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Conserved domains on  [gi|1820342288|ref|NP_001365710|]
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hydroxyacylglutathione hydrolase-like protein isoform e [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02469 super family cl31885
hydroxyacylglutathione hydrolase
 1-254 1.38e-85

hydroxyacylglutathione hydrolase


The actual alignment was detected with superfamily member PLN02469:

Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 255.46  E-value: 1.38e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288   1 MKVKVIPVLEDNYMYLIIEEHTREAVAIDVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVL-GAD 79
Cdd:PLN02469    1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYgGSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  80 ERICALTRRLEHGEGLQFGA-IHVRCLLTPGHTSGHMSYFlweddcpdspalfsgtvqpgfiylpnstVPSLPPSDPLCS 158
Cdd:PLN02469   81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYY----------------------------VTGKEGEDPAVF 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288 159 LGDALSVAGCGWHLEDTAQQMYQSLAKTLGTLPPETKVFCGHEHTLSNLEFAQKVEPCNEHVQAKLSWAQERDDEDIPTV 238
Cdd:PLN02469  133 TGDTLFIAGCGKFFEGTAEQMYQSLCVTLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTV 212

                         250
                  ....*....|....*.
gi 1820342288 239 PSTLGEELMYNPFLRV 254
Cdd:PLN02469  213 PSTIEEELETNPFMRV 228
 
Name Accession Description Interval E-value
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 1-254 1.38e-85

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 255.46  E-value: 1.38e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288   1 MKVKVIPVLEDNYMYLIIEEHTREAVAIDVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVL-GAD 79
Cdd:PLN02469    1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYgGSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  80 ERICALTRRLEHGEGLQFGA-IHVRCLLTPGHTSGHMSYFlweddcpdspalfsgtvqpgfiylpnstVPSLPPSDPLCS 158
Cdd:PLN02469   81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYY----------------------------VTGKEGEDPAVF 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288 159 LGDALSVAGCGWHLEDTAQQMYQSLAKTLGTLPPETKVFCGHEHTLSNLEFAQKVEPCNEHVQAKLSWAQERDDEDIPTV 238
Cdd:PLN02469  133 TGDTLFIAGCGKFFEGTAEQMYQSLCVTLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTV 212

                         250
                  ....*....|....*.
gi 1820342288 239 PSTLGEELMYNPFLRV 254
Cdd:PLN02469  213 PSTIEEELETNPFMRV 228
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 6-253 1.74e-80

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: 242.06  E-value: 1.74e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288   6 IPVLEDNYMYLIIEEHTReAVAIDVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPgLAVLG-ADERICA 84
Cdd:TIGR03413   4 IPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAFP-APVYGpAEERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  85 LTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFSgtvqpgfiylpnstvpslppsdplcslGDALS 164
Cdd:TIGR03413  82 ITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYL-----PDSPALFC---------------------------GDTLF 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288 165 VAGCGWHLEDTAQQMYQSLAKtLGTLPPETKVFCGHEHTLSNLEFAQKVEPCNEHVQAKLSWAQERDDEDIPTVPSTLGE 244
Cdd:TIGR03413 130 SAGCGRLFEGTPEQMYDSLQR-LAALPDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGL 208


                  ....*....
gi 1820342288 245 ELMYNPFLR 253
Cdd:TIGR03413 209 ERATNPFLR 217
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 4-200 2.01e-68

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: 208.47  E-value: 2.01e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288   4 KVIPVLEDNYMYLIIEEHTREAVAIDVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVLG-ADERI 82
Cdd:cd07723     1 VPIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGpAEDRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  83 CALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFSgtvqpgfiylpnstvpslppsdplcslGDA 162
Cdd:cd07723    81 PGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV-----PDEPALFT---------------------------GDT 128

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1820342288 163 LSVAGCGWHLEDTAQQMYQSLAKtLGTLPPETKVFCGH 200
Cdd:cd07723   129 LFSGGCGRFFEGTAEQMYASLQK-LLALPDDTLVYCGH 165
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 201-254 9.25e-26

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: 96.35  E-value: 9.25e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1820342288 201 EHTLSNLEFAQKVEPCNEHVQAKLSWAQERDDEDIPTVPSTLGEELMYNPFLRV 254
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRV 54
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 11-205 1.57e-25

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: 99.76  E-value: 1.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  11 DNYMYLIieEHTREAVAID----VAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELA---------------HILP 71
Cdd:COG0491    14 GVNSYLI--VGGDGAVLIDtglgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAeafgapvyahaaeaeALEA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  72 GLAVLGADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFSgtvqpgfiylpnstvpslp 151
Cdd:COG0491    92 PAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV-----PDEKVLFT------------------- 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820342288 152 psdplcslGDALSVAGCGW--HLEDTAQQMYQSLAKtLGTLPPETkVFCGHEHTLS 205
Cdd:COG0491   148 --------GDALFSGGVGRpdLPDGDLAQWLASLER-LLALPPDL-VIPGHGPPTT 193
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-200 2.79e-16

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: 74.13  E-value: 2.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288   13 YMYLIieEHTREAVAID--VAVAERLLEIAGREGVS-LTMVLSTHHHWDHTRGNAELAHI------------------LP 71
Cdd:smart00849   1 NSYLV--RDDGGAILIDtgPGEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLEApgapvyapegtaellkdlLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288   72 GLAVLGADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFSgtvqpgfiylpnstvpslp 151
Cdd:smart00849  79 LLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL-----PEGKILFT------------------- 134

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820342288  152 psdplcslGDALSVAGCG-WHLEDTAQQMYQSLAKTLGTL-PPETKVFCGH 200
Cdd:smart00849 135 --------GDLLFAGGDGrTLVDGGDAAASDALESLLKLLkLLPKLVVPGH 177
 
Name Accession Description Interval E-value
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 1-254 1.38e-85

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 255.46  E-value: 1.38e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288   1 MKVKVIPVLEDNYMYLIIEEHTREAVAIDVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVL-GAD 79
Cdd:PLN02469    1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYgGSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  80 ERICALTRRLEHGEGLQFGA-IHVRCLLTPGHTSGHMSYFlweddcpdspalfsgtvqpgfiylpnstVPSLPPSDPLCS 158
Cdd:PLN02469   81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYY----------------------------VTGKEGEDPAVF 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288 159 LGDALSVAGCGWHLEDTAQQMYQSLAKTLGTLPPETKVFCGHEHTLSNLEFAQKVEPCNEHVQAKLSWAQERDDEDIPTV 238
Cdd:PLN02469  133 TGDTLFIAGCGKFFEGTAEQMYQSLCVTLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTV 212

                         250
                  ....*....|....*.
gi 1820342288 239 PSTLGEELMYNPFLRV 254
Cdd:PLN02469  213 PSTIEEELETNPFMRV 228
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 6-253 1.74e-80

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: 242.06  E-value: 1.74e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288   6 IPVLEDNYMYLIIEEHTReAVAIDVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPgLAVLG-ADERICA 84
Cdd:TIGR03413   4 IPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAFP-APVYGpAEERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  85 LTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFSgtvqpgfiylpnstvpslppsdplcslGDALS 164
Cdd:TIGR03413  82 ITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYL-----PDSPALFC---------------------------GDTLF 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288 165 VAGCGWHLEDTAQQMYQSLAKtLGTLPPETKVFCGHEHTLSNLEFAQKVEPCNEHVQAKLSWAQERDDEDIPTVPSTLGE 244
Cdd:TIGR03413 130 SAGCGRLFEGTPEQMYDSLQR-LAALPDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGL 208


                  ....*....
gi 1820342288 245 ELMYNPFLR 253
Cdd:TIGR03413 209 ERATNPFLR 217
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 4-200 2.01e-68

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: 208.47  E-value: 2.01e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288   4 KVIPVLEDNYMYLIIEEHTREAVAIDVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVLG-ADERI 82
Cdd:cd07723     1 VPIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGpAEDRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  83 CALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFSgtvqpgfiylpnstvpslppsdplcslGDA 162
Cdd:cd07723    81 PGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV-----PDEPALFT---------------------------GDT 128

