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Conserved domains on  [gi|389400709|gb|EIM62931|]
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Zn-dependent hydrolase, glyoxylase [Desulfobacter postgatei 2ac9]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10888683)

uncharacterized member of the MBL fold metallo-hydrolase superfamily

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 7-260 1.59e-123

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: 293839  Cd Length: 252  Bit Score: 352.95  E-value: 1.59e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709   7 FIVIRGNSMRLDGGTMFGNAPKALWQKWVRADERGMIDIASNCLLVKTGNYNLLFETGCGAYLSPDMKARFaVQEETHIL 86
Cdd:cd16281    3 LHSIEGGYFKLDGGAMFGVVPKPLWQKWYPADEDNRITLAMRCLLIETGGRNILIDTGIGDKQDPKFRSIY-VQHSEHSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  87 LKALSEQGLSDSDISHVVLSHLHFDHAGGLLSAWEpDREPALLFPNALFVVGEEHFRRSKSPHPRDRASFIPGLAEKLQA 166
Cdd:cd16281   82 LKSLARLGLSPEDITDVILTHLHFDHCGGATRADD-DGLVELLFPNATYWVQKRHWEWALNPNPRERASFLPENIEPLEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 167 TGRLVLKQGGDRLTvgALTIEFFQSQGHTPGMLVSLIQARGGTVIYTGDLIPGLPWVNLPITMGYDRFAEKLVDEKKQIL 246
Cdd:cd16281  161 SGRLKLIDGSDAEL--GPGIRFHLSDGHTPGQMLPEISTPGGTVVFAADLIPTSAHIPLPWVMGYDRRPLLTIEEKERLL 238

                        250
                 ....*....|....
gi 389400709 247 DRAVAEDALLVFPH 260
Cdd:cd16281  239 DEAVEEGGRLFFEH 252
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 7-260 1.59e-123

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: 293839  Cd Length: 252  Bit Score: 352.95  E-value: 1.59e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709   7 FIVIRGNSMRLDGGTMFGNAPKALWQKWVRADERGMIDIASNCLLVKTGNYNLLFETGCGAYLSPDMKARFaVQEETHIL 86
Cdd:cd16281    3 LHSIEGGYFKLDGGAMFGVVPKPLWQKWYPADEDNRITLAMRCLLIETGGRNILIDTGIGDKQDPKFRSIY-VQHSEHSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  87 LKALSEQGLSDSDISHVVLSHLHFDHAGGLLSAWEpDREPALLFPNALFVVGEEHFRRSKSPHPRDRASFIPGLAEKLQA 166
Cdd:cd16281   82 LKSLARLGLSPEDITDVILTHLHFDHCGGATRADD-DGLVELLFPNATYWVQKRHWEWALNPNPRERASFLPENIEPLEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 167 TGRLVLKQGGDRLTvgALTIEFFQSQGHTPGMLVSLIQARGGTVIYTGDLIPGLPWVNLPITMGYDRFAEKLVDEKKQIL 246
Cdd:cd16281  161 SGRLKLIDGSDAEL--GPGIRFHLSDGHTPGQMLPEISTPGGTVVFAADLIPTSAHIPLPWVMGYDRRPLLTIEEKERLL 238

                        250
                 ....*....|....
gi 389400709 247 DRAVAEDALLVFPH 260
Cdd:cd16281  239 DEAVEEGGRLFFEH 252
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 34-271 1.62e-20

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: 87.44  E-value: 1.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  34 WVRADERGMIDIASNCLLVKTGNYNLLFETGCGAylspdmkarfavqEETHILLKALSEQGLsdsDISHVVLSHLHFDHA 113
Cdd:COG0491    2 YVLPGGTPGAGLGVNSYLIVGGDGAVLIDTGLGP-------------ADAEALLAALAALGL---DIKAVLLTHLHPDHV 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 114 GGLlsAWEPDRepallfPNALFVVGEEHFRRSKSPHPRDRASFIPGLAEklqatgRLVlkQGGDRLTVGALTIEFFQSQG 193
Cdd:COG0491   66 GGL--AALAEA------FGAPVYAHAAEAEALEAPAAGALFGREPVPPD------RTL--EDGDTLELGGPGLEVIHTPG 129

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 389400709 194 HTPGMLVSLIqaRGGTVIYTGDLipgLPWVNLPITMGYDRFAEKLVDEKKQILDRavaEDALLVFPHDPVHVAARVER 271
Cdd:COG0491  130 HTPGHVSFYV--PDEKVLFTGDA---LFSGGVGRPDLPDGDLAQWLASLERLLAL---PPDLVIPGHGPPTTAEAIDY 199
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
47-260 3.69e-17

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 77.79  E-value: 3.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709   47 SNCLLVKTGNYNLLFETGCGAylspdmkarfavqeeTHILLKALSEQGLSDSDISHVVLSHLHFDHAGGLLSAWEpdrep 126
Cdd:pfam00753   6 VNSYLIEGGGGAVLIDTGGSA---------------EAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAE----- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  127 alLFPNALFVVGEEHFRRSKsPHPRDRASFIPGLAEKLQATGRLVLKQGGDRLTVGALTIEFFQSQGHTPGMLVslIQAR 206
Cdd:pfam00753  66 --ATDVPVIVVAEEARELLD-EELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVV--VYYG 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 389400709  207 GGTVIYTGDLIP--GLPWVNLPITMGYDRFAEKLVDEKKQILDRAVAEDALLVFPH 260
Cdd:pfam00753 141 GGKVLFTGDLLFagEIGRLDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 48-260 1.45e-16

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 75.67  E-value: 1.45e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709    48 NCLLVKTGNYNLLFETGCGaylspdmkarfavqeETHILLKALSEQGLSDsdISHVVLSHLHFDHAGGLlsawepdrePA 127
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPG---------------EAEDLLAELKKLGPKK--IDAIILTHGHPDHIGGL---------PE 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709   128 LL-FPNALFVVGEEHFRrskspHPRDRASFIPGLAEKLQATGRLVLKQGGDRLTVGALTIEFFQSQGHTPGMLVSLIqaR 206
Cdd:smart00849  55 LLeAPGAPVYAPEGTAE-----LLKDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL--P 127

