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Conserved domains on  [gi|119591009|gb|EAW70603|]
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paroxysmal nonkinesiogenic dyskinesia, isoform CRA_b [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 119591009   97 VLPIPVLSDNYSYLIIDTQAQlAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDG 176
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAF-PAPVYGPAEER 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009  177 IPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLG 256
Cdd:TIGR03413  79 IPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPA-----LFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009  257 LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALgpgpGP 336
Cdd:TIGR03413 154 LPDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAAL----GS 229

                         250       260
                  ....*....|....*....|
gi 119591009  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 119591009   97 VLPIPVLSDNYSYLIIDTQAQlAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDG 176
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAF-PAPVYGPAEER 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009  177 IPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLG 256
Cdd:TIGR03413  79 IPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPA-----LFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009  257 LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALgpgpGP 336
Cdd:TIGR03413 154 LPDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAAL----GS 229

                         250       260
                  ....*....|....*....|
gi 119591009  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 119591009  99 PIPVLSDNYSYLIIDTQAQLAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQDGIP 178
Cdd:cd07723    2 PIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAEDRIP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 179 YLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLGLG 258
Cdd:cd07723   82 GLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEP-----ALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLALP 156


                 ....*....
gi 119591009 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 119591009  96 KVLPIPVLSDNYSYLIIDTQAQLAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQD 175
Cdd:PLN02469   2 KIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 176 GIPYLTHPLCHQDVVSVGR-LQIRALATPGHTQGHLVYLLDGEPYKGPScLFSGDLLFLSGCGRTFEGNAETMLSSLDTV 254
Cdd:PLN02469  82 NVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDPA-VFTGDTLFIAGCGKFFEGTAEQMYQSLCVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 255 LG-LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALGpg 333
Cdd:PLN02469 161 LGsLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVG-- 238

                        250       260
                 ....*....|....*....|...
gi 119591009 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 119591009 101 PVLSDNYSYLIIDTQAqlAVAVDP----SDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQDg 176
Cdd:COG0491   10 GAGLGVNSYLIVGGDG--AVLIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAAL-AEAFGAPVYAHAAE- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 177 IPYLT----------------HPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRT- 239
Cdd:COG0491   86 AEALEapaagalfgrepvppdRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKV-----LFTGDALFSGGVGRPd 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 240 -FEGNAETMLSSLDTVLGLGDDtLLWPGHEYAeenlgfagvvepenlarerkmqwVQRQRLERKGTCPSTLGEERsyNPF 318
Cdd:COG0491  161 lPDGDLAQWLASLERLLALPPD-LVIPGHGPP-----------------------TTAEAIDYLEELLAALGERA--NPF 214


                 .
gi 119591009 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 119591009   107 YSYLIIDTQAqlAVAVDP--SDPRAVQASIEKEGV-TLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQD-------- 175
Cdd:smart00849   1 NSYLVRDDGG--AILIDTgpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAP-GAPVYAPEGTaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009   176 ----------GIPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTF-EGNA 244
Cdd:smart00849  78 allgelgaeaEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKI-----LFTGDLLFAGGDGRTLvDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 119591009   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 119591009  268 EYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALGPGpgptgdddySRAQL 347
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGET---------DPVEV 71


                  ....*....
gi 119591009  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 119591009   97 VLPIPVLSDNYSYLIIDTQAQlAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDG 176
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAF-PAPVYGPAEER 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009  177 IPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLG 256
Cdd:TIGR03413  79 IPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPA-----LFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009  257 LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALgpgpGP 336
Cdd:TIGR03413 154 LPDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAAL----GS 229

                         250       260
                  ....*....|....*....|
gi 119591009  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 119591009  99 PIPVLSDNYSYLIIDTQAQLAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQDGIP 178
Cdd:cd07723    2 PIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAEDRIP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 179 YLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLGLG 258
Cdd:cd07723   82 GLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEP-----ALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLALP 156


                 ....*....
gi 119591009 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 119591009  96 KVLPIPVLSDNYSYLIIDTQAQLAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQD 175
Cdd:PLN02469   2 KIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 176 GIPYLTHPLCHQDVVSVGR-LQIRALATPGHTQGHLVYLLDGEPYKGPScLFSGDLLFLSGCGRTFEGNAETMLSSLDTV 254
Cdd:PLN02469  82 NVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDPA-VFTGDTLFIAGCGKFFEGTAEQMYQSLCVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 255 LG-LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALGpg 333
Cdd:PLN02469 161 LGsLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVG-- 238

                        250       260
                 ....*....|....*....|...
gi 119591009 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 119591009  29 SPRGCRARRGLRGLLMAHSQrLLFRIGYsLYTRTWLGYLFYRQqLRRARNRYPKGHSKTQPRLFNGVKVLPIPVLSDNYS 108
Cdd:PLN02398  13 SFRCSRRIRGQLCVRPGVRQ-LCLRKSL-LYGVMKLLSMPLKT-LRGAGRTLKVAQFCSVSNVSSSLQIELVPCLKDNYA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 109 YLIIDTQAQLAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSP--QDGIPYLTHPLCH 186
Cdd:PLN02398  90 YLLHDEDTGTVGVVDPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARY-GAKVIGSAvdKDRIPGIDIVLKD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 187 QDVVSVGRLQIRALATPGHTQGHLVYLldgepYKGPSCLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLGLGDDTLLWPG 266
Cdd:PLN02398 169 GDKWMFAGHEVLVMETPGHTRGHISFY-----FPGSGAIFTGDTLFSLSCGKLFEGTPEQMLSSLQKIISLPDDTNIYCG 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 267 HEYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALGPgpgPTGDDDysrAQ 346
Cdd:PLN02398 244 HEYTLSNSKFALSIEPNNEVLQSYAAHVAHLRSKGLPTIPTTVKMEKACNPFLRTSSTDIRKSLSI---PDTADE---AE 317

                        330
                 ....*....|
gi 119591009 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 119591009 105 DNYSYLIIDTQAQLAVAVDPS-DPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDgIPYLT-- 181
Cdd:cd16275   11 INYSYIIIDKATREAAVVDPAwDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKY-DAPVYMSKEE-IDYYGfr 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 182 ----HPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGepykgpsCLFSGDLLFLSGCGRT--FEGNAETMLSSLDTVL 255
Cdd:cd16275   89 cpnlIPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGD-------SLFTGDTLFIEGCGRCdlPGGDPEEMYESLQRLK 161

                        170
                 ....*....|...
gi 119591009 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 119591009 100 IPVLSDNYSYLIIDTQAQlAVAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQDGIPY 179
Cdd:PRK10241   6 IPAFDDNYIWVLNDEAGR-CLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQETQDKG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 180 LTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLldGEPYkgpscLFSGDLLFLSGCGRTFEGNAETMLSSLDTVLGLGD 259
Cdd:PRK10241  85 TTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF--SKPY-----LFCGDTLFSGGCGRLFEGTASQMYQSLKKINALPD 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119591009 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 119591009 107 YSYLIIDTQAQLAVAVDPSDPRA--VQASIEKEGVTLVAILCTHKHWDH-SGGnRDLSRRHrDCRVYGSPQDGIPYLTHP 183
Cdd:cd07724   13 LSYLVGDPETGEAAVIDPVRDSVdrYLDLAAELGLKITYVLETHVHADHvSGA-RELAERT-GAPIVIGEGAPASFFDRL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 184 LCHQDVVSVGRLQIRALATPGHTQGHLVYLLDgepykGPSCLFSGDLLFLSGCGRT-----FEGNAETMLSSL-DTVLGL 257
Cdd:cd07724   91 LKDGDVLELGNLTLEVLHTPGHTPESVSYLVG-----DPDAVFTGDTLFVGDVGRPdlpgeAEGLARQLYDSLqRKLLLL 165

                        170
                 ....*....|..
gi 119591009 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 119591009 101 PVLSDNYSYLIIDTQAqlAVAVDP----SDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQDg 176
Cdd:COG0491   10 GAGLGVNSYLIVGGDG--AVLIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAAL-AEAFGAPVYAHAAE- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 177 IPYLT----------------HPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRT- 239
Cdd:COG0491   86 AEALEapaagalfgrepvppdRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKV-----LFTGDALFSGGVGRPd 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 240 -FEGNAETMLSSLDTVLGLGDDtLLWPGHEYAeenlgfagvvepenlarerkmqwVQRQRLERKGTCPSTLGEERsyNPF 318
Cdd:COG0491  161 lPDGDLAQWLASLERLLALPPD-LVIPGHGPP-----------------------TTAEAIDYLEELLAALGERA--NPF 214


                 .
gi 119591009 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 119591009  96 KVLPIPVLSDNySYLIIDTQAQlAVAVDPSDP--RAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSP 173
Cdd:cd06262    1 KRLPVGPLQTN-CYLVSDEEGE-AILIDPGAGalEKILEAIEELGLKIKAILLTHGHFDHIGGLAEL-KEAPGAPVYIHE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 174 QDgIPYLTHPLCHQ--------------------DVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGDLLFL 233
Cdd:cd06262   78 AD-AELLEDPELNLaffgggplpppepdilledgDTIELGGLELEVIHTPGHTPGSVCFYIEEEG-----VLFTGDTLFA 151

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 119591009 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 119591009  95 VKVLPIPVLSDNySYLIIDTQAQLAVAVDPSDPR-AVQASIEKEGVTLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSP 173
Cdd:cd16322    1 VRPFTLGPLQEN-TYLVADEGGGEAVLVDPGDESeKLLARFGTTGLTLLYILLTHAHFDHVGGVADL-RRHPGAPVYLHP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 174 QD----------------GIPYLT---HPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpSCLFSGDLLFLS 234
Cdd:cd16322   79 DDlplyeaadlgakafglGIEPLPppdRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEE-----GLLFSGDLLFQG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 235 GCGRT--FEGNAETMLSSLDTVLGLGDDTLLWPGHeyaeenlgfaGVvepenlarerkmqwvqrqrlerkgtcPSTLGEE 312
Cdd:cd16322  154 SIGRTdlPGGDPKAMAASLRRLLTLPDETRVFPGH----------GP--------------------------PTTLGEE 197


                 ....*..
gi 119591009 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 119591009   107 YSYLIIDTQAqlAVAVDP--SDPRAVQASIEKEGV-TLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQD-------- 175
Cdd:smart00849   1 NSYLVRDDGG--AILIDTgpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAP-GAPVYAPEGTaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009   176 ----------GIPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTF-EGNA 244
Cdd:smart00849  78 allgelgaeaEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKI-----LFTGDLLFAGGDGRTLvDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 119591009   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 119591009  268 EYAEENLGFAGVVEPENLARERKMQWVQRQRLERKGTCPSTLGEERSYNPFLRTHCLALQEALGPGpgptgdddySRAQL 347
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGET---------DPVEV 71


                  ....*....
gi 119591009  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 119591009 100 IPV--LSDNySYLIIDTQAQLAVAVDP-SDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQD- 175
Cdd:cd07737    4 IPVtpFQQN-CSLIWCEETKEAAVIDPgGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAEL-AEHYGVPIIGPHKEd 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 176 --------------GIPYL-----THPLCHQDVVSVGRLQIRALATPGHTQGHLVYLldGEPYKgpsCLFSGDLLFLSGC 236
Cdd:cd07737   82 kfllenlpeqsqmfGFPPAeaftpDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFF--NRESK---LAIVGDVLFKGSI 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 119591009 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 119591009 108 SYlIIDTQAQLAVaVDP--SDPRAVQASIEK-EGVTLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDGIPYL---- 180
Cdd:cd16278   20 TY-LLGAPDGVVV-IDPgpDDPAHLDALLAAlGGGRVSAILVTHTHRDHSPGAARLAERT-GAPVRAFGPHRAGGQdtdf 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 181 --THPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGDLLFlsGCGRTF----EGNAETMLSSLDTV 254
Cdd:cd16278   97 apDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEG-----ALFTGDHVM--GWSTTViappDGDLGDYLASLERL 169

                        170
                 ....*....|...
gi 119591009 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 119591009 104 SDNYSYLIIDTQ--AQLAVAVDPSDpRAVQ---ASIEKEGVTLVAILCTHKHWDHSGG-----NRDLSRRHRDCRVYGSP 173
Cdd:PLN02962  21 SSTYTYLLADVShpDKPALLIDPVD-KTVDrdlSLVKELGLKLIYAMNTHVHADHVTGtgllkTKLPGVKSIISKASGSK 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 174 QDgipyltHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLL-DGEPYKGPSCLFSGDLLFLSGCGRT-FE-GNAETMLSS 250
Cdd:PLN02962 100 AD------LFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTgEGPDQPQPRMAFTGDALLIRGCGRTdFQgGSSDQLYKS 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 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 119591009 108 SYLIIDTqAQLAVAVDPSDPRAVQASiekEGVTLVAILCTHKHWDHSGGNRDLSRRHRD--CRVYGSP---------QDG 176
Cdd:cd07722   28 RRILIDT-GEGRPSYIPLLKSVLDSE---GNATISDILLTHWHHDHVGGLPDVLDLLRGpsPRVYKFPrpeededpdEDG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 177 IPYltHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGD-LLflsGCGRT-FEGNAETMlSSLDTV 254
Cdd:cd07722  104 GDI--HDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEEN-----ALFTGDcVL---GHGTAvFEDLAAYM-ASLKKL 172

                        170
                 ....*....|...
gi 119591009 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 119591009  95 VKVLPIPVLSDNYSYLIIDTqaqlAVAVdPSDPRAVQASIEKEGVTLVAI---LCTHKHWDHSGGNRDLSRRhRDCRVYG 171
Cdd:cd07725   12 LGHVNVYLLRDGDETTLIDT----GLAT-EEDAEALWEGLKELGLKPSDIdrvLLTHHHPDHIGLAGKLQEK-SGATVYI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 172 SPqdgipylTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpSCLFSGD--LLFLSGCG----RTFEGNAE 245
Cdd:cd07725   86 LD-------VTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDR-----RELFVGDavLPKITPNVslwaVRVEDPLG 153

                        170       180
                 ....*....|....*....|..
gi 119591009 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 119591009  94 GVKVLPIPVLSdnYSYLIIDtqAQLAVAVD---PSDPRAVQASIEKEGVT---LVAILCTHKHWDHSGGNRDLsRRHRDC 167
Cdd:cd07721    1 GVYQLPLLPPV--NAYLIED--DDGLTLIDtglPGSAKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAAL-KEAPGA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 168 RVYGSPQDgIPYLTH---PLCHQDVVSVGRLQ-------------------------IRALATPGHTQGHLVYLLDGEpy 219
Cdd:cd07721   76 PVYAHERE-APYLEGekpYPPPVRLGLLGLLSpllpvkpvpvdrtledgdtldlaggLRVIHTPGHTPGHISLYLEED-- 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119591009 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 119591009 102 VLSDNYSYLIIDTqaqlavAVDPSDPRAVQASIEKEGVTLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQDgIPYLT 181
Cdd:cd07743   13 YVFGDKEALLIDS------GLDEDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYL-QKKTGCKVYAPKIE-KAFIE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 182 HPL------------------------------CHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpsCLFSGDLL 231
Cdd:cd07743   85 NPLlepsylggayppkelrnkflmakpskvddiIEEGELELGGVGLEIIPLPGHSFGQIGILTPDG------VLFAGDAL 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 119591009 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 119591009  107 YSYLIIDTQAqlAVAVDP--SDPRAVQASIEKEGV---TLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGS--------- 172
Cdd:pfam00753   7 NSYLIEGGGG--AVLIDTggSAEAALLLLLAALGLgpkDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAeearellde 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009  173 -------------PQDGIPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLldgepYKGPSCLFSGDLLFLSGCGRT 239
Cdd:pfam00753  85 elglaasrlglpgPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVY-----YGGGKVLFTGDLLFAGEIGRL 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 119591009  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 119591009 110 LIIDTQAQLAVAvdpsdpRAVQASIEKEG---VTLVAIlcTHKHWDHSGGN-----------------RDLSRRHRDCRV 169
Cdd:cd16282   27 VVIDTGASPRLA------RALLAAIRKVTdkpVRYVVN--THYHGDHTLGNaafadagapiiahentrEELAARGEAYLE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 170 YGSPQDG-------IPYLTHPLCHQDVVSVGRLQIRALAT-PGHTQGHLVYLLDGEpykgpSCLFSGDLLFLSGCGRTFE 241
Cdd:cd16282   99 LMRRLGGdamagteLVLPDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEE-----GVLFAGDLVFNGRIPFLPD 173

                        170       180
                 ....*....|....*....|....*.
gi 119591009 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 119591009  73 LRRARNRYPKGHSKTQPRLFNGVKVLPIpvlsdnYSYLI--------IDTQAQLAVAVDPSDPRAVQASIEKEGVTLVAI 144
Cdd:cd07729    5 LDYGTVTVDKSSLFYYGRGPGEPIDLPV------YAYLIehpegtilVDTGFHPDAADDPGGLELAFPPGVTEEQTLEEQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 145 L--------------CTHKHWDHSGGNRDL-------SRR-----HRDCRVYGSPQDGIPYLTHPLCHQDVVSV-GRLQ- 196
Cdd:cd07729   79 LarlgldpedidyviLSHLHFDHAGGLDLFpnatiivQRAeleyaTGPDPLAAGYYEDVLALDDDLPGGRVRLVdGDYDl 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 197 ---IRALATPGHTQGHLVYLLDGEpyKGPsCLFSGDL-----LFLSGCGRTFEGNAETMLSSLDTVLGL--GDDTLLWPG 266
Cdd:cd07729  159 fpgVTLIPTPGHTPGHQSVLVRLP--EGT-VLLAGDAaytyeNLEEGRPPGINYDPEAALASLERLKALaeREGARVIPG 235


                 ..
gi 119591009 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 119591009 127 PRAVQASIEKEgVTLVAilcTHKHWDHSGGN----------RDLSRRHRDCRVYGSPQDGIPY------LTHPLCHQDVV 190
Cdd:cd07712   33 KEYVRTLTDLP-LLVVA---THGHFDHIGGLhefeevyvhpADAEILAAPDNFETLTWDAATYsvppagPTLPLRDGDVI 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 191 SVGRLQIRALATPGHTQGHLVyLLDgepyKGPSCLFSGD------LLFLSGCgrtfeGNAETMLSSLDTVLGLGDD-TLL 263
Cdd:cd07712  109 DLGDRQLEVIHTPGHTPGSIA-LLD----RANRLLFSGDvvydgpLIMDLPH-----SDLDDYLASLEKLSKLPDEfDKV 178


                 ....
gi 119591009 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 119591009 108 SYLIiDTQAQLAVaVDP---SDPRAVQASIEKEGVTLV---AILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQdGIPYLT 181
Cdd:cd07726   18 SYLL-DGEGRPAL-IDTgpsSSVPRLLAALEALGIAPEdvdYIILTHIHLDHAGGAGLLAEALPNAKVYVHPR-GARHLI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119591009 182 HP--------------------------------LCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpSCLFSGD 229
Cdd:cd07726   95 DPsklwasaravygdeadrlggeilpvpeervivLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEES-----DGLFTGD 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 119591009 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 119591009 108 SYLII-DTQAQLAVAVDPSDPRAVQASIEKEGVTLV---AILCTHKHWDHSGGnrdLSRRHRD--CRVYGSPQD------ 175
Cdd:cd16310   24 SYLITsNHGAILLDGGLEENAALIEQNIKALGFKLSdikIIINTHAHYDHAGG---LAQLKADtgAKLWASRGDrpalea 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 119591009 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 119591009 132 ASIEKEGV---TLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGS----------PQDGIPYLTHPLCHQDVV-------S 191
Cdd:cd16280   50 DGLEKLGLdpaDIKYILITHGHGDHYGGAAYL-KDLYGAKVVMSeadwdmmeepPEEGDNPRWGPPPERDIVikdgdtlT 128

                         90       100       110
                 ....*....|....*....|....*....|..
gi 119591009 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 119591009 114 TQAQLAVAVDPSDPRA---VQASIEKEGVTL---VAILCTHKHWDHSGGNRDLsRRHRDCRVYGSP------QDGIP--- 178
Cdd:cd16312   28 TSPQGHVLLDGALPQSaplIIANIEALGFRIedvKLILNSHAHWDHAGGIAAL-QKASGATVAASAhgaqvlQSGTNgkd 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 119591009 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 119591009 122 VDPSDPRAVQA---SIEKEG-----VTLVaiLCTHKHWDHSGGNRDLSR-RHrdcrVYGSPQDGIPYLTHPLCHQDVVSV 192
Cdd:cd07711   36 VDTGTPWDRDLllkALAEHGlspedIDYV--VLTHGHPDHIGNLNLFPNaTV----IVGWDICGDSYDDHSLEEGDGYEI 109

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 119591009 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 119591009 109 YLIID----TQAQL-AVAVDPSDPRAvqasiekegvtlvaILCTHKHWDHSGG------NRDLSRRHRDCRVYGsPQDGI 177
Cdd:COG1234   30 RLLIDcgegTQRQLlRAGLDPRDIDA--------------IFITHLHGDHIAGlpgllsTRSLAGREKPLTIYG-PPGTK 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119591009 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 119591009 108 SYLIIDTQAQLAVAVD-PSDPRAVQASIEKEGVTLV---AILCTHKHWDHSGGNRDLSRR--------HRDCRV------ 169
Cdd:cd16307   24 SYLITTPRGNILINSNlESSVPQIKASIEKLGFKFSdtkILLISHAHFDHAAGSALIKREthakymvmDGDVDVvesggk 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 119591009 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 119591009 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 119591009 108 SYLIIDTQAqlAVAVDPSDPRAV---QASIEKEGVT---LVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQD------ 175
Cdd:cd16288   24 SYLITTPQG--LILIDTGLESSApmiKANIRKLGFKpsdIKILLNSHAHLDHAGGLAAL-KKLTGAKLMASAEDaallas 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 119591009 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 119591009 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 119591009 137 EGVTLVaiLCTHKHWDHSGGN---------------------RDLSRRHRDCRVYGSPQDGIPYLTHPlchqdVVSVGRL 195
Cdd:cd16277   62 EDVDYV--LCTHLHVDHVGWNtrlvdgrwvptfpnarylfsrAEYDHWSSPDAGGPPNRGVFEDSVLP-----VIEAGLA 134

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 119591009 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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