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Conserved domains on  [gi|9910442|ref|NP_064383|]
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probable hydrolase PNKD isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GSH_gloB super family cl30131
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 96-355 2.72e-94

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: 281.35  E-value: 2.72e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442     96 VLPIPVLSDNYSYLIIDTQaGLAVAVDPSDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDG 175
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPD-GQAAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAF-PAPVYGPAEER 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442    176 IPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTFEGTAETMLSSLDTVLD 255
Cdd:TIGR03413  79 IPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPA-----LFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442    256 LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRMERKSTCPSTLGEERAYNPFLRTHCLELQEALGPgpgp 335
Cdd:TIGR03413 154 LPDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAALGS---- 229

                         250       260
                  ....*....|....*....|
gi 9910442    336 tsdDGCSRAQLLEELRRLKD 355
Cdd:TIGR03413 230 ---QGADPVEVFAALRAWKD 246
 
Name Accession Description Interval E-value
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 96-355 2.72e-94

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: 281.35  E-value: 2.72e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442     96 VLPIPVLSDNYSYLIIDTQaGLAVAVDPSDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDG 175
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPD-GQAAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAF-PAPVYGPAEER 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442    176 IPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTFEGTAETMLSSLDTVLD 255
Cdd:TIGR03413  79 IPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPA-----LFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442    256 LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRMERKSTCPSTLGEERAYNPFLRTHCLELQEALGPgpgp 335
Cdd:TIGR03413 154 LPDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAALGS---- 229

                         250       260
                  ....*....|....*....|
gi 9910442    336 tsdDGCSRAQLLEELRRLKD 355
Cdd:TIGR03413 230 ---QGADPVEVFAALRAWKD 246
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 98-266 3.37e-88

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 262.78  E-value: 3.37e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442   98 PIPVLSDNYSYLIIDTQAGLAVAVDPSDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQDGIP 177
Cdd:cd07723   2 PIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAEDRIP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  178 YLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGDLLFLSGCGRTFEGTAETMLSSLDTVLDLG 257
Cdd:cd07723  82 GLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEP-----ALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLALP 156


                ....*....
gi 9910442  258 DDTLLWPGH 266
Cdd:cd07723 157 DDTLVYCGH 165
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 95-355 1.95e-86

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 261.62  E-value: 1.95e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442    95 KVLPIPVLSDNYSYLIIDTQAGLAVAVDPSDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQD 174
Cdd:PLN02469   2 KIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442   175 GIPYLTHPLCHQDVVSVGR-LQIRALATPGHTQGHLVYLLDGEPYKGPScLFSGDLLFLSGCGRTFEGTAETMLSSLDTV 253
Cdd:PLN02469  82 NVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDPA-VFTGDTLFIAGCGKFFEGTAEQMYQSLCVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442   254 L-DLGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRMERKSTCPSTLGEERAYNPFLRTHCLELQEALgpg 332
Cdd:PLN02469 161 LgSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKV--- 237

                        250       260
                 ....*....|....*....|....
gi 9910442   333 pgptsddGC-SRAQLLEELRRLKD 355
Cdd:PLN02469 238 -------GCeSPVEALREVRKMKD 254
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 100-318 6.23e-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: 137.90  E-value: 6.23e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  100 PVLSDNYSYLIIDTqaGLAVAVDP----SDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQDg 175
Cdd:COG0491  10 GAGLGVNSYLIVGG--DGAVLIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAAL-AEAFGAPVYAHAAE- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  176 IPYLT----------------HPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRT- 238
Cdd:COG0491  86 AEALEapaagalfgrepvppdRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKV-----LFTGDALFSGGVGRPd 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  239 -FEGTAETMLSSLDTVLDLGDDtLLWPGHEYAeenlgfagvvepenlarerkmqwVQRQRMERKSTCPSTLGEERayNPF 317
Cdd:COG0491 161 lPDGDLAQWLASLERLLALPPD-LVIPGHGPP-----------------------TTAEAIDYLEELLAALGERA--NPF 214


                .
gi 9910442  318 L 318
Cdd:COG0491 215 L 215
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 106-266 9.99e-29

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 109.57  E-value: 9.99e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442     106 YSYLIIDTqaGLAVAVDP--SDPRAVQASIEKERV-NLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQD-------- 174
Cdd:smart00849   1 NSYLVRDD--GGAILIDTgpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAP-GAPVYAPEGTaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442     175 ----------GIPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpSCLFSGDLLFLSGCGRTF-EGTA 243
Cdd:smart00849  78 allgelgaeaEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEG-----KILFTGDLLFAGGDGRTLvDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 9910442     244 ETMLSSLDTVLDL--GDDTLLWPGH 266
Cdd:smart00849 153 AAASDALESLLKLlkLLPKLVVPGH 177
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 267-355 4.61e-28

Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of hydroxyacylglutathione hydrolase enzymes. Substrate binding occurs at the interface between this domain and the catalytic domain (pfam00753).