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 389400709   207 GGTVIYTGDLIPGlpwvNLPITMGYDRFAEKLVDEKKQILDRAVAEDALLVFPH 260
Cdd:smart00849 128 EGKILFTGDLLFA----GGDGRTLVDGGDAAASDALESLLKLLKLLPKLVVPGH 177
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 7-260 1.59e-123

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: 293839  Cd Length: 252  Bit Score: 352.95  E-value: 1.59e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709   7 FIVIRGNSMRLDGGTMFGNAPKALWQKWVRADERGMIDIASNCLLVKTGNYNLLFETGCGAYLSPDMKARFaVQEETHIL 86
Cdd:cd16281    3 LHSIEGGYFKLDGGAMFGVVPKPLWQKWYPADEDNRITLAMRCLLIETGGRNILIDTGIGDKQDPKFRSIY-VQHSEHSL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  87 LKALSEQGLSDSDISHVVLSHLHFDHAGGLLSAWEpDREPALLFPNALFVVGEEHFRRSKSPHPRDRASFIPGLAEKLQA 166
Cdd:cd16281   82 LKSLARLGLSPEDITDVILTHLHFDHCGGATRADD-DGLVELLFPNATYWVQKRHWEWALNPNPRERASFLPENIEPLEE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 167 TGRLVLKQGGDRLTvgALTIEFFQSQGHTPGMLVSLIQARGGTVIYTGDLIPGLPWVNLPITMGYDRFAEKLVDEKKQIL 246
Cdd:cd16281  161 SGRLKLIDGSDAEL--GPGIRFHLSDGHTPGQMLPEISTPGGTVVFAADLIPTSAHIPLPWVMGYDRRPLLTIEEKERLL 238

                        250
                 ....*....|....
gi 389400709 247 DRAVAEDALLVFPH 260
Cdd:cd16281  239 DEAVEEGGRLFFEH 252
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 11-260 7.46e-39

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. 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: 293814  Cd Length: 249  Bit Score: 136.62  E-value: 7.46e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  11 RGNSMRLDGGTMFGNAPKALWQKWVRADERGMIDIASNCLLVKTGNYNLLFETGCG-AYLSPDMKARFAVQEETHILlKA 89
Cdd:cd07728    7 DGGVTHLDGGAMFGVVPKPLWSKKYPANEKNQIELRTDPILIQYQGKNYLIDAGIGnGKLTEKQKRNFGVTEESSIE-ES 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  90 LSEQGLSDSDISHVVLSHLHFDHAGGlLSAWEPDREpALLFPNALFVVGEEHFRRSKSPHPRDRASFipgLAEKLQATGR 169
Cdd:cd07728   86 LAELGLTPEDIDYVLMTHLHFDHASG-LTKVKGEQL-VSVFPNATIYVSEIEWEEMRNPNIRSKNTY---WKENWEPIED 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 170 LVLKQGGDRLTVGAltIEFFQSQGHTPGMLVSLIQARGGTVIYTGDLIPGLP-----WVnlpitMGYDRFAEKLVDEKKQ 244
Cdd:cd07728  161 QVKTFSDEIEIVPG--ITMIHTGGHSDGHSIIEIEQGGETAIHMADLMPTHAhqnplWV-----LAYDDYPMTSIEAKEK 233

                        250
                 ....*....|....*.
gi 389400709 245 ILDRAVAEDALLVFPH 260
Cdd:cd07728  234 WLKEGIKNNYWFTFYH 249
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 17-262 1.01e-31

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: 117.70  E-value: 1.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  17 LDGGTMfgNAPKAlWQKWVRADERGMIDIASNCLLVKTGNYNLLFETGCGAYLSPDMKARFAVQEETHILLKALSEQ--- 93
Cdd:cd07729    5 LDYGTV--TVDKS-SLFYYGRGPGEPIDLPVYAYLIEHPEGTILVDTGFHPDAADDPGGLELAFPPGVTEEQTLEEQlar 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  94 -GLSDSDISHVVLSHLHFDHAGGLlsawepdrepaLLFPNALFVVGEEHFRRSKSPHPRDRASFIPGLAEKLQATGRLVL 172
Cdd:cd07729   82 lGLDPEDIDYVILSHLHFDHAGGL-----------DLFPNATIIVQRAELEYATGPDPLAAGYYEDVLALDDDLPGGRVR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 173 KQGGDRLTVGalTIEFFQSQGHTPGMLVSLIQARGGTVIYTGDLIPGlpWVNL----PITMGYDRfaEKLVDEKKQILDR 248
Cdd:cd07729  151 LVDGDYDLFP--GVTLIPTPGHTPGHQSVLVRLPEGTVLLAGDAAYT--YENLeegrPPGINYDP--EAALASLERLKAL 224

                        250
                 ....*....|....
gi 389400709 249 AVAEDALLVFPHDP 262
Cdd:cd07729  225 AEREGARVIPGHDP 238
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 22-260 1.47e-26

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: 104.55  E-value: 1.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  22 MFGNAPKALWQKWVRADERGMIDIASNCLLVKTGNYNLLFETGCGAYLSPDMKArfavqeethiLLKALSEQGLSDSDIS 101
Cdd:cd07720   24 LGGAAPEAEAALLAAFLPPDPVETSVNAFLVRTGGRLILVDTGAGGLFGPTAGK----------LLANLAAAGIDPEDID 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 102 HVVLSHLHFDHAGGLLSAwepDREPAllFPNALFVVGE---EHFRR--SKSPHPRDRASFIPGLAEKLQATGRLVLKQGG 176
Cdd:cd07720   94 DVLLTHLHPDHIGGLVDA---GGKPV--FPNAEVHVSEaewDFWLDdaNAAKAPEGAKRFFDAARDRLRPYAAAGRFEDG 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 177 DRLTVGaltIEFFQSQGHTPGMLVSLIQARGGTVIYTGDLIPGlPWVNLP---ITMGYDRFAEKLVDEKKQILDRAVAED 253
Cdd:cd07720  169 DEVLPG---ITAVPAPGHTPGHTGYRIESGGERLLIWGDIVHH-PALQFAhpdWTIAFDVDPEQAAATRRRLLDRAAAEG 244


                 ....*..
gi 389400709 254 ALLVFPH 260
Cdd:cd07720  245 LLVAGAH 251
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 34-262 8.59e-23

