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Conserved domains on  [gi|545090032|ref|WP_021459651|]
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MULTISPECIES: N-acyl homoserine lactonase family protein [Staphylococcus]

Protein Classification

N-acyl homoserine lactonase family protein( domain architecture ID 10870091)

N-acyl homoserine lactonase family protein similar to Bacillus N-acyl homoserine lactonase and Mesorhizobium loti 4-pyridoxolactonase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 10-266 3.99e-75

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: 229.02  E-value: 3.99e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  10 KIYVLDNGRMKMDKNLMIANanqatldaPNAPNEMHEFPIYTVFIDHPDAKILFDTACNPNAMGENGrwisATQKAFPYF 89
Cdd:cd07729    1 KLYALDYGTVTVDKSSLFYY--------GRGPGEPIDLPVYAYLIEHPEGTILVDTGFHPDAADDPG----GLELAFPPG 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  90 ADESCHLPNRLEQIGVDPKEVDFVVASHLHLDHAGCLEYFTNATIIVHDDELSGAMKTYARNqqAGAYIWADIDAWIKSN 169
Cdd:cd07729   69 VTEEQTLEEQLARLGLDPEDIDYVILSHLHFDHAGGLDLFPNATIIVQRAELEYATGPDPLA--AGYYEDVLALDDDLPG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032 170 LTWRTVskeDDNLKLVEGVRVLNYGsGHAWGLIGLEIESSElGTIILASDAIYTKESMGTPfKPPGILYDSIGWTKSVEK 249
Cdd:cd07729  147 GRVRLV---DGDYDLFPGVTLIPTP-GHTPGHQSVLVRLPE-GTVLLAGDAAYTYENLEEG-RPPGINYDPEAALASLER 220

                        250
                 ....*....|....*..
gi 545090032 250 IKKLADEKNAQIWFGHD 266
Cdd:cd07729  221 LKALAEREGARVIPGHD 237
 
Name Accession Description Interval E-value
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 10-266 3.99e-75

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: 229.02  E-value: 3.99e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  10 KIYVLDNGRMKMDKNLMIANanqatldaPNAPNEMHEFPIYTVFIDHPDAKILFDTACNPNAMGENGrwisATQKAFPYF 89
Cdd:cd07729    1 KLYALDYGTVTVDKSSLFYY--------GRGPGEPIDLPVYAYLIEHPEGTILVDTGFHPDAADDPG----GLELAFPPG 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  90 ADESCHLPNRLEQIGVDPKEVDFVVASHLHLDHAGCLEYFTNATIIVHDDELSGAMKTYARNqqAGAYIWADIDAWIKSN 169
Cdd:cd07729   69 VTEEQTLEEQLARLGLDPEDIDYVILSHLHFDHAGGLDLFPNATIIVQRAELEYATGPDPLA--AGYYEDVLALDDDLPG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032 170 LTWRTVskeDDNLKLVEGVRVLNYGsGHAWGLIGLEIESSElGTIILASDAIYTKESMGTPfKPPGILYDSIGWTKSVEK 249
Cdd:cd07729  147 GRVRLV---DGDYDLFPGVTLIPTP-GHTPGHQSVLVRLPE-GTVLLAGDAAYTYENLEEG-RPPGINYDPEAALASLER 220

                        250
                 ....*....|....*..
gi 545090032 250 IKKLADEKNAQIWFGHD 266
Cdd:cd07729  221 LKALAEREGARVIPGHD 237
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 39-267 4.94e-17

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: 77.81  E-value: 4.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  39 NAPNEMHEFPIYTVFIDHPDAKILFDTACNPNAMGEngrwisatqkafpyfadeschLPNRLEQIGVDpkeVDFVVASHL 118
Cdd:COG0491    5 PGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEA---------------------LLAALAALGLD---IKAVLLTHL 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032 119 HLDHAGCLEYF---TNATIIVHDDELSGAMKTYARNQQAGAYIWADidawiksnltwRTVsKEDDNLKL-VEGVRVLnYG 194
Cdd:COG0491   61 HPDHVGGLAALaeaFGAPVYAHAAEAEALEAPAAGALFGREPVPPD-----------RTL-EDGDTLELgGPGLEVI-HT 127

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545090032 195 SGHAWGLIGLEIESselGTIILASDAIYTkESMGTPFKPPGilyDSIGWTKSVEKIKKLADEknaQIWFGHDG 267
Cdd:COG0491  128 PGHTPGHVSFYVPD---EKVLFTGDALFS-GGVGRPDLPDG---DLAQWLASLERLLALPPD---LVIPGHGP 190
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
46-265 1.28e-16

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 76.25  E-value: 1.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032   46 EFPIYTVFIDHPDAKILFDTACNPNAMGENgrwisatqkafpyfadeschlpnRLEQIGVDPKEVDFVVASHLHLDHAGC 125
Cdd:pfam00753   3 PGQVNSYLIEGGGGAVLIDTGGSAEAALLL-----------------------LLAALGLGPKDIDAVILTHGHFDHIGG 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  126 LEYFTNATIIV--HDDELSGAMKTYARNQQAGAYIWADIDAWIKSNLTWrtvsKEDDNLKLVEGVRV-LNYGSGHAWGLI 202
Cdd:pfam00753  60 LGELAEATDVPviVVAEEARELLDEELGLAASRLGLPGPPVVPLPPDVV----LEEGDGILGGGLGLlVTHGPGHGPGHV 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545090032  203 GLEIESselGTIILASDAIYTKES-MGTPFKPPGILYDSIGWTKSVEKIKKLADEKNAQIWFGH 265
Cdd:pfam00753 136 VVYYGG---GKVLFTGDLLFAGEIgRLDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 50-265 6.75e-14

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: 68.35  E-value: 6.75e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032    50 YTVFIDHPDAKILFDTacnpnamgengrwisatqkafpyFADESCHLPNRLEQIGvdPKEVDFVVASHLHLDHAGCLEYF 129
Cdd:smart00849   1 NSYLVRDDGGAILIDT-----------------------GPGEAEDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPEL 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032   130 ---TNATIIVHDDElsgamktyARNQQAGAYIWADIDAWIKSNLTWRTVsKEDDNLKL-VEGVRVLNYGsGHAWGLIGLE 205
Cdd:smart00849  56 leaPGAPVYAPEGT--------AELLKDLLALLGELGAEAEPAPPDRTL-KDGDELDLgGGELEVIHTP-GHTPGSIVLY 125

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032   206 IESselGTIILASDAIYTKESMGTPFKPPGILYDSigwtkSVEKIKKLADEKNAQIWFGH 265
Cdd:smart00849 126 LPE---GKILFTGDLLFAGGDGRTLVDGGDAAASD-----ALESLLKLLKLLPKLVVPGH 177
 
Name Accession Description Interval E-value
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 10-266 3.99e-75

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: 229.02  E-value: 3.99e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  10 KIYVLDNGRMKMDKNLMIANanqatldaPNAPNEMHEFPIYTVFIDHPDAKILFDTACNPNAMGENGrwisATQKAFPYF 89
Cdd:cd07729    1 KLYALDYGTVTVDKSSLFYY--------GRGPGEPIDLPVYAYLIEHPEGTILVDTGFHPDAADDPG----GLELAFPPG 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  90 ADESCHLPNRLEQIGVDPKEVDFVVASHLHLDHAGCLEYFTNATIIVHDDELSGAMKTYARNqqAGAYIWADIDAWIKSN 169
Cdd:cd07729   69 VTEEQTLEEQLARLGLDPEDIDYVILSHLHFDHAGGLDLFPNATIIVQRAELEYATGPDPLA--AGYYEDVLALDDDLPG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032 170 LTWRTVskeDDNLKLVEGVRVLNYGsGHAWGLIGLEIESSElGTIILASDAIYTKESMGTPfKPPGILYDSIGWTKSVEK 249
Cdd:cd07729  147 GRVRLV---DGDYDLFPGVTLIPTP-GHTPGHQSVLVRLPE-GTVLLAGDAAYTYENLEEG-RPPGINYDPEAALASLER 220

                        250
                 ....*....|....*..
gi 545090032 250 IKKLADEKNAQIWFGHD 266
Cdd:cd07729  221 LKALAEREGARVIPGHD 237
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 39-266 9.05e-24