Pssm-ID: 465030 [Multi-domain]  Cd Length: 82  Bit Score: 104.83  E-value: 4.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442    267 EYAEENLGFAGVVEPENLARERKMQWVQRQRMERKSTCPSTLGEERAYNPFLRTHCLELQEALGpgpgptsddGCSRAQL 346
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATG---------ETDPVEV 71


                  ....*....
gi 9910442    347 LEELRRLKD 355
Cdd:pfam16123  72 FAALRELKD 80
 
Name Accession Description Interval E-value
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 96-355 2.72e-94

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: 281.35  E-value: 2.72e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442     96 VLPIPVLSDNYSYLIIDTQaGLAVAVDPSDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDG 175
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPD-GQAAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAF-PAPVYGPAEER 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442    176 IPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRTFEGTAETMLSSLDTVLD 255
Cdd:TIGR03413  79 IPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPA-----LFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442    256 LGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRMERKSTCPSTLGEERAYNPFLRTHCLELQEALGPgpgp 335
Cdd:TIGR03413 154 LPDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAALGS---- 229

                         250       260
                  ....*....|....*....|
gi 9910442    336 tsdDGCSRAQLLEELRRLKD 355
Cdd:TIGR03413 230 ---QGADPVEVFAALRAWKD 246
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 98-266 3.37e-88

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 262.78  E-value: 3.37e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442   98 PIPVLSDNYSYLIIDTQAGLAVAVDPSDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQDGIP 177
Cdd:cd07723   2 PIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPAEDRIP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  178 YLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGDLLFLSGCGRTFEGTAETMLSSLDTVLDLG 257
Cdd:cd07723  82 GLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEP-----ALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLALP 156


                ....*....
gi 9910442  258 DDTLLWPGH 266
Cdd:cd07723 157 DDTLVYCGH 165
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 95-355 1.95e-86

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 261.62  E-value: 1.95e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442    95 KVLPIPVLSDNYSYLIIDTQAGLAVAVDPSDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQD 174
Cdd:PLN02469   2 KIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSLD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442   175 GIPYLTHPLCHQDVVSVGR-LQIRALATPGHTQGHLVYLLDGEPYKGPScLFSGDLLFLSGCGRTFEGTAETMLSSLDTV 253
Cdd:PLN02469  82 NVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGEDPA-VFTGDTLFIAGCGKFFEGTAEQMYQSLCVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442   254 L-DLGDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRMERKSTCPSTLGEERAYNPFLRTHCLELQEALgpg 332
Cdd:PLN02469 161 LgSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKV--- 237

                        250       260
                 ....*....|....*....|....
gi 9910442   333 pgptsddGC-SRAQLLEELRRLKD 355
Cdd:PLN02469 238 -------GCeSPVEALREVRKMKD 254
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 99-355 1.96e-53

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 179.27  E-value: 1.96e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442    99 IPVLSDNYSYLIIDTQAGLAVAVDPSDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSP--QDGI 176
Cdd:PLN02398  81 VPCLKDNYAYLLHDEDTGTVGVVDPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARY-GAKVIGSAvdKDRI 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442   177 PYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLldgepYKGPSCLFSGDLLFLSGCGRTFEGTAETMLSSLDTVLDL 256
Cdd:PLN02398 160 PGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFY-----FPGSGAIFTGDTLFSLSCGKLFEGTPEQMLSSLQKIISL 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442   257 GDDTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRMERKSTCPSTLGEERAYNPFLRTHCLELQEALG-PGpgp 335
Cdd:PLN02398 235 PDDTNIYCGHEYTLSNSKFALSIEPNNEVLQSYAAHVAHLRSKGLPTIPTTVKMEKACNPFLRTSSTDIRKSLSiPD--- 311

                        250       260
                 ....*....|....*....|
gi 9910442   336 TSDDgcsrAQLLEELRRLKD 355
Cdd:PLN02398 312 TADE----AEALGIIRRAKD 327
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 104-266 5.63e-44

Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; Bacillus amyloliquefaciens BaeB may play a role in the synthesis of the antibiotic polyketide bacillaene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293833 [Multi-domain]  Cd Length: 174  Bit Score: 149.61  E-value: 5.63e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  104 DNYSYLIIDTQAGLAVAVDPS-DPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDgIPYLT-- 180
Cdd:cd16275  11 INYSYIIIDKATREAAVVDPAwDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKY-DAPVYMSKEE-IDYYGfr 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  181 ----HPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGepykgpsCLFSGDLLFLSGCGRT--FEGTAETMLSSLDTVL 254
Cdd:cd16275  89 cpnlIPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGD-------SLFTGDTLFIEGCGRCdlPGGDPEEMYESLQRLK 161

                       170
                ....*....|...
gi 9910442  255 DL-GDDTLLWPGH 266
Cdd:cd16275 162 KLpPPNTRVYPGH 174
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 99-325 1.16e-43

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 151.52  E-value: 1.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442    99 IPVLSDNYSYLIIDtQAGLAVAVDPSDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQDGIPY 178
Cdd:PRK10241   6 IPAFDDNYIWVLND-EAGRCLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQETQDKG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442   179 LTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLldGEPYkgpscLFSGDLLFLSGCGRTFEGTAETMLSSLDTVLDLGD 258
Cdd:PRK10241  85 TTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF--SKPY-----LFCGDTLFSGGCGRLFEGTASQMYQSLKKINALPD 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9910442   259 DTLLWPGHEYAEENLGFAGVVEPENLARERKMQWVQRQRMERKSTCPSTLGEERAYNPFLRTHCLEL 325
Cdd:PRK10241 158 DTLICCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINLFLRTEDIDL 224
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 106-268 4.11e-40

ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; MBL-fold metallo-hydrolase domain; Persulfide dioxygenase (PDO, also known as sulfur dioxygenase, SDO, EC 1.13.11.18) is a non-heme iron-dependent oxygenase which catalyzes the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria. Mutations in ethe1 (the human PDO gene) are responsible for a rare autosomal recessive metabolic disorder called ethylmalonic encephalopathy. Arabidopsis thaliana ETHE1 is essential for embryo and endosperm development. Bacterial ETHE1-type PDOs are also called Type 1 PDOs. Type II PDOs (also called PDOAs), are mainly proteobacterial. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293810 [Multi-domain]  Cd Length: 177  Bit Score: 139.46  E-value: 4.11e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  106 YSYLIIDTQAGLAVAVDPSDPRA--VQASIEKERVNLVAILCTHKHWDH-SGGnRDLSRRHrDCRVYGSPQDGIPYLTHP 182
Cdd:cd07724  13 LSYLVGDPETGEAAVIDPVRDSVdrYLDLAAELGLKITYVLETHVHADHvSGA-RELAERT-GAPIVIGEGAPASFFDRL 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  183 LCHQDVVSVGRLQIRALATPGHTQGHLVYLLDgepykGPSCLFSGDLLFLSGCGRT-----FEGTAETMLSSL-DTVLDL 256
Cdd:cd07724  91 LKDGDVLELGNLTLEVLHTPGHTPESVSYLVG-----DPDAVFTGDTLFVGDVGRPdlpgeAEGLARQLYDSLqRKLLLL 165

                       170
                ....*....|..
gi 9910442  257 GDDTLLWPGHEY 268
Cdd:cd07724 166 PDETLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 100-318 6.23e-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: 137.90  E-value: 6.23e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  100 PVLSDNYSYLIIDTqaGLAVAVDP----SDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQDg 175
Cdd:COG0491  10 GAGLGVNSYLIVGG--DGAVLIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAAL-AEAFGAPVYAHAAE- 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  176 IPYLT----------------HPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPYkgpscLFSGDLLFLSGCGRT- 238
Cdd:COG0491  86 AEALEapaagalfgrepvppdRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKV-----LFTGDALFSGGVGRPd 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  239 -FEGTAETMLSSLDTVLDLGDDtLLWPGHEYAeenlgfagvvepenlarerkmqwVQRQRMERKSTCPSTLGEERayNPF 317
Cdd:COG0491 161 lPDGDLAQWLASLERLLALPPD-LVIPGHGPP-----------------------TTAEAIDYLEELLAALGERA--NPF 214


