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Conserved domains on  [gi|213983201|ref|NP_001135503|]
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hydroxyacylglutathione hydrolase, mitochondrial precursor [Xenopus tropicalis]

Protein Classification

hydroxyacylglutathione hydrolase( domain architecture ID 1004484)

hydroxyacylglutathione hydrolase catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid

CATH:  3.60.15.10
EC:  3.1.2.6
Gene Ontology:  GO:0004416|GO:0019243|GO:0046872
SCOP:  4002292

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02469 super family cl31885
hydroxyacylglutathione hydrolase
 54-309 1.33e-136

hydroxyacylglutathione hydrolase


The actual alignment was detected with superfamily member PLN02469:

Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 387.19  E-value: 1.33e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  54 MKVELIPALTDNYMYLLIDEESKEAAIVDPVQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMVSGLKVYGGD- 132
Cdd:PLN02469   1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 133 SRIGALTQKVSHLTTFQVGS-LHVKCLYTPCHTSGHICYYVT-KPNstEPPAVFTGDTLFVAGCGKFFEGTPEEMYAALI 210
Cdd:PLN02469  81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTgKEG--EDPAVFTGDTLFIAGCGKFFEGTAEQMYQSLC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 211 EVLGRLPPETRVYCGHEYTINNLKFARHVEPCNDAIKQKLAWAKETYNSGEPTIPSTLAEEFTFNPFMRVREKSVQEHAG 290
Cdd:PLN02469 159 VTLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVG 238

                        250
                 ....*....|....*....
gi 213983201 291 ERDPISTMGAIRKEKDHFK 309
Cdd:PLN02469 239 CESPVEALREVRKMKDNWK 257
 
Name Accession Description Interval E-value
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 54-309 1.33e-136

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 387.19  E-value: 1.33e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  54 MKVELIPALTDNYMYLLIDEESKEAAIVDPVQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMVSGLKVYGGD- 132
Cdd:PLN02469   1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 133 SRIGALTQKVSHLTTFQVGS-LHVKCLYTPCHTSGHICYYVT-KPNstEPPAVFTGDTLFVAGCGKFFEGTPEEMYAALI 210
Cdd:PLN02469  81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTgKEG--EDPAVFTGDTLFIAGCGKFFEGTAEQMYQSLC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 211 EVLGRLPPETRVYCGHEYTINNLKFARHVEPCNDAIKQKLAWAKETYNSGEPTIPSTLAEEFTFNPFMRVREKSVQEHAG 290
Cdd:PLN02469 159 VTLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVG 238

                        250
                 ....*....|....*....
gi 213983201 291 ERDPISTMGAIRKEKDHFK 309
Cdd:PLN02469 239 CESPVEALREVRKMKDNWK 257
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 59-308 1.25e-106

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: 310.62  E-value: 1.25e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201   59 IPALTDNYMYLLIDEEsKEAAIVDPVQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKmVSGLKVYGG-DSRIGA 137
Cdd:TIGR03413   4 IPALSDNYIWLLHDPD-GQAAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLE-AFPAPVYGPaEERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  138 LTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYvtkpnSTEPPAVFTGDTLFVAGCGKFFEGTPEEMYAALiEVLGRLP 217
Cdd:TIGR03413  82 ITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYY-----LPDSPALFCGDTLFSAGCGRLFEGTPEQMYDSL-QRLAALP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  218 PETRVYCGHEYTINNLKFARHVEPCNDAIKQKLAWAKETYNSGEPTIPSTLAEEFTFNPFMRVREKSVQEHAGER--DPI 295
Cdd:TIGR03413 156 DDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAALGSQgaDPV 235

                         250
                  ....*....|...
gi 213983201  296 STMGAIRKEKDHF 308
Cdd:TIGR03413 236 EVFAALRAWKDNF 248
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 59-226 1.81e-98

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: 287.05  E-value: 1.81e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  59 IPALTDNYMYLLIDEESKEAAIVDPVQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMVSGLKVYGG-DSRIGA 137
Cdd:cd07723    3 IPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPaEDRIPG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 138 LTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYVtkpnsTEPPAVFTGDTLFVAGCGKFFEGTPEEMYAALIEVLGrLP 217
Cdd:cd07723   83 LDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV-----PDEPALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLA-LP 156


                 ....*....
gi 213983201 218 PETRVYCGH 226
Cdd:cd07723  157 DDTLVYCGH 165
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 227-308 1.62e-41

