlLWPGH 267
Cdd:cd07722 173 LSLGPGR-IYPGH 184
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 95-267 1.79e-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: 73.87  E-value: 1.79e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352  95 VKVLPIPVLSDNYSYLIIDTqaqlAVAVdPSDPRAVQASIEKEGVTLVAI---LCTHKHWDHSGGNRDLSRRhRDCRVYG 171
Cdd:cd07725  12 LGHVNVYLLRDGDETTLIDT----GLAT-EEDAEALWEGLKELGLKPSDIdrvLLTHHHPDHIGLAGKLQEK-SGATVYI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 172 SPqdgipylTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpSCLFSGD--LLFLSGCG----RTFEGNAE 245
Cdd:cd07725  86 LD-------VTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDR-----RELFVGDavLPKITPNVslwaVRVEDPLG 153

                       170       180
                ....*....|....*....|..
gi 21703352 246 TMLSSLDTVLGLGDDtLLWPGH 267
Cdd:cd07725 154 AYLESLDKLEKLDVD-LAYPGH 174
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 94-267 7.35e-14

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: 69.56  E-value: 7.35e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352  94 GVKVLPIPVLSdnYSYLIIDtqAQLAVAVD---PSDPRAVQASIEKEGVT---LVAILCTHKHWDHSGGNRDLsRRHRDC 167
Cdd:cd07721   1 GVYQLPLLPPV--NAYLIED--DDGLTLIDtglPGSAKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAAL-KEAPGA 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 168 RVYGSPQDgIPYLTH---PLCHQDVVSVGRLQ-------------------------IRALATPGHTQGHLVYLLDGEpy 219
Cdd:cd07721  76 PVYAHERE-APYLEGekpYPPPVRLGLLGLLSpllpvkpvpvdrtledgdtldlaggLRVIHTPGHTPGHISLYLEED-- 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 21703352 220 kgpSCLFSGDLLFLSGcGRTFEGNA------ETMLSSLDTVLGLGDDTLLwPGH 267
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 ...
 102-267 1.28e-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: 1.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 102 VLSDNYSYLIIDTqaqlavAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQDgIPYLT 181
Cdd:cd07743  13 YVFGDKEALLIDS------GLDEDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYL-QKKTGCKVYAPKIE-KAFIE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 182 HPL------------------------------CHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpsCLFSGDLL 231
Cdd:cd07743  85 NPLlepsylggayppkelrnkflmakpskvddiIEEGELELGGVGLEIIPLPGHSFGQIGILTPDG------VLFAGDAL 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 21703352 232 F----LSGCGRTFEGNAETMLSSLDTVLGLGDDTLLwPGH 267
Cdd:cd07743 159 FgeevLEKYGIPFLYDVEEQLETLEKLEELDADYYV-PGH 197
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
107-267 1.48e-13

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 68.55  E-value: 1.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352   107 YSYLIIDTQAqlAVAVDP--SDPRAVQASIEKEGV---TLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGS--------- 172
Cdd:pfam00753   7 NSYLIEGGGG--AVLIDTggSAEAALLLLLAALGLgpkDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAeearellde 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352   173 -------------PQDGIPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLldgepYKGPSCLFSGDLLFLSGCGRT 239
Cdd:pfam00753  85 elglaasrlglpgPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVY-----YGGGKVLFTGDLLFAGEIGRL 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 21703352   240 ----------FEGNAETMLSSLDTVLGLgDDTLLWPGH 267
Cdd:pfam00753 160 dlplggllvlHPSSAESSLESLLKLAKL-KAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 110-267 1.52e-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: 1.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 110 LIIDTQAQLAVAvdpsdpRAVQASIEKEG---VTLVAIlcTHKHWDHSGGN-----------------RDLSRRHRDCRV 169
Cdd:cd16282  27 VVIDTGASPRLA------RALLAAIRKVTdkpVRYVVN--THYHGDHTLGNaafadagapiiahentrEELAARGEAYLE 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 170 YGSPQDG-------IPYLTHPLCHQDVVSVGRLQIRALAT-PGHTQGHLVYLLDGEpykgpSCLFSGDLLFLSGCGRTFE 241
Cdd:cd16282  99 LMRRLGGdamagteLVLPDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEE-----GVLFAGDLVFNGRIPFLPD 173

                       170       180
                ....*....|....*....|....*.
gi 21703352 242 GNAETMLSSLDTVLGLGDDTLLwPGH 267
Cdd:cd16282 174 GSLAGWIAALDRLLALDATVVV-PGH 198
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 73-268 2.78e-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: 62.62  E-value: 2.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352  73 LRRARNRYPKGHSKTQPRLFNGVKVLPIpvlsdnYSYLI--------IDTQAQLAVAVDPSDPRAVQASIEKEGVTLVAI 144
Cdd:cd07729   5 LDYGTVTVDKSSLFYYGRGPGEPIDLPV------YAYLIehpegtilVDTGFHPDAADDPGGLELAFPPGVTEEQTLEEQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 145 L--------------CTHKHWDHSGGNRDL-------SRR-----HRDCRVYGSPQDGIPYLTHPLCHQDVVSV-GRLQ- 196
Cdd:cd07729  79 LarlgldpedidyviLSHLHFDHAGGLDLFpnatiivQRAeleyaTGPDPLAAGYYEDVLALDDDLPGGRVRLVdGDYDl 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 197 ---IRALATPGHTQGHLVYLLDGEpyKGPsCLFSGDL-----LFLSGCGRTFEGNAETMLSSLDTVLGL--GDDTLLWPG 266
Cdd:cd07729 159 fpgVTLIPTPGHTPGHQSVLVRLP--EGT-VLLAGDAaytyeNLEEGRPPGINYDPEAALASLERLKALaeREGARVIPG 235


                ..
gi 21703352 267 HE 268
Cdd:cd07729 236 HD 237
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 127-267 3.34e-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: 55.71  E-value: 3.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 127 PRAVQASIEKEgVTLVAilcTHKHWDHSGGN----------RDLSRRHRDCRVYGSPQDGIPY------LTHPLCHQDVV 190
Cdd:cd07712  33 KEYVRTLTDLP-LLVVA---THGHFDHIGGLhefeevyvhpADAEILAAPDNFETLTWDAATYsvppagPTLPLRDGDVI 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 191 SVGRLQIRALATPGHTQGHLVyLLDgepyKGPSCLFSGD------LLFLSGCgrtfeGNAETMLSSLDTVLGLGDD-TLL 263
Cdd:cd07712 109 DLGDRQLEVIHTPGHTPGSIA-LLD----RANRLLFSGDvvydgpLIMDLPH-----SDLDDYLASLEKLSKLPDEfDKV 178


                ....
gi 21703352 264 WPGH 267
Cdd:cd07712 179 LPGH 182
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 108-267 3.37e-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: 3.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 108 SYLIiDTQAQLAVaVDP---SDPRAVQASIEKEGVTLV---AILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQdGIPYLT 181
Cdd:cd07726  18 SYLL-DGEGRPAL-IDTgpsSSVPRLLAALEALGIAPEdvdYIILTHIHLDHAGGAGLLAEALPNAKVYVHPR-GARHLI 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 182 HP--------------------------------LCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpSCLFSGD 229
Cdd:cd07726  95 DPsklwasaravygdeadrlggeilpvpeervivLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEES-----DGLFTGD 169

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 21703352 230 LLFLSGCGRTFEG---------NAETMLSSLDTVLGLGDDTLLwPGH 267
Cdd:cd07726 170 AAGVRYPELDVVGppstpppdfDPEAWLESLDRLLSLKPERIY-LTH 215
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 108-208 7.48e-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: 7.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 108 SYLII-DTQAQLAVAVDPSDPRAVQASIEKEGVTLV---AILCTHKHWDHSGGnrdLSRRHRD--CRVYGSPQD------ 175
Cdd:cd16310  24 SYLITsNHGAILLDGGLEENAALIEQNIKALGFKLSdikIIINTHAHYDHAGG---LAQLKADtgAKLWASRGDrpalea 100

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 21703352 176 ----------GIPY----LTHPLCHQDVVSVGRLQIRALATPGHTQG 208
Cdd:cd16310 101 gkhigdnitqPAPFpavkVDRILGDGEKIKLGDITLTATLTPGHTKG 147
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 132-219 6.34e-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: 6.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 132 ASIEKEGV---TLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGS----------PQDGIPYLTHPLCHQDVV-------S 191
Cdd:cd16280  50 DGLEKLGLdpaDIKYILITHGHGDHYGGAAYL-KDLYGAKVVMSeadwdmmeepPEEGDNPRWGPPPERDIVikdgdtlT 128

                        90       100       110
                ....*....|....*....|....*....|..
gi 21703352 192 VGRLQIRALATPGHTQGHLVYLLD----GEPY 219
Cdd:cd16280 129 LGDTTITVYLTPGHTPGTLSLIFPvkdgGKTH 160
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 114-208 3.39e-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: 44.98  E-value: 3.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 114 TQAQLAVAVDPSDPRA---VQASIEKEGVTL---VAILCTHKHWDHSGGNRDLsRRHRDCRVYGSP------QDGIP--- 178
Cdd:cd16312  28 TSPQGHVLLDGALPQSaplIIANIEALGFRIedvKLILNSHAHWDHAGGIAAL-QKASGATVAASAhgaqvlQSGTNgkd 106

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 21703352 179 ---YLTHPLCH------------QDVVSVGRLQIRALATPGHTQG 208
Cdd:cd16312 107 dpqYQAKPVVHvakvakvkevgeGDTLKVGPLRLTAHMTPGHTPG 151
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 122-230 8.30e-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: 8.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 122 VDPSDPRAVQA---SIEKEG-----VTLVaiLCTHKHWDHSGGNRDLSR-RHrdcrVYGSPQDGIPYLTHPLCHQDVVSV 192
Cdd:cd07711  36 VDTGTPWDRDLllkALAEHGlspedIDYV--VLTHGHPDHIGNLNLFPNaTV----IVGWDICGDSYDDHSLEEGDGYEI 109

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 21703352 193 GrLQIRALATPGHTQGHLVYLLDGEPYKgpSCLFSGDL 230
Cdd:cd07711 110 D-ENVEVIPTPGHTPEDVSVLVETEKKG--TVAVAGDL 144
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
109-229 1.27e-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: 1.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 109 YLIID----TQAQL-AVAVDPSDPRAvqasiekegvtlvaILCTHKHWDHSGG------NRDLSRRHRDCRVYGsPQDGI 177
Cdd:COG1234  30 RLLIDcgegTQRQLlRAGLDPRDIDA--------------IFITHLHGDHIAGlpgllsTRSLAGREKPLTIYG-PPGTK 94

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21703352 178 PYLT----------------HPLCHQDVVSVGRLQIRALATPgHTQGHLVYLLDgepYKGPSCLFSGD 229
Cdd:COG1234  95 EFLEallkasgtdldfplefHEIEPGEVFEIGGFTVTAFPLD-HPVPAYGYRFE---EPGRSLVYSGD 158
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 108-208 1.52e-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: 42.82  E-value: 1.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 108 SYLIIDTQAQLAVAVD-PSDPRAVQASIEKEGVTLV---AILCTHKHWDHSGGNRDLSRR--------HRDCRV------ 169
Cdd:cd16307  24 SYLITTPRGNILINSNlESSVPQIKASIEKLGFKFSdtkILLISHAHFDHAAGSALIKREthakymvmDGDVDVvesggk 103

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 21703352 170 ----YGSPqdgiPYLTHPLCHQD-------VVSVGRLQIRALATPGHTQG 208
Cdd:cd16307 104 sdffYGND----PSTYFPPAHVDkvlhdgeQVELGGTVLTAHLTAGHTKG 149
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 197-232 1.65e-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: 1.65e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 21703352 197 IRALATPGHTQGHLVYLLDGepyKGPSCLFSGDLLF 232
Cdd:cd07720 175 ITAVPAPGHTPGHTGYRIES---GGERLLIWGDIVH 207
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 108-208 2.37e-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: 2.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 108 SYLIIDTQAqlAVAVDPSDPRAV---QASIEKEGVT---LVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQD------ 175
Cdd:cd16288  24 SYLITTPQG--LILIDTGLESSApmiKANIRKLGFKpsdIKILLNSHAHLDHAGGLAAL-KKLTGAKLMASAEDaallas 100

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 21703352 176 --------GIPYLTHP-------LCHQDVVSVGRLQIRALATPGHTQG 208
Cdd:cd16288 101 ggksdfhyGDDSLAFPpvkvdrvLKDGDRVTLGGTTLTAHLTPGHTRG 148
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 197-234 3.16e-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: 41.03  E-value: 3.16e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 21703352 197 IRALATPGHTQGHLVYLldgepYKGPSCLFSGDLLFLS 234
Cdd:cd07727 104 LTLIPVPGHTRGSVVLL-----YKEKGVLFTGDHLAWS 136
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 137-231 6.14e-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: 40.58  E-value: 6.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21703352 137 EGVTLVaiLCTHKHWDHSGGN---------------------RDLSRRHRDCRVYGSPQDGIPYLTHPlchqdVVSVGRL 195
Cdd:cd16277  62 EDVDYV--LCTHLHVDHVGWNtrlvdgrwvptfpnarylfsrAEYDHWSSPDAGGPPNRGVFEDSVLP-----VIEAGLA 134

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 21703352 196 Q-----------IRALATPGHTQGHLVYLLDGEpykGPSCLFSGDLL 231
Cdd:cd16277 135 DlvdddheildgIRLEPTPGHTPGHVSVELESG---GERALFTGDVM 178
 
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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