NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|489419388|ref|WP_003325150|]
View 

N-acyl homoserine lactonase AiiA [Bacillus atrophaeus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 5-238 1.21e-79

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: 239.42  E-value: 1.21e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388   5 KLYFLLAGSCYLDQSAVNKNLA-PGRLLEMPVWSFLLETTDGPILIDTGMPDAFVNNPEYfkgtkREGRVVPKMTANDKI 83
Cdd:cd07729    1 KLYALDYGTVTVDKSSLFYYGRgPGEPIDLPVYAYLIEHPEGTILVDTGFHPDAADDPGG-----LELAFPPGVTEEQTL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  84 VNILKSAGYRAGDIQAVISSHLHLDHAGGNGHFPKTPIFIQQAEFDAAMGND--------DYSPEECRLPDLQYQIIEGD 155
Cdd:cd07729   76 EEQLARLGLDPEDIDYVILSHLHFDHAGGLDLFPNATIIVQRAELEYATGPDplaagyyeDVLALDDDLPGGRVRLVDGD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 156 REVAPGVQIFSTPGHSPGHQSVLVTTEHsGPILLTIDVAYTRENFDNGVPF-LSYDSESTVRSIKRMKGLIEKVqPSKVF 234
Cdd:cd07729  156 YDLFPGVTLIPTPGHTPGHQSVLVRLPE-GTVLLAGDAAYTYENLEEGRPPgINYDPEAALASLERLKALAERE-GARVI 233


                 ....
gi 489419388 235 FGHD 238
Cdd:cd07729  234 PGHD 237
 
Name Accession Description Interval E-value
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 5-238 1.21e-79

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: 239.42  E-value: 1.21e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388   5 KLYFLLAGSCYLDQSAVNKNLA-PGRLLEMPVWSFLLETTDGPILIDTGMPDAFVNNPEYfkgtkREGRVVPKMTANDKI 83
Cdd:cd07729    1 KLYALDYGTVTVDKSSLFYYGRgPGEPIDLPVYAYLIEHPEGTILVDTGFHPDAADDPGG-----LELAFPPGVTEEQTL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  84 VNILKSAGYRAGDIQAVISSHLHLDHAGGNGHFPKTPIFIQQAEFDAAMGND--------DYSPEECRLPDLQYQIIEGD 155
Cdd:cd07729   76 EEQLARLGLDPEDIDYVILSHLHFDHAGGLDLFPNATIIVQRAELEYATGPDplaagyyeDVLALDDDLPGGRVRLVDGD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 156 REVAPGVQIFSTPGHSPGHQSVLVTTEHsGPILLTIDVAYTRENFDNGVPF-LSYDSESTVRSIKRMKGLIEKVqPSKVF 234
Cdd:cd07729  156 YDLFPGVTLIPTPGHTPGHQSVLVRLPE-GTVLLAGDAAYTYENLEEGRPPgINYDPEAALASLERLKALAERE-GARVI 233


                 ....
gi 489419388 235 FGHD 238
Cdd:cd07729  234 PGHD 237
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 26-245 4.70e-25

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: 98.61  E-value: 4.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  26 APGRLLEMPVWSFLLETTDGPILIDTGMPDAFVnnpeyfkgtkregrvvpkmtanDKIVNILKSAGyraGDIQAVISSHL 105
Cdd:COG0491    6 GGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADA----------------------EALLAALAALG---LDIKAVLLTHL 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 106 HLDHAGGNGHFPK---TPIFIQQAEFDAAMGNDDYSPEECRLPDLQYQIIEGDR-EVA-PGVQIFSTPGHSPGHQSVLVT 180
Cdd:COG0491   61 HPDHVGGLAALAEafgAPVYAHAAEAEALEAPAAGALFGREPVPPDRTLEDGDTlELGgPGLEVIHTPGHTPGHVSFYVP 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489419388 181 TEhsgPILLTIDVAYTRenfDNGVPFLSY-DSESTVRSIKRMKGLiekvQPSKVFFGHDRVQAREA 245
Cdd:COG0491  141 DE---KVLFTGDALFSG---GVGRPDLPDgDLAQWLASLERLLAL----PPDLVIPGHGPPTTAEA 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 37-237 4.34e-24

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: 94.93  E-value: 4.34e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388    37 SFLLETTDGPILIDTGMPDAfvnnpeyfkgtkregrvvpkmtanDKIVNILKSAGYRagDIQAVISSHLHLDHAGGNGHF 116
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEA------------------------EDLLAELKKLGPK--KIDAIILTHGHPDHIGGLPEL 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388   117 ---PKTPIFIQQAEFDAAMGNDDYSPEECRLPDLQYQII---EGDREV--APGVQIFSTPGHSPGHQSVLVtteHSGPIL 188
Cdd:smart00849  56 leaPGAPVYAPEGTAELLKDLLALLGELGAEAEPAPPDRtlkDGDELDlgGGELEVIHTPGHTPGSIVLYL---PEGKIL 132

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 489419388   189 LTIDVAYTRENFDNGVPFLSYDSESTVRSIKRMKGLIEKVqpskVFFGH 237
Cdd:smart00849 133 FTGDLLFAGGDGRTLVDGGDAAASDALESLLKLLKLLPKL----VVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
34-237 1.06e-18

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 81.26  E-value: 1.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388   34 PVWSFLLETTDGPILIDTGMPDAFvnnpeyfkgtkregrvvpkmtandKIVNILKSAGYRAGDIQAVISSHLHLDHAGGN 113
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTGGSAEA------------------------ALLLLLAALGLGPKDIDAVILTHGHFDHIGGL 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  114 GHFPKT---PIFIQQAEFDAAMGNDDYS--------PEECRLPDLQYQIIEGDREVAPGVQIFSTPGHSPGHQSVLVTTE 182
Cdd:pfam00753  61 GELAEAtdvPVIVVAEEARELLDEELGLaasrlglpGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYG 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489419388  183 hSGPILLTIDVAYTREN------FDNGVPFLSYDSESTVRSIKRMKGLiekvQPSKVFFGH 237
Cdd:pfam00753 141 -GGKVLFTGDLLFAGEIgrldlpLGGLLVLHPSSAESSLESLLKLAKL----KAAVIVPGH 196
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 86-238 9.16e-05

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 42.83  E-value: 9.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  86 ILKSAGYRAGDIQAVISSHLHLDHAGGNGHFPKTPIFIQQaeFDAAMGNddyspeecrLPDLQYQIIEGDR-EVAPGVQI 164
Cdd:PLN02469  36 VLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKV--YGGSLDN---------VKGCTHPVENGDKlSLGKDVNI 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489419388 165 FS--TPGHSPGHQSVLVT-TEHSGPILLTIDVAYTR--ENFDNGVPFLSYDSEStvrsikrmKGLIEKVQPSKVFFGHD 238
Cdd:PLN02469 105 LAlhTPCHTKGHISYYVTgKEGEDPAVFTGDTLFIAgcGKFFEGTAEQMYQSLC--------VTLGSLPKPTQVYCGHE 175
 
Name Accession Description Interval E-value
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 5-238 1.21e-79

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: 239.42  E-value: 1.21e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388   5 KLYFLLAGSCYLDQSAVNKNLA-PGRLLEMPVWSFLLETTDGPILIDTGMPDAFVNNPEYfkgtkREGRVVPKMTANDKI 83
Cdd:cd07729    1 KLYALDYGTVTVDKSSLFYYGRgPGEPIDLPVYAYLIEHPEGTILVDTGFHPDAADDPGG-----LELAFPPGVTEEQTL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  84 VNILKSAGYRAGDIQAVISSHLHLDHAGGNGHFPKTPIFIQQAEFDAAMGND--------DYSPEECRLPDLQYQIIEGD 155
Cdd:cd07729   76 EEQLARLGLDPEDIDYVILSHLHFDHAGGLDLFPNATIIVