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Conserved domains on  [gi|1785411060|ref|XP_031748408|]
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hydroxyacylglutathione hydrolase, mitochondrial isoform X2 [Xenopus tropicalis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02469 super family cl31885
hydroxyacylglutathione hydrolase
 72-327 1.48e-135

hydroxyacylglutathione hydrolase


The actual alignment was detected with superfamily member PLN02469:

Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 385.27  E-value: 1.48e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  72 MKVELIPALTDNYMYLLIDEESKEAAIVDPVQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMVSGLKVYGGD- 150
Cdd:PLN02469    1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 151 SRIGALTQKVSHLTTFQVGS-LHVKCLYTPCHTSGHICYYVT-KPNstEPPAVFTGDTLFVAGCGKFFEGTPEEMYAALI 228
Cdd:PLN02469   81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTgKEG--EDPAVFTGDTLFIAGCGKFFEGTAEQMYQSLC 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 229 EVLGRLPPETRVYCGHEYTINNLKFARHVEPCNDAIKQKLAWAKETYNSGEPTIPSTLAEEFTFNPFMRVREKSVQEHAG 308
Cdd:PLN02469  159 VTLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVG 238

                         250
                  ....*....|....*....
gi 1785411060 309 ERDPISTMGAIRKEKDHFK 327
Cdd:PLN02469  239 CESPVEALREVRKMKDNWK 257
 
Name Accession Description Interval E-value
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 72-327 1.48e-135

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 385.27  E-value: 1.48e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  72 MKVELIPALTDNYMYLLIDEESKEAAIVDPVQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMVSGLKVYGGD- 150
Cdd:PLN02469    1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 151 SRIGALTQKVSHLTTFQVGS-LHVKCLYTPCHTSGHICYYVT-KPNstEPPAVFTGDTLFVAGCGKFFEGTPEEMYAALI 228
Cdd:PLN02469   81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTgKEG--EDPAVFTGDTLFIAGCGKFFEGTAEQMYQSLC 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 229 EVLGRLPPETRVYCGHEYTINNLKFARHVEPCNDAIKQKLAWAKETYNSGEPTIPSTLAEEFTFNPFMRVREKSVQEHAG 308
Cdd:PLN02469  159 VTLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVG 238

                         250
                  ....*....|....*....
gi 1785411060 309 ERDPISTMGAIRKEKDHFK 327
Cdd:PLN02469  239 CESPVEALREVRKMKDNWK 257
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 77-326 8.54e-107

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: 311.78  E-value: 8.54e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  77 IPALTDNYMYLLIDEEsKEAAIVDPVQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKmVSGLKVYGG-DSRIGA 155
Cdd:TIGR03413   4 IPALSDNYIWLLHDPD-GQAAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLE-AFPAPVYGPaEERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 156 LTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYvtkpnSTEPPAVFTGDTLFVAGCGKFFEGTPEEMYAALiEVLGRLP 235
Cdd:TIGR03413  82 ITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYY-----LPDSPALFCGDTLFSAGCGRLFEGTPEQMYDSL-QRLAALP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 236 PETRVYCGHEYTINNLKFARHVEPCNDAIKQKLAWAKETYNSGEPTIPSTLAEEFTFNPFMRVREKSVQEHAGER--DPI 313
Cdd:TIGR03413 156 DDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAALGSQgaDPV 235

                         250
                  ....*....|...
gi 1785411060 314 STMGAIRKEKDHF 326
Cdd:TIGR03413 236 EVFAALRAWKDNF 248
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 77-244 7.31e-99

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: 288.59  E-value: 7.31e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  77 IPALTDNYMYLLIDEESKEAAIVDPVQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMVSGLKVYGG-DSRIGA 155
Cdd:cd07723     3 IPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPaEDRIPG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 156 LTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYVtkpnsTEPPAVFTGDTLFVAGCGKFFEGTPEEMYAALIEVLGrLP 235
Cdd:cd07723    83 LDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV-----PDEPALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLA-LP 156