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: 96.57  E-value: 9.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  39 NAPNEMHEFPIYTVFIDHPD-AKILFDTACNPnamgengRWISATQKAFPYFADESCHLP------NRLEQIGVDPKEVD 111
Cdd:cd07730   13 GGPLKRVTFPALAFLIEHPTgGKILFDLGYRK-------DFEEYTPRVPERLYRTPVPLEveedvaEQLAAGGIDPEDID 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032 112 FVVASHLHLDHAGCLEYFTNATIIVHDDELSGAMKTYARNQQAGAYIWADIDAwiksNLTWRTVSKEDDNLKL--VEGVR 189
Cdd:cd07730   86 AVILSHLHWDHIGGLSDFPNARLIVGPGAKEALRPPGYPSGFLPELLPSDFEG----RLVRWEEDDFLWVPLGpfPRALD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032 190 VLNYGS-------GHAWGLIGLEIESSELGTIILASDAIYTKESMGTPFKPPGILYDSIGWTK-----SVEKIKKLADEK 257
Cdd:cd07730  162 LFGDGSlylvdlpGHAPGHLGLLARTTSGTWVFLAGDACHHRIGLLRPSPLLPLPDLDDGADReaareTLARLRELDAAP 241


                 ....*....
gi 545090032 258 NAQIWFGHD 266
Cdd:cd07730  242 DVRVVLAHD 250
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 54-266 3.03e-18

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: 80.32  E-value: 3.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  54 IDHPDAKILFDTACNPNAMgengrwisatqkafpyfadescHLPNRLEQIGVDPKEVDFVVASHLHLDHAGCLEYFTNAT 133
Cdd:cd07711   27 IKDGGKNILVDTGTPWDRD----------------------LLLKALAEHGLSPEDIDYVVLTHGHPDHIGNLNLFPNAT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032 134 IIVHDDElsgamktyarnqqagayiwadidaWIKSNLTWRTvsKEDDNLKLVEGVRVLNyGSGHAWGLIGLEIESSELGT 213
Cdd:cd07711   85 VIVGWDI------------------------CGDSYDDHSL--EEGDGYEIDENVEVIP-TPGHTPEDVSVLVETEKKGT 137

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 545090032 214 IILASDAIYTKESMGTPFKPPGILYDSIGWTKSVEKIKKLADeknaQIWFGHD 266
Cdd:cd07711  138 VAVAGDLFEREEDLEDPILWDPLSEDPELQEESRKRILALAD----WIIPGHG 186
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 39-267 4.94e-17

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: 77.81  E-value: 4.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  39 NAPNEMHEFPIYTVFIDHPDAKILFDTACNPNAMGEngrwisatqkafpyfadeschLPNRLEQIGVDpkeVDFVVASHL 118
Cdd:COG0491    5 PGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEA---------------------LLAALAALGLD---IKAVLLTHL 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032 119 HLDHAGCLEYF---TNATIIVHDDELSGAMKTYARNQQAGAYIWADidawiksnltwRTVsKEDDNLKL-VEGVRVLnYG 194
Cdd:COG0491   61 HPDHVGGLAALaeaFGAPVYAHAAEAEALEAPAAGALFGREPVPPD-----------RTL-EDGDTLELgGPGLEVI-HT 127

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545090032 195 SGHAWGLIGLEIESselGTIILASDAIYTkESMGTPFKPPGilyDSIGWTKSVEKIKKLADEknaQIWFGHDG 267
Cdd:COG0491  128 PGHTPGHVSFYVPD---EKVLFTGDALFS-GGVGRPDLPDG---DLAQWLASLERLLALPPD---LVIPGHGP 190
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
46-265 1.28e-16

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 76.25  E-value: 1.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032   46 EFPIYTVFIDHPDAKILFDTACNPNAMGENgrwisatqkafpyfadeschlpnRLEQIGVDPKEVDFVVASHLHLDHAGC 125
Cdd:pfam00753   3 PGQVNSYLIEGGGGAVLIDTGGSAEAALLL-----------------------LLAALGLGPKDIDAVILTHGHFDHIGG 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  126 LEYFTNATIIV--HDDELSGAMKTYARNQQAGAYIWADIDAWIKSNLTWrtvsKEDDNLKLVEGVRV-LNYGSGHAWGLI 202
Cdd:pfam00753  60 LGELAEATDVPviVVAEEARELLDEELGLAASRLGLPGPPVVPLPPDVV----LEEGDGILGGGLGLlVTHGPGHGPGHV 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545090032  203 GLEIESselGTIILASDAIYTKES-MGTPFKPPGILYDSIGWTKSVEKIKKLADEKNAQIWFGH 265
Cdd:pfam00753 136 VVYYGG---GKVLFTGDLLFAGEIgRLDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 9-222 5.92e-14

