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Conserved domains on  [gi|518288150|ref|WP_019458358|]
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MULTISPECIES: hydroxyacylglutathione hydrolase [Acinetobacter]

Protein Classification

hydroxyacylglutathione hydrolase( domain architecture ID 11496813)

hydroxyacylglutathione hydrolase is a type II glyoxalase that catalyzes the hydrolysis of (R)-S-lactoylglutathione to (R)-lactate and glutathione

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 5-243 1.05e-125

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: 356.08  E-value: 1.05e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150    5 IHFIdvqNALQ-NYIWILEDTETHeAVAVDPTEGGLVTQFCNDHHLTLKQIWLTHWHKDHIGGVADLTANSTLAVYGPRD 83
Cdd:TIGR03413   1 IIPI---PALSdNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAFPAPVYGPAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150   84 ElsKIPGITHPLQHDDHLKFNDLKAEIIATPGHTLGHIVYFIEELNALFCGDTLFAMGCGRLFEGTAEQMYHSLNRLAAL 163
Cdd:TIGR03413  77 E--RIPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAAL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  164 PTTTKVYCTHEYTLSNAEFSLSVEPENHALQERAEQVRILRKEGKITLPSSIELELATNPFLRAES-------------- 229
Cdd:TIGR03413 155 PDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDpavraalgsqgadp 234

                         250
                  ....*....|....
gi 518288150  230 VEEFAHLRSLKDNF 243
Cdd:TIGR03413 235 VEVFAALRAWKDNF 248
 
Name Accession Description Interval E-value
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 5-243 1.05e-125

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: 356.08  E-value: 1.05e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150    5 IHFIdvqNALQ-NYIWILEDTETHeAVAVDPTEGGLVTQFCNDHHLTLKQIWLTHWHKDHIGGVADLTANSTLAVYGPRD 83
Cdd:TIGR03413   1 IIPI---PALSdNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAFPAPVYGPAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150   84 ElsKIPGITHPLQHDDHLKFNDLKAEIIATPGHTLGHIVYFIEELNALFCGDTLFAMGCGRLFEGTAEQMYHSLNRLAAL 163
Cdd:TIGR03413  77 E--RIPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAAL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  164 PTTTKVYCTHEYTLSNAEFSLSVEPENHALQERAEQVRILRKEGKITLPSSIELELATNPFLRAES-------------- 229
Cdd:TIGR03413 155 PDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDpavraalgsqgadp 234

                         250
                  ....*....|....
gi 518288150  230 VEEFAHLRSLKDNF 243
Cdd:TIGR03413 235 VEVFAALRAWKDNF 248
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 16-173 1.14e-80

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: 238.90  E-value: 1.14e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  16 NYIWILEDTETHEAVAVDPTEGGLVTQFCNDHHLTLKQIWLTHWHKDHIGGVADL-TANSTLAVYGPRDElsKIPGITHP 94
Cdd:cd07723    9 NYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELkALFPDAPVYGPAED--RIPGLDHP 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518288150  95 LQHDDHLKFNDLKAEIIATPGHTLGHIVYFIEELNALFCGDTLFAMGCGRLFEGTAEQMYHSLNRLAALPTTTKVYCTH 173
Cdd:cd07723   87 VKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLALPDDTLVYCGH 165
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 16-243 8.87e-71

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 217.32  E-value: 8.87e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  16 NYIWILEDTETHEAVAVDPTEGGLVTQFCNDHHLTLKQIWLTHWHKDHIGGVADLTAN-STLAVYGprDELSKIPGITHP 94
Cdd:PLN02469  12 NYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLvPGIKVYG--GSLDNVKGCTHP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  95 LQHDDHLKF-NDLKAEIIATPGHTLGHIVYFI----EELNALFCGDTLFAMGCGRLFEGTAEQMYHSLNR-LAALPTTTK 168
Cdd:PLN02469  90 VENGDKLSLgKDVNILALHTPCHTKGHISYYVtgkeGEDPAVFTGDTLFIAGCGKFFEGTAEQMYQSLCVtLGSLPKPTQ 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150 169 VYCTHEYTLSNAEFSLSVEPENHALQERAEQVRILRKEGKITLPSSIELELATNPFLRAE------------SVEEFAHL 236
Cdd:PLN02469 170 VYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDlpeiqekvgcesPVEALREV 249


                 ....*..
gi 518288150 237 RSLKDNF 243
Cdd:PLN02469 250 RKMKDNW 256
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 3-181 9.99e-41