                  ....*....
gi 1785411060 236 PETRVYCGH 244
Cdd:cd07723   157 DDTLVYCGH 165
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 245-326 3.06e-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: 138.34  E-value: 3.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 245 EYTINNLKFARHVEPCNDAIKQKLAWAKETYNSGEPTIPSTLAEEFTFNPFMRVREKSVQEHAGERDPISTMGAIRKEKD 324
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGETDPVEVFAALRELKD 80


                  ..
gi 1785411060 325 HF 326
Cdd:pfam16123  81 NF 82
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 74-258 5.85e-38

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: 134.43  E-value: 5.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  74 VELIPALTDNYMYLLIDEEskEAAIVDP----VQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMvSGLKVYGG 149
Cdd:COG0491     6 GGTPGAGLGVNSYLIVGGD--GAVLIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEA-FGAPVYAH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 150 DSRIGALTQKVSHL----------------TTFQVGSLHVKCLYTPCHTSGHICYYVtkpnsTEPPAVFTGDTLFVAGCG 213
Cdd:COG0491    83 AAEAEALEAPAAGAlfgrepvppdrtledgDTLELGGPGLEVIHTPGHTPGHVSFYV-----PDEKVLFTGDALFSGGVG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1785411060 214 K--FFEGTPEEMYAALiEVLGRLPPEtRVYCGHEYTINNLKFARHVE 258
Cdd:COG0491   158 RpdLPDGDLAQWLASL-ERLLALPPD-LVIPGHGPPTTAEAIDYLEE 202
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 84-244 1.20e-28

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 108.79  E-value: 1.20e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060   84 YMYLLIDEesKEAAIVDPV--QPQKVVDAVKKHGV-KLTTVLTTHHHWDHAGGNEKLVKMvSGLKVYG------------ 148
Cdd:smart00849   1 NSYLVRDD--GGAILIDTGpgEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEA-PGAPVYApegtaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  149 -------GDSRIGALTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYVtkpnsTEPPAVFTGDTLFVAGCG-KFFEGTP 220
Cdd:smart00849  78 allgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL-----PEGKILFTGDLLFAGGDGrTLVDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 1785411060  221 EEMYAALIEVLGRL-PPETRVYCGH 244
Cdd:smart00849 153 AAASDALESLLKLLkLLPKLVVPGH 177
 
Name Accession Description Interval E-value
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 72-327 1.48e-135

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 385.27  E-value: 1.48e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  72 MKVELIPALTDNYMYLLIDEESKEAAIVDPVQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMVSGLKVYGGD- 150
Cdd:PLN02469    1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYGGSl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 151 SRIGALTQKVSHLTTFQVGS-LHVKCLYTPCHTSGHICYYVT-KPNstEPPAVFTGDTLFVAGCGKFFEGTPEEMYAALI 228
Cdd:PLN02469   81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTgKEG--EDPAVFTGDTLFIAGCGKFFEGTAEQMYQSLC 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 229 EVLGRLPPETRVYCGHEYTINNLKFARHVEPCNDAIKQKLAWAKETYNSGEPTIPSTLAEEFTFNPFMRVREKSVQEHAG 308
Cdd:PLN02469  159 VTLGSLPKPTQVYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEKVG 238

                         250
                  ....*....|....*....
gi 1785411060 309 ERDPISTMGAIRKEKDHFK 327
Cdd:PLN02469  239 CESPVEALREVRKMKDNWK 257
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 77-326 8.54e-107

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: 311.78  E-value: 8.54e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  77 IPALTDNYMYLLIDEEsKEAAIVDPVQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKmVSGLKVYGG-DSRIGA 155
Cdd:TIGR03413   4 IPALSDNYIWLLHDPD-GQAAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLE-AFPAPVYGPaEERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 156 LTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYvtkpnSTEPPAVFTGDTLFVAGCGKFFEGTPEEMYAALiEVLGRLP 235
Cdd:TIGR03413  82 ITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYY-----LPDSPALFCGDTLFSAGCGRLFEGTPEQMYDSL-QRLAALP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 236 PETRVYCGHEYTINNLKFARHVEPCNDAIKQKLAWAKETYNSGEPTIPSTLAEEFTFNPFMRVREKSVQEHAGER--DPI 313
Cdd:TIGR03413 156 DDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPAVRAALGSQgaDPV 235

                         250
                  ....*....|...
gi 1785411060 314 STMGAIRKEKDHF 326
Cdd:TIGR03413 236 EVFAALRAWKDNF 248
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 77-244 7.31e-99

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: 288.59  E-value: 7.31e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  77 IPALTDNYMYLLIDEESKEAAIVDPVQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMVSGLKVYGG-DSRIGA 155
Cdd:cd07723     3 IPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGPaEDRIPG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 156 LTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYVtkpnsTEPPAVFTGDTLFVAGCGKFFEGTPEEMYAALIEVLGrLP 235
Cdd:cd07723    83 LDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV-----PDEPALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLA-LP 156


                  ....*....
gi 1785411060 236 PETRVYCGH 244
Cdd:cd07723   157 DDTLVYCGH 165
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 71-326 5.50e-72

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 226.26  E-value: 5.50e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  71 TMKVELIPALTDNYMYLLIDEESKEAAIVDPVQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLvKMVSGLKVYGGD 150
Cdd:PLN02398   75 SLQIELVPCLKDNYAYLLHDEDTGTVGVVDPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLEL-KARYGAKVIGSA 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 151 ---SRIGALTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYVtkPNSTeppAVFTGDTLFVAGCGKFFEGTPEEMYAAL 227
Cdd:PLN02398  154 vdkDRIPGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYF--PGSG---AIFTGDTLFSLSCGKLFEGTPEQMLSSL 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 228 IEVLGrLPPETRVYCGHEYTINNLKFARHVEPCNDAIKQKLAWAKETYNSGEPTIPSTLAEEFTFNPFMRVREK------ 301
Cdd:PLN02398  229 QKIIS-LPDDTNIYCGHEYTLSNSKFALSIEPNNEVLQSYAAHVAHLRSKGLPTIPTTVKMEKACNPFLRTSSTdirksl 307

                         250       260
                  ....*....|....*....|....*
gi 1785411060 302 SVQEHAGERDpisTMGAIRKEKDHF 326
Cdd:PLN02398  308 SIPDTADEAE---ALGIIRRAKDNF 329
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 72-326 8.87e-51

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 168.85  E-value: 8.87e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  72 MKVELIPALTDNYMYLLIDEESKeAAIVDPVQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMVSGLKVYG-GD 150
Cdd:PRK10241    1 MNLNSIPAFDDNYIWVLNDEAGR-CLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGpQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 151 SRIGALTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYvtkpnstEPPAVFTGDTLFVAGCGKFFEGTPEEMYAALIEV 230
Cdd:PRK10241   80 TQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF-------SKPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 231 lGRLPPETRVYCGHEYTINNLKFARHVEPCNDAIKQKLAWAKETYNSGEPTIPSTLAEEFTFNPFMRVRE----KSVQEH 306
Cdd:PRK10241  153 -NALPDDTLICCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINLFLRTEDidliNVINEE 231

                         250       260
                  ....*....|....*....|
gi 1785411060 307 AGERDPISTMGAIRKEKDHF 326
Cdd:PRK10241  232 TLLQQPEERFAWLRSKKDRF 251
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 82-244 1.43e-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: 144.99  E-value: 1.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  82 DNYMYLLIDEESKEAAIVDPV-QPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMVsGLKVYGGDSRI------- 153
Cdd:cd16275    11 INYSYIIIDKATREAAVVDPAwDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKY-DAPVYMSKEEIdyygfrc 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 154 GALtQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYVtkPNSteppaVFTGDTLFVAGCG--KFFEGTPEEMYAAlIEVL 231
Cdd:cd16275    90 PNL-IPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLL--GDS-----LFTGDTLFIEGCGrcDLPGGDPEEMYES-LQRL 160

                         170
                  ....*....|....
gi 1785411060 232 GRLPPE-TRVYCGH 244
Cdd:cd16275   161 KKLPPPnTRVYPGH 174
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 245-326 3.06e-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: 138.34  E-value: 3.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 245 EYTINNLKFARHVEPCNDAIKQKLAWAKETYNSGEPTIPSTLAEEFTFNPFMRVREKSVQEHAGERDPISTMGAIRKEKD 324
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGETDPVEVFAALRELKD 80


                  ..
gi 1785411060 325 HF 326
Cdd:pfam16123  81 NF 82
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 86-246 2.04e-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: 134.45  E-value: 2.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  86 YLLIDEESKEAAIVDPV--QPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMVsGLKVYGGDSRIGALT-QKVSH 162
Cdd:cd07724    15 YLVGDPETGEAAVIDPVrdSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERT-GAPIVIGEGAPASFFdRLLKD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 163 LTTFQVGSLHVKCLYTPCHTSGHICYYVTKPNsteppAVFTGDTLFVAGCG-----KFFEGTPEEMYAALIEVLGRLPPE 237
Cdd:cd07724    94 GDVLELGNLTLEVLHTPGHTPESVSYLVGDPD-----AVFTGDTLFVGDVGrpdlpGEAEGLARQLYDSLQRKLLLLPDE 168


                  ....*....
gi 1785411060 238 TRVYCGHEY 246
Cdd:cd07724   169 TLVYPGHDY 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 74-258 5.85e-38

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: 134.43  E-value: 5.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  74 VELIPALTDNYMYLLIDEEskEAAIVDP----VQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMvSGLKVYGG 149
Cdd:COG0491     6 GGTPGAGLGVNSYLIVGGD--GAVLIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEA-FGAPVYAH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 150 DSRIGALTQKVSHL----------------TTFQVGSLHVKCLYTPCHTSGHICYYVtkpnsTEPPAVFTGDTLFVAGCG 213
Cdd:COG0491    83 AAEAEALEAPAAGAlfgrepvppdrtledgDTLELGGPGLEVIHTPGHTPGHVSFYV-----PDEKVLFTGDALFSGGVG 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1785411060 214 K--FFEGTPEEMYAALiEVLGRLPPEtRVYCGHEYTINNLKFARHVE 258
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; ...
 86-244 6.75e-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: 130.87  E-value: 6.75e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  86 YLLIDEEsKEAAIVDPVQP--QKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMvSGLKVY---------------- 147
Cdd:cd06262    13 YLVSDEE-GEAILIDPGAGalEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEA-PGAPVYiheadaelledpelnl 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 148 ----GGDSRIGALTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYVTKPNsteppAVFTGDTLFVAGCGK--FFEGTPE 221
Cdd:cd06262    91 affgGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEG-----VLFTGDTLFAGSIGRtdLPGGDPE 165

                         170       180
                  ....*....|....*....|...
gi 1785411060 222 EMYAALIEVLGRLPPETRVYCGH 244
Cdd:cd06262   166 QLIESIKKLLLLLPDDTVVYPGH 188
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 84-244 1.20e-28

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 108.79  E-value: 1.20e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060   84 YMYLLIDEesKEAAIVDPV--QPQKVVDAVKKHGV-KLTTVLTTHHHWDHAGGNEKLVKMvSGLKVYG------------ 148
Cdd:smart00849   1 NSYLVRDD--GGAILIDTGpgEAEDLLAELKKLGPkKIDAIILTHGHPDHIGGLPELLEA-PGAPVYApegtaellkdll 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  149 -------GDSRIGALTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYVtkpnsTEPPAVFTGDTLFVAGCG-KFFEGTP 220
Cdd:smart00849  78 allgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL-----PEGKILFTGDLLFAGGDGrTLVDGGD 152

                          170       180
                   ....*....|....*....|....*
gi 1785411060  221 EEMYAALIEVLGRL-PPETRVYCGH 244
Cdd:smart00849 153 AAASDALESLLKLLkLLPKLVVPGH 177
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 86-296 9.65e-25