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: 69.88  E-value: 5.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032   9 MKIYVLDNGRMKMDKNLMIANAN---QATLDAPNAPNEMHEFPIYTVFIDHPDAKILFDTACNPNAMGENGRwisatqka 85
Cdd:cd07720    6 FEVTALSDGTLPLPLDLLLGGAApeaEAALLAAFLPPDPVETSVNAFLVRTGGRLILVDTGAGGLFGPTAGK-------- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  86 fpyfadeschLPNRLEQIGVDPKEVDFVVASHLHLDHAGCL------EYFTNATIIVHDDE----LSGAMKTYArNQQAG 155
Cdd:cd07720   78 ----------LLANLAAAGIDPEDIDDVLLTHLHPDHIGGLvdaggkPVFPNAEVHVSEAEwdfwLDDANAAKA-PEGAK 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545090032 156 AYIWADIDAwIKSNLTWRTVSKEDDnlkLVEGVRVLNYGsGHAWGLIGLEIESSElGTIILASDAIY 222
Cdd:cd07720  147 RFFDAARDR-LRPYAAAGRFEDGDE---VLPGITAVPAP-GHTPGHTGYRIESGG-ERLLIWGDIVH 207
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 50-265 6.75e-14

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: 68.35  E-value: 6.75e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032    50 YTVFIDHPDAKILFDTacnpnamgengrwisatqkafpyFADESCHLPNRLEQIGvdPKEVDFVVASHLHLDHAGCLEYF 129
Cdd:smart00849   1 NSYLVRDDGGAILIDT-----------------------GPGEAEDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPEL 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032   130 ---TNATIIVHDDElsgamktyARNQQAGAYIWADIDAWIKSNLTWRTVsKEDDNLKL-VEGVRVLNYGsGHAWGLIGLE 205
Cdd:smart00849  56 leaPGAPVYAPEGT--------AELLKDLLALLGELGAEAEPAPPDRTL-KDGDELDLgGGELEVIHTP-GHTPGSIVLY 125

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032   206 IESselGTIILASDAIYTKESMGTPFKPPGILYDSigwtkSVEKIKKLADEKNAQIWFGH 265
Cdd:smart00849 126 LPE---GKILFTGDLLFAGGDGRTLVDGGDAAASD-----ALESLLKLLKLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 9-221 2.59e-10

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 59.43  E-value: 2.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032   9 MKIYVLDNGRMKMDKNLMIANANQATLDAPNAPNEMHEFPIYT--VFIDHPDAKILFDTAcnpnaMGEngRWisaTQKAF 86
Cdd:cd16281    1 MQLHSIEGGYFKLDGGAMFGVVPKPLWQKWYPADEDNRITLAMrcLLIETGGRNILIDTG-----IGD--KQ---DPKFR 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  87 PYFADESCH-LPNRLEQIGVDPKEVDFVVASHLHLDHA-GCLEY---------FTNATIIVHDDELSGAMKTYARNqqAG 155
Cdd:cd16281   71 SIYVQHSEHsLLKSLARLGLSPEDITDVILTHLHFDHCgGATRAdddglvellFPNATYWVQKRHWEWALNPNPRE--RA 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545090032 156 AYIWADIDAWIKS-NLTWrtvsKEDDNLKLVEGVRVLnYGSGHAWGLIGLEIESSElGTIILASDAI 221
Cdd:cd16281  149 SFLPENIEPLEESgRLKL----IDGSDAELGPGIRFH-LSDGHTPGQMLPEISTPG-GTVVFAADLI 209
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 46-265 2.74e-10

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: 58.39  E-value: 2.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  46 EFPIYTVFIDHPDAKILFDTAcnpnamgengrwisatqkaFPYFADescHLPNRLEQIGVDPKEVDFVVASHLHLDHAGC 125
Cdd:cd07721    8 LPPVNAYLIEDDDGLTLIDTG-------------------LPGSAK---RILKALRELGLSPKDIRRILLTHGHIDHIGS 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032 126 LEYF---TNATIIVHDDELSGAMKTYARNQQAGAYIWADIDAWIKSNLTWRTVS-KEDDNLKLVEGVRVLnYGSGHAWGL 201
Cdd:cd07721   66 LAALkeaPGAPVYAHEREAPYLEGEKPYPPPVRLGLLGLLSPLLPVKPVPVDRTlEDGDTLDLAGGLRVI-HTPGHTPGH 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545090032 202 IGLEIESSElgtIILASDAIYTKESMGTPfkPPGILYDSigWTKSVEKIKKLADEKNAQIWFGH 265
Cdd:cd07721  145 ISLYLEEDG---VLIAGDALVTVGGELVP--PPPPFTWD--MEEALESLRKLAELDPEVLAPGH 201
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 52-191 5.49e-10