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1820342288 163 LSVAGCGWHLEDTAQQMYQSLAKtLGTLPPETKVFCGH 200
Cdd:cd07723   129 LFSGGCGRFFEGTAEQMYASLQK-LLALPDDTLVYCGH 165
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 1-255 1.50e-51

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 170.79  E-value: 1.50e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288   1 MKVKVIPVLEDNYMYLIIEEHTREAVAIDVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILpGLAVLGAD- 79
Cdd:PLN02398   76 LQIELVPCLKDNYAYLLHDEDTGTVGVVDPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARY-GAKVIGSAv 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  80 --ERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFSGtvqpgfiylpnstvpslppsDPLC 157
Cdd:PLN02398  155 dkDRIPGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYF-----PGSGAIFTG--------------------DTLF 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288 158 SLGdalsvagCGWHLEDTAQQMYQSLAKTLgTLPPETKVFCGHEHTLSNLEFAQKVEPCNEHVQAKLSWAQERDDEDIPT 237
Cdd:PLN02398  210 SLS-------CGKLFEGTPEQMLSSLQKII-SLPDDTNIYCGHEYTLSNSKFALSIEPNNEVLQSYAAHVAHLRSKGLPT 281

                         250
                  ....*....|....*...
gi 1820342288 238 VPSTLGEELMYNPFLRVT 255
Cdd:PLN02398  282 IPTTVKMEKACNPFLRTS 299
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 1-254 2.56e-32

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 118.77  E-value: 2.56e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288   1 MKVKVIPVLEDNYMYLIIEEHTReAVAIDVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVLGADE 80
Cdd:PRK10241    1 MNLNSIPAFDDNYIWVLNDEAGR-CLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  81 -RICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFlweddcpDSPALFsgtvqpgfiylpnstvpslppsdplCsl 159
Cdd:PRK10241   80 tQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF-------SKPYLF-------------------------C-- 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288 160 GDALSVAGCGWHLEDTAQQMYQSLAKtLGTLPPETKVFCGHEHTLSNLEFAQKVEPCNEHVQAKLSWAQERDDEDIPTVP 239
Cdd:PRK10241  126 GDTLFSGGCGRLFEGTASQMYQSLKK-INALPDDTLICCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLP 204

                         250
                  ....*....|....*
gi 1820342288 240 STLGEELMYNPFLRV 254
Cdd:PRK10241  205 VILKNERQINLFLRT 219
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 11-200 2.40e-31

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: 113.79  E-value: 2.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  11 DNYMYLIIEEHTREAVAIDVA-VAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVLGADERI-----CA 84
Cdd:cd16275    11 INYSYIIIDKATREAAVVDPAwDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDyygfrCP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  85 LTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweDDCpdspaLFSG-TVqpgFIYlpnstvpslppsdplcslgdal 163
Cdd:cd16275    91 NLIPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLL--GDS-----LFTGdTL---FIE---------------------- 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1820342288 164 svaGCGwhLEDT----AQQMYQSLAKTLGTLPPETKVFCGH 200
Cdd:cd16275   139 ---GCG--RCDLpggdPEEMYESLQRLKKLPPPNTRVYPGH 174
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 15-200 9.67e-29

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: 107.10  E-value: 9.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  15 YLIIEEHTREAVAID--VAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVLGADERICALTRRLEHG 92
Cdd:cd07724    15 YLVGDPETGEAAVIDpvRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGEGAPASFFDRLLKDG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  93 EGLQFGAIHVRCLLTPGHTSGHMSYfLWEDdcPDspALFSgtvqpgfiylpnstvpslppsdplcslGDALSVAGCG--- 169
Cdd:cd07724    95 DVLELGNLTLEVLHTPGHTPESVSY-LVGD--PD--AVFT---------------------------GDTLFVGDVGrpd 142

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1820342288 170 --WHLEDTAQQMYQSLAKTLGTLPPETKVFCGH 200
Cdd:cd07724   143 lpGEAEGLARQLYDSLQRKLLLLPDETLVYPGH 175
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 201-254 9.25e-26

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: 96.35  E-value: 9.25e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1820342288 201 EHTLSNLEFAQKVEPCNEHVQAKLSWAQERDDEDIPTVPSTLGEELMYNPFLRV 254
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRV 54
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 11-205 1.57e-25

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: 99.76  E-value: 1.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  11 DNYMYLIieEHTREAVAID----VAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELA---------------HILP 71
Cdd:COG0491    14 GVNSYLI--VGGDGAVLIDtglgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAeafgapvyahaaeaeALEA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  72 GLAVLGADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFSgtvqpgfiylpnstvpslp 151
Cdd:COG0491    92 PAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV-----PDEKVLFT------------------- 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1820342288 152 psdplcslGDALSVAGCGW--HLEDTAQQMYQSLAKtLGTLPPETkVFCGHEHTLS 205
Cdd:COG0491   148 --------GDALFSGGVGRpdLPDGDLAQWLASLER-LLALPPDL-VIPGHGPPTT 193
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 15-200 4.86e-24

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: 95.05  E-value: 4.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  15 YLIIEEhTREAVAIDVA--VAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAEL---------AH----------ILPGL 73
Cdd:cd06262    13 YLVSDE-EGEAILIDPGagALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELkeapgapvyIHeadaelledpELNLA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  74 AVLGADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFlweddCPDSPALFSG-TVQPGFIYLPNstvpsLPP 152
Cdd:cd06262    92 FFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFY-----IEEEGVLFTGdTLFAGSIGRTD-----LPG 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1820342288 153 SDPlcslgdalsvagcgwhledtaQQMYQSLAKTLGTLPPETKVFCGH 200
Cdd:cd06262   162 GDP---------------------EQLIESIKKLLLLLPDDTVVYPGH 188
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 5-252 7.34e-18

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: 79.32  E-value: 7.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288   5 VIPVLEDNyMYLIIEEHTREAVAIDVAV-AERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVLGAD---- 79
Cdd:cd16322     5 TLGPLQEN-TYLVADEGGGEAVLVDPGDeSEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDdlpl 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  80 ---------------ERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFlweddCPDSPALFSGTVqpgfiyLPN 144
Cdd:cd16322    84 yeaadlgakafglgiEPLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFY-----VEEEGLLFSGDL------LFQ 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288 145 STV--PSLPPSDPlcslgdalsvagcgwhledtaQQMYQSLAKTLgTLPPETKVFCGHehtlsnlefaqkvepcnehvqa 222
Cdd:cd16322   153 GSIgrTDLPGGDP---------------------KAMAASLRRLL-TLPDETRVFPGH---------------------- 188

                         250       260       270
                  ....*....|....*....|....*....|
gi 1820342288 223 klswaqerddedipTVPSTLGEELMYNPFL 252
Cdd:cd16322   189 --------------GPPTTLGEERRTNPFL 204
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-200 2.79e-16

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: 74.13  E-value: 2.79e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288   13 YMYLIieEHTREAVAID--VAVAERLLEIAGREGVS-LTMVLSTHHHWDHTRGNAELAHI------------------LP 71
Cdd:smart00849   1 NSYLV--RDDGGAILIDtgPGEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLEApgapvyapegtaellkdlLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288   72 GLAVLGADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFSgtvqpgfiylpnstvpslp 151
Cdd:smart00849  79 LLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL-----PEGKILFT------------------- 134

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1820342288  152 psdplcslGDALSVAGCG-WHLEDTAQQMYQSLAKTLGTL-PPETKVFCGH 200
Cdd:smart00849 135 --------GDLLFAGGDGrTLVDGGDAAASDALESLLKLLkLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 34-133 1.58e-14

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: 69.44  E-value: 1.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  34 ERLLEIAGREGVSLTMVlsTHHHWDHTRGNAELAHiLPGLAVLGADERI-------CALTRRLEHGEGLQFGAIHVRCLL 106
Cdd:cd16278    43 DALLAALGGGRVSAILV--THTHRDHSPGAARLAE-RTGAPVRAFGPHRaggqdtdFAPDRPLADGEVIEGGGLRLTVLH 119

                          90       100
                  ....*....|....*....|....*..
gi 1820342288 107 TPGHTSGHMSYFLweddcPDSPALFSG 133
Cdd:cd16278   120 TPGHTSDHLCFAL-----EDEGALFTG 141
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 3-200 5.20e-13

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: 65.65  E-value: 5.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288   3 VKVIPV--LEDNyMYLIIEEHTREAVAIDV-AVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELA----------HI 69
Cdd:cd07737     1 YQIIPVtpFQQN-CSLIWCEETKEAAVIDPgGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAehygvpiigpHK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  70 --------LPGLAVL--GADERICALTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFlweddCPDSPALFSGTVqpgf 139
Cdd:cd07737    80 edkfllenLPEQSQMfgFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFF-----NRESKLAIVGDV---- 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820342288 140 iyLPNSTV--PSLPPSDplcslgdalsvagcgwhledtAQQMYQSLAKTLGTLPPETKVFCGH 200
Cdd:cd07737   151 --LFKGSIgrTDFPGGN---------------------HAQLIASIKEKLLPLGDDVTFIPGH 190
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 13-252 8.82e-13

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 65.97  E-value: 8.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  13 YMYLI--IEEHTREAVAIDVA--VAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPGLAVLGADERICALTRR 88
Cdd:PLN02962   24 YTYLLadVSHPDKPALLIDPVdkTVDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVKSIISKASGSKADLF 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  89 LEHGEGLQFGAIHVRCLLTPGHTSGHMSYFlwEDDCPDSPalfsgtvQPGFIYlpnstvpslppsdplcsLGDALSVAGC 168
Cdd:PLN02962  104 VEPGDKIYFGDLYLEVRATPGHTAGCVTYV--TGEGPDQP-------QPRMAF-----------------TGDALLIRGC 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288 169 GW--HLEDTAQQMYQSLAKTLGTLPPETKVFCGHE---HTLsnlefaqkvepcnehvqaklswaqerddediptvpSTLG 243
Cdd:PLN02962  158 GRtdFQGGSSDQLYKSVHSQIFTLPKDTLIYPAHDykgFTV-----------------------------------STVG 202


                  ....*....
gi 1820342288 244 EELMYNPFL 252
Cdd:PLN02962  203 EEMLYNPRL 211
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 2-200 5.80e-10

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: 57.23  E-value: 5.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288   2 KVKVIPVLEDNYMYLIIEEhtREAVAIDVAV---AERLLEIAGREGVS---LTMVLSTHHHWDHTrGNAELAHILPGLAV 75
Cdd:cd07721     1 GVYQLPLLPPVNAYLIEDD--DGLTLIDTGLpgsAKRILKALRELGLSpkdIRRILLTHGHIDHI-GSLAALKEAPGAPV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  76 L-GADE----------------------------RICALTRRLEHGEGLQF-GAIHVrcLLTPGHTSGHMSYFLWEDDcp 125
Cdd:cd07721    78 YaHEREapylegekpypppvrlgllgllspllpvKPVPVDRTLEDGDTLDLaGGLRV--IHTPGHTPGHISLYLEEDG-- 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820342288 126 dspALFSGTVqpgFIYLPNSTVPSLPP--SDPlcslgdalsvagcgwhledtaQQMYQSLAKtLGTLPPETkVFCGH 200
Cdd:cd07721   154 ---VLIAGDA---LVTVGGELVPPPPPftWDM---------------------EEALESLRK-LAELDPEV-LAPGH 201
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 29-156 3.38e-09

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: 55.00  E-value: 3.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  29 DVAVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHilpglaVLGADErICALTRRLEHGEGLQFGAIHVRCLLTP 108
Cdd:cd07725    38 DAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQE------KSGATV-YILDVTPVKDGDKIDLGGLRLKVIETP 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1820342288 109 GHTSGHMSYFlweddCPDSPALFSG-TVQPGfiYLPNSTVPSLPPSDPL 156
Cdd:cd07725   111 GHTPGHIVLY-----DEDRRELFVGdAVLPK--ITPNVSLWAVRVEDPL 152
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 7-200 5.94e-08