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: 92.65  E-value: 8.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  34 WVRADERGMIDIASNCLLVKTGNYNLLFETGCgaylsPDMKARfavqeethiLLKALSEQGLSDSDISHVVLSHLHFDHA 113
Cdd:cd07711    9 YARRDSDGGFRASSTVTLIKDGGKNILVDTGT-----PWDRDL---------LLKALAEHGLSPEDIDYVVLTHGHPDHI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 114 GGLlsawepdrepaLLFPNALFVVGEEHFRRSKSPHPrdrasfipglaeklqatgrlVLKQGGDRLTVGaltIEFFQSQG 193
Cdd:cd07711   75 GNL-----------NLFPNATVIVGWDICGDSYDDHS--------------------LEEGDGYEIDEN---VEVIPTPG 120

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 389400709 194 HTPGMlVSLI--QARGGTVIYTGDLIP---GLPWVNLPITMGYDRfaEKLVDEKKQILDRAvaedALLVFPHDP 262
Cdd:cd07711  121 HTPED-VSVLveTEKKGTVAVAGDLFEreeDLEDPILWDPLSEDP--ELQEESRKRILALA----DWIIPGHGP 187
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 34-271 1.62e-20

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: 87.44  E-value: 1.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  34 WVRADERGMIDIASNCLLVKTGNYNLLFETGCGAylspdmkarfavqEETHILLKALSEQGLsdsDISHVVLSHLHFDHA 113
Cdd:COG0491    2 YVLPGGTPGAGLGVNSYLIVGGDGAVLIDTGLGP-------------ADAEALLAALAALGL---DIKAVLLTHLHPDHV 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 114 GGLlsAWEPDRepallfPNALFVVGEEHFRRSKSPHPRDRASFIPGLAEklqatgRLVlkQGGDRLTVGALTIEFFQSQG 193
Cdd:COG0491   66 GGL--AALAEA------FGAPVYAHAAEAEALEAPAAGALFGREPVPPD------RTL--EDGDTLELGGPGLEVIHTPG 129

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 389400709 194 HTPGMLVSLIqaRGGTVIYTGDLipgLPWVNLPITMGYDRFAEKLVDEKKQILDRavaEDALLVFPHDPVHVAARVER 271
Cdd:COG0491  130 HTPGHVSFYV--PDEKVLFTGDA---LFSGGVGRPDLPDGDLAQWLASLERLLAL---PPDLVIPGHGPPTTAEAIDY 199
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 49-260 5.81e-18

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: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 80.64  E-value: 5.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  49 CLLVKTGNYNLLFETGCGAYLSPDMKARFAvQEETHiLLKALSEQGLSDSDISHVVLSHLHFDHAGGLLSaWEPDR-EPA 127
Cdd:cd16277   15 SWLVRTPGRTILVDTGIGNDKPRPGPPAFH-NLNTP-YLERLAAAGVRPEDVDYVLCTHLHVDHVGWNTR-LVDGRwVPT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 128 llFPNALFVVGE---EHFRRSKSPHPRDRASF----IPglaekLQATGRLVLKQGGDRLTVGaltIEFFQSQGHTPGMLV 200
Cdd:cd16277   92 --FPNARYLFSRaeyDHWSSPDAGGPPNRGVFedsvLP-----VIEAGLADLVDDDHEILDG---IRLEPTPGHTPGHVS 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 389400709 201 SLIQARGGTVIYTGDLI--------PGLPwvnlpitMGYDRFAEKLVDEKKQILDRAVAEDALLVFPH 260
Cdd:cd16277  162 VELESGGERALFTGDVMhhpiqvarPDWS-------SVFDEDPAQAAATRRRLLERAADTDTLLFPAH 222
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
47-260 3.69e-17

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 77.79  E-value: 3.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709   47 SNCLLVKTGNYNLLFETGCGAylspdmkarfavqeeTHILLKALSEQGLSDSDISHVVLSHLHFDHAGGLLSAWEpdrep 126
Cdd:pfam00753   6 VNSYLIEGGGGAVLIDTGGSA---------------EAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAE----- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  127 alLFPNALFVVGEEHFRRSKsPHPRDRASFIPGLAEKLQATGRLVLKQGGDRLTVGALTIEFFQSQGHTPGMLVslIQAR 206
Cdd:pfam00753  66 --ATDVPVIVVAEEARELLD-EELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVV--VYYG 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 389400709  207 GGTVIYTGDLIP--GLPWVNLPITMGYDRFAEKLVDEKKQILDRAVAEDALLVFPH 260
Cdd:pfam00753 141 GGKVLFTGDLLFagEIGRLDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 48-260 1.45e-16

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 75.67  E-value: 1.45e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709    48 NCLLVKTGNYNLLFETGCGaylspdmkarfavqeETHILLKALSEQGLSDsdISHVVLSHLHFDHAGGLlsawepdrePA 127
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPG---------------EAEDLLAELKKLGPKK--IDAIILTHGHPDHIGGL---------PE 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709   128 LL-FPNALFVVGEEHFRrskspHPRDRASFIPGLAEKLQATGRLVLKQGGDRLTVGALTIEFFQSQGHTPGMLVSLIqaR 206
Cdd:smart00849  55 LLeAPGAPVYAPEGTAE-----LLKDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL--P 127

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 389400709   207 GGTVIYTGDLIPGlpwvNLPITMGYDRFAEKLVDEKKQILDRAVAEDALLVFPH 260
Cdd:smart00849 128 EGKILFTGDLLFA----GGDGRTLVDGGDAAASDALESLLKLLKLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 45-259 1.96e-14

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: 70.01  E-value: 1.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  45 IASNCLLVKTG-NYNLLFETGCGAYlspdmkarfavqeetHILLKALSEQGLsdsDISHVVLSHLHFDHAGGLlsawepd 123
Cdd:cd06262    8 LQTNCYLVSDEeGEAILIDPGAGAL---------------EKILEAIEELGL---KIKAILLTHGHFDHIGGL------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 124 rePALL-FPNALFVVGEEHFRRSKSPHprDRASFIPGLAEKLQATGRLVlkQGGDRLTVGALTIEFFQSQGHTPGMLVSL 202
Cdd:cd06262   63 --AELKeAPGAPVYIHEADAELLEDPE--LNLAFFGGGPLPPPEPDILL--EDGDTIELGGLELEVIHTPGHTPGSVCFY 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 389400709 203 IQARGgtVIYTGDLIP--GLPWVNLPitmgyDRFAEKLVDEKKQILdrAVAEDALLVFP 259
Cdd:cd06262  137 IEEEG--VLFTGDTLFagSIGRTDLP-----GGDPEQLIESIKKLL--LLLPDDTVVYP 186
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 86-228 4.35e-13