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: 138.73  E-value: 1.62e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  227 EYTINNLKFARHVEPCNDAIKQKLAWAKETYNSGEPTIPSTLAEEFTFNPFMRVREKSVQEHAGERDPISTMGAIRKEKD 306
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGETDPVEVFAALRELKD 80


                  ..
gi 213983201  307 HF 308
Cdd:pfam16123  81 NF 82
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 56-240 1.01e-37

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: 133.28  E-value: 1.01e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  56 VELIPALTDNYMYLLIDEEskEAAIVDP----VQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMvSGLKVYGG 131
Cdd:COG0491    6 GGTPGAGLGVNSYLIVGGD--GAVLIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEA-FGAPVYAH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 132 DSRIGALTQKVSHL----------------TTFQVGSLHVKCLYTPCHTSGHICYYVtkpnsTEPPAVFTGDTLFVAGCG 195
Cdd:COG0491   83 AAEAEALEAPAAGAlfgrepvppdrtledgDTLELGGPGLEVIHTPGHTPGHVSFYV-----PDEKVLFTGDALFSGGVG 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 213983201 196 K--FFEGTPEEMYAALiEVLGRLPPEtRVYCGHEYTINNLKFARHVE 240
Cdd:COG0491  158 RpdLPDGDLAQWLASL-ERLLALPPD-LVIPGHGPPTTAEAIDYLEE 202
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 66-226 1.40e-28

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 108.41  E-value: 1.40e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201    66 YMYLLIDEesKEAAIVDPV--QPQKVVDAVKKHGV-KLTTVLTTHHHWDHAGGNEKLVKMvSGLKVYG------------ 130
Cdd:smart00849   1 NSYLVRDD--GGAILIDTGpgEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEA-PGAPVYApegtaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201   131 -------GDSRIGALTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYVtkpnsTEPPAVFTGDTLFVAGCG-KFFEGTP 202
Cdd:smart00849  78 allgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL-----PEGKILFTGDLLFAGGDGrTLVDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 213983201   203 EEMYAALIEVLGRL-PPETRVYCGH 226
Cdd:smart00849 153 AAASDALESLLKLLkLLPKLVVPGH 177
 
Name Accession Description Interval E-value
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 54-309 1.33e-136

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 387.19  E-value: 1.33e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  54 MKVELIPALTDNYMYLLIDEESKEAAIVDPVQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMVSGLKVYGGD- 132
Cdd:PLN02469   1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 133 SRIGALTQKVSHLTTFQVGS-LHVKCLYTPCHTSGHICYYVT-KPNstEPPAVFTGDTLFVAGCGKFFEGTPEEMYAALI 210
Cdd:PLN02469  81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTgKEG--EDPAVFTGDTLFIAGCGKFFEGTAEQMYQSLC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 211 EVLGRLPPETRVYCGHEYTINNLKFARHVEPCNDAIKQKLAWAKETYNSGEPTIPSTLAEEFTFNPFMRVREKSVQEHAG 290
Cdd:PLN02469 159 VTLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVG 238

                        250
                 ....*....|....*....
gi 213983201 291 ERDPISTMGAIRKEKDHFK 309
Cdd:PLN02469 239 CESPVEALREVRKMKDNWK 257
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 59-308 1.25e-106

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: 310.62  E-value: 1.25e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201   59 IPALTDNYMYLLIDEEsKEAAIVDPVQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKmVSGLKVYGG-DSRIGA 137
Cdd:TIGR03413   4 IPALSDNYIWLLHDPD-GQAAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLE-AFPAPVYGPaEERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  138 LTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYvtkpnSTEPPAVFTGDTLFVAGCGKFFEGTPEEMYAALiEVLGRLP 217
Cdd:TIGR03413  82 ITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYY-----LPDSPALFCGDTLFSAGCGRLFEGTPEQMYDSL-QRLAALP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  218 PETRVYCGHEYTINNLKFARHVEPCNDAIKQKLAWAKETYNSGEPTIPSTLAEEFTFNPFMRVREKSVQEHAGER--DPI 295
Cdd:TIGR03413 156 DDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAALGSQgaDPV 235

                         250
                  ....*....|...
gi 213983201  296 STMGAIRKEKDHF 308
Cdd:TIGR03413 236 EVFAALRAWKDNF 248
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 59-226 1.81e-98