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: 58.79  E-value: 5.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  52 VFIDHPDAKILFDTacnpnamGENGRWISatqkafpyfadeschlpNrLEQIGVDPKEVDFVVASHLHLDHAGCLEYF-- 129
Cdd:cd07713   23 LLIETEGKKILFDT-------GQSGVLLH-----------------N-AKKLGIDLSDIDAVVLSHGHYDHTGGLKALle 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545090032 130 --TNATIIVHDDELSgamKTYARNQQAGAYIWADIDAWIKSNLTWRTVskeDDNLKLVEGVRVL 191
Cdd:cd07713   78 lnPKAPVYAHPDAFE---PRYSKRGGGKKGIGIGREELEKAGARLVLV---EEPTEIAPGVYLT 135
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 95-137 1.31e-09

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: 56.73  E-value: 1.31e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 545090032  95 HLPNRLEQIGVDPKEVDFVVASHLHLDHAG----CLEYFTNATIIVH 137
Cdd:cd07726   40 RLLAALEALGIAPEDVDYIILTHIHLDHAGgaglLAEALPNAKVYVH 86
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 98-239 2.22e-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: 2.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  98 NRLEQIGVDPKEVDFVVASHLHLDHAGCLEYFTNATIIVHDDELSGAMKTYARN--QQAGAYIWADIDAWI---KSNLTW 172
Cdd:cd07742   69 RQIEALGFDPSDVRHIVLTHLDLDHAGGLADFPHATVHVHAAELDAATSPRTRYerRRYRPQQLAHGPWWVtyaAGGERW 148

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545090032 173 RtvskeddNLklvEGVRVLNYGS---------GHAWGLIGLEIESSElGTIILASDAIYTKESMGTPFKPPGILYD 239
Cdd:cd07742  149 F-------GF---EAVRPLDGLPpeillvplpGHTRGHCGVAVRTGD-RWLLHAGDAYFHHGELDPLPPPPPPLRL 213
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 54-141 1.10e-08

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: 54.07  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  54 IDHPDAKILFDTACnpnamGeNGRwisaTQKAFPYFADESCHLPNRLEQIGVDPKEVDFVVASHLHLDHAGCLEY----- 128
Cdd:cd16277   18 VRTPGRTILVDTGI-----G-NDK----PRPGPPAFHNLNTPYLERLAAAGVRPEDVDYVLCTHLHVDHVGWNTRlvdgr 87

                         90
                 ....*....|....*..
gi 545090032 129 ----FTNATIIVHDDEL 141
Cdd:cd16277   88 wvptFPNARYLFSRAEY 104
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 100-265 1.42e-08

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: 53.44  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032 100 LEQIGVDPKEVDFVVASHLHLDHAGCLEYF---TNATIIVHDDELSGAMKTYARNQQAGAYIWADIDAWIksnltwrTVs 176
Cdd:cd06262   36 LEAIEELGLKIKAILLTHGHFDHIGGLAELkeaPGAPVYIHEADAELLEDPELNLAFFGGGPLPPPEPDI-------LL- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032 177 KEDDNLKLVE-GVRVLNYGsGHAWGLIGLEIESselGTIILASDAIYTKESMGTPFkPPGILYDSIgwtKSVEKIKKLAD 255
Cdd:cd06262  108 EDGDTIELGGlELEVIHTP-GHTPGSVCFYIEE---EGVLFTGDTLFAGSIGRTDL-PGGDPEQLI---ESIKKLLLLLP 179

                        170
                 ....*....|
gi 545090032 256 EkNAQIWFGH 265
Cdd:cd06262  180 D-DTVVYPGH 188
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 9-140 3.54e-06