                .
gi 9910442  318 L 318
Cdd:COG0491 215 L 215
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 94-318 1.01e-34

uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 126.31  E-value: 1.01e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442   94 VKVLPIPVLSDNySYLIIDTQAGLAVAVDPSDPR-AVQASIEKERVNLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSP 172
Cdd:cd16322   1 VRPFTLGPLQEN-TYLVADEGGGEAVLVDPGDESeKLLARFGTTGLTLLYILLTHAHFDHVGGVADL-RRHPGAPVYLHP 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  173 QD----------------GIPYLT---HPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpSCLFSGDLLFLS 233
Cdd:cd16322  79 DDlplyeaadlgakafglGIEPLPppdRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEE-----GLLFSGDLLFQG 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  234 GCGRT-FEGTA-ETMLSSLDTVLDLGDDTLLWPGHeyaeenlgfagvvepenlarerkmqwvqrqrMErkstcPSTLGEE 311
Cdd:cd16322 154 SIGRTdLPGGDpKAMAASLRRLLTLPDETRVFPGH-------------------------------GP-----PTTLGEE 197


                ....*..
gi 9910442  312 RAYNPFL 318
Cdd:cd16322 198 RRTNPFL 204
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 95-266 1.74e-34

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


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 125.09  E-value: 1.74e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442   95 KVLPIPVLSDNySYLIIDtQAGLAVAVDPSDP--RAVQASIEKERVNLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSP 172
Cdd:cd06262   1 KRLPVGPLQTN-CYLVSD-EEGEAILIDPGAGalEKILEAIEELGLKIKAILLTHGHFDHIGGLAEL-KEAPGAPVYIHE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  173 QDgIPYLTHPLCHQ--------------------DVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGDLLFL 232
Cdd:cd06262  78 AD-AELLEDPELNLaffgggplpppepdilledgDTIELGGLELEVIHTPGHTPGSVCFYIEEEG-----VLFTGDTLFA 151

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 9910442  233 SGCGRT--FEGTAETMLSSLDTVLD-LGDDTLLWPGH 266
Cdd:cd06262 152 GSIGRTdlPGGDPEQLIESIKKLLLlLPDDTVVYPGH 188
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 106-266 9.99e-29

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 109.57  E-value: 9.99e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442     106 YSYLIIDTqaGLAVAVDP--SDPRAVQASIEKERV-NLVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQD-------- 174
Cdd:smart00849   1 NSYLVRDD--GGAILIDTgpGEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEAP-GAPVYAPEGTaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442     175 ----------GIPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpSCLFSGDLLFLSGCGRTF-EGTA 243
Cdd:smart00849  78 allgelgaeaEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEG-----KILFTGDLLFAGGDGRTLvDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 9910442     244 ETMLSSLDTVLDL--GDDTLLWPGH 266
Cdd:smart00849 153 AAASDALESLLKLlkLLPKLVVPGH 177
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 267-355 4.61e-28

Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of hydroxyacylglutathione hydrolase enzymes. Substrate binding occurs at the interface between this domain and the catalytic domain (pfam00753).


Pssm-ID: 465030 [Multi-domain]  Cd Length: 82  Bit Score: 104.83  E-value: 4.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442    267 EYAEENLGFAGVVEPENLARERKMQWVQRQRMERKSTCPSTLGEERAYNPFLRTHCLELQEALGpgpgptsddGCSRAQL 346
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATG---------ETDPVEV 71


                  ....*....
gi 9910442    347 LEELRRLKD 355
Cdd:pfam16123  72 FAALRELKD 80
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 107-266 1.70e-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: 101.41  E-value: 1.70e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  107 SYlIIDTQAGLAVaVDP--SDP---RAVQASIEKERVnlVAILCTHKHWDHSGGNRDLSRRHrDCRVYGSPQDGIPYL-- 179
Cdd:cd16278  20 TY-LLGAPDGVVV-IDPgpDDPahlDALLAALGGGRV--SAILVTHTHRDHSPGAARLAERT-GAPVRAFGPHRAGGQdt 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  180 ----THPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGDLLFlsGCGRTF----EGTAETMLSSLD 251
Cdd:cd16278  95 dfapDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEG-----ALFTGDHVM--GWSTTViappDGDLGDYLASLE 167

                       170
                ....*....|....*
gi 9910442  252 TVLDLgDDTLLWPGH 266
Cdd:cd16278 168 RLLAL-DDRLLLPGH 181
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 99-266 1.25e-23