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: 139.06  E-value: 9.99e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150   3 YRIHFIDVQNALQNYIWILEDTEthEAVAVDP----TEGGLVTQFCNDHHLTLKQIWLTHWHKDHIGGVADLTANSTLAV 78
Cdd:COG0491    2 YVLPGGTPGAGLGVNSYLIVGGD--GAVLIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  79 YGPRDEL-------------SKIPGITHPLQHDDHLKFNDLKAEIIATPGHTLGHIVYFIEELNALFCGDTLFAMGCGR- 144
Cdd:COG0491   80 YAHAAEAealeapaagalfgREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRp 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 518288150 145 -LFEGTAEQMYHSLNRLAALPTTTkVYCTHEYTLSNAE 181
Cdd:COG0491  160 dLPDGDLAQWLASLERLLALPPDL-VIPGHGPPTTAEA 196
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 174-243 2.51e-30

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: 107.91  E-value: 2.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  174 EYTLSNAEFSLSVEPENHALQERAEQVRILRKEGKITLPSSIELELATNPFLRAES------------VEEFAHLRSLKD 241
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDpavqkatgetdpVEVFAALRELKD 80


                  ..
gi 518288150  242 NF 243
Cdd:pfam16123  81 NF 82
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 17-173 6.40e-25

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: 96.85  E-value: 6.40e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150    17 YIWILEDTEthEAVAVDPTEG---GLVTQFCNDHHLTLKQIWLTHWHKDHIGGVADLTANSTLAVYGPRDEL-------- 85
Cdd:smart00849   1 NSYLVRDDG--GAILIDTGPGeaeDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAellkdlla 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150    86 --------SKIPGITHPLQHDDHLKFNDLKAEIIATPGHTLGHIVYFIEELNALFCGDTLFAMGCGRLF-EGTAEQMYHS 156
Cdd:smart00849  79 llgelgaeAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLvDGGDAAASDA 158

                          170
                   ....*....|....*....
gi 518288150   157 LNRLAAL--PTTTKVYCTH 173
Cdd:smart00849 159 LESLLKLlkLLPKLVVPGH 177
 
Name Accession Description Interval E-value
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 5-243 1.05e-125

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: 356.08  E-value: 1.05e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150    5 IHFIdvqNALQ-NYIWILEDTETHeAVAVDPTEGGLVTQFCNDHHLTLKQIWLTHWHKDHIGGVADLTANSTLAVYGPRD 83
Cdd:TIGR03413   1 IIPI---PALSdNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAFPAPVYGPAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150   84 ElsKIPGITHPLQHDDHLKFNDLKAEIIATPGHTLGHIVYFIEELNALFCGDTLFAMGCGRLFEGTAEQMYHSLNRLAAL 163
Cdd:TIGR03413  77 E--RIPGITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRLFEGTPEQMYDSLQRLAAL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  164 PTTTKVYCTHEYTLSNAEFSLSVEPENHALQERAEQVRILRKEGKITLPSSIELELATNPFLRAES-------------- 229
Cdd:TIGR03413 155 PDDTLVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDpavraalgsqgadp 234

                         250
                  ....*....|....
gi 518288150  230 VEEFAHLRSLKDNF 243
Cdd:TIGR03413 235 VEVFAALRAWKDNF 248
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 16-173 1.14e-80

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: 238.90  E-value: 1.14e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  16 NYIWILEDTETHEAVAVDPTEGGLVTQFCNDHHLTLKQIWLTHWHKDHIGGVADL-TANSTLAVYGPRDElsKIPGITHP 94
Cdd:cd07723    9 NYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELkALFPDAPVYGPAED--RIPGLDHP 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518288150  95 LQHDDHLKFNDLKAEIIATPGHTLGHIVYFIEELNALFCGDTLFAMGCGRLFEGTAEQMYHSLNRLAALPTTTKVYCTH 173
Cdd:cd07723   87 VKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGRFFEGTAEQMYASLQKLLALPDDTLVYCGH 165
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 16-243 8.87e-71

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 217.32  E-value: 8.87e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  16 NYIWILEDTETHEAVAVDPTEGGLVTQFCNDHHLTLKQIWLTHWHKDHIGGVADLTAN-STLAVYGprDELSKIPGITHP 94
Cdd:PLN02469  12 NYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLvPGIKVYG--GSLDNVKGCTHP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  95 LQHDDHLKF-NDLKAEIIATPGHTLGHIVYFI----EELNALFCGDTLFAMGCGRLFEGTAEQMYHSLNR-LAALPTTTK 168
Cdd:PLN02469  90 VENGDKLSLgKDVNILALHTPCHTKGHISYYVtgkeGEDPAVFTGDTLFIAGCGKFFEGTAEQMYQSLCVtLGSLPKPTQ 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150 169 VYCTHEYTLSNAEFSLSVEPENHALQERAEQVRILRKEGKITLPSSIELELATNPFLRAE------------SVEEFAHL 236
Cdd:PLN02469 170 VYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDlpeiqekvgcesPVEALREV 249


                 ....*..
gi 518288150 237 RSLKDNF 243
Cdd:PLN02469 250 RKMKDNW 256
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 16-243 2.14e-65

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 203.52  E-value: 2.14e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  16 NYIWILEDTEThEAVAVDPTEGGLVTQFCNDHHLTLKQIWLTHWHKDHIGGVADLTAN-STLAVYGPRDELSKipGITHP 94
Cdd:PRK10241  12 NYIWVLNDEAG-RCLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKfPQIVVYGPQETQDK--GTTQV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  95 LQHDDHLKFNDLKAEIIATPGHTLGHIVYFIEELnaLFCGDTLFAMGCGRLFEGTAEQMYHSLNRLAALPTTTKVYCTHE 174
Cdd:PRK10241  89 VKDGETAFVLGHEFSVFATPGHTLGHICYFSKPY--LFCGDTLFSGGCGRLFEGTASQMYQSLKKINALPDDTLICCAHE 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150 175 YTLSNAEFSLSVEPENHALQERAEQVRILRKEGKITLPSSIELELATNPFLRAE----------------SVEEFAHLRS 238
Cdd:PRK10241 167 YTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINLFLRTEdidlinvineetllqqPEERFAWLRS 246


                 ....*
gi 518288150 239 LKDNF 243
Cdd:PRK10241 247 KKDRF 251
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 16-231 8.52e-65

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 204.31  E-value: 8.52e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  16 NYIWILEDTETHEAVAVDPTEGGLVTQFCNDHHLTLKQIWLTHWHKDHIGGVADLTANSTLAVYGPRDELSKIPGITHPL 95
Cdd:PLN02398  87 NYAYLLHDEDTGTVGVVDPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVDKDRIPGIDIVL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  96 QHDDHLKFNDLKAEIIATPGHTLGHIVYFIEELNALFCGDTLFAMGCGRLFEGTAEQMYHSLNRLAALPTTTKVYCTHEY 175
Cdd:PLN02398 167 KDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGDTLFSLSCGKLFEGTPEQMLSSLQKIISLPDDTNIYCGHEY 246

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 518288150 176 TLSNAEFSLSVEPENHALQERAEQVRILRKEGKITLPSSIELELATNPFLRAESVE 231
Cdd:PLN02398 247 TLSNSKFALSIEPNNEVLQSYAAHVAHLRSKGLPTIPTTVKMEKACNPFLRTSSTD 302
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 3-181 9.99e-41

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: 139.06  E-value: 9.99e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150   3 YRIHFIDVQNALQNYIWILEDTEthEAVAVDP----TEGGLVTQFCNDHHLTLKQIWLTHWHKDHIGGVADLTANSTLAV 78
Cdd:COG0491    2 YVLPGGTPGAGLGVNSYLIVGGD--GAVLIDTglgpADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  79 YGPRDEL-------------SKIPGITHPLQHDDHLKFNDLKAEIIATPGHTLGHIVYFIEELNALFCGDTLFAMGCGR- 144
Cdd:COG0491   80 YAHAAEAealeapaagalfgREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRp 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 518288150 145 -LFEGTAEQMYHSLNRLAALPTTTkVYCTHEYTLSNAE 181
Cdd:COG0491  160 dLPDGDLAQWLASLERLLALPPDL-VIPGHGPPTTAEA 196
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 16-170 3.98e-38

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: 131.12  E-value: 3.98e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  16 NYIWILEDTETHEAVAVDP---TEGglVTQFCNDHHLTLKQIWLTHWHKDHIGGVADLTANSTLAVYGPRDELsKIPGIT 92
Cdd:cd16275   12 NYSYIIIDKATREAAVVDPawdIEK--ILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEI-DYYGFR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  93 ----HPLQHDDHLKFNDLKAEIIATPGHTLGHIVYFIEelNALFCGDTLFAMGCGR--LFEGTAEQMYHSLNRLAAL-PT 165
Cdd:cd16275   89 cpnlIPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLG--DSLFTGDTLFIEGCGRcdLPGGDPEEMYESLQRLKKLpPP 166


                 ....*
gi 518288150 166 TTKVY 170
Cdd:cd16275  167 NTRVY 171
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 12-173 4.66e-38

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: 131.25  E-value: 4.66e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  12 NALQNYIWILEDtETHEAVAVDPTEGGL--VTQFCNDHHLTLKQIWLTHWHKDHIGGVADLTANSTLAVYGPRDELS--- 86
Cdd:cd06262    6 GPLQTNCYLVSD-EEGEAILIDPGAGALekILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAElle 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  87 --------------KIPGITHPLQHDDHLKFNDLKAEIIATPGHTLGHIVYFIEELNALFCGDTLFAMGCGR--LFEGTA 150
Cdd:cd06262   85 dpelnlaffgggplPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRtdLPGGDP 164

                        170       180
                 ....*....|....*....|....
gi 518288150 151 EQMYHSL-NRLAALPTTTKVYCTH 173
Cdd:cd06262  165 EQLIESIkKLLLLLPDDTVVYPGH 188
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 14-173 3.10e-34

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


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 121.69  E-value: 3.10e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  14 LQNYIWILEDTETHEAVAVDPTEGGL-VTQFCNDHHLTLKQIWLTHWHKDHIGGVADLTANSTLAVYGPRDELS------ 86
Cdd:cd16322    9 LQENTYLVADEGGGEAVLVDPGDESEkLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDLPlyeaad 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  87 -----------KIPGITHPLQHDDHLKFNDLKAEIIATPGHTLGHIVYFIEELNALFCGDTLFAMGCGR--LFEGTAEQM 153
Cdd:cd16322   89 lgakafglgiePLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRtdLPGGDPKAM 168

                        170       180
                 ....*....|....*....|
gi 518288150 154 YHSLNRLAALPTTTKVYCTH 173
Cdd:cd16322  169 AASLRRLLTLPDETRVFPGH 188
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 19-175 6.89e-32

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: 114.80  E-value: 6.89e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  19 WILEDTETHEAVAVDPTEGGL--VTQFCNDHHLTLKQIWLTHWHKDHIGGVADLtANSTLA--VYGPRDELSkipGITHP 94
Cdd:cd07724   15 YLVGDPETGEAAVIDPVRDSVdrYLDLAAELGLKITYVLETHVHADHVSGAREL-AERTGApiVIGEGAPAS---FFDRL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  95 LQHDDHLKFNDLKAEIIATPGHTLGHIVYFIEELNALFCGDTLFAMGCGR-----LFEGTAEQMYHSL-NRLAALPTTTK 168
Cdd:cd07724   91 LKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRpdlpgEAEGLARQLYDSLqRKLLLLPDETL 170


                 ....*..
gi 518288150 169 VYCTHEY 175
Cdd:cd07724  171 VYPGHDY 177
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 174-243 2.51e-30

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: 107.91  E-value: 2.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  174 EYTLSNAEFSLSVEPENHALQERAEQVRILRKEGKITLPSSIELELATNPFLRAES------------VEEFAHLRSLKD 241
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDpavqkatgetdpVEVFAALRELKD 80


                  ..
gi 518288150  242 NF 243
Cdd:pfam16123  81 NF 82
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 20-173 4.19e-28

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: 105.33  E-value: 4.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  20 ILEDTETHEAVAVDPteGG---LVTQFCNDHHLTLKQIWLTHWHKDHIGGVADLTANSTLAVYGP--RDE--LSKIPGIT 92
Cdd:cd07737   15 LIWCEETKEAAVIDP--GGdadKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPhkEDKflLENLPEQS 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  93 -----------HP---LQHDDHLKFNDLKAEIIATPGHTLGHIVYFIEELNALFCGDTLFAMGCGR--LFEGTAEQMYHS 156
Cdd:cd07737   93 qmfgfppaeafTPdrwLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRtdFPGGNHAQLIAS 172

                        170
                 ....*....|....*...
gi 518288150 157 L-NRLAALPTTTKVYCTH 173
Cdd:cd07737  173 IkEKLLPLGDDVTFIPGH 190
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 17-173 6.40e-25

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: 96.85  E-value: 6.40e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150    17 YIWILEDTEthEAVAVDPTEG---GLVTQFCNDHHLTLKQIWLTHWHKDHIGGVADLTANSTLAVYGPRDEL-------- 85
Cdd:smart00849   1 NSYLVRDDG--GAILIDTGPGeaeDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAellkdlla 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150    86 --------SKIPGITHPLQHDDHLKFNDLKAEIIATPGHTLGHIVYFIEELNALFCGDTLFAMGCGRLF-EGTAEQMYHS 156
Cdd:smart00849  79 llgelgaeAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLvDGGDAAASDA 158

                          170
                   ....*....|....*....
gi 518288150   157 LNRLAAL--PTTTKVYCTH 173
Cdd:smart00849 159 LESLLKLlkLLPKLVVPGH 177
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 51-173 8.72e-20

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: 83.81  E-value: 8.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  51 LKQIWLTHWHKDHIGGVADLTANSTLAVYGPRDELS--------------------------KIPGITHPLQHDDHLKFN 104
Cdd:cd07721   50 IRRILLTHGHIDHIGSLAALKEAPGAPVYAHEREAPylegekpypppvrlgllgllspllpvKPVPVDRTLEDGDTLDLA 129

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518288150 105 DlKAEIIATPGHTLGHIVYFIEELNALFCGDTLFAMGcGRLFEGTA------EQMYHSLNRLAALPTTTkVYCTH 173
Cdd:cd07721  130 G-GLRVIHTPGHTPGHISLYLEEDGVLIAGDALVTVG-GELVPPPPpftwdmEEALESLRKLAELDPEV-LAPGH 201
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 50-173 2.00e-18

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


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 79.88  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  50 TLKQIWLTHWHKDHIGGVADLTAnstlAVYGPRDELSKIPGITHPLQHD-DHLKFNDLKA-----------EIIATPGHT 117
Cdd:cd07722   56 TISDILLTHWHHDHVGGLPDVLD----LLRGPSPRVYKFPRPEEDEDPDeDGGDIHDLQDgqvfkvegatlRVIHTPGHT 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 518288150 118 LGHIVYFIEELNALFCGDTLfaMGCGR-LFEGTAEQMyHSLNRLAALPtTTKVYCTH 173
Cdd:cd07722  132 TDHVCFLLEEENALFTGDCV--LGHGTaVFEDLAAYM-ASLKKLLSLG-PGRIYPGH 184
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 53-164 8.94e-16

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: 72.91  E-value: 8.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  53 QIWLTHWHKDHIGGVADLTANSTLAVYGPRDELSKIPGIT----HPLQHDDHLKFNDLKAEIIATPGHTLGHIVYFIEEL 128
Cdd:cd16278   56 AILVTHTHRDHSPGAARLAERTGAPVRAFGPHRAGGQDTDfapdRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDE 135

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 518288150 129 NALFCGDTLfaMGCGRLF----EGTAEQMYHSLNRLAALP 164
Cdd:cd16278  136 GALFTGDHV--MGWSTTViappDGDLGDYLASLERLLALD 173
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 17-175 3.74e-14

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 69.83  E-value: 3.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  17 YIWILEDTETHE--AVAVDPTEGGLVTQFCNDHHLTLKQIWL--THWHKDHIGGVADLTANstlaVYGPRDELSKIPG-- 90
Cdd:PLN02962  24 YTYLLADVSHPDkpALLIDPVDKTVDRDLSLVKELGLKLIYAmnTHVHADHVTGTGLLKTK----LPGVKSIISKASGsk 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  91 ITHPLQHDDHLKFNDLKAEIIATPGHTLGHIVYFIEE------LNALFCGDTLFAMGCGRL-FE-GTAEQMYHSL-NRLA 161
Cdd:PLN02962 100 ADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEgpdqpqPRMAFTGDALLIRGCGRTdFQgGSSDQLYKSVhSQIF 179

                        170
                 ....*....|....
gi 518288150 162 ALPTTTKVYCTHEY 175
Cdd:PLN02962 180 TLPKDTLIYPAHDY 193
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 53-140 9.94e-14

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: 67.32  E-value: 9.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  53 QIWLTHWHKDHIGGVADLTANSTLAVYGPRDElskipgithPLQHDDHLKFNDLKAEIIATPGHTLGHIVYFIEELNALF 132
Cdd:cd07725   58 RVLLTHHHPDHIGLAGKLQEKSGATVYILDVT---------PVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELF 128


                 ....*...
gi 518288150 133 CGDTLFAM 140
Cdd:cd07725  129 VGDAVLPK 136
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
49-173 8.19e-12

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 62.39  E-value: 8.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150   49 LTLKQIWLTHWHKDHIGGVADLTANSTLAVYGPRDEL---------------------SKIPGITHPLQHDDHLKFNDLK 107
Cdd:pfam00753  42 KDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEArelldeelglaasrlglpgppVVPLPPDVVLEEGDGILGGGLG 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518288150  108 AEIIATPGHTLGHIVYFIEELNALFCGDTLFAMGCGR--LFEGTAEQMYHSLN-------RLAALPTTTKVYCTH 173
Cdd:pfam00753 122 LLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRldLPLGGLLVLHPSSAessleslLKLAKLKAAVIVPGH 196
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 51-173 3.18e-11

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: 60.97  E-value: 3.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  51 LKQIWLTHWHKDHIGGVADLTA------------------------NSTLAVYGPR--DELSKIPGI----THPLQHDDH 100
Cdd:cd07726   55 VDYIILTHIHLDHAGGAGLLAEalpnakvyvhprgarhlidpsklwASARAVYGDEadRLGGEILPVpeerVIVLEDGET 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150 101 LKFNDLKAEIIATPGHTLGHIVYFIEELNALFCGDTLFAMGCGRLFEGTA---------EQMYHSLNRLAALPtTTKVYC 171
Cdd:cd07726  135 LDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDAAGVRYPELDVVGPPstpppdfdpEAWLESLDRLLSLK-PERIYL 213


                 ..
gi 518288150 172 TH 173
Cdd:cd07726  214 TH 215
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 56-173 4.66e-10

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: 56.87  E-value: 4.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  56 LTHWHKDHIGGV----------ADLTA-----NSTLAVYGPRDELSKIPGITHPLQHDDHLKFNDLKAEIIATPGHTLGH 120
Cdd:cd07712   48 ATHGHFDHIGGLhefeevyvhpADAEIlaapdNFETLTWDAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGS 127

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 518288150 121 IVYFIEELNALFCGDTLFAmgcGRLFE----GTAEQMYHSLNRLAALPTT-TKVYCTH 173
Cdd:cd07712  128 IALLDRANRLLFSGDVVYD---GPLIMdlphSDLDDYLASLEKLSKLPDEfDKVLPGH 182
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 45-138 5.78e-10

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: 57.16  E-value: 5.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  45 NDHHLTLKQIWLTHWHKDHIGGVADLTANSTLAVYGPRDELSKI---------------------------PGITHPLQH 97
Cdd:cd07743   40 EELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAFIenpllepsylggayppkelrnkflmakPSKVDDIIE 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 518288150  98 DDHLKFNDLKAEIIATPGHTLGHIVYFIEElNALFCGDTLF 138
Cdd:cd07743  120 EGELELGGVGLEIIPLPGHSFGQIGILTPD-GVLFAGDALF 159
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 56-167 1.60e-07

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: 50.26  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  56 LTHWHKDHIGG--------------------VADLTANSTLAVYGPRDELSKIPGITHP---LQHDDHLKFNDLKAEIIA 112
Cdd:cd16282   58 NTHYHGDHTLGnaafadagapiiahentreeLAARGEAYLELMRRLGGDAMAGTELVLPdrtFDDGLTLDLGGRTVELIH 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 518288150 113 T-PGHTLGHIVYFIEELNALFCGDTLFAMGCGRLFEGTAEQMYHSLNRLAALPTTT 167
Cdd:cd16282  138 LgPAHTPGDLVVWLPEEGVLFAGDLVFNGRIPFLPDGSLAGWIAALDRLLALDATV 193
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 50-126 1.57e-06

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. 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: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 47.23  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  50 TLKQIWLTHWHKDHIGGVADL--TANSTLAVYGPRDE-----LSKIPGI---THPLQHDDHLKFNDLKaeIIATP-GH-- 116
Cdd:cd07736   66 SIDAILLTHFHMDHVQGLFHLrwGVGDPIPVYGPPDPqgcadLFKHPGIldfQPLVAPFQSFELGGLK--ITPLPlNHsk 143

                         90
                 ....*....|.
gi 518288150 117 -TLGhivYFIE 126
Cdd:cd07736  144 pTFG---YLLE 151
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 56-163 2.67e-06

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: 46.82  E-value: 2.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  56 LTHWHKDHIGGVADLTaNSTLAVygPRDELSKI---PGITHPLQHDDHLKFNDLKA----------------EIIATPGH 116
Cdd:cd07729   94 LSHLHFDHAGGLDLFP-NATIIV--QRAELEYAtgpDPLAAGYYEDVLALDDDLPGgrvrlvdgdydlfpgvTLIPTPGH 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 518288150 117 TLGHIVYFI--EELNALFCGDTLFA---MGCGRLFE--GTAEQMYHSLNRLAAL 163
Cdd:cd07729  171 TPGHQSVLVrlPEGTVLLAGDAAYTyenLEEGRPPGinYDPEAALASLERLKAL 224
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 4-135 8.95e-06

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 45.62  E-value: 8.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150   4 RIHFIDVQNALqnyiWILEDTETHEAVAVD-------PTEGGLVTQFCNDHHLT-LKQIWLTHWHKDHIGGVADLTAN-- 73
Cdd:COG2333    2 RVTFLDVGQGD----AILIRTPDGKTILIDtgprpsfDAGERVVLPYLRALGIRrLDLLVLTHPDADHIGGLAAVLEAfp 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  74 ----------STLAVYGPRDELSKIPGITH-PLQHDDHLKFNDLKAEIIATPGHTLGH-------IVYFIE--ELNALFC 133
Cdd:COG2333   78 vgrvlvsgppDTSETYERLLEALKEKGIPVrPCRAGDTWQLGGVRFEVLWPPEDLLEGsdennnsLVLRLTygGFSFLLT 157


                 ..
gi 518288150 134 GD 135
Cdd:COG2333  158 GD 159
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 46-121 2.83e-05

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


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 43.34  E-value: 2.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  46 DHHLTLKQI---WLTHWHKDHIGGVaDLTANSTLAVYGprdELSKIPGITHPL-QHDDHLKFNDLkaEIIATPGHTLGHI 121
Cdd:cd07711   53 EHGLSPEDIdyvVLTHGHPDHIGNL-NLFPNATVIVGW---DICGDSYDDHSLeEGDGYEIDENV--EVIPTPGHTPEDV 126
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 109-164 9.46e-05

uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YmaE and Nostoc all1228 proteins.Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 41.80  E-value: 9.46e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518288150 109 EIIATPGHTLGHIVYFIEELNALFCGDTLFAMGCGRLFEGT--------AEQMYhSLNRLAALP 164
Cdd:cd07727  105 TLIPVPGHTRGSVVLLYKEKGVLFTGDHLAWSRRRGWLSAFryvcwyswPEQAE-SVERLADLD 167
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 33-134 1.59e-04

Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Bacillus cereus Beta-lactamase 2, also called BcII. 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 being most closely related to each other. BcII is a chromosome-encoded B1 MBL. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293862 [Multi-domain]  Cd Length: 212  Bit Score: 41.50  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  33 DPTEGgLVTQFCNDHHLTLKQIWLTHWHKDHIGGVADLTANSTLAVYGPRD-ELSKIPGITHP---LQHDDHLKFNDLKA 108
Cdd:cd16304   47 EQTEE-LLDWIKKKLKKPVTLAIVTHAHDDRIGGIKALQKRGIPVYSTKLTaQLAKKQGYPSPdgiLKDDTTLKFGNTKI 125

                         90       100
                 ....*....|....*....|....*..
gi 518288150 109 EII-ATPGHTLGHIVYFIEELNALFCG 134
Cdd:cd16304  126 ETFyPGEGHTADNIVVWLPQSKILFGG 152
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 56-139 2.13e-04

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 41.38  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  56 LTHWHKDHIGGVadLTANSTLA-----VYGPRDEL---------SKIPGIT-----------HPLQhdDHLKFNDlKAEI 110
Cdd:cd07720   97 LTHLHPDHIGGL--VDAGGKPVfpnaeVHVSEAEWdfwlddanaAKAPEGAkrffdaardrlRPYA--AAGRFED-GDEV 171

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 518288150 111 ------IATPGHTLGHIVYFIEELNA--LFCGDTLFA 139
Cdd:cd07720  172 lpgitaVPAPGHTPGHTGYRIESGGErlLIWGDIVHH 208
PRK11539 PRK11539
ComEC family competence protein; Provisional
 47-89 3.20e-04

ComEC family competence protein; Provisional


Pssm-ID: 236924 [Multi-domain]  Cd Length: 755  Bit Score: 41.52  E-value: 3.20e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 518288150  47 HHLTLKQIWLTHWHKDHIGGVADL-TANSTLAVYGPRDELSKIP 89
Cdd:PRK11539 548 HGLTPEGIILSHEHLDHRGGLASLlHAWPMAWIRSPLNWANHLP 591
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 56-205 6.14e-04

Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism];


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 39.88  E-value: 6.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  56 LTHWHKDHIGGVADLTA---NSTLAVYGPRDELSKI------------PGIT-HPLQHDDHLKFNDLKAEIIATP---GH 116
Cdd:COG1235   74 LTHEHADHIAGLDDLRPrygPNPIPVYATPGTLEALerrfpylfapypGKLEfHEIEPGEPFEIGGLTVTPFPVPhdaGD 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150 117 TLGhivYFIEELN--ALFCGDTL--------FAMGCGRL-FEGT--AEQMYHS-----LNRLAALPtTTKVYCTHeytls 178
Cdd:COG1235  154 PVG---YRIEDGGkkLAYATDTGyipeevleLLRGADLLiLDATydDPEPGHLsneeaLELLARLG-PKRLVLTH----- 224

                        170       180
                 ....*....|....*....|....*..
gi 518288150 179 naefsLSVEPENHALQERAEQVRILRK 205
Cdd:COG1235  225 -----LSPDNNDHELDYDELEAALLPA 246
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 50-225 2.18e-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.


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 38.33  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  50 TLKQIWLTHWHKDHIGGVADLTANstlavYGPRDELSKI---------------PGITHP-----LQHDDHLKFNDLKAE 109
Cdd:cd16280   61 DIKYILITHGHGDHYGGAAYLKDL-----YGAKVVMSEAdwdmmeeppeegdnpRWGPPPerdivIKDGDTLTLGDTTIT 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150 110 IIATPGHTLGHIVYFIEELNAlfcGDTLFAMgcgrLFEGTA----------EQMYHSLNRLAALPTTTKVycthEYTLSN 179
Cdd:cd16280  136 VYLTPGHTPGTLSLIFPVKDG---GKTHRAG----LWGGTGlntgpnlerrEQYIASLERFKKIAEEAGV----DVFLSN 204

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 518288150 180 AEFSlsvepeNHALqERAEQVRiLRKEGkitlpssielelATNPFL 225
Cdd:cd16280  205 HPFQ------DGSL-EKREALR-NRKPG------------EPNPFV 230
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 24-119 2.61e-03

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: 38.20  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518288150  24 TETHEAVAVD--PTEGG-LVTQFCNDHHLTLKQIWL---THWHKDHIGGVADLTANSTLAVYGPRDELSKIP-------- 89
Cdd:cd16310   28 TSNHGAILLDggLEENAaLIEQNIKALGFKLSDIKIiinTHAHYDHAGGLAQLKADTGAKLWASRGDRPALEagkhigdn 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 518288150  90 ---GITHPLQHDDH-------LKFNDLKAEIIATPGHTLG 119
Cdd:cd16310  108 itqPAPFPAVKVDRilgdgekIKLGDITLTATLTPGHTKG 147
RAWUL_PCGF1 cd17081
RING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in polycomb group RING ...
 40-59 3.48e-03

RING finger- and WD40-associated ubiquitin-like (RAWUL) domain found in polycomb group RING finger protein 1 (PCGF1) and similar proteins; PCGF1, also termed nervous system Polycomb-1 (NSPc1), or RING finger protein 68 (RNF68), is one of six PcG RING finger (PCGF) homologs (PCGF1/NSPc1, PCGF2/Mel-18, PCGF3, PCGF4/BMI1, PCGF5, and PCGF6/MBLR) and serves as the core component of a noncanonical Polycomb repressive complex 1 (PRC1)-like BCOR complex that also contains RING1, RNF2, RYBP, SKP1, as well as the BCL6 co-repressor BCOR and the histone demethylase KDM2B, and is required to maintain the transcriptionally repressive state of some genes, such as Hox genes, BCL6 and the cyclin-dependent kinase inhibitor, CDKN1A. PCGF1 promotes cell cycle progression and enhances cell proliferation as well. It is a cell growth regulator that acts as a transcriptional repressor of p21Waf1/Cip1 via the retinoid acid response element (RARE element). Moreover, PCGF1 functions as an epigenetic regulator involved in hematopoietic cell differentiation. It cooperates with the transcription factor runt-related transcription factor 1 (Runx1) in regulating differentiation and self-renewal of hematopoietic cells. Furthermore, PCGF1 represents a physical and functional link between Polycomb function and pluripotency. PCGF1 contains a C3HC4-type RING-HC finger and a RAWUL domain.


Pssm-ID: 340601  Cd Length: 92  Bit Score: 35.76  E-value: 3.48e-03
                         10        20
                 ....*....|....*....|....
gi 518288150  40 VTQFCNDH----HLTLKQIWLTHW 59
Cdd:cd17081   57 VQILCNNEvlpdHMTMKQIWLSHW 80
 
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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