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: 47.25  E-value: 3.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032   9 MKIYVLDNGRMKMDKNLMIANANQATLDAPNAPNEMHEFPIYT--VFIDHPDAKILFDTACNPNAMGENgrwisatQKAF 86
Cdd:cd07728    1 IKLTWLDGGVTHLDGGAMFGVVPKPLWSKKYPANEKNQIELRTdpILIQYQGKNYLIDAGIGNGKLTEK-------QKRN 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545090032  87 pYFADESCHLPNRLEQIGVDPKEVDFVVASHLHLDHAGCLEY---------FTNATIIVHDDE 140
Cdd:cd07728   74 -FGVTEESSIEESLAELGLTPEDIDYVLMTHLHFDHASGLTKvkgeqlvsvFPNATIYVSEIE 135
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 60-133 1.52e-05

cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; MBL-fold metallo-hydrolase domain; CPSF3 (also known as cleavage and polyadenylation specificity factor 73 kDa subunit/CPSF-73) functions as a 3' endonuclease in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and in 3' end processing of metazoan histone pre-mRNAs. This subgroup also contains the yeast homolog of CPSF-73, Ysh1/Brr5 which has roles in mRNA and snoRNA synthesis. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain, and a RMMBL domain (RNA-metabolizing metallo-beta-lactamase). 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: 293850  Cd Length: 194  Bit Score: 44.50  E-value: 1.52e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545090032  60 KILFDTACNPNAMGENgrwisatqkAFPYFaDEschlpnrleqigVDPKEVDFVVASHLHLDHAGCLEYFTNAT 133
Cdd:cd16292   25 TIMLDCGIHPGYSGLA---------SLPFF-DE------------IDLSEIDLLLITHFHLDHCGALPYFLQKT 76
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 52-122 2.41e-05

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: 43.79  E-value: 2.41e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545090032  52 VFIDHPDAKILFDtaCNPNAMGengrwisatqkafpyfadeschlpnRLEQIGVDPKEVDFVVASHLHLDH 122
Cdd:cd16272   20 YLLETGGTRILLD--CGEGTVY-------------------------RLLKAGVDPDKLDAIFLSHFHLDH 63
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 52-191 3.30e-05

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: 44.08  E-value: 3.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  52 VFIDHPDAK-ILFDTacnpnamGENGRWISATQKAFPYfadeschlpnrLEQIGVDpkEVDFVVASHLHLDHAGCL---- 126
Cdd:COG2333   14 ILIRTPDGKtILIDT-------GPRPSFDAGERVVLPY-----------LRALGIR--RLDLLVLTHPDADHIGGLaavl 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032 127 EYFTNATIIV----HDDELSGAMKTYARNQQAGAYIWADIDAWIKSNLTWR-------TVSKEDDN-----LKLV-EGVR 189
Cdd:COG2333   74 EAFPVGRVLVsgppDTSETYERLLEALKEKGIPVRPCRAGDTWQLGGVRFEvlwppedLLEGSDENnnslvLRLTyGGFS 153


                 ..
gi 545090032 190 VL 191
Cdd:COG2333  154 FL 155
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 100-265 5.17e-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: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 43.32  E-value: 5.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032 100 LEQI-GVDPKEVDFVVASHLHLDHAGCLEYFTN--ATIIVHDDELSgAMKTYARNQQAGAYIWADiDAWIKSNLTW--RT 174
Cdd:cd16282   42 LAAIrKVTDKPVRYVVNTHYHGDHTLGNAAFADagAPIIAHENTRE-ELAARGEAYLELMRRLGG-DAMAGTELVLpdRT 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032 175 VSkEDDNLKLveG---VRVLNYGSGHAWGLIGLEIESSElgtIILASDAIYTKesmGTPFKPPGilyDSIGWTKSVEKIK 251
Cdd:cd16282  120 FD-DGLTLDL--GgrtVELIHLGPAHTPGDLVVWLPEEG---VLFAGDLVFNG---RIPFLPDG---SLAGWIAALDRLL 187

                        170
                 ....*....|....
gi 545090032 252 KLADEknaQIWFGH 265
Cdd:cd16282  188 ALDAT---VVVPGH 198
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 101-208 1.29e-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: 42.06  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032 101 EQIGVDPKEVDFVVASHLHLDHAGCL-----EYF------TNATIivhddELSGAM-KTYARNQQAGA--------YIWA 160
Cdd:cd16295   43 EPFPFDPKEIDAVILTHAHLDHSGRLpllvkEGFrgpiyaTPATK-----DLAELLlLDSAKIQEEEAehppaeplYTEE 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 545090032 161 DIDAWIKSnltWRTVsKEDDNLKLVEGVRVLNYGSGH----AWglIGLEIES 208
Cdd:cd16295  118 DVEKALKH---FRPV-EYGEPFEIGPGVKVTFYDAGHilgsAS--VELEIGG 163
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 52-191 1.35e-04