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


Pssm-ID: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 96.47  E-value: 1.25e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442   99 IPV--LSDNySYLIIDTQAGLAVAVDP-SDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQD- 174
Cdd:cd07737   4 IPVtpFQQN-CSLIWCEETKEAAVIDPgGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAEL-AEHYGVPIIGPHKEd 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  175 --------------GIPYL-----THPLCHQDVVSVGRLQIRALATPGHTQGHLVYLldGEPYKgpsCLFSGDLLFLSGC 235
Cdd:cd07737  82 kfllenlpeqsqmfGFPPAeaftpDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFF--NRESK---LAIVGDVLFKGSI 156

                       170       180       190
                ....*....|....*....|....*....|....
gi 9910442  236 GRT-F-EGTAETMLSSL-DTVLDLGDDTLLWPGH 266
Cdd:cd07737 157 GRTdFpGGNHAQLIASIkEKLLPLGDDVTFIPGH 190
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 107-266 4.42e-18

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


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 81.04  E-value: 4.42e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  107 SYLIIDTQAGLaVAVDPSDPRAVQASIEKErvnLVAILCTHKHWDHSGGNRDLSRRHRD--CRVYGSP---------QDG 175
Cdd:cd07722  28 RRILIDTGEGR-PSYIPLLKSVLDSEGNAT---ISDILLTHWHHDHVGGLPDVLDLLRGpsPRVYKFPrpeededpdEDG 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  176 IPYltHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEPykgpsCLFSGD-LLflsGCGRT-FEGTAETMlSSLDTV 253
Cdd:cd07722 104 GDI--HDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLEEEN-----ALFTGDcVL---GHGTAvFEDLAAYM-ASLKKL 172

                       170
                ....*....|...
gi 9910442  254 LDLGDDTlLWPGH 266
Cdd:cd07722 173 LSLGPGR-IYPGH 184
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 94-266 4.44e-17

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 78.11  E-value: 4.44e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442   94 VKVLPIPVLSDNYSYLIIDTqaGLAVavdPSDPRAVQASIEKERVNLVAI---LCTHKHWDHSGGNRDLSRRhRDCRVYG 170
Cdd:cd07725  12 LGHVNVYLLRDGDETTLIDT--GLAT---EEDAEALWEGLKELGLKPSDIdrvLLTHHHPDHIGLAGKLQEK-SGATVYI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  171 SPqdgipylTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpSCLFSGD--LLFLSGCG----RTFEGTAE 244
Cdd:cd07725  86 LD-------VTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDR-----RELFVGDavLPKITPNVslwaVRVEDPLG 153

                       170       180
                ....*....|....*....|..
gi 9910442  245 TMLSSLDTVLDLGDDtLLWPGH 266
Cdd:cd07725 154 AYLESLDKLEKLDVD-LAYPGH 174
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 103-318 1.27e-16

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 78.30  E-value: 1.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442   103 SDNYSYLIIDTQ--AGLAVAVDPSDpRAVQ---ASIEKERVNLVAILCTHKHWDHSGG-----NRDLSRRHRDCRVYGSP 172
Cdd:PLN02962  21 SSTYTYLLADVShpDKPALLIDPVD-KTVDrdlSLVKELGLKLIYAMNTHVHADHVTGtgllkTKLPGVKSIISKASGSK 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442   173 QDgipyltHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLL-DGEPYKGPSCLFSGDLLFLSGCGRT-FE-GTAETMLSS 249
Cdd:PLN02962 100 AD------LFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTgEGPDQPQPRMAFTGDALLIRGCGRTdFQgGSSDQLYKS 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442   250 LDT-VLDLGDDTLLWPGHEYaeenlgfagvvepenlarerkmqwvqrqrmerKSTCPSTLGEERAYNPFL 318
Cdd:PLN02962 174 VHSqIFTLPKDTLIYPAHDY--------------------------------KGFTVSTVGEEMLYNPRL 211
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
106-266 4.52e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 70.09  E-value: 4.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442    106 YSYLIIDTqaGLAVAVDP--SDPRAVQASIEKERVN---LVAILCTHKHWDHSGGNRDLSRRHRDCRVYGS--------- 171
Cdd:pfam00753   7 NSYLIEGG--GGAVLIDTggSAEAALLLLLAALGLGpkdIDAVILTHGHFDHIGGLGELAEATDVPVIVVAeearellde 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442    172 -------------PQDGIPYLTHPLCHQDVVSVGRLQIRALATPGHTQGHLVYLldgepYKGPSCLFSGDLLFLSGCGRT 238
Cdd:pfam00753  85 elglaasrlglpgPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVY-----YGGGKVLFTGDLLFAGEIGRL 159