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: 66.75  E-value: 4.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  86 LLKALSEQGLSDSDISHVVLSHLHFDHAGGllsAWEpdrepaLL--FPNALFVVgeehfrrskspHPRdrasFIPGLA-- 161
Cdd:cd07726   41 LLAALEALGIAPEDVDYIILTHIHLDHAGG---AGL------LAeaLPNAKVYV-----------HPR----GARHLIdp 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 162 EKLQAT---------------------GRLVLKQGGDRLTVGALTIEFFQSQGHTPGMLVSLIQARGGtvIYTGD----L 216
Cdd:cd07726   97 SKLWASaravygdeadrlggeilpvpeERVIVLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESDG--LFTGDaagvR 174

                        170
                 ....*....|..
gi 389400709 217 IPGLPWVNLPIT 228
Cdd:cd07726  175 YPELDVVGPPST 186
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-215 1.88e-12

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


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 65.75  E-value: 1.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  35 VRADERGMIDIASNCLLVKTGNY-NLLFETGcgayLSPD-----------MKARFAVQEETHILLKALSEQGLSDSDISH 102
Cdd:cd07730   11 LRGGPLKRVTFPALAFLIEHPTGgKILFDLG----YRKDfeeytprvperLYRTPVPLEVEEDVAEQLAAGGIDPEDIDA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 103 VVLSHLHFDHAGGLlsawepdrepaLLFPNALFVVGE---EHFRRSKSPHpRDRASFIPGlaeklQATGRLVLKQGGDRL 179
Cdd:cd07730   87 VILSHLHWDHIGGL-----------SDFPNARLIVGPgakEALRPPGYPS-GFLPELLPS-----DFEGRLVRWEEDDFL 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 389400709 180 tvGALTIEFFQS--------------QGHTPGMLVSLIQ-ARGGTVIYTGD 215
Cdd:cd07730  150 --WVPLGPFPRAldlfgdgslylvdlPGHAPGHLGLLARtTSGTWVFLAGD 198
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 47-217 3.08e-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: 61.47  E-value: 3.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  47 SNCLLVKTGNYNLLFETGCgaylsPDMKARfavqeethiLLKALSEQGLSDSDISHVVLSHLHFDHAGGLlsawepdreP 126
Cdd:cd07721   11 VNAYLIEDDDGLTLIDTGL-----PGSAKR---------ILKALRELGLSPKDIRRILLTHGHIDHIGSL---------A 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 127 ALL-FPNALFVVGEE---HFRRSKSPHPRDRASFIPGLAEKLQATGRLVLK--QGGDRL-TVGALTIefFQSQGHTPGMl 199
Cdd:cd07721   68 ALKeAPGAPVYAHEReapYLEGEKPYPPPVRLGLLGLLSPLLPVKPVPVDRtlEDGDTLdLAGGLRV--IHTPGHTPGH- 144

                        170
                 ....*....|....*...
gi 389400709 200 VSLIQARGGTVIyTGDLI 217
Cdd:cd07721  145 ISLYLEEDGVLI-AGDAL 161
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 49-172 4.97e-11

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. 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: 293799  Cd Length: 269  Bit Score: 61.87  E-value: 4.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  49 CLLVKTGNYNLLFETGCGAylspdmkarfavqeethILLKALSEQGLSDSDISHVVLSHLHFDHAGGLlsawepdrePAL 128
Cdd:cd07713   22 SLLIETEGKKILFDTGQSG-----------------VLLHNAKKLGIDLSDIDAVVLSHGHYDHTGGL---------KAL 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 389400709 129 L--FPNALFVVGEEHFRRSKSPHPRDRASFIPGLAEKLQATGRLVL 172
Cdd:cd07713   76 LelNPKAPVYAHPDAFEPRYSKRGGGKKGIGIGREELEKAGARLVL 121
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 46-215 9.34e-10

Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. 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: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 56.89  E-value: 9.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  46 ASNCLLVKTGNYNLLFETGCGAylspdmkarfavqeethilLKALSEQGLSDSDISHVVLSHLHFDHAGGLlsawepdre 125
Cdd:cd16272   16 NTSSYLLETGGTRILLDCGEGT-------------------VYRLLKAGVDPDKLDAIFLSHFHLDHIGGL--------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 126 PALLFPNalfvvgeEHFRRSKSPH---PRDRASFIPGLAEKLQATGRLV-------LKQGGDRLTVGALTIEFFQSQgHT 195
Cdd:cd16272   68 PTLLFAR-------RYGGRKKPLTiygPKGIKEFLEKLLNFPVEILPLGfpleieeLEEGGEVLELGDLKVEAFPVK-HS 139

                        170       180
                 ....*....|....*....|
gi 389400709 196 PGMLVSLIQARGGTVIYTGD 215
Cdd:cd16272  140 VESLGYRIEAEGKSIVYSGD 159
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 80-203 2.79e-09

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 56.44  E-value: 2.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  80 QEETHILLKALSEQGLSDSDISHVVLSHLHFDHAGG------------LLS--AWEPDREPALLFPNalfvvgeehfRRS 145
Cdd:cd16280   42 NEAADLIVDGLEKLGLDPADIKYILITHGHGDHYGGaaylkdlygakvVMSeaDWDMMEEPPEEGDN----------PRW 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 389400709 146 KSPHPRDrasfipglaeklqatgrLVLKqGGDRLTVGALTIEFFQSQGHTPGMLvSLI 203
Cdd:cd16280  112 GPPPERD-----------------IVIK-DGDTLTLGDTTITVYLTPGHTPGTL-SLI 150
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 49-154 2.90e-09

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 56.48  E-value: 2.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  49 CLLVKTGNYNLLFETGCG--AYLSPD----------MKARFAvQEETHIL-LKALseqGLSDSDISHVVLSHLHFDHAGG 115
Cdd:cd07742   21 CLLVETDDGLVLVDTGFGlaDVADPKrrlggpfrrlLRPRLD-EDETAVRqIEAL---GFDPSDVRHIVLTHLDLDHAGG 96

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 389400709 116 LlsawePDrepallFPNALFVVGEEHFRRSKSPHPRDRA 154
Cdd:cd07742   97 L-----AD------FPHATVHVHAAELDAATSPRTRYER 124
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
46-215 3.01e-09

Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 56.36  E-value: 3.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  46 ASNCLLVKTGNYNLLFETGCGAylspdmkarfavqeethilLKALSEQGLSDSDISHVVLSHLHFDHAGGL----LSAWE 121
Cdd:COG1234   18 ATSSYLLEAGGERLLIDCGEGT-------------------QRQLLRAGLDPRDIDAIFITHLHGDHIAGLpgllSTRSL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 122 PDREPALLfpnalfVVGeehfrrsksphPRDRASFIPGLAEKLQATGRLVLK----QGGDRLTVGALTIEFFQSQgHTP- 196
Cdd:COG1234   79 AGREKPLT------IYG-----------PPGTKEFLEALLKASGTDLDFPLEfheiEPGEVFEIGGFTVTAFPLD-HPVp 140

                        170       180
                 ....*....|....*....|.
gi 389400709 197 --GMlvsLIQARGGTVIYTGD 215
Cdd:COG1234  141 ayGY---RFEEPGRSLVYSGD 158
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 46-218 2.93e-08

Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 52.52  E-value: 2.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  46 ASNCLLVKTGNYNLLFETGCGAYLspdmkaRFAvqeethillkalsEQGLSDSDISHVVLSHLHFDHAGGL----LSAWE 121
Cdd:cd07719   17 AGPSTLVVVGGRVYLVDAGSGVVR------RLA-------------QAGLPLGDLDAVFLTHLHSDHVADLpallLTAWL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 122 PDREPAL----------LFPNALFVVGEEHFRRsksphPRDRASFIPGLAEKLQAT----GRLVLKQggDRLTVGALTIE 187
Cdd:cd07719   78 AGRKTPLpvygppgtraLVDGLLAAYALDIDYR-----ARIGDEGRPDPGALVEVHeiaaGGVVYED--DGVKVTAFLVD 150

                        170       180       190
                 ....*....|....*....|....*....|....
gi 389400709 188 ffqsqgHTPgMLVSL---IQARGGTVIYTGDLIP 218
Cdd:cd07719  151 ------HGP-VPPALayrFDTPGRSVVFSGDTGP 177
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 49-216 9.40e-08

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: 51.78  E-value: 9.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  49 CLLVKTG-NYNLLFETGcgaylspdmkARFAVQEETHILLKALSEQGLSDsdISHVVLSHLHFDHAGGLlsawepdrePA 127
Cdd:COG2333   13 AILIRTPdGKTILIDTG----------PRPSFDAGERVVLPYLRALGIRR--LDLLVLTHPDADHIGGL---------AA 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 128 LL--FPNALFVVgeehfrrSKSPHPRDRASFIPGLAEKLQATGRLVLKqgGDRLTVGALTIEFFQSQGHTPGM------- 198
Cdd:COG2333   72 VLeaFPVGRVLV-------SGPPDTSETYERLLEALKEKGIPVRPCRA--GDTWQLGGVRFEVLWPPEDLLEGsdennns 142

                        170
                 ....*....|....*...
gi 389400709 199 LVSLIQARGGTVIYTGDL 216
Cdd:COG2333  143 LVLRLTYGGFSFLLTGDA 160
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 44-215 1.00e-07

uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. Members of this bacterial 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: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 50.90  E-value: 1.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  44 DIASNCLLVKTGNYNLLFETGCGAyLSpdmkarfAVQEetHILLkalseqglsdSDISHVVLSHLHFDH---AGGLLSAW 120
Cdd:cd07716   15 GGACSGYLLEADGFRILLDCGSGV-LS-------RLQR--YIDP----------EDLDAVVLSHLHPDHcadLGVLQYAR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 121 EpdrepallfpnalfvVGEEHFRRSKSP-----HPRDRASFIPGLAEklqATGRLVLKQgGDRLTVGALTIEFFQSQGHT 195
Cdd:cd07716   75 R---------------YHPRGARKPPLPlygpaGPAERLAALYGLED---VFDFHPIEP-GEPLEIGPFTITFFRTVHPV 135

                        170       180
                 ....*....|....*....|
gi 389400709 196 PGMLVSlIQARGGTVIYTGD 215
Cdd:cd07716  136 PCYAMR-IEDGGKVLVYTGD 154
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
49-172 1.88e-07

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 51.04  E-value: 1.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  49 CLLVKTGNYNLLFETGCGAylspdmkarfavqeethILLKALSEQGLSDSDISHVVLSHLHFDHAGGLlsawepdrePAL 128
Cdd:COG1237   24 SALIETEGKRILFDTGQSD-----------------VLLKNAEKLGIDLSDIDAVVLSHGHYDHTGGL---------PAL 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 389400709 129 LF--PNALFVVGEEHFRRSKSPHPRDRASFIPGLAEKLQATG-RLVL 172
Cdd:COG1237   78 LElnPKAPVYAHPDAFEKRYSKRPGGKYIGIPFSREELEKLGaRLIL 124
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 34-217 4.31e-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: 49.49  E-value: 4.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  34 WVRADERGMIDIaSNCLLVKTGNYNLLFETGcgayLSPDMKARfavqeethiLLKALSEqgLSDSDISHVVLSHLHFDHA 113
Cdd:cd16282    3 YALIGPDGGGFI-SNIGFIVGDDGVVVIDTG----ASPRLARA---------LLAAIRK--VTDKPVRYVVNTHYHGDHT 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 114 GGlLSAWEPDREPallfpnalfVVGEEHFRRS-KSPHPRDRASFIPGLAEKLQATgRLVL----KQGGDRLTVGALTIEF 188
Cdd:cd16282   67 LG-NAAFADAGAP---------IIAHENTREElAARGEAYLELMRRLGGDAMAGT-ELVLpdrtFDDGLTLDLGGRTVEL 135

                        170       180       190
                 ....*....|....*....|....*....|
gi 389400709 189 FQ-SQGHTPGMLVSLIQARGgtVIYTGDLI 217
Cdd:cd16282  136 IHlGPAHTPGDLVVWLPEEG--VLFAGDLV 163
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 48-216 1.15e-06

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 48.74  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  48 NCLLVKTGNYNLLFETGcgaylsPDMKArfavqeethiLLKALseqGLSDSDISHVVLSHLHFDHAGGLLsawepdrepa 127
Cdd:COG1235   36 SSILVEADGTRLLIDAG------PDLRE----------QLLRL---GLDPSKIDAILLTHEHADHIAGLD---------- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 128 llfpnalfvvgeeHFRRSKSPHP----------RDRASFIPGLAEKLQATGRLVLKQGGDRLTVGALTIEFFqSQGHTPG 197
Cdd:COG1235   87 -------------DLRPRYGPNPipvyatpgtlEALERRFPYLFAPYPGKLEFHEIEPGEPFEIGGLTVTPF-PVPHDAG 152

                        170       180
                 ....*....|....*....|
gi 389400709 198 MLVSL-IQARGGTVIYTGDL 216
Cdd:COG1235  153 DPVGYrIEDGGKKLAYATDT 172
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 86-215 1.36e-06

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: 47.45  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  86 LLKALSEQGLsdsDISHVVLSHLHFDHAGGLLSAWEpdrepalLFPNALfVVGEEHFRrsksphprdrasfIPGLAEKLQ 165
Cdd:cd07723   33 VLAALEKNGL---TLTAILTTHHHWDHTGGNAELKA-------LFPDAP-VYGPAEDR-------------IPGLDHPVK 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 389400709 166 atgrlvlkqGGDRLTVGALTIEFFQSQGHTPGMLVSLIQARGgtVIYTGD 215
Cdd:cd07723   89 ---------DGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEP--ALFTGD 127
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 48-259 1.86e-06

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: 47.29  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  48 NCLLVKTGNYNLLFETGcgaylspdmkarFAVQEETHILLKALSEQGLSDSDISHVVLSHLHFDHAGGLLSAWEPDREPa 127
Cdd:cd07725   16 NVYLLRDGDETTLIDTG------------LATEEDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGAT- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 128 llfpnaLFVVGEEHFRrsksphprdrasfipglaeklqatgrlvlkqGGDRLTVGALTIEFFQSQGHTPGMLVslIQARG 207
Cdd:cd07725   83 ------VYILDVTPVK-------------------------------DGDKIDLGGLRLKVIETPGHTPGHIV--LYDED 123

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 389400709 208 GTVIYTGDLIpgLPWVNLPITMgYDRFAEKLVDEKKQILDRAVAEDALLVFP 259
Cdd:cd07725  124 RRELFVGDAV--LPKITPNVSL-WAVRVEDPLGAYLESLDKLEKLDVDLAYP 172
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 103-245 2.31e-06

uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 46.85  E-value: 2.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 103 VVLSHLHFDHAGGLLS---AWEPDREPALLfpnalfvvgeehfrrsKSPHPRDRASFIPGLAEKLQATGRLVLKQgGDRL 179
Cdd:cd07712   46 VVATHGHFDHIGGLHEfeeVYVHPADAEIL----------------AAPDNFETLTWDAATYSVPPAGPTLPLRD-GDVI 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 180 TVGALTIEFFQSQGHTPGMLVSLIQARG----GTVIYTGDLIPGLPWVNLPItmgYDRFAEKLVDEKKQI 245
Cdd:cd07712  109 DLGDRQLEVIHTPGHTPGSIALLDRANRllfsGDVVYDGPLIMDLPHSDLDD---YLASLEKLSKLPDEF 175
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 48-275 2.74e-06

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 47.22  E-value: 2.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  48 NCLLVKTGNYNLLFETGCGAYLSPDMKARFAVQEEThillkalseqglsdsDISHVVLSHLHFDHAGgllsawePDREPA 127
Cdd:COG2220   12 ATFLIETGGKRILIDPVFSGRASPVNPLPLDPEDLP---------------KIDAVLVTHDHYDHLD-------DATLRA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 128 LLFPNALFVVgeehfrrsksphprdrasfIPGLAEKLQATG--RLVLKQGGDRLTVGALTIEFFQSQgHTPGMLVS---- 201
Cdd:COG2220   70 LKRTGATVVA-------------------PLGVAAWLRAWGfpRVTELDWGESVELGGLTVTAVPAR-HSSGRPDRnggl 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 202 ----LIQARGGTVIYTGD--LIPGLPWVN---------LPI-----TMGYD---RFAEKLvdEKKQILdrAVAEDALLVF 258
Cdd:COG2220  130 wvgfVIETDGKTIYHAGDtgYFPEMKEIGerfpidvalLPIgaypfTMGPEeaaEAARDL--KPKVVI--PIHYGTFPLL 205

                        250
                 ....*....|....*...
gi 389400709 259 PHDPV-HVAARVERDPVK 275
Cdd:COG2220  206 DEDPLeRFAAALAAAGVR 223
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 47-219 3.83e-06

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


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 46.37  E-value: 3.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  47 SNCLLVKTGNYNLLFETGCG--AYLSpdmkarfavqeethiLLKALSEQgLSDSDISHVVLSHLHFDHAGGLlsawepdr 124
Cdd:cd07722   18 TNTYLVGTGKRRILIDTGEGrpSYIP---------------LLKSVLDS-EGNATISDILLTHWHHDHVGGL-------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 125 ePALLfpnALFvvGEEHFRRSKSPHPRDRASFIPGlaeklqaTGRLVLKQGGDRLTVGALTIEFFQSQGHTPGMLVSLIQ 204
Cdd:cd07722   74 -PDVL---DLL--RGPSPRVYKFPRPEEDEDPDED-------GGDIHDLQDGQVFKVEGATLRVIHTPGHTTDHVCFLLE 140

                        170
                 ....*....|....*
gi 389400709 205 ARGgtVIYTGDLIPG 219
Cdd:cd07722  141 EEN--ALFTGDCVLG 153
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 87-217 4.37e-06

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: 46.57  E-value: 4.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  87 LKALSEQGLSDSDISHVVLSHLHFDHAGGLlsawepdrEPALLFPNALFVVgeehfrrskspHPRDrasfiPGLAEKLQA 166
Cdd:cd16322   34 EKLLARFGTTGLTLLYILLTHAHFDHVGGV--------ADLRRHPGAPVYL-----------HPDD-----LPLYEAADL 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 389400709 167 TGRL------------VLKQGGDRLTVGALTIEFFQSQGHTPGMLVSLIQARGgtVIYTGDLI 217
Cdd:cd16322   90 GAKAfglgieplpppdRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEG--LLFSGDLL 150
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 87-215 5.17e-06

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 46.10  E-value: 5.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  87 LKALSEQGLSDSDISHVVLSHLHFDHAGGLlsawepdrePALLFpNALFVVgeehfRRSK-----SPHP-RDRA-----S 155
Cdd:cd07740   37 LIALKRAGIDPNAIDAIFITHLHGDHFGGL---------PFFLL-DAQFVA-----KRTRpltiaGPPGlRERLrrameA 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 389400709 156 FIPGLAEKLQATG-RLVLKQGGDRLTVGALTIEFFQSQgHTPGMLvSL---IQARGGTVIYTGD 215
Cdd:cd07740  102 LFPGSSKVPRRFDlEVIELEPGEPTTLGGVTVTAFPVV-HPSGAL-PLalrLEAAGRVLAYSGD 163
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 40-216 9.00e-06

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized Enterococcus faecalis EF2904. 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: 293818 [Multi-domain]  Cd Length: 202  Bit Score: 45.68  E-value: 9.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  40 RGMIDIASNCLLVKTGNYNLLFEtgCGAYLSPDMKARFAVQE--ETHILLK--------ALSEQGLSDSDISH--VVLSH 107
Cdd:cd07732    6 RGTNEIGGNCIEVETGGTRILLD--FGLPLDPESKYFDEVLDflELGLLPDivglyrdpLLLGGLRSEEDPSVdaVLLSH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 108 LHFDHAgGLLSAWEPD-----REPALLFPNALFvvgeeHFRRSKSPHPRDRASFIPglaeklqatgrlvlkqgGDRLTVG 182
Cdd:cd07732   84 AHLDHY-GLLNYLRPDipvymGEATKRILKALL-----PFFGEGDPVPRNIRVFES-----------------GKSFTIG 140

                        170       180       190
                 ....*....|....*....|....*....|....
gi 389400709 183 ALTIEFFQSQGHTPGMLVSLIQARGGTVIYTGDL 216
Cdd:cd07732  141 DFTVTPYLVDHSAPGAYAFLIEAPGKRIFYTGDF 174
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 94-199 1.19e-05

Erythrobacter vulgaris EVM-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 EVM-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: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 45.80  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  94 GLSDSDISHVVLSHLHFDHAGGLLSAWEPDREPALLFPNALFVVgeehfrRSKSPHPRD-RASFIPGLAEklQATGRLVl 172
Cdd:cd16315   55 GFDPKDVRWLLSSHEHFDHVGGLAALQRATGARVAASAAAAPVL------ESGKPAPDDpQAGLHEPFPP--VRVDRIV- 125

                         90       100
                 ....*....|....*....|....*..
gi 389400709 173 kQGGDRLTVGALTIEFFQSQGHTPGML 199
Cdd:cd16315  126 -EDGDTVALGSLRLTAHATPGHTPGAL 151
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 41-197 2.58e-05

metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B3 MBLs include Fluoribacter gormanii FEZ-1, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) GOB-1, Stenotrophomonas Maltophilia L1, and Bradyrhizobium diazoefficiens BJP-1, Serratia marcescens SMB-1, and Pseudomonas Aeruginosa AIM-1. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293794 [Multi-domain]  Cd Length: 248  Bit Score: 44.46  E-value: 2.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  41 GMIDIASncLLVKTGNYNLLFETGcgaylspdmkarfaVQEETHILLKALSEQGLSDSDISHVVLSHLHFDHAGGLLsaw 120
Cdd:cd07708   18 GTDDLAA--YLIVTPQGNILIDGD--------------MEQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSA--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 121 EPDREPAllfpnALFVVGEEH---FRR--SKSPH-PRDRASFIPGlaeklQATGRLVLKqgGDRLTVGALTIEFFQSQGH 194
Cdd:cd07708   79 EIKKQTG-----AKVMAGAEDvslLLSggSSDFHyANDSSTYFPQ-----STVDRAVHD--GERVTLGGTVLTAHATPGH 146


                 ...
gi 389400709 195 TPG 197
Cdd:cd07708  147 TPG 149
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 49-216 4.60e-05

Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes proteins required for natural transformation competence including Neisseria gonorrhoeae ComA, Pseudomonas stutzeri ComA, Bacillus subtilis ComEC (also known as ComE operon protein 3) and Haemophilus influenza ORF2 encoded by the rec-2 gene, as well as Escherichia coli YcaI which does not mediate spontaneous plasmid transformation on nutrient-containing agar plates. It also includes the phosphorylcholine esterase (Pce) domain of choline-binding protein e from streptococcus pneumonia. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 43.28  E-value: 4.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  49 CLLVKTGNYNLLFETGcgaylspdmkARFAVQEEthILLKALSEQGlsDSDISHVVLSHLHFDHAGGLlsawepdrePAL 128
Cdd:cd07731   12 AILIQTPGKTILIDTG----------PRDSFGED--VVVPYLKARG--IKKLDYLILTHPDADHIGGL---------DAV 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 129 L--FPnalfvVGEehFRRSKSPHPRDRASFIPGLAEKLQATGRLVLKqgGDRLTVGALTIEFFQSQGHTPG-----MLVS 201
Cdd:cd07731   69 LknFP-----VKE--VYMPGVTHTTKTYEDLLDAIKEKGIPVTPCKA--GDRWQLGGVSFEVLSPPKDDYDdlnnnSCVL 139

                        170
                 ....*....|....*
gi 389400709 202 LIQARGGTVIYTGDL 216
Cdd:cd07731  140 RLTYGGTSFLLTGDA 154
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 62-261 4.62e-05

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: 43.16  E-value: 4.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  62 ETGCGAYLSPDMKARFA-----VQEETHILLKALSEQGLSdsdISHVVLSHLHFDH--AGGLLSAwepdrepallFPNAL 134
Cdd:cd07724    9 GLGTLSYLVGDPETGEAavidpVRDSVDRYLDLAAELGLK---ITYVLETHVHADHvsGARELAE----------RTGAP 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 135 FVVGEehfrrsksphpRDRASFipglaeklqaTGRLVlkQGGDRLTVGALTIEFFQSQGHTPGMLVSLIqaRGGTVIYTG 214
Cdd:cd07724   76 IVIGE-----------GAPASF----------FDRLL--KDGDVLELGNLTLEVLHTPGHTPESVSYLV--GDPDAVFTG 130