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: 287.05  E-value: 1.81e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  59 IPALTDNYMYLLIDEESKEAAIVDPVQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMVSGLKVYGG-DSRIGA 137
Cdd:cd07723    3 IPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPaEDRIPG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 138 LTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYVtkpnsTEPPAVFTGDTLFVAGCGKFFEGTPEEMYAALIEVLGrLP 217
Cdd:cd07723   83 LDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV-----PDEPALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLA-LP 156


                 ....*....
gi 213983201 218 PETRVYCGH 226
Cdd:cd07723  157 DDTLVYCGH 165
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 53-308 4.21e-72

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 225.88  E-value: 4.21e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  53 TMKVELIPALTDNYMYLLIDEESKEAAIVDPVQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLvKMVSGLKVYGGD 132
Cdd:PLN02398  75 SLQIELVPCLKDNYAYLLHDEDTGTVGVVDPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLEL-KARYGAKVIGSA 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 133 ---SRIGALTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYVtkPNSTeppAVFTGDTLFVAGCGKFFEGTPEEMYAAL 209
Cdd:PLN02398 154 vdkDRIPGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYF--PGSG---AIFTGDTLFSLSCGKLFEGTPEQMLSSL 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 210 IEVLGrLPPETRVYCGHEYTINNLKFARHVEPCNDAIKQKLAWAKETYNSGEPTIPSTLAEEFTFNPFMRVREK------ 283
Cdd:PLN02398 229 QKIIS-LPDDTNIYCGHEYTLSNSKFALSIEPNNEVLQSYAAHVAHLRSKGLPTIPTTVKMEKACNPFLRTSSTdirksl 307

                        250       260
                 ....*....|....*....|....*
gi 213983201 284 SVQEHAGERDpisTMGAIRKEKDHF 308
Cdd:PLN02398 308 SIPDTADEAE---ALGIIRRAKDNF 329
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 54-308 3.35e-51

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 169.62  E-value: 3.35e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  54 MKVELIPALTDNYMYLLIDEESKeAAIVDPVQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMVSGLKVYG-GD 132
Cdd:PRK10241   1 MNLNSIPAFDDNYIWVLNDEAGR-CLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGpQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 133 SRIGALTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYvtkpnstEPPAVFTGDTLFVAGCGKFFEGTPEEMYAALIEV 212
Cdd:PRK10241  80 TQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF-------SKPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 213 lGRLPPETRVYCGHEYTINNLKFARHVEPCNDAIKQKLAWAKETYNSGEPTIPSTLAEEFTFNPFMRVRE----KSVQEH 288
Cdd:PRK10241 153 -NALPDDTLICCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINLFLRTEDidliNVINEE 231

                        250       260
                 ....*....|....*....|
gi 213983201 289 AGERDPISTMGAIRKEKDHF 308
Cdd:PRK10241 232 TLLQQPEERFAWLRSKKDRF 251
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 64-226 1.96e-42

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: 144.22  E-value: 1.96e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  64 DNYMYLLIDEESKEAAIVDPV-QPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMVsGLKVYGGDSRI------- 135
Cdd:cd16275   11 INYSYIIIDKATREAAVVDPAwDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKY-DAPVYMSKEEIdyygfrc 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 136 GALtQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYVtkPNSteppaVFTGDTLFVAGCG--KFFEGTPEEMYAAlIEVL 213
Cdd:cd16275   90 PNL-IPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLL--GDS-----LFTGDTLFIEGCGrcDLPGGDPEEMYES-LQRL 160

                        170
                 ....*....|....
gi 213983201 214 GRLPPE-TRVYCGH 226
Cdd:cd16275  161 KKLPPPnTRVYPGH 174
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 227-308 1.62e-41

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: 138.73  E-value: 1.62e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  227 EYTINNLKFARHVEPCNDAIKQKLAWAKETYNSGEPTIPSTLAEEFTFNPFMRVREKSVQEHAGERDPISTMGAIRKEKD 306
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGETDPVEVFAALRELKD 80


                  ..
gi 213983201  307 HF 308
Cdd:pfam16123  81 NF 82
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 68-228 2.19e-38

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: 133.68  E-value: 2.19e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  68 YLLIDEESKEAAIVDPV--QPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMVsGLKVYGGDSRIGALT-QKVSH 144
Cdd:cd07724   15 YLVGDPETGEAAVIDPVrdSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERT-GAPIVIGEGAPASFFdRLLKD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 145 LTTFQVGSLHVKCLYTPCHTSGHICYYVTKPNsteppAVFTGDTLFVAGCG-----KFFEGTPEEMYAALIEVLGRLPPE 219
Cdd:cd07724   94 GDVLELGNLTLEVLHTPGHTPESVSYLVGDPD-----AVFTGDTLFVGDVGrpdlpGEAEGLARQLYDSLQRKLLLLPDE 168


                 ....*....
gi 213983201 220 TRVYCGHEY 228
Cdd:cd07724  169 TLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 56-240 1.01e-37

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: 133.28  E-value: 1.01e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  56 VELIPALTDNYMYLLIDEEskEAAIVDP----VQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMvSGLKVYGG 131
Cdd:COG0491    6 GGTPGAGLGVNSYLIVGGD--GAVLIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEA-FGAPVYAH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 132 DSRIGALTQKVSHL----------------TTFQVGSLHVKCLYTPCHTSGHICYYVtkpnsTEPPAVFTGDTLFVAGCG 195
Cdd:COG0491   83 AAEAEALEAPAAGAlfgrepvppdrtledgDTLELGGPGLEVIHTPGHTPGHVSFYV-----PDEKVLFTGDALFSGGVG 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 213983201 196 K--FFEGTPEEMYAALiEVLGRLPPEtRVYCGHEYTINNLKFARHVE 240
Cdd:COG0491  158 RpdLPDGDLAQWLASL-ERLLALPPD-LVIPGHGPPTTAEAIDYLEE 202
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 68-226 8.12e-37

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: 130.10  E-value: 8.12e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  68 YLLIDEEsKEAAIVDPVQP--QKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMvSGLKVY---------------- 129
Cdd:cd06262   13 YLVSDEE-GEAILIDPGAGalEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEA-PGAPVYiheadaelledpelnl 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 130 ----GGDSRIGALTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYVTKPNsteppAVFTGDTLFVAGCGK--FFEGTPE 203
Cdd:cd06262   91 affgGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEG-----VLFTGDTLFAGSIGRtdLPGGDPE 165

                        170       180
                 ....*....|....*....|...
gi 213983201 204 EMYAALIEVLGRLPPETRVYCGH 226
Cdd:cd06262  166 QLIESIKKLLLLLPDDTVVYPGH 188
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 66-226 1.40e-28

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 108.41  E-value: 1.40e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201    66 YMYLLIDEesKEAAIVDPV--QPQKVVDAVKKHGV-KLTTVLTTHHHWDHAGGNEKLVKMvSGLKVYG------------ 130
Cdd:smart00849   1 NSYLVRDD--GGAILIDTGpgEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEA-PGAPVYApegtaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201   131 -------GDSRIGALTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYVtkpnsTEPPAVFTGDTLFVAGCG-KFFEGTP 202
Cdd:smart00849  78 allgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL-----PEGKILFTGDLLFAGGDGrTLVDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 213983201   203 EEMYAALIEVLGRL-PPETRVYCGH 226
Cdd:smart00849 153 AAASDALESLLKLLkLLPKLVVPGH 177
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 68-278 1.58e-24

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: 98.19  E-value: 1.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  68 YLLIDEESKEAAIVDP-VQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMvSGLKVY--GGDSRI------GAL 138
Cdd:cd16322   14 YLVADEGGGEAVLVDPgDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRH-PGAPVYlhPDDLPLyeaadlGAK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 139 TQKVS------------HLTTFQVGSLHVKCLYTPCHTSGHICYYVtkpnsTEPPAVFTGDTLFVAGCGK--FFEGTPEE 204
Cdd:cd16322   93 AFGLGieplpppdrlleDGQTLTLGGLEFKVLHTPGHSPGHVCFYV-----EEEGLLFSGDLLFQGSIGRtdLPGGDPKA 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 213983201 205 MYAALIEVLgRLPPETRVYCGHeytinnlkfarhvepcndaikqklawaketynsGEPTipsTLAEEFTFNPFM 278
Cdd:cd16322  168 MAASLRRLL-TLPDETRVFPGH---------------------------------GPPT---TLGEERRTNPFL 204
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 68-226 6.41e-22

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: 90.69  E-value: 6.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  68 YLLIDEESKEAAIVDP-VQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMvSGLKVYG---GD----------S 133
Cdd:cd07737   14 SLIWCEETKEAAVIDPgGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEH-YGVPIIGphkEDkfllenlpeqS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 134 RIGAL--------TQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYvtkpnSTEPPAVFTGDTLFVAGCGK--FFEGTPE 203
Cdd:cd07737   93 QMFGFppaeaftpDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFF-----NRESKLAIVGDVLFKGSIGRtdFPGGNHA 167

                        170       180
                 ....*....|....*....|...
gi 213983201 204 EMYAALIEVLGRLPPETRVYCGH 226
Cdd:cd07737  168 QLIASIKEKLLPLGDDVTFIPGH 190
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 66-228 2.47e-17

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 79.84  E-value: 2.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  66 YMYLLID--EESKEAAIVDPVQpqKVVDA----VKKHGVKLTTVLTTHHHWDHAGGNEKLVKMVSGLKvyggdSRIG-AL 138
Cdd:PLN02962  24 YTYLLADvsHPDKPALLIDPVD--KTVDRdlslVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVK-----SIISkAS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 139 TQKVSHLT----TFQVGSLHVKCLYTPCHTSGHICYyVT--KPNSTEPPAVFTGDTLFVAGCGK--FFEGTPEEMYAALI 210
Cdd:PLN02962  97 GSKADLFVepgdKIYFGDLYLEVRATPGHTAGCVTY-VTgeGPDQPQPRMAFTGDALLIRGCGRtdFQGGSSDQLYKSVH 175

                        170
                 ....*....|....*...
gi 213983201 211 EVLGRLPPETRVYCGHEY 228
Cdd:PLN02962 176 SQIFTLPKDTLIYPAHDY 193
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 55-226 1.18e-14

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 71.10  E-value: 1.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  55 KVELIPALTDNYMYLLIDEEskEAAIVD---PVQPQKVVDAVKKHGVK---LTTVLTTHHHWDHAGGNEKLVKMvSGLKV 128
Cdd:cd07721    1 GVYQLPLLPPVNAYLIEDDD--GLTLIDtglPGSAKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAALKEA-PGAPV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 129 Y------------------GGDSRIGALTQKVSHLTTFQV------------GSLHVkcLYTPCHTSGHICYYVTKPNst 178
Cdd:cd07721   78 YahereapylegekpypppVRLGLLGLLSPLLPVKPVPVDrtledgdtldlaGGLRV--IHTPGHTPGHISLYLEEDG-- 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 213983201 179 eppAVFTGDTLFVAGcGKFFEGTP---EEMYAAL--IEVLGRLPPETrVYCGH 226
Cdd:cd07721  154 ---VLIAGDALVTVG-GELVPPPPpftWDMEEALesLRKLAELDPEV-LAPGH 201
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 68-195 2.73e-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: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 67.13  E-value: 2.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  68 YLLidEESKEAAIVDPvQP------QKVVDAVKkhGVKLTTVLTTHHHWDHAGGNEKLVKMVsGLKVYGGDSRIGALTQK 141
Cdd:cd16278   21 YLL--GAPDGVVVIDP-GPddpahlDALLAALG--GGRVSAILVTHTHRDHSPGAARLAERT-GAPVRAFGPHRAGGQDT 94

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 213983201 142 -------VSHLTTFQVGSLHVKCLYTPCHTSGHICYYVtkpnsTEPPAVFTGDTlfVAGCG 195
Cdd:cd16278   95 dfapdrpLADGEVIEGGGLRLTVLHTPGHTSDHLCFAL-----EDEGALFTGDH--VMGWS 148
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 91-226 2.85e-13

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: 67.17  E-value: 2.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  91 DAVKKHGVK-LTTVLTTHHHWDHAGGNEKLVKMVSG--LKVY-----GGDSRIGALTQKVSHLT---TFQVGSLHVKCLY 159
Cdd:cd07722   47 SVLDSEGNAtISDILLTHWHHDHVGGLPDVLDLLRGpsPRVYkfprpEEDEDPDEDGGDIHDLQdgqVFKVEGATLRVIH 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 213983201 160 TPCHTSGHICYYVtkpnsTEPPAVFTGDTlfVAGCGKffegTPEEMYAALIEVLGRLP--PETRVYCGH 226
Cdd:cd07722  127 TPGHTTDHVCFLL-----EEENALFTGDC--VLGHGT----AVFEDLAAYMASLKKLLslGPGRIYPGH 184
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 68-226 1.91e-12

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: 65.21  E-value: 1.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  68 YLLIDEesKEAAIVDP---VQPQKVVDAVKKHGV---KLTTVLTTHHHWDHAGG---------N---------------- 116
Cdd:cd07726   19 YLLDGE--GRPALIDTgpsSSVPRLLAALEALGIapeDVDYIILTHIHLDHAGGagllaealpNakvyvhprgarhlidp 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 117 EKLVKmvSGLKVYGGD-------------SRIGALTqkvsHLTTFQVGSLHVKCLYTPCHTSGHICYYVTKPNSteppaV 183
Cdd:cd07726   97 SKLWA--SARAVYGDEadrlggeilpvpeERVIVLE----DGETLDLGGRTLEVIDTPGHAPHHLSFLDEESDG-----L 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 213983201 184 FTGDTLFVAGCGKFFEGTPE--------EMYAALIEVLGRLPPEtRVYCGH 226
Cdd:cd07726  166 FTGDAAGVRYPELDVVGPPStpppdfdpEAWLESLDRLLSLKPE-RIYLTH 215
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 62-189 1.33e-10

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: 59.62  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  62 LTDNYMYLLIDeeskeAAIVDPVQPQKVVDAVKKHGVKL---TTVLTTHHHWDHAGGNEKLVKmVSGLKVYGGDSRIgal 138
Cdd:cd07725   20 LRDGDETTLID-----TGLATEEDAEALWEGLKELGLKPsdiDRVLLTHHHPDHIGLAGKLQE-KSGATVYILDVTP--- 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 213983201 139 tqkVSHLTTFQVGSLHVKCLYTPCHTSGHICYYVTKpnSTEppaVFTGDTL 189
Cdd:cd07725   91 ---VKDGDKIDLGGLRLKVIETPGHTPGHIVLYDED--RRE---LFVGDAV 133
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
68-226 1.83e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 59.30  E-value: 1.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201   68 YLLIDEEskEAAIVDP-----VQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVK-------MVSGLKVYGGDSRI 135
Cdd:pfam00753   9 YLIEGGG--GAVLIDTggsaeAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEatdvpviVVAEEARELLDEEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  136 GALTQKVSHLTTFQVGSLHVKCLY--------------TPCHTSGHICYYVTKPNSTeppAVFTGDTLFVAGCGK--FFE 199
Cdd:pfam00753  87 GLAASRLGLPGPPVVPLPPDVVLEegdgilggglgllvTHGPGHGPGHVVVYYGGGK---VLFTGDLLFAGEIGRldLPL 163

                         170       180       190
                  ....*....|....*....|....*....|...
gi 213983201  200 GTPEEMYAALIEVLGRL------PPETRVYCGH 226
Cdd:pfam00753 164 GGLLVLHPSSAESSLESllklakLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 78-226 8.99e-09

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: 54.49  E-value: 8.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  78 AAIVD----PVQPQKVVDAVKKH-GVKLTTVLTTHHHWDHAGGN-------------------------EKLVKMVSGLK 127
Cdd:cd16282   26 VVVIDtgasPRLARALLAAIRKVtDKPVRYVVNTHYHGDHTLGNaafadagapiiahentreelaargeAYLELMRRLGG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 128 VYGGDSRIGALTQKVSHLTTFQVGSLHVKCLYT-PCHTSGHICYYVTKPNsteppAVFTGDTLFVAGCGKFFEGTPEEMY 206
Cdd:cd16282  106 DAMAGTELVLPDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEG-----VLFAGDLVFNGRIPFLPDGSLAGWI 180

                        170       180
                 ....*....|....*....|
gi 213983201 207 AALiEVLGRLPPETRVyCGH 226
Cdd:cd16282  181 AAL-DRLLALDATVVV-PGH 198
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 87-227 7.11e-08

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: 52.22  E-value: 7.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  87 QKVVDAVKKHGVK---LTTVLTTHHHWDHAGGNEKLVK------------MVSGLKVYGGDSRIGAltQKVSHLTTFQVG 151
Cdd:cd07729   73 QTLEEQLARLGLDpedIDYVILSHLHFDHAGGLDLFPNatiivqraeleyATGPDPLAAGYYEDVL--ALDDDLPGGRVR 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 152 SLH--------VKCLYTPCHTSGHICYYVtkpNSTEPPAVFTGDTLFVA-----GCGKFFEGTPEEMYAAL--IEVLGRL 216
Cdd:cd07729  151 LVDgdydlfpgVTLIPTPGHTPGHQSVLV---RLPEGTVLLAGDAAYTYenleeGRPPGINYDPEAALASLerLKALAER 227

                        170
                 ....*....|.
gi 213983201 217 PPeTRVYCGHE 227
Cdd:cd07729  228 EG-ARVIPGHD 237
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 38-203 1.22e-07

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: 51.79  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  38 QTPFELR-NSKVVTQCTMKVELIpalTDNYMYLLIDEESkeaaivdPVQPQKVVDAVKKHGVKLTTV---LTTHHHWDHA 113
Cdd:cd16313    5 QEPFQIYgNTYYVGTGGISAVLI---TSPQGHILIDGGF-------PKSPEQIAASIRQLGFKLEDVkyiLSSHDHWDHA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 114 GGNEKLVKMvSGLKVYGGDSRIGALTQKVS--------HLTTF---------------QVGSLHVKCLYTPCHTSGHICY 170
Cdd:cd16313   75 GGIAALQKL-TGAQVLASPATVAVLRSGSMgkddpqfgGLTPMppvasvravrdgevvKLGPLAVTAHATPGHTTGGTSW 153

                        170       180       190
                 ....*....|....*....|....*....|....
gi 213983201 171 YVTKPNSTEPPAVFTGDTLFVAGCGKF-FEGTPE 203
Cdd:cd16313  154 TWQSCEQGRCANMVFADSLTAVSADGYrFSAHPA 187
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 69-168 1.04e-06

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: 48.35  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  69 LLIDEESKeaAIVDPVQP---QKVVDAVKKHGVKL---TTVLTTHHHWDHAGGNE--KLVKMVSGLKVYGGDSRIGALTQ 140
Cdd:cd07711   26 LIKDGGKN--ILVDTGTPwdrDLLLKALAEHGLSPediDYVVLTHGHPDHIGNLNlfPNATVIVGWDICGDSYDDHSLEE 103

                         90       100
                 ....*....|....*....|....*...
gi 213983201 141 kvshLTTFQVGSlHVKCLYTPCHTSGHI 168
Cdd:cd07711  104 ----GDGYEIDE-NVEVIPTPGHTPEDV 126
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 66-226 3.45e-06

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: 46.47  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  66 YMYLLidEESKEAAIVDPVQPQK-VVDAVKKHGVKLTTVLTTHHHWDHAGGNE---------------KLVKMVSGLKVY 129
Cdd:cd07712   10 NIYLL--RGRDRALLIDTGLGIGdLKEYVRTLTDLPLLVVATHGHFDHIGGLHefeevyvhpadaeilAAPDNFETLTWD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 130 GGDSRI--GALTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYVTKPNsteppAVFTGDTLFVAGCGKFFEGTPEEMYA 207
Cdd:cd07712   88 AATYSVppAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANR-----LLFSGDVVYDGPLIMDLPHSDLDDYL 162

                        170       180
                 ....*....|....*....|
gi 213983201 208 ALIEVLGRLPPETR-VYCGH 226
Cdd:cd07712  163 ASLEKLSKLPDEFDkVLPGH 182
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 62-193 4.12e-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: 47.06  E-value: 4.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  62 LTDNYMYLLIDEESKEAAivdpvqpqKVVDA-VKKHGVKLTTV---LTTHHHWDHAGGNEKLvKMVSGLKVYGGDSRIGA 137
Cdd:cd16310   27 ITSNHGAILLDGGLEENA--------ALIEQnIKALGFKLSDIkiiINTHAHYDHAGGLAQL-KADTGAKLWASRGDRPA 97

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 213983201 138 LTQ-----------------KVSHL----TTFQVGSLHVKCLYTPCHTSGHICYYVTKPNSTEPPAVFTGDTLFVAG 193
Cdd:cd16310   98 LEAgkhigdnitqpapfpavKVDRIlgdgEKIKLGDITLTATLTPGHTKGCTTWSTTVKENGRPLRVVFPCSLSVAG 174
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 63-211 8.14e-06

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: 46.38  E-value: 8.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  63 TDNYMYLLIdEESKEAAIVDPVQPQK---VVDAVKKHGVKLTTV---LTTHHHWDHAGGNEkLVKMVSGLKVYGGDSRIG 136
Cdd:cd07708   19 TDDLAAYLI-VTPQGNILIDGDMEQNapmIKANIKKLGFKFSDTkliLISHAHFDHAGGSA-EIKKQTGAKVMAGAEDVS 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201 137 ALTQKVS--------HLTTF---------------QVGSLHVKCLYTPCHTSGHICYYVTKPNSTEPPAVFTGDTLFVAG 193
Cdd:cd07708   97 LLLSGGSsdfhyandSSTYFpqstvdravhdgervTLGGTVLTAHATPGHTPGCTTWTMTLKDHGKQYQVVFADSLTVNP 176

                        170
                 ....*....|....*...
gi 213983201 194 CGKfFEGTPEemYAALIE 211
Cdd:cd07708  177 GYR-LVDNPT--YPKIVE 191
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 70-129 1.01e-05

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: 45.60  E-value: 1.01e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 213983201  70 LIDEESKEAAIVDPVQPQKVVDAVKK----HGVKLTTVLTTHHHWDHAGGNEKLVKMvSGLKVY 129
Cdd:cd07743   12 VYVFGDKEALLIDSGLDEDAGRKIRKileeLGWKLKAIINTHSHADHIGGNAYLQKK-TGCKVY 74
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 75-112 2.77e-05

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: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 44.03  E-value: 2.77e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 213983201  75 SKEAAIVDPV----QPQKVVDAVKKHGVKLTTVLTTHHHWDH 112
Cdd:cd07739   24 ETEAVLVDAQftraDAERLADWIKASGKTLTTIYITHGHPDH 65
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 ...
 98-166 2.12e-04

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: 41.95  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 213983201  98 VKLttVLTTHHHWDHAGGNEKLVKMvSGLKVYGGDSRIGAL-----------------------TQKVSHLTTFQVGSLH 154
Cdd:cd16290   61 VKL--ILNSHAHFDHAGGIAALQRD-SGATVAASPAGAAALrsggvdpddpqagaadpfppvakVRVVADGEVVKLGPLA 137

                         90
                 ....*....|..
gi 213983201 155 VKCLYTPCHTSG 166
Cdd:cd16290  138 VTAHATPGHTPG 149
IND_BlaB-like_MBL-B1 cd16299
IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 65-115 1.05e-03

IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded metallo-beta-lactamases Chryseobacterium indologenes IND-1, IND-2, and IND-7, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB, Chryseobacterium gleum CGB-1, and Empedobacter brevis EBR-1. 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 MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293857  Cd Length: 212  Bit Score: 39.74  E-value: 1.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 213983201  65 NYMYLLideeSKEAAIV-----DPVQPQKVVDAVK-KHGVKLTTVLTTHHHWDHAGG 115
Cdd:cd16299   27 NAMYLV----TKKGVILfdtpwDKDQYQPLLDSIRkKHNLPVIAVIATHSHEDRAGG 79
SPM-1-like_MBL-B1-B2-like cd16286
Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; ...
 69-132 1.34e-03

Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; MBL-fold metallo-hydrolase domain; SPM-1 was first identified in a Pseudomonas aeruginosa strain from a paediatric leukaemia patient and is a major clinical problem. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs are most closely related to each other. SPM-1 appears to be a hybrid B1/B2 MBL.


Pssm-ID: 293844 [Multi-domain]  Cd Length: 236  Bit Score: 39.44  E-value: 1.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 213983201  69 LLIDEESKEAAIVDP----VQPQKVVDAV-KKHGVKLTTVLTTHHHWDHAGGNEKLVKMvsGLKVYGGD 132
Cdd:cd16286   30 LVVKMLDGTVVIVDSpytnLATQTVLDWIaKTMGPRKVVAINTHFHLDGTGGNEALKKR--GIPTWGSD 96
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 83-115 1.74e-03

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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 39.17  E-value: 1.74e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 213983201  83 PVQPQK-VVDAVKKHGVKL---TTVLTTHHHWDHAGG 115
Cdd:cd07730   63 PLEVEEdVAEQLAAGGIDPediDAVILSHLHWDHIGG 99
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 87-132 3.53e-03

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. 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: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 37.88  E-value: 3.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 213983201  87 QKVVDAVKKHGV-KLTTVLTTHHHWDHAGGNEKLVKMVSGLKVYGGD 132
Cdd:cd07731   35 DVVVPYLKARGIkKLDYLILTHPDADHIGGLDAVLKNFPVKEVYMPG 81
 
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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