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: 41.74  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  52 VFIDHPDAKILFDTAcnpnamgenGRWISATQKAFPYfadeschlpnrLEQIGVdpKEVDFVVASHLHLDHAG----CLE 127
Cdd:cd07731   13 ILIQTPGKTILIDTG---------PRDSFGEDVVVPY-----------LKARGI--KKLDYLILTHPDADHIGgldaVLK 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545090032 128 YFTNATIIV----HDDELSGAMKTYARNQQAGAYIWADIDAWIKSNLTWRTVS-----KEDDN-----LKLV-EGVRVL 191
Cdd:cd07731   71 NFPVKEVYMpgvtHTTKTYEDLLDAIKEKGIPVTPCKAGDRWQLGGVSFEVLSppkddYDDLNnnscvLRLTyGGTSFL 149
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 101-126 1.72e-04

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 42.48  E-value: 1.72e-04
                         10        20
                 ....*....|....*....|....*.
gi 545090032 101 EQIGVDPKEVDFVVASHLHLDHAGCL 126
Cdd:COG1236   42 PPFPFRPSDVDAVVLTHAHLDHSGAL 67
NorV COG0426
Flavorubredoxin [Energy production and conversion];
99-137 2.71e-04

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 41.74  E-value: 2.71e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 545090032  99 RLEQIgVDPKEVDFVVASHLHLDHAGCL----EYFTNATIIVH 137
Cdd:COG0426   61 NLSKV-IDPKKIDYIIVNHQEPDHSGSLpellELAPNAKIVCS 102
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
52-126 5.80e-04

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 40.56  E-value: 5.80e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545090032  52 VFIDHPDAKILFDtacnpnaMGEngrwisATQkafpyfadeschlpNRLEQIGVDPKEVDFVVASHLHLDHAGCL 126
Cdd:COG1234   22 YLLEAGGERLLID-------CGE------GTQ--------------RQLLRAGLDPRDIDAIFITHLHGDHIAGL 69
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 98-268 6.83e-04

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: 39.59  E-value: 6.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  98 NRLEQIGVDPKEVDFVVASHLHLDHAGCLEYFTNATIIVhddelsgamktyarnqqagAYIwadidawiksnLTWRTVsK 177
Cdd:cd07725   44 EGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGAT-------------------VYI-----------LDVTPV-K 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032 178 EDDNLKL-VEGVRVLnYGSGHAWGLIGLeieSSELGTIILASDAIYTKesmgtpFKPPGILYDSIG------WTKSVEKI 250
Cdd:cd07725   93 DGDKIDLgGLRLKVI-ETPGHTPGHIVL---YDEDRRELFVGDAVLPK------ITPNVSLWAVRVedplgaYLESLDKL 162

                        170
                 ....*....|....*...
gi 545090032 251 KKLADEKnaqIWFGHDGE 268
Cdd:cd07725  163 EKLDVDL---AYPGHGGP 177
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 99-129 8.17e-04

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: 39.55  E-value: 8.17e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 545090032  99 RLEQIGVDPKEVDFVVASHLHLDHAGCLEYF 129
Cdd:cd07740   39 ALKRAGIDPNAIDAIFITHLHGDHFGGLPFF 69
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 99-137 1.20e-03

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. 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. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 39.39  E-value: 1.20e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 545090032  99 RLEQIgVDPKEVDFVVASHLHLDHAGCL----EYFTNATIIVH 137
Cdd:cd07709   59 NLEEV-IDPRKIDYIVVNHQEPDHSGSLpellELAPNAKIVCS 100
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 100-219 1.73e-03

Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; CPSF3 (cleavage and polyadenylation specificity factor subunit 3; also known as cleavage and polyadenylation specificity factor 73 kDa subunit, CPSF-73) and CPSF2 (also known as cleavage and polyadenylation specificity factor 100 kDa subunit /CPSF-100) are components of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. CPSF3 functions as a 3' endonuclease. Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)), and Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74) are subunits of Integrator, a metazoan-specific multifunctional protein complex composed of 14 subunits. Integrator 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: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 38.47  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032 100 LEQIGVDPKEVDFVVASHLHLDHAGCLEYFTNATIIVHDDELSGAMKTYARNQQAGAYIWADIDAWIKSNLTWRTVSKED 179
Cdd:cd07734   40 LPQFELLPPEIDAILISHFHLDHCGALPYLFRGFIFRGPIYATHPTVALGRLLLEDYVKSAERIGQDQSLYTPEDIEEAL 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 545090032 180 DNLKLVE---------GVRVLNYGSGHAWGLIGLEIEsSELGTIILASD 219
Cdd:cd07734  120 KHIVPLGygqsidlfpALSLTAYNAGHVLGAAMWEIQ-IYGEKLVYTGD 167
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 60-130 2.12e-03

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: 38.40  E-value: 2.12e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545090032  60 KILFDtaCNPNaMGENgrwisaTQKAFPYFadeschlpNRLEQIGVDPKEVDFVVASHLHLDHAGCLEYFT 130
Cdd:cd16291   23 NIMFD--CGMH-MGYN------DERRFPDF--------SYISQNGPFTEHIDCVIISHFHLDHCGALPYFT 76
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 99-124 3.45e-03

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


Pssm-ID: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 37.94  E-value: 3.45e-03
                         10        20
                 ....*....|....*....|....*.
gi 545090032  99 RLEQIGVDPKEVDFVVASHLHLDHAG 124
Cdd:cd07741   43 RMCRPKLDPTKLDAIILSHRHLDHSN 68
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 52-128 3.87e-03

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: 37.59  E-value: 3.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545090032  52 VFIDHPDAKILFDtacnpnaMGENgrwISATQKAFPYFADESCHLPNR-LEQIGVDP-----------KEVDFVVASHLH 119
Cdd:cd07732   16 IEVETGGTRILLD-------FGLP---LDPESKYFDEVLDFLELGLLPdIVGLYRDPlllgglrseedPSVDAVLLSHAH 85


                 ....*....
gi 545090032 120 LDHAGCLEY 128
Cdd:cd07732   86 LDHYGLLNY 94
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 87-133 4.05e-03

Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of L1- and Pom-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: 293847  Cd Length: 239  Bit Score: 37.87  E-value: 4.05e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 545090032  87 PYFADescHLPNRLEQIGVDPKEVDFVVASHLHLDHAGCLEYFTNAT 133
Cdd:cd16289   41 PQAAD---MLLDNMRALGVAPGDLKLILHSHAHADHAGPLAALKRAT 84
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-126 5.47e-03

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: 37.33  E-value: 5.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545090032  49 IYTVFIDHPDAKILFDtacnpnamgengrwiSATQKAFPYFADEschlpnrLEQIGVDPKEVDFVVASHLHLDHAGCL 126
Cdd:cd16315   22 ISAILITGDDGHVLID---------------SGTEEAAPLVLAN-------IRKLGFDPKDVRWLLSSHEHFDHVGGL 77
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 99-122 6.35e-03

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: 36.73  E-value: 6.35e-03
                         10        20
                 ....*....|....*....|....
gi 545090032  99 RLEQIGVDPKEVDFVVASHLHLDH 122
Cdd:cd07719   41 RLAQAGLPLGDLDAVFLTHLHSDH 64
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 100-157 7.55e-03

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


Pssm-ID: 293846 [Multi-domain]  Cd Length: 254  Bit Score: 36.92  E-value: 7.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545090032 100 LEQIGVDPKEVDFVVASHLHLDHAGCLEYF---TNATIIVHDDE----LSGAMKTYARNQQAGAY 157
Cdd:cd16288   51 IRKLGFKPSDIKILLNSHAHLDHAGGLAALkklTGAKLMASAEDaallASGGKSDFHYGDDSLAF 115
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 52-129 8.67e-03

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: 36.09  E-value: 8.67e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545090032  52 VFIDHPDAKILFDTacnpnamgenGRWISATQKafpyfadeschlpnRLEQIGVDPKEVDFVVASHLHLDHAGCLEYF 129
Cdd:cd07733   12 TYLETEDGKLLIDA----------GLSGRKITG--------------RLAEIGRDPEDIDAILVTHEHADHIKGLGVL 65
 
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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