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: 99.35  E-value: 9.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  86 YLLIDEESKEAAIVDP-VQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMvSGLKVY--GGDSRI------GAL 156
Cdd:cd16322    14 YLVADEGGGEAVLVDPgDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRH-PGAPVYlhPDDLPLyeaadlGAK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 157 TQKVS------------HLTTFQVGSLHVKCLYTPCHTSGHICYYVtkpnsTEPPAVFTGDTLFVAGCGK--FFEGTPEE 222
Cdd:cd16322    93 AFGLGieplpppdrlleDGQTLTLGGLEFKVLHTPGHSPGHVCFYV-----EEEGLLFSGDLLFQGSIGRtdLPGGDPKA 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785411060 223 MYAALIEVLgRLPPETRVYCGHeytinnlkfarhvepcndaikqklawaketynsGEPTipsTLAEEFTFNPFM 296
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 ...
 86-244 8.75e-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: 8.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  86 YLLIDEESKEAAIVDP-VQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVKMvSGLKVYG---GD----------S 151
Cdd:cd07737    14 SLIWCEETKEAAVIDPgGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEH-YGVPIIGphkEDkfllenlpeqS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 152 RIGAL--------TQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYvtkpnSTEPPAVFTGDTLFVAGCGK--FFEGTPE 221
Cdd:cd07737    93 QMFGFppaeaftpDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFF-----NRESKLAIVGDVLFKGSIGRtdFPGGNHA 167

                         170       180
                  ....*....|....*....|...
gi 1785411060 222 EMYAALIEVLGRLPPETRVYCGH 244
Cdd:cd07737   168 QLIASIKEKLLPLGDDVTFIPGH 190
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 84-246 3.71e-17

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 79.46  E-value: 3.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  84 YMYLLID--EESKEAAIVDPVQpqKVVDA----VKKHGVKLTTVLTTHHHWDHAGGNEKLVKMVSGLKvyggdSRIG-AL 156
Cdd:PLN02962   24 YTYLLADvsHPDKPALLIDPVD--KTVDRdlslVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVK-----SIISkAS 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 157 TQKVSHLT----TFQVGSLHVKCLYTPCHTSGHICYyVT--KPNSTEPPAVFTGDTLFVAGCGK--FFEGTPEEMYAALI 228
Cdd:PLN02962   97 GSKADLFVepgdKIYFGDLYLEVRATPGHTAGCVTY-VTgeGPDQPQPRMAFTGDALLIRGCGRtdFQGGSSDQLYKSVH 175

                         170
                  ....*....|....*...
gi 1785411060 229 EVLGRLPPETRVYCGHEY 246
Cdd:PLN02962  176 SQIFTLPKDTLIYPAHDY 193
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 73-244 7.67e-15

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: 71.87  E-value: 7.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  73 KVELIPALTDNYMYLLIDEEskEAAIVD---PVQPQKVVDAVKKHGVK---LTTVLTTHHHWDHAGGNEKLVKMvSGLKV 146
Cdd:cd07721     1 GVYQLPLLPPVNAYLIEDDD--GLTLIDtglPGSAKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAALKEA-PGAPV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 147 Y------------------GGDSRIGALTQKVSHLTTFQV------------GSLHVkcLYTPCHTSGHICYYVTKPNst 196
Cdd:cd07721    78 YahereapylegekpypppVRLGLLGLLSPLLPVKPVPVDrtledgdtldlaGGLRV--IHTPGHTPGHISLYLEEDG-- 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1785411060 197 eppAVFTGDTLFVAGcGKFFEGTP---EEMYAAL--IEVLGRLPPETrVYCGH 244
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 ...
 86-213 1.39e-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: 67.90  E-value: 1.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  86 YLLidEESKEAAIVDPvQP------QKVVDAVKkhGVKLTTVLTTHHHWDHAGGNEKLVKMVsGLKVYGGDSRIGALTQK 159
Cdd:cd16278    21 YLL--GAPDGVVVIDP-GPddpahlDALLAALG--GGRVSAILVTHTHRDHSPGAARLAERT-GAPVRAFGPHRAGGQDT 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785411060 160 -------VSHLTTFQVGSLHVKCLYTPCHTSGHICYYVtkpnsTEPPAVFTGDTlfVAGCG 213
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 ...
 109-244 2.57e-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: 67.56  E-value: 2.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 109 DAVKKHGVK-LTTVLTTHHHWDHAGGNEKLVKMVSG--LKVY-----GGDSRIGALTQKVSHLT---TFQVGSLHVKCLY 177
Cdd:cd07722    47 SVLDSEGNAtISDILLTHWHHDHVGGLPDVLDLLRGpsPRVYkfprpEEDEDPDEDGGDIHDLQdgqVFKVEGATLRVIH 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785411060 178 TPCHTSGHICYYVtkpnsTEPPAVFTGDTlfVAGCGKffegTPEEMYAALIEVLGRLP--PETRVYCGH 244
Cdd:cd07722   127 TPGHTTDHVCFLL-----EEENALFTGDC--VLGHGT----AVFEDLAAYMASLKKLLslGPGRIYPGH 184
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 86-244 1.17e-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: 65.98  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  86 YLLIDEesKEAAIVDP---VQPQKVVDAVKKHGV---KLTTVLTTHHHWDHAGG---------N---------------- 134
Cdd:cd07726    19 YLLDGE--GRPALIDTgpsSSVPRLLAALEALGIapeDVDYIILTHIHLDHAGGagllaealpNakvyvhprgarhlidp 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 135 EKLVKmvSGLKVYGGD-------------SRIGALTqkvsHLTTFQVGSLHVKCLYTPCHTSGHICYYVTKPNSteppaV 201
Cdd:cd07726    97 SKLWA--SARAVYGDEadrlggeilpvpeERVIVLE----DGETLDLGGRTLEVIDTPGHAPHHLSFLDEESDG-----L 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1785411060 202 FTGDTLFVAGCGKFFEGTPE--------EMYAALIEVLGRLPPEtRVYCGH 244
Cdd:cd07726   166 FTGDAAGVRYPELDVVGPPStpppdfdpEAWLESLDRLLSLKPE-RIYLTH 215
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 80-207 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 1785411060  80 LTDNYMYLLIDeeskeAAIVDPVQPQKVVDAVKKHGVKL---TTVLTTHHHWDHAGGNEKLVKmVSGLKVYGGDSRIgal 156
Cdd:cd07725    20 LRDGDETTLID-----TGLATEEDAEALWEGLKELGLKPsdiDRVLLTHHHPDHIGLAGKLQE-KSGATVYILDVTP--- 90

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1785411060 157 tqkVSHLTTFQVGSLHVKCLYTPCHTSGHICYYVTKpnSTEppaVFTGDTL 207
Cdd:cd07725    91 ---VKDGDKIDLGGLRLKVIETPGHTPGHIVLYDED--RRE---LFVGDAV 133
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
86-244 1.35e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 59.69  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  86 YLLIDEEskEAAIVDP-----VQPQKVVDAVKKHGVKLTTVLTTHHHWDHAGGNEKLVK-------MVSGLKVYGGDSRI 153
Cdd:pfam00753   9 YLIEGGG--GAVLIDTggsaeAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEatdvpviVVAEEARELLDEEL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 154 GALTQKVSHLTTFQVGSLHVKCLY--------------TPCHTSGHICYYVTKPNSTeppAVFTGDTLFVAGCGK--FFE 217
Cdd:pfam00753  87 GLAASRLGLPGPPVVPLPPDVVLEegdgilggglgllvTHGPGHGPGHVVVYYGGGK---VLFTGDLLFAGEIGRldLPL 163

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1785411060 218 GTPEEMYAALIEVLGRL------PPETRVYCGH 244
Cdd:pfam00753 164 GGLLVLHPSSAESSLESllklakLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 96-244 6.62e-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: 55.26  E-value: 6.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  96 AAIVD----PVQPQKVVDAVKKH-GVKLTTVLTTHHHWDHAGGN-------------------------EKLVKMVSGLK 145
Cdd:cd16282    26 VVVIDtgasPRLARALLAAIRKVtDKPVRYVVNTHYHGDHTLGNaafadagapiiahentreelaargeAYLELMRRLGG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 146 VYGGDSRIGALTQKVSHLTTFQVGSLHVKCLYT-PCHTSGHICYYVTKPNsteppAVFTGDTLFVAGCGKFFEGTPEEMY 224
Cdd:cd16282   106 DAMAGTELVLPDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEG-----VLFAGDLVFNGRIPFLPDGSLAGWI 180

                         170       180
                  ....*....|....*....|
gi 1785411060 225 AALiEVLGRLPPETRVyCGH 244
Cdd:cd16282   181 AAL-DRLLALDATVVV-PGH 198
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 105-245 6.01e-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: 52.60  E-value: 6.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 105 QKVVDAVKKHGVK---LTTVLTTHHHWDHAGGNEKLVK------------MVSGLKVYGGDSRIGAltQKVSHLTTFQVG 169
Cdd:cd07729    73 QTLEEQLARLGLDpedIDYVILSHLHFDHAGGLDLFPNatiivqraeleyATGPDPLAAGYYEDVL--ALDDDLPGGRVR 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 170 SLH--------VKCLYTPCHTSGHICYYVtkpNSTEPPAVFTGDTLFVA-----GCGKFFEGTPEEMYAAL--IEVLGRL 234
Cdd:cd07729   151 LVDgdydlfpgVTLIPTPGHTPGHQSVLV---RLPEGTVLLAGDAAYTYenleeGRPPGINYDPEAALASLerLKALAER 227

                         170
                  ....*....|.
gi 1785411060 235 PPeTRVYCGHE 245
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 ...
 56-221 1.35e-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: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  56 QTPFELR-NSKVVTQCTMKVELIpalTDNYMYLLIDEESkeaaivdPVQPQKVVDAVKKHGVKLTTV---LTTHHHWDHA 131
Cdd:cd16313     5 QEPFQIYgNTYYVGTGGISAVLI---TSPQGHILIDGGF-------PKSPEQIAASIRQLGFKLEDVkyiLSSHDHWDHA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 132 GGNEKLVKMvSGLKVYGGDSRIGALTQKVS--------HLTTF---------------QVGSLHVKCLYTPCHTSGHICY 188
Cdd:cd16313    75 GGIAALQKL-TGAQVLASPATVAVLRSGSMgkddpqfgGLTPMppvasvravrdgevvKLGPLAVTAHATPGHTTGGTSW 153

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1785411060 189 YVTKPNSTEPPAVFTGDTLFVAGCGKF-FEGTPE 221
Cdd:cd16313   154 TWQSCEQGRCANMVFADSLTAVSADGYrFSAHPA 187
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 87-186 1.36e-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: 47.97  E-value: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  87 LLIDEESKeaAIVDPVQP---QKVVDAVKKHGVKL---TTVLTTHHHWDHAGGNE--KLVKMVSGLKVYGGDSRIGALTQ 158
Cdd:cd07711    26 LIKDGGKN--ILVDTGTPwdrDLLLKALAEHGLSPediDYVVLTHGHPDHIGNLNlfPNATVIVGWDICGDSYDDHSLEE 103

                          90       100
                  ....*....|....*....|....*...
gi 1785411060 159 kvshLTTFQVGSlHVKCLYTPCHTSGHI 186
Cdd:cd07711   104 ----GDGYEIDE-NVEVIPTPGHTPEDV 126
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 84-244 3.74e-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: 3.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  84 YMYLLidEESKEAAIVDPVQPQK-VVDAVKKHGVKLTTVLTTHHHWDHAGGNE---------------KLVKMVSGLKVY 147
Cdd:cd07712    10 NIYLL--RGRDRALLIDTGLGIGdLKEYVRTLTDLPLLVVATHGHFDHIGGLHefeevyvhpadaeilAAPDNFETLTWD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 148 GGDSRI--GALTQKVSHLTTFQVGSLHVKCLYTPCHTSGHICYYVTKPNsteppAVFTGDTLFVAGCGKFFEGTPEEMYA 225
Cdd:cd07712    88 AATYSVppAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANR-----LLFSGDVVYDGPLIMDLPHSDLDDYL 162

                         170       180
                  ....*....|....*....|
gi 1785411060 226 ALIEVLGRLPPETR-VYCGH 244
Cdd:cd07712   163 ASLEKLSKLPDEFDkVLPGH 182
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 80-211 5.69e-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: 5.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  80 LTDNYMYLLIDEESKEAAivdpvqpqKVVDA-VKKHGVKLTTV---LTTHHHWDHAGGNEKLvKMVSGLKVYGGDSRIGA 155
Cdd:cd16310    27 ITSNHGAILLDGGLEENA--------ALIEQnIKALGFKLSDIkiiINTHAHYDHAGGLAQL-KADTGAKLWASRGDRPA 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785411060 156 LTQ-----------------KVSHL----TTFQVGSLHVKCLYTPCHTSGHICYYVTKPNSTEPPAVFTGDTLFVAG 211
Cdd:cd16310    98 LEAgkhigdnitqpapfpavKVDRIlgdgEKIKLGDITLTATLTPGHTKGCTTWSTTVKENGRPLRVVFPCSLSVAG 174
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 81-229 8.93e-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: 8.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060  81 TDNYMYLLIdEESKEAAIVDPVQPQK---VVDAVKKHGVKLTTV---LTTHHHWDHAGGNEkLVKMVSGLKVYGGDSRIG 154
Cdd:cd07708    19 TDDLAAYLI-VTPQGNILIDGDMEQNapmIKANIKKLGFKFSDTkliLISHAHFDHAGGSA-EIKKQTGAKVMAGAEDVS 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 155 ALTQKVS--------HLTTF---------------QVGSLHVKCLYTPCHTSGHICYYVTKPNSTEPPAVFTGDTLFVAG 211
Cdd:cd07708    97 LLLSGGSsdfhyandSSTYFpqstvdravhdgervTLGGTVLTAHATPGHTPGCTTWTMTLKDHGKQYQVVFADSLTVNP 176

                         170
                  ....*....|....*...
gi 1785411060 212 CGKfFEGTPEemYAALIE 229
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 ...
 88-147 9.47e-06

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 9.47e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785411060  88 LIDEESKEAAIVDPVQPQKVVDAVKK----HGVKLTTVLTTHHHWDHAGGNEKLVKMvSGLKVY 147
Cdd:cd07743    12 VYVFGDKEALLIDSGLDEDAGRKIRKileeLGWKLKAIINTHSHADHIGGNAYLQKK-TGCKVY 74
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 93-130 3.00e-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: 3.00e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1785411060  93 SKEAAIVDPV----QPQKVVDAVKKHGVKLTTVLTTHHHWDH 130
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 ...
 116-184 2.31e-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: 2.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785411060 116 VKLttVLTTHHHWDHAGGNEKLVKMvSGLKVYGGDSRIGAL-----------------------TQKVSHLTTFQVGSLH 172
Cdd:cd16290    61 VKL--ILNSHAHFDHAGGIAALQRD-SGATVAASPAGAAALrsggvdpddpqagaadpfppvakVRVVADGEVVKLGPLA 137

                          90
                  ....*....|..
gi 1785411060 173 VKCLYTPCHTSG 184
Cdd:cd16290   138 VTAHATPGHTPG 149
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 101-133 1.30e-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: 39.56  E-value: 1.30e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1785411060 101 PVQPQK-VVDAVKKHGVKL---TTVLTTHHHWDHAGG 133
Cdd:cd07730    63 PLEVEEdVAEQLAAGGIDPediDAVILSHLHWDHIGG 99
IND_BlaB-like_MBL-B1 cd16299
IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 83-133 1.57e-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: 39.35  E-value: 1.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1785411060  83 NYMYLLideeSKEAAIV-----DPVQPQKVVDAVK-KHGVKLTTVLTTHHHWDHAGG 133
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; ...
 87-150 1.62e-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: 1.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785411060  87 LLIDEESKEAAIVDP----VQPQKVVDAV-KKHGVKLTTVLTTHHHWDHAGGNEKLVKMvsGLKVYGGD 150
Cdd:cd16286    30 LVVKMLDGTVVIVDSpytnLATQTVLDWIaKTMGPRKVVAINTHFHLDGTGGNEALKKR--GIPTWGSD 96
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 105-150 4.34e-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: 37.50  E-value: 4.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1785411060 105 QKVVDAVKKHGV-KLTTVLTTHHHWDHAGGNEKLVKMVSGLKVYGGD 150
Cdd:cd07731    35 DVVVPYLKARGIkKLDYLILTHPDADHIGGLDAVLKNFPVKEVYMPG 81
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
112-147 9.72e-03

Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440850  Cd Length: 273  Bit Score: 37.17  E-value: 9.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1785411060 112 KKHGVKLTT----VLTtHHHWDHAGGNEKLVKMVSGLKVY 147
Cdd:COG1237    49 EKLGIDLSDidavVLS-HGHYDHTGGLPALLELNPKAPVY 87
 
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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