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: 51.09  E-value: 5.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288   7 PVLEDNY---MYLIieEHTREAVAIDVAVAER-LLEIAgregVSLT----MVLSTHHHWDHTRGN----------AELAH 68
Cdd:cd07712     1 LFIEEDDrvnIYLL--RGRDRALLIDTGLGIGdLKEYV----RTLTdlplLVVATHGHFDHIGGLhefeevyvhpADAEI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  69 I-----LPGLAVLGADERICA--LTRRLEHGEGLQFGAIHVRCLLTPGHTSGHMSyfLWEddcPDSPALFSG-TVQPGFI 140
Cdd:cd07712    75 LaapdnFETLTWDAATYSVPPagPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIA--LLD---RANRLLFSGdVVYDGPL 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1820342288 141 YLpnsTVPSLPPSDplcslgdalsvagcgwhledtaqqMYQSLAKtLGTLPPE-TKVFCGH 200
Cdd:cd07712   150 IM---DLPHSDLDD------------------------YLASLEK-LSKLPDEfDKVLPGH 182
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 15-154 7.38e-07

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: 48.64  E-value: 7.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  15 YLIIEEhtREAVAIDVAVA------ERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILPG---------------- 72
Cdd:cd07726    19 YLLDGE--GRPALIDTGPSssvprlLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLAEALPNakvyvhprgarhlidp 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  73 -------LAVLGAD-------------ERICAltrrLEHGEGLQFGAIHVRCLLTPGHTSGHMSYFLweddcPDSPALFS 132
Cdd:cd07726    97 sklwasaRAVYGDEadrlggeilpvpeERVIV----LEDGETLDLGGRTLEVIDTPGHAPHHLSFLD-----EESDGLFT 167

                         170       180
                  ....*....|....*....|....
gi 1820342288 133 GTVQpGFIY--LPNSTVPSLPPSD 154
Cdd:cd07726   168 GDAA-GVRYpeLDVVGPPSTPPPD 190
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 39-133 4.46e-06

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: 45.99  E-value: 4.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  39 IAGREGVSLTMVLSTHHHWDHTRGnaeLAHIL-----------------PGLAVLGADERICaltrRLEHGEGLQFGAIH 101
Cdd:cd07722    49 LDSEGNATISDILLTHWHHDHVGG---LPDVLdllrgpsprvykfprpeEDEDPDEDGGDIH----DLQDGQVFKVEGAT 121

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1820342288 102 VRCLLTPGHTSGHMSYFLWEDDcpdspALFSG 133
Cdd:cd07722   122 LRVIHTPGHTTDHVCFLLEEEN-----ALFTG 148
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 50-117 7.25e-06

SMB-1, 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 SMB-1- and 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: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 46.01  E-value: 7.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  50 VLSTHHHWDHTRGNAELAHiLPGLAVLGADERICAL-----------------------TRRLEHGEGLQFGAIHVRCLL 106
Cdd:cd16313    64 ILSSHDHWDHAGGIAALQK-LTGAQVLASPATVAVLrsgsmgkddpqfggltpmppvasVRAVRDGEVVKLGPLAVTAHA 142

                          90
                  ....*....|.
gi 1820342288 107 TPGHTSGHMSY 117
Cdd:cd16313   143 TPGHTTGGTSW 153
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 34-116 1.58e-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: 44.50  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  34 ERLLEIAGREGVSL---TMVLSTHHHWDHTrGNAEL---AHILPGLAVLGaderICALTRRLEHGEGLQFGAiHVRCLLT 107
Cdd:cd07711    45 DLLLKALAEHGLSPediDYVVLTHGHPDHI-GNLNLfpnATVIVGWDICG----DSYDDHSLEEGDGYEIDE-NVEVIPT 118


                  ....*....
gi 1820342288 108 PGHTSGHMS 116
Cdd:cd07711   119 PGHTPEDVS 127
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 50-117 3.85e-05

AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Pseudomonas Aeruginosa AIM-1, Serratia marcescens SMB-1, Erythrobacter vulgaris EVM-1, and Janthinobacterium lividum THIN-B. 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 AIM-1-,SMB-1-, EVM-1-, 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: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 43.88  E-value: 3.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  50 VLSTHHHWDHTRGNAELAHI--------LPGLAVL------------GADERICALT--RRLEHGEGLQFGAIHVRCLLT 107
Cdd:cd16290    64 ILNSHAHFDHAGGIAALQRDsgatvaasPAGAAALrsggvdpddpqaGAADPFPPVAkvRVVADGEVVKLGPLAVTAHAT 143

                          90
                  ....*....|
gi 1820342288 108 PGHTSGHMSY 117
Cdd:cd16290   144 PGHTPGGTSW 153
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
15-155 5.78e-05

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 42.74  E-value: 5.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  15 YLIieEHTREAVAIDV-----AVAERLLEIAGREGVSLTMVLSTHHHWDHTRGNAELAHILP--------GLAVLGADER 81
Cdd:pfam00753   9 YLI--EGGGGAVLIDTggsaeAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDvpvivvaeEARELLDEEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  82 ICALTRRLEHG------------EGLQFGAIHVRCLL---TPGHTSGHMSYFLweddcPDSPALFSG-TVQPGFIYLPNS 145
Cdd:pfam00753  87 GLAASRLGLPGppvvplppdvvlEEGDGILGGGLGLLvthGPGHGPGHVVVYY-----GGGKVLFTGdLLFAGEIGRLDL 161

                         170
                  ....*....|
gi 1820342288 146 TVPSLPPSDP 155
Cdd:pfam00753 162 PLGGLLVLHP 171
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-133 1.08e-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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 42.17  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  22 TREAVA-ID----VAVAERLLE-IAGREGVSLTMVLSTHHHWDHTRGNAEL--------AH-------------ILPGLA 74
Cdd:cd16282    22 GDDGVVvIDtgasPRLARALLAaIRKVTDKPVRYVVNTHYHGDHTLGNAAFadagapiiAHentreelaargeaYLELMR 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1820342288  75 VLGADE----RICALTRRLEHGEGLQFGAIHVRCL-LTPGHTSGHMSYFLweddcPDSPALFSG 133
Cdd:cd16282   102 RLGGDAmagtELVLPDRTFDDGLTLDLGGRTVELIhLGPAHTPGDLVVWL-----PEEGVLFAG 160
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 18-116 3.55e-04

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: 40.66  E-value: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  18 IEEHTREAVAIDVAVAERLLEIagreGVS---LTMVLSTHHHWDHTrGNAEL---AHIL-----------PGLAVLGADE 80
Cdd:cd07729    61 LELAFPPGVTEEQTLEEQLARL----GLDpedIDYVILSHLHFDHA-GGLDLfpnATIIvqraeleyatgPDPLAAGYYE 135

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1820342288  81 RICALTRRLEhgeGLQFGAIH--------VRCLLTPGHTSGHMS 116
Cdd:cd07729   136 DVLALDDDLP---GGRVRLVDgdydlfpgVTLIPTPGHTPGHQS 176
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 47-150 5.46e-04

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. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B3 MBLs include Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Stenotrophomonas Maltophilia L1, and Bradyrhizobium diazoefficiens BJP-1, Serratia marcescens SMB-1, and Pseudomonas Aeruginosa AIM-1. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 40.22  E-value: 5.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820342288  47 LTMVLSTHHHWDHTRGNAELAHiLPGLAVLGADERICAL-----------------------TRRLEHGEGLQFGAIHVR 103
Cdd:cd07708    61 TKLILISHAHFDHAGGSAEIKK-QTGAKVMAGAEDVSLLlsggssdfhyandsstyfpqstvDRAVHDGERVTLGGTVLT 139

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1820342288 104 CLLTPGHTSGHMSyflWE----DDCPDSPALF--SGTVQPGFIYLPNSTVPSL 150
Cdd:cd07708   140 AHATPGHTPGCTT---WTmtlkDHGKQYQVVFadSLTVNPGYRLVDNPTYPKI 189
 
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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