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 389400709 215 D--LIPGLPWVNLPITMGYDrfAEKLVD---EKKQILDravaeDALLVFP-HD 261
Cdd:cd07724  131 DtlFVGDVGRPDLPGEAEGL--ARQLYDslqRKLLLLP-----DETLVYPgHD 176
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 86-228 7.96e-05

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 42.57  E-value: 7.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  86 LLKALSEqgLSDSDISHVVLSHLHFDHAGGllsawepdrepALLFP--NALFVVGEEhfrrsksphprdrasfipgLAEK 163
Cdd:cd16276   34 LLAAIRK--VTDKPVTHVVYSHNHADHIGG-----------ASIFKdeGATIIAHEA-------------------TAEL 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 389400709 164 LQATG--RLVLK----QGGDRLTVGALTIEF-FQSQGHTPGMLVslIQARGGTVIYTGDLI-PG-LPWVNLPIT 228
Cdd:cd16276   82 LKRNPdpKRPVPtvtfDDEYTLEVGGQTLELsYFGPNHGPGNIV--IYLPKQKVLMAVDLInPGwVPFFNFAGS 153
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 49-216 1.74e-04

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. 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: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 41.68  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  49 CLLVKTGNYNLLFEtgCGAYlspdmkarfavQEETHILLKALSEQGLSDSDISHVVLSHLHFDHAGGL--LS-------- 118
Cdd:cd16295   14 CYLLETGGKRILLD--CGLF-----------QGGKELEELNNEPFPFDPKEIDAVILTHAHLDHSGRLplLVkegfrgpi 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 119 -AWEPDREPA-LLFPNALFVVGEEHFRRSKSPhprdraSFIPGLAEKLQAtgRLVLKQGGDRLTVGA-LTIEFFQSqGHT 195
Cdd:cd16295   81 yATPATKDLAeLLLLDSAKIQEEEAEHPPAEP------LYTEEDVEKALK--HFRPVEYGEPFEIGPgVKVTFYDA-GHI 151

                        170       180
                 ....*....|....*....|..
gi 389400709 196 PG-MLVSLIQARGGTVIYTGDL 216
Cdd:cd16295  152 LGsASVELEIGGGKRILFSGDL 173
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 44-116 2.11e-04

Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a metazoan-specific multisubunit, multifunctional protein complex composed of 14 subunits named Int1-Int14 (Integrator subunits). This subgroup includes Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)). Integrator complex has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. 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: 293849  Cd Length: 199  Bit Score: 41.48  E-value: 2.11e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 389400709  44 DIASNCLLVKTGNYNLLFEtgCGAYLSPDMKARFAVqeethilLKALSEQGLSDSDISHVVLSHLHFDHAGGL 116
Cdd:cd16291    9 DVGRSCILVTIGGKNIMFD--CGMHMGYNDERRFPD-------FSYISQNGPFTEHIDCVIISHFHLDHCGAL 72
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 84-197 2.75e-04

Pseudomonas Aeruginosa AIM-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 AIM-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: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 41.42  E-value: 2.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  84 HILLKALSEQ------------GLSDSDISHVVLSHLHFDHAGGlLSAWEPD-------REPALlfpnalfvvgeEHFRR 144
Cdd:cd16314   33 HILIDGGTDKaaplieaniralGFRPEDVRYIVSSHEHFDHAGG-IARLQRAtgapvvaREPAA-----------TTLER 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 389400709 145 SKSphPRDRASFIpgLAEKLQATGRLVLKQGGDRLTVGALTIEFFQSQGHTPG 197
Cdd:cd16314  101 GRS--DRSDPQFL--VVEKFPPVASVQRIGDGEVLRVGPLALTAHATPGHTPG 149
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 48-116 9.55e-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: 38.78  E-value: 9.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 389400709  48 NCLLVKTGNYNLLFETGcgaylspdmkarFAVQEethiLLKALSEQGLSDSDISHVVLSHLHFDHAGGL 116
Cdd:cd07733   10 NCTYLETEDGKLLIDAG------------LSGRK----ITGRLAEIGRDPEDIDAILVTHEHADHIKGL 62
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 48-216 2.38e-03

RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 39.01  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709  48 NCLLVKTGNYNLLFEtgCGayLSPDMKARfavqeethillkALSEQGLSDSDISHVVLSHLHFDHAGGL--LSAWEPDRE 125
Cdd:COG1236   15 SCYLLETGGTRILID--CG--LFQGGKER------------NWPPFPFRPSDVDAVVLTHAHLDHSGALplLVKEGFRGP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389400709 126 ----PA------LLFPNALFVVGEEHfrrsksphprdRASFIPGLAEKLQATGRLVLKQGGDRLTVGALTIEFFQSqGHT 195
Cdd:COG1236   79 iyatPAtadlarILLGDSAKIQEEEA-----------EAEPLYTEEDAERALELFQTVDYGEPFEIGGVRVTFHPA-GHI 146

                        170       180
                 ....*....|....*....|....
gi 389400709 196 PGmlvS---LIQARGGTVIYTGDL 216
Cdd:COG1236  147 LG---SaqvELEVGGKRIVFSGDY 167
Amphi-Trp pfam20068
Amphi-Trp domain;
146-181 3.94e-03

Amphi-Trp domain;


Pssm-ID: 437900  Cd Length: 93  Bit Score: 36.01  E-value: 3.94e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 389400709  146 KSPHPRDR---ASFIPGLAEKLQATGRLVLKQGGDRLTV 181
Cdd:pfam20068   8 KSEERQSRaeiAAYLRTVADKLEAGGSVTLSAGDESVTL 46
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 86-118 9.63e-03

Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and is related to pfam00753.


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 36.52  E-value: 9.63e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 389400709   86 LLKALSEQGLSDSDISHVVLSHLHFDHAGGLLS 118
Cdd:pfam12706  15 ALPALQPGRLRDDPIDAVLLTHDHYDHLAGLLD 47
 
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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