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 9910442    239 ----------FEGTAETMLSSLDTVLDLgDDTLLWPGH 266
Cdd:pfam00753 160 dlplggllvlHPSSAESSLESLLKLAKL-KAAVIVPGH 196
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 93-266 1.43e-13

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 68.79  E-value: 1.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442   93 GVKVLPIPVLSdnYSYLI--------IDTqaGLavavdPSDPRAVQASIEKERVN---LVAILCTHKHWDHSGGNRDLsR 161
Cdd:cd07721   1 GVYQLPLLPPV--NAYLIedddgltlIDT--GL-----PGSAKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAAL-K 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  162 RHRDCRVYGSPQDgIPYLTH---PLCHQDVVSVGRLQ-------------------------IRALATPGHTQGHLVYLL 213
Cdd:cd07721  71 EAPGAPVYAHERE-APYLEGekpYPPPVRLGLLGLLSpllpvkpvpvdrtledgdtldlaggLRVIHTPGHTPGHISLYL 149

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 9910442  214 DGEpykgpSCLFSGDLLFLSGcGRTFEGTA------ETMLSSLDTVLDLGDDTLLwPGH 266
Cdd:cd07721 150 EED-----GVLIAGDALVTVG-GELVPPPPpftwdmEEALESLRKLAELDPEVLA-PGH 201
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 109-266 4.18e-13

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 67.59  E-value: 4.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  109 LIIDTQAGLAVAvdpsdpRAVQASIEK---ERVNLVAIlcTHKHWDHSGGN-----------------RDLSRRHRDCRV 168
Cdd:cd16282  27 VVIDTGASPRLA------RALLAAIRKvtdKPVRYVVN--THYHGDHTLGNaafadagapiiahentrEELAARGEAYLE 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  169 YGSPQDG-------IPYLTHPLCHQDVVSVGRLQIRALAT-PGHTQGHLVYLLDGEpykgpSCLFSGDLLFLSGCGRTFE 240
Cdd:cd16282  99 LMRRLGGdamagteLVLPDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEE-----GVLFAGDLVFNGRIPFLPD 173

                       170       180
                ....*....|....*....|....*.
gi 9910442  241 GTAETMLSSLDTVLDLGDDTLLwPGH 266
Cdd:cd16282 174 GSLAGWIAALDRLLALDATVVV-PGH 198
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 101-266 6.67e-13

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 66.79  E-value: 6.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  101 VLSDNYSYLIIDTqaGLavavDPSDPRAVQASIEKERVNLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQDgIPYLT 180
Cdd:cd07743  13 YVFGDKEALLIDS--GL----DEDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYL-QKKTGCKVYAPKIE-KAFIE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  181 HPL------------------------------CHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpsCLFSGDLL 230
Cdd:cd07743  85 NPLlepsylggayppkelrnkflmakpskvddiIEEGELELGGVGLEIIPLPGHSFGQIGILTPDG------VLFAGDAL 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 9910442  231 FlsgcgrtfegTAETM--------------LSSLDTVLDLGDDTLLwPGH 266
Cdd:cd07743 159 F----------GEEVLekygipflydveeqLETLEKLEELDADYYV-PGH 197
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 72-267 2.08e-11

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 63.00  E-value: 2.08e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442   72 LRRARNRYPKGHSKTQPRLFNGVKVLPIpvlsdnYSYLI--------IDTqaGL--AVAVDPSDPRAVQASIEKERVNLV 141
Cdd:cd07729   5 LDYGTVTVDKSSLFYYGRGPGEPIDLPV------YAYLIehpegtilVDT--GFhpDAADDPGGLELAFPPGVTEEQTLE 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  142 AIL--------------CTHKHWDHSGGNRDL-------SRR-----HRDCRVYGSPQDGIPYLTHPLCHQDVVSV-GRL 194
Cdd:cd07729  77 EQLarlgldpedidyviLSHLHFDHAGGLDLFpnatiivQRAeleyaTGPDPLAAGYYEDVLALDDDLPGGRVRLVdGDY 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  195 Q----IRALATPGHTQGHLVYLLDGEpyKGPsCLFSGDL-----LFLSGCGRTFEGTAETMLSSLDTVLDL--GDDTLLW 263
Cdd:cd07729 157 DlfpgVTLIPTPGHTPGHQSVLVRLP--EGT-VLLAGDAaytyeNLEEGRPPGINYDPEAALASLERLKALaeREGARVI 233


                ....
gi 9910442  264 PGHE 267
Cdd:cd07729 234 PGHD 237
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 107-266 1.96e-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: 57.12  E-value: 1.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  107 SYLIiDTQAGLAVaVDP----SDPRAVQASIEK--ERVNLVAILCTHKHWDHSGGNRDLSRRHRDCRVYGSPQdGIPYLT 180
Cdd:cd07726  18 SYLL-DGEGRPAL-IDTgpssSVPRLLAALEALgiAPEDVDYIILTHIHLDHAGGAGLLAEALPNAKVYVHPR-GARHLI 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  181 HP--------------------------------LCHQDVVSVGRLQIRALATPGHTQGHLVYLLDGEpykgpSCLFSGD 228
Cdd:cd07726  95 DPsklwasaravygdeadrlggeilpvpeervivLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEES-----DGLFTGD 169

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 9910442  229 LLFLSGCGRTFEGTAET---------MLSSLDTVLDLGDDTLLwPGH 266
Cdd:cd07726 170 AAGVRYPELDVVGPPSTpppdfdpeaWLESLDRLLSLKPERIY-LTH 215
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 109-266 5.90e-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: 54.94  E-value: 5.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  109 LIIDTQAGLAvavdpSDPRAVQASIEKErvnLVAILcTHKHWDHSGGN----------RDLSRRHRDCRVYGSPQDGIPY 178
Cdd:cd07712  21 LLIDTGLGIG-----DLKEYVRTLTDLP---LLVVA-THGHFDHIGGLhefeevyvhpADAEILAAPDNFETLTWDAATY 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  179 ------LTHPLCHQDVVSVGRLQIRALATPGHTQGHLVyLLDgepyKGPSCLFSGDL-----LFLSGCGRTFegtaETML 247
Cdd:cd07712  92 svppagPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIA-LLD----RANRLLFSGDVvydgpLIMDLPHSDL----DDYL 162

                       170       180
                ....*....|....*....|
gi 9910442  248 SSLDTVLDLGDD-TLLWPGH 266
Cdd:cd07712 163 ASLEKLSKLPDEfDKVLPGH 182
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 107-207 3.41e-06

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


Pssm-ID: 293868  Cd Length: 252  Bit Score: 47.83  E-value: 3.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  107 SYLIIDTQAGLAVAVDPSDPRA-VQASIEKERVNLV---AILCTHKHWDHSGGnrdLSRRHRD--CRVYGSPQD------ 174
Cdd:cd16310  24 SYLITSNHGAILLDGGLEENAAlIEQNIKALGFKLSdikIIINTHAHYDHAGG---LAQLKADtgAKLWASRGDrpalea 100

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 9910442  175 ----------GIPY----LTHPLCHQDVVSVGRLQIRALATPGHTQG 207
Cdd:cd16310 101 gkhigdnitqPAPFpavkVDRILGDGEKIKLGDITLTATLTPGHTKG 147
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 110-218 6.14e-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: 6.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  110 IIDTQAGLAV--AVDPSDPRAV-QASIEKERVN---LVAILCTHKHWDHSGGNRDLsRRHRDCRVYGS----------PQ 173
Cdd:cd16280  26 AIDTGDGLILidALNNNEAADLiVDGLEKLGLDpadIKYILITHGHGDHYGGAAYL-KDLYGAKVVMSeadwdmmeepPE 104

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 9910442  174 DGIPYLTHPLCHQDVV-------SVGRLQIRALATPGHTQGHLVYLLD----GEPY 218
Cdd:cd16280 105 EGDNPRWGPPPERDIVikdgdtlTLGDTTITVYLTPGHTPGTLSLIFPvkdgGKTH 160
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 196-231 1.02e-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: 43.31  E-value: 1.02e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 9910442  196 IRALATPGHTQGHLVYLLDGepyKGPSCLFSGDLLF 231
Cdd:cd07720 175 ITAVPAPGHTPGHTGYRIES---GGERLLIWGDIVH 207
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 123-207 1.24e-04

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


Pssm-ID: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 43.05  E-value: 1.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  123 PSDPRAVQASIEK-----ERVNLvaILCTHKHWDHSGGNRDLsRRHRDCRVYGSP------QDGIP------YLTHPLCH 185
Cdd:cd16312  41 PQSAPLIIANIEAlgfriEDVKL--ILNSHAHWDHAGGIAAL-QKASGATVAASAhgaqvlQSGTNgkddpqYQAKPVVH 117

                        90       100       110
                ....*....|....*....|....*....|....
gi 9910442  186 ------------QDVVSVGRLQIRALATPGHTQG 207
Cdd:cd16312 118 vakvakvkevgeGDTLKVGPLRLTAHMTPGHTPG 151
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 143-229 1.50e-04

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


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 42.19  E-value: 1.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  143 ILCTHKHWDHSGGNRDLSR-RHrdcrVYGSPQDGIPYLTHPLCHQDVVSVGrLQIRALATPGHTQGHLVYLLDGEPYKgp 221
Cdd:cd07711  64 VVLTHGHPDHIGNLNLFPNaTV----IVGWDICGDSYDDHSLEEGDGYEID-ENVEVIPTPGHTPEDVSVLVETEKKG-- 136


                ....*...
gi 9910442  222 SCLFSGDL 229
Cdd:cd07711 137 TVAVAGDL 144
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
142-228 1.62e-04

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 42.49  E-value: 1.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  142 AILCTHKHWDHSGG------NRDLSRRHRDCRVYGsPQDGIPYLT----------------HPLCHQDVVSVGRLQIRAL 199
Cdd:COG1234  55 AIFITHLHGDHIAGlpgllsTRSLAGREKPLTIYG-PPGTKEFLEallkasgtdldfplefHEIEPGEVFEIGGFTVTAF 133

                        90       100
                ....*....|....*....|....*....
gi 9910442  200 ATPgHTQGHLVYLLDgepYKGPSCLFSGD 228
Cdd:COG1234 134 PLD-HPVPAYGYRFE---EPGRSLVYSGD 158
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 107-207 2.34e-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: 2.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  107 SYLIiDTQAGLaVAVDPSDPRAV---QASIEK---ERVNLVAILCTHKHWDHSGGNRDLsRRHRDCRVYGSPQD------ 174
Cdd:cd16288  24 SYLI-TTPQGL-ILIDTGLESSApmiKANIRKlgfKPSDIKILLNSHAHLDHAGGLAAL-KKLTGAKLMASAEDaallas 100

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 9910442  175 --------GIPYLTHP-------LCHQDVVSVGRLQIRALATPGHTQG 207
Cdd:cd16288 101 ggksdfhyGDDSLAFPpvkvdrvLKDGDRVTLGGTTLTAHLTPGHTRG 148
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 196-233 2.49e-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: 41.41  E-value: 2.49e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 9910442  196 IRALATPGHTQGHLVYLldgepYKGPSCLFSGDLLFLS 233
Cdd:cd07727 104 LTLIPVPGHTRGSVVLL-----YKEKGVLFTGDHLAWS 136
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 136-230 7.28e-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: 7.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  136 ERVNLVaiLCTHKHWDHSGGN---------------------RDLSRRHRDCRVYGSPQDGIPYLTHPlchqdVVSVGRL 194
Cdd:cd16277  62 EDVDYV--LCTHLHVDHVGWNtrlvdgrwvptfpnarylfsrAEYDHWSSPDAGGPPNRGVFEDSVLP-----VIEAGLA 134

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 9910442  195 Q-----------IRALATPGHTQGHLVYLLDGEpykGPSCLFSGDLL 230
Cdd:cd16277 135 DlvdddheildgIRLEPTPGHTPGHVSVELESG---GERALFTGDVM 178
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 107-207 8.53e-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: 40.51  E-value: 8.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9910442  107 SYLIIDTQAGLAVAVD-PSDPRAVQASIEKE--RVNLVAI-LCTHKHWDHSGGNRDLSRR--------HRDCRV------ 168
Cdd:cd16307  24 SYLITTPRGNILINSNlESSVPQIKASIEKLgfKFSDTKIlLISHAHFDHAAGSALIKREthakymvmDGDVDVvesggk 103

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 9910442  169 ----YGSPqdgiPYLTHPLCHQD-------VVSVGRLQIRALATPGHTQG 207
Cdd:cd16307 104 sdffYGND----PSTYFPPAHVDkvlhdgeQVELGGTVLTAHLTAGHTKG 149
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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