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Conserved domains on  [gi|1622915736|ref|XP_028697218|]
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hydroxyacylglutathione hydrolase-like protein isoform X2 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 4-133 3.76e-57

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: 183.43  E-value: 3.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736   4 KVIPVLEDNYMYLVIEEITREAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAVLG-ADERI 82
Cdd:cd07723     1 VPIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGpAEDRI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622915736  83 FSLTRRLAHGEELRFGAIHVRCLLTPGHTSGHMSYFLweddcPDPPALFSG 133
Cdd:cd07723    81 PGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV-----PDEPALFTG 126
PLN02469 super family cl31885
hydroxyacylglutathione hydrolase
 1-333 1.32e-54

hydroxyacylglutathione hydrolase


The actual alignment was detected with superfamily member PLN02469:

Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 180.34  E-value: 1.32e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736   1 MKVKVIPVLEDNYMYLVIEEITREAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAVL-GAD 79
Cdd:PLN02469    1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYgGSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  80 ERIFSLTRRLAHGEELRFGA-IHVRCLLTPGHTSGHMSYFLWEDDCPDpPALFSGTrsaerahpasrrprpicsdppspa 158
Cdd:PLN02469   81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGED-PAVFTGD------------------------ 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736 159 rgravggrlRLVPGGqrpadvpePGRAGHPAPRDgerawalpsspvgagptlctctvpGVQSECPPEGSRrgeatpaara 238
Cdd:PLN02469  136 ---------TLFIAG--------CGKFFEGTAEQ------------------------MYQSLCVTLGSL---------- 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736 239 lsPRAHRalflqkVFCGHEHTLSNLEFAQKVEPCNDHVRAKLSWAKKRDEDDVPTVPSTLGEERLYNPFLRVAEEPVRKF 318
Cdd:PLN02469  165 --PKPTQ------VYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEK 236

                         330
                  ....*....|....*
gi 1622915736 319 TGKAVPADVLEALYK 333
Cdd:PLN02469  237 VGCESPVEALREVRK 251
 
Name Accession Description Interval E-value
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 4-133 3.76e-57

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: 183.43  E-value: 3.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736   4 KVIPVLEDNYMYLVIEEITREAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAVLG-ADERI 82
Cdd:cd07723     1 VPIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGpAEDRI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622915736  83 FSLTRRLAHGEELRFGAIHVRCLLTPGHTSGHMSYFLweddcPDPPALFSG 133
Cdd:cd07723    81 PGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV-----PDEPALFTG 126
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 1-333 1.32e-54

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 180.34  E-value: 1.32e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736   1 MKVKVIPVLEDNYMYLVIEEITREAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAVL-GAD 79
Cdd:PLN02469    1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYgGSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  80 ERIFSLTRRLAHGEELRFGA-IHVRCLLTPGHTSGHMSYFLWEDDCPDpPALFSGTrsaerahpasrrprpicsdppspa 158
Cdd:PLN02469   81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGED-PAVFTGD------------------------ 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736 159 rgravggrlRLVPGGqrpadvpePGRAGHPAPRDgerawalpsspvgagptlctctvpGVQSECPPEGSRrgeatpaara 238
Cdd:PLN02469  136 ---------TLFIAG--------CGKFFEGTAEQ------------------------MYQSLCVTLGSL---------- 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736 239 lsPRAHRalflqkVFCGHEHTLSNLEFAQKVEPCNDHVRAKLSWAKKRDEDDVPTVPSTLGEERLYNPFLRVAEEPVRKF 318
Cdd:PLN02469  165 --PKPTQ------VYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEK 236

                         330
                  ....*....|....*
gi 1622915736 319 TGKAVPADVLEALYK 333
Cdd:PLN02469  237 VGCESPVEALREVRK 251
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 6-338 4.07e-51

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: 170.79  E-value: 4.07e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736   6 IPVLEDNYMYLVIEEITReAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARlRPGLAVLG-ADERIFS 84
Cdd:TIGR03413   4 IPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLE-AFPAPVYGpAEERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  85 LTRRLAHGEELRFGAIHVRCLLTPGHTSGHMSYFLweddcPDPPALFSGtrsaerahpasrrprpicsDppspargravg 164
Cdd:TIGR03413  82 ITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYL-----PDSPALFCG-------------------D----------- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736 165 grlrlvpggqrpadvpepgraghpaprdgerawalpsspvgagpTL--CTCtvpgvqsecppegSRRGEATPAA------ 236
Cdd:TIGR03413 127 --------------------------------------------TLfsAGC-------------GRLFEGTPEQmydslq 149

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736 237 --RALSPRAhralflqKVFCGHEHTLSNLEFAQKVEPCNDHVRAKLSWAKKRDEDDVPTVPSTLGEERLYNPFLRVAEEP 314
Cdd:TIGR03413 150 rlAALPDDT-------LVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPA 222

                         330       340
                  ....*....|....*....|....*.
gi 1622915736 315 VRKFTGK--AVPADVLEALYKERARF 338
Cdd:TIGR03413 223 VRAALGSqgADPVEVFAALRAWKDNF 248
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 257-338 2.66e-31

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: 113.30  E-value: 2.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736 257 EHTLSNLEFAQKVEPCNDHVRAKLSWAKKRDEDDVPTVPSTLGEERLYNPFLRVAEEPVRKFTGKAVPADVLEALYKERA 336
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGETDPVEVFAALRELKD 80


                  ..
gi 1622915736 337 RF 338
Cdd:pfam16123  81 NF 82
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 11-133 8.00e-21

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: 89.36  E-value: 8.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  11 DNYMYLVIEeiTREAVAVD----VAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELAR---------------LRP 71
Cdd:COG0491    14 GVNSYLIVG--GDGAVLIDtglgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEafgapvyahaaeaeaLEA 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622915736  72 GLAVLGADERIFSLTRRLAHGEELRFGAIHVRCLLTPGHTSGHMSYFLweddcPDPPALFSG 133
Cdd:COG0491    92 PAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV-----PDEKVLFTG 148
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-133 7.00e-18

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: 80.29  E-value: 7.00e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736   13 YMYLVieEITREAVAVD--VAVPKRLLEIVGREGVS-LTAVLTTHHHWDHARGNPELARlRPGLAVLG------------ 77
Cdd:smart00849   1 NSYLV--RDDGGAILIDtgPGEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLE-APGAPVYApegtaellkdll 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622915736   78 -------ADERIFSLTRRLAHGEELRFGAIHVRCLLTPGHTSGHMSYFLweddcPDPPALFSG 133
Cdd:smart00849  78 allgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL-----PEGKILFTG 135
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 1-133 4.49e-13

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 68.31  E-value: 4.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736   1 MKVKVIPVLEDNYMYLVIEEITReAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAVLGADE 80
Cdd:PRK10241    1 MNLNSIPAFDDNYIWVLNDEAGR-CLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622915736  81 -RIFSLTRRLAHGEELRFGAIHVRCLLTPGHTSGHMSYFlweddcpDPPALFSG 133
Cdd:PRK10241   80 tQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF-------SKPYLFCG 126
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
34-133 2.76e-06

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 47.36  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  34 KRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARlRPGLAVLGADERIFSLTRRLAHGEELRFGA-------------- 99
Cdd:pfam00753  31 LLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAE-ATDVPVIVVAEEARELLDEELGLAASRLGLpgppvvplppdvvl 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622915736 100 -----IHVRCLL-----TPGHTSGHMSYFLweddcPDPPALFSG 133
Cdd:pfam00753 110 eegdgILGGGLGllvthGPGHGPGHVVVYY-----GGGKVLFTG 148
 
Name Accession Description Interval E-value
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 4-133 3.76e-57

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: 183.43  E-value: 3.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736   4 KVIPVLEDNYMYLVIEEITREAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAVLG-ADERI 82
Cdd:cd07723     1 VPIPALSDNYIYLIVDEATGEAAVVDPGEAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFPDAPVYGpAEDRI 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622915736  83 FSLTRRLAHGEELRFGAIHVRCLLTPGHTSGHMSYFLweddcPDPPALFSG 133
Cdd:cd07723    81 PGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYV-----PDEPALFTG 126
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 1-333 1.32e-54

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 180.34  E-value: 1.32e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736   1 MKVKVIPVLEDNYMYLVIEEITREAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAVL-GAD 79
Cdd:PLN02469    1 MKIIPVPCLEDNYAYLIIDESTKDAAVVDPVDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKVYgGSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  80 ERIFSLTRRLAHGEELRFGA-IHVRCLLTPGHTSGHMSYFLWEDDCPDpPALFSGTrsaerahpasrrprpicsdppspa 158
Cdd:PLN02469   81 DNVKGCTHPVENGDKLSLGKdVNILALHTPCHTKGHISYYVTGKEGED-PAVFTGD------------------------ 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736 159 rgravggrlRLVPGGqrpadvpePGRAGHPAPRDgerawalpsspvgagptlctctvpGVQSECPPEGSRrgeatpaara 238
Cdd:PLN02469  136 ---------TLFIAG--------CGKFFEGTAEQ------------------------MYQSLCVTLGSL---------- 164

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736 239 lsPRAHRalflqkVFCGHEHTLSNLEFAQKVEPCNDHVRAKLSWAKKRDEDDVPTVPSTLGEERLYNPFLRVAEEPVRKF 318
Cdd:PLN02469  165 --PKPTQ------VYCGHEYTVKNLKFALTVEPDNEKLKQKLEWAEKQRQAGLPTVPSTIEEELETNPFMRVDLPEIQEK 236

                         330
                  ....*....|....*
gi 1622915736 319 TGKAVPADVLEALYK 333
Cdd:PLN02469  237 VGCESPVEALREVRK 251
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 6-338 4.07e-51

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: 170.79  E-value: 4.07e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736   6 IPVLEDNYMYLVIEEITReAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARlRPGLAVLG-ADERIFS 84
Cdd:TIGR03413   4 IPALSDNYIWLLHDPDGQ-AAVVDPGEAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLE-AFPAPVYGpAEERIPG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  85 LTRRLAHGEELRFGAIHVRCLLTPGHTSGHMSYFLweddcPDPPALFSGtrsaerahpasrrprpicsDppspargravg 164
Cdd:TIGR03413  82 ITHPVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYL-----PDSPALFCG-------------------D----------- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736 165 grlrlvpggqrpadvpepgraghpaprdgerawalpsspvgagpTL--CTCtvpgvqsecppegSRRGEATPAA------ 236
Cdd:TIGR03413 127 --------------------------------------------TLfsAGC-------------GRLFEGTPEQmydslq 149

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736 237 --RALSPRAhralflqKVFCGHEHTLSNLEFAQKVEPCNDHVRAKLSWAKKRDEDDVPTVPSTLGEERLYNPFLRVAEEP 314
Cdd:TIGR03413 150 rlAALPDDT-------LVYCAHEYTLSNLRFALTVEPDNPALQERLKEVEALRAQGQPTLPSTLGLERATNPFLRADDPA 222

                         330       340
                  ....*....|....*....|....*.
gi 1622915736 315 VRKFTGK--AVPADVLEALYKERARF 338
Cdd:TIGR03413 223 VRAALGSqgADPVEVFAALRAWKDNF 248
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 257-338 2.66e-31

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: 113.30  E-value: 2.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736 257 EHTLSNLEFAQKVEPCNDHVRAKLSWAKKRDEDDVPTVPSTLGEERLYNPFLRVAEEPVRKFTGKAVPADVLEALYKERA 336
Cdd:pfam16123   1 EYTLSNLKFALSVEPDNEALQKRLAWVEALRAAGEPTVPSTLGDEKATNPFLRVDDPAVQKATGETDPVEVFAALRELKD 80


                  ..
gi 1622915736 337 RF 338
Cdd:pfam16123  81 NF 82
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 11-133 6.81e-28

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: 107.62  E-value: 6.81e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  11 DNYMYLVIEEITREAVAVDvavP----KRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARlRPGLAV-LGADERIFS- 84
Cdd:cd16275    11 INYSYIIIDKATREAAVVD---PawdiEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLA-KYDAPVyMSKEEIDYYg 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622915736  85 -LTRRLA---HGEELRFGAIHVRCLLTPGHTSGHMSYFLweDDCpdppaLFSG 133
Cdd:cd16275    87 fRCPNLIpleDGDTIKIGDTEITCLLTPGHTPGSMCYLL--GDS-----LFTG 132
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 1-338 4.15e-26

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 106.47  E-value: 4.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736   1 MKVKVIPVLEDNYMYLVIEEITREAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELaRLRPGLAVLGAD- 79
Cdd:PLN02398   76 LQIELVPCLKDNYAYLLHDEDTGTVGVVDPSEAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLEL-KARYGAKVIGSAv 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  80 --ERIFSLTRRLAHGEELRFGAIHVRCLLTPGHTSGHMSYFlweddcpdppalFSGTRSaerahpasrrprpicsdppsp 157
Cdd:PLN02398  155 dkDRIPGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFY------------FPGSGA--------------------- 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736 158 argravggrlrlvpggqrpadvpepgraghpaprdgerawalpsspVGAGPTLCTCTVpGVQSECPPEgsrrgeatpaaR 237
Cdd:PLN02398  202 ----------------------------------------------IFTGDTLFSLSC-GKLFEGTPE-----------Q 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736 238 ALSPrahralfLQK---------VFCGHEHTLSNLEFAQKVEPCNDHVRAKLSWAKKRDEDDVPTVPSTLGEERLYNPFL 308
Cdd:PLN02398  224 MLSS-------LQKiislpddtnIYCGHEYTLSNSKFALSIEPNNEVLQSYAAHVAHLRSKGLPTIPTTVKMEKACNPFL 296

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1622915736 309 RVAEEPVRK---FTGKAVPADVLEALYKERARF 338
Cdd:PLN02398  297 RTSSTDIRKslsIPDTADEAEALGIIRRAKDNF 329
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 15-133 3.35e-23

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: 94.77  E-value: 3.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  15 YLVIEEITREAVAVD--VAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARlRPGLA-VLGADERIFSLTRRLAH 91
Cdd:cd07724    15 YLVGDPETGEAAVIDpvRDSVDRYLDLAAELGLKITYVLETHVHADHVSGARELAE-RTGAPiVIGEGAPASFFDRLLKD 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622915736  92 GEELRFGAIHVRCLLTPGHTSGHMSYfLWEddcpDPPALFSG 133
Cdd:cd07724    94 GDVLELGNLTLEVLHTPGHTPESVSY-LVG----DPDAVFTG 130
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 11-133 8.00e-21

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: 89.36  E-value: 8.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  11 DNYMYLVIEeiTREAVAVD----VAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELAR---------------LRP 71
Cdd:COG0491    14 GVNSYLIVG--GDGAVLIDtglgPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEafgapvyahaaeaeaLEA 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622915736  72 GLAVLGADERIFSLTRRLAHGEELRFGAIHVRCLLTPGHTSGHMSYFLweddcPDPPALFSG 133
Cdd:COG0491    92 PAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV-----PDEKVLFTG 148
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 15-133 8.60e-21

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: 88.50  E-value: 8.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  15 YLVIEEiTREAVAVDVA--VPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARL-------------------RPGL 73
Cdd:cd06262    13 YLVSDE-EGEAILIDPGagALEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEApgapvyiheadaelledpeLNLA 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  74 AVLGADERIFSLTRRLAHGEELRFGAIHVRCLLTPGHTSGHMSYFlweddCPDPPALFSG 133
Cdd:cd06262    92 FFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFY-----IEEEGVLFTG 146
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 13-133 7.00e-18

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: 80.29  E-value: 7.00e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736   13 YMYLVieEITREAVAVD--VAVPKRLLEIVGREGVS-LTAVLTTHHHWDHARGNPELARlRPGLAVLG------------ 77
Cdd:smart00849   1 NSYLV--RDDGGAILIDtgPGEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLE-APGAPVYApegtaellkdll 77

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622915736   78 -------ADERIFSLTRRLAHGEELRFGAIHVRCLLTPGHTSGHMSYFLweddcPDPPALFSG 133
Cdd:smart00849  78 allgelgAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL-----PEGKILFTG 135
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-133 1.95e-14

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 70.98  E-value: 1.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  35 RLLEIVGREGVSltAVLTTHHHWDHARGNPELARlRPGLAVLGADERI-------FSLTRRLAHGEELRFGAIHVRCLLT 107
Cdd:cd16278    44 ALLAALGGGRVS--AILVTHTHRDHSPGAARLAE-RTGAPVRAFGPHRaggqdtdFAPDRPLADGEVIEGGGLRLTVLHT 120

                          90       100
                  ....*....|....*....|....*.
gi 1622915736 108 PGHTSGHMSyFLWEDDcpdpPALFSG 133
Cdd:cd16278   121 PGHTSDHLC-FALEDE----GALFTG 141
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 5-133 9.63e-14

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: 69.30  E-value: 9.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736   5 VIPVLEDNyMYLVIEEITREAVAVDVAVPK-RLLEIVGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAVLGADE--- 80
Cdd:cd16322     5 TLGPLQEN-TYLVADEGGGEAVLVDPGDESeKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDlpl 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622915736  81 --------RIFSL--------TRRLAHGEELRFGAIHVRCLLTPGHTSGHMSYFlweddCPDPPALFSG 133
Cdd:cd16322    84 yeaadlgaKAFGLgieplpppDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFY-----VEEEGLLFSG 147
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 1-133 4.49e-13

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 68.31  E-value: 4.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736   1 MKVKVIPVLEDNYMYLVIEEITReAVAVDVAVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAVLGADE 80
Cdd:PRK10241    1 MNLNSIPAFDDNYIWVLNDEAGR-CLIVDPGEAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622915736  81 -RIFSLTRRLAHGEELRFGAIHVRCLLTPGHTSGHMSYFlweddcpDPPALFSG 133
Cdd:PRK10241   80 tQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYF-------SKPYLFCG 126
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 3-118 3.95e-12

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: 64.50  E-value: 3.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736   3 VKVIPV--LEDNyMYLVIEEITREAVAVDV-AVPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARL---------- 69
Cdd:cd07737     1 YQIIPVtpFQQN-CSLIWCEETKEAAVIDPgGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHygvpiigphk 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622915736  70 --RPGLAVLGADERIFSL--------TRRLAHGEELRFGAIHVRCLLTPGHTSGHMSYF 118
Cdd:cd07737    80 edKFLLENLPEQSQMFGFppaeaftpDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFF 138
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 2-133 1.84e-11

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: 62.62  E-value: 1.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736   2 KVKVIPVLEDNYMYLVIEEitREAVAVDVAVP---KRLLEIVGREGVS---LTAVLTTHHHWDHARGNPELARlRPGLAV 75
Cdd:cd07721     1 GVYQLPLLPPVNAYLIEDD--DGLTLIDTGLPgsaKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAALKE-APGAPV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  76 L-GADE----------------------------RIFSLTRRLAHGEELRF-GAIHVrcLLTPGHTSGHMSYFLWEDDcp 125
Cdd:cd07721    78 YaHEREapylegekpypppvrlgllgllspllpvKPVPVDRTLEDGDTLDLaGGLRV--IHTPGHTPGHISLYLEEDG-- 153


                  ....*...
gi 1622915736 126 dppALFSG 133
Cdd:cd07721   154 ---VLIAG 158
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 34-118 8.38e-09

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


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 54.61  E-value: 8.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  34 KRLLEIVGREGVSLTAVLTTHHHWDHARGNPELArlrpglAVLGADERIfSLTRRLAHGEELRFGAIHVRCLLTPGHTSG 113
Cdd:cd07725    43 WEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQ------EKSGATVYI-LDVTPVKDGDKIDLGGLRLKVIETPGHTPG 115


                  ....*
gi 1622915736 114 HMSYF 118
Cdd:cd07725   116 HIVLY 120
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 34-133 3.66e-08

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: 52.92  E-value: 3.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  34 KRLLEivGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAV-------LGADERIFSLTRR---LAHGEELRFGAIHVR 103
Cdd:cd07722    46 KSVLD--SEGNATISDILLTHWHHDHVGGLPDVLDLLRGPSPrvykfprPEEDEDPDEDGGDihdLQDGQVFKVEGATLR 123

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622915736 104 CLLTPGHTSGHMSYFLWEDDcpdppALFSG 133
Cdd:cd07722   124 VIHTPGHTTDHVCFLLEEEN-----ALFTG 148
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 15-133 7.43e-08

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: 52.49  E-value: 7.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  15 YLVIEEitREAVAVD----VAVPkRLLEIVGREGVS---LTAVLTTHHHWDHARGNPELARLRPG--------------- 72
Cdd:cd07726    19 YLLDGE--GRPALIDtgpsSSVP-RLLAALEALGIApedVDYIILTHIHLDHAGGAGLLAEALPNakvyvhprgarhlid 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  73 --------LAVLGAD-------------ERIFSLtrrlAHGEELRFGAIHVRCLLTPGHTSGHMSYFLWEDDcpdppALF 131
Cdd:cd07726    96 psklwasaRAVYGDEadrlggeilpvpeERVIVL----EDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESD-----GLF 166


                  ..
gi 1622915736 132 SG 133
Cdd:cd07726   167 TG 168
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 13-133 8.80e-07

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 49.80  E-value: 8.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  13 YMYLV--IEEITREAVAVDvAVPK---RLLEIVGREGVSLTAVLTTHHHWDHARGNPELARLRPGLAVL-----GADERI 82
Cdd:PLN02962   24 YTYLLadVSHPDKPALLID-PVDKtvdRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLKTKLPGVKSIiskasGSKADL 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622915736  83 FsltrrLAHGEELRFGAIHVRCLLTPGHTSGHMSYFLWE-DDCPDPPALFSG 133
Cdd:PLN02962  103 F-----VEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEgPDQPQPRMAFTG 149
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 7-133 1.24e-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: 48.39  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736   7 PVLEDNY---MYLVieEITREAVAVDVAVPKR-LLEIVgregVSLTA----VLTTHHHWDHARGN------------PEL 66
Cdd:cd07712     1 LFIEEDDrvnIYLL--RGRDRALLIDTGLGIGdLKEYV----RTLTDlpllVVATHGHFDHIGGLhefeevyvhpadAEI 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622915736  67 ARLRPGLAVLGADERIFSL-----TRRLAHGEELRFGAIHVRCLLTPGHTSGHMSyfLWEddcPDPPALFSG 133
Cdd:cd07712    75 LAAPDNFETLTWDAATYSVppagpTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIA--LLD---RANRLLFSG 141
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
34-133 2.76e-06

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 47.36  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  34 KRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARlRPGLAVLGADERIFSLTRRLAHGEELRFGA-------------- 99
Cdd:pfam00753  31 LLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAE-ATDVPVIVVAEEARELLDEELGLAASRLGLpgppvvplppdvvl 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622915736 100 -----IHVRCLL-----TPGHTSGHMSYFLweddcPDPPALFSG 133
Cdd:pfam00753 110 eegdgILGGGLGllvthGPGHGPGHVVVYY-----GGGKVLFTG 148
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 50-117 2.10e-05

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: 45.62  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  50 VLTTHHHWDHARGNPELARLRpGLAVLGADERIFSL-----------------------TRRLAHGEELRFGAIHVRCLL 106
Cdd:cd16313    64 ILSSHDHWDHAGGIAALQKLT-GAQVLASPATVAVLrsgsmgkddpqfggltpmppvasVRAVRDGEVVKLGPLAVTAHA 142

                          90
                  ....*....|.
gi 1622915736 107 TPGHTSGHMSY 117
Cdd:cd16313   143 TPGHTTGGTSW 153
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 ...
 26-117 1.18e-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: 43.11  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  26 VAVDVAVPK---RLLEIVGREGVSLTAV---LTTHHHWDHARGNPELARLR--------PGLAVL-----GADERIFSL- 85
Cdd:cd16290    34 ILIDGALPQsapQIEANIRALGFRLEDVkliLNSHAHFDHAGGIAALQRDSgatvaaspAGAAALrsggvDPDDPQAGAa 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1622915736  86 --------TRRLAHGEELRFGAIHVRCLLTPGHTSGHMSY 117
Cdd:cd16290   114 dpfppvakVRVVADGEVVKLGPLAVTAHATPGHTPGGTSW 153
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 47-114 2.60e-04

L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 41.83  E-value: 2.60e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622915736  47 LTAVLTTHHHWDHArGNPELARLRPGLAV----LGADERI----FSLTRRLAHGEELRFGAIHVRCllTPG-HTSGH 114
Cdd:COG2220    49 IDAVLVTHDHYDHL-DDATLRALKRTGATvvapLGVAAWLrawgFPRVTELDWGESVELGGLTVTA--VPArHSSGR 122
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 46-133 3.16e-04

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


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 41.82  E-value: 3.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  46 SLTAVLTTHHHWDHArGN---------------------PELARLRPGLAVLGADERIFSLTRRLAHGE-ELrFGAIHVr 103
Cdd:cd07729    88 DIDYVILSHLHFDHA-GGldlfpnatiivqraeleyatgPDPLAAGYYEDVLALDDDLPGGRVRLVDGDyDL-FPGVTL- 164

                          90       100       110
                  ....*....|....*....|....*....|
gi 1622915736 104 cLLTPGHTSGHMSYFLwedDCPDPPALFSG 133
Cdd:cd07729   165 -IPTPGHTPGHQSVLV---RLPEGTVLLAG 190
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 34-116 5.89e-04

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


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 40.26  E-value: 5.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  34 KRLLEIVGREGVSL---TAVLTTHHHWDHARGNP--ELARLrpglaVLGADERIFSLTR-RLAHGEELRFGAiHVRCLLT 107
Cdd:cd07711    45 DLLLKALAEHGLSPediDYVVLTHGHPDHIGNLNlfPNATV-----IVGWDICGDSYDDhSLEEGDGYEIDE-NVEVIPT 118


                  ....*....
gi 1622915736 108 PGHTSGHMS 116
Cdd:cd07711   119 PGHTPEDVS 127
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 50-113 7.79e-04

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: 40.51  E-value: 7.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  50 VLTTHHHWDHARGnpeLARL--------------RPGLAVlGA--DERIFSLT--------RRLAHGEELRFGAIHVRCL 105
Cdd:cd16310    64 IINTHAHYDHAGG---LAQLkadtgaklwasrgdRPALEA-GKhiGDNITQPApfpavkvdRILGDGEKIKLGDITLTAT 139


                  ....*...
gi 1622915736 106 LTPGHTSG 113
Cdd:cd16310   140 LTPGHTKG 147
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 12-68 9.02e-04

uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YycJ 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: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 39.17  E-value: 9.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622915736  12 NYMYLvieEITREAVAVDVAVPKR----LLEIVGREGVSLTAVLTTHHHWDHARGNPELAR 68
Cdd:cd07733    10 NCTYL---ETEDGKLLIDAGLSGRkitgRLAEIGRDPEDIDAILVTHEHADHIKGLGVLAR 67
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 50-119 1.35e-03

Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of GOB-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 39.76  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  50 VLTTHHHWDHARGNPELAR---------------LRPGLA---VLGADERIF---SLTRRLAHGEELRFGAIHVRCLLTP 108
Cdd:cd16308    64 LLTTQAHYDHVGAMAAIKQqtgakmmvdekdakvLADGGKsdyEMGGYGSTFapvKADKLLHDGDTIKLGGTKLTLLHHP 143

                          90
                  ....*....|.
gi 1622915736 109 GHTSGHMSYFL 119
Cdd:cd16308   144 GHTKGSCSFLF 154
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 50-118 1.80e-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: 39.49  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  50 VLTTHHHWDHARG--------NP---------ELARLRPGLavlGADERIFSLTRR---LAHGEELRFGAIHVRCLLTPG 109
Cdd:cd16280    65 ILITHGHGDHYGGaaylkdlyGAkvvmseadwDMMEEPPEE---GDNPRWGPPPERdivIKDGDTLTLGDTTITVYLTPG 141


                  ....*....
gi 1622915736 110 HTSGHMSYF 118
Cdd:cd16280   142 HTPGTLSLI 150
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 21-113 2.46e-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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 38.70  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  21 ITREAVAV-----DVAVPKRLLE-IVGREGVSLTAVLTTHHHWDHARGN-------------------------PELARL 69
Cdd:cd16282    21 VGDDGVVVidtgaSPRLARALLAaIRKVTDKPVRYVVNTHYHGDHTLGNaafadagapiiahentreelaargeAYLELM 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1622915736  70 RPGLAVLGADERIFSLTRRLAHGEELRFGAIHVRCL-LTPGHTSG 113
Cdd:cd16282   101 RRLGGDAMAGTELVLPDRTFDDGLTLDLGGRTVELIhLGPAHTPG 145
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 50-117 2.49e-03

BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; This subgroup of B3 subclass MBLs includes Bradyrhizobium diazoefficiens BJP-1, Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Caulobacter crescentus Mbl1b. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 39.23  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622915736  50 VLTTHHHWDHARGNPELARL-----------RPGLA-------VLGADERIFS---LTRRLAHGEELRFGAIHVRCLLTP 108
Cdd:cd16288    64 LLNSHAHLDHAGGLAALKKLtgaklmasaedAALLAsggksdfHYGDDSLAFPpvkVDRVLKDGDRVTLGGTTLTAHLTP 143


                  ....*....
gi 1622915736 109 GHTSGHMSY 117
Cdd:cd16288   144 GHTRGCTTW 152
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 32-76 2.59e-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) 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: 38.67  E-value: 2.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622915736  32 VPKRLLEIVGREGVSLTAVLTTHHHWDHARGNPELARlRPGLAVL 76
Cdd:cd07743    31 AGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQK-KTGCKVY 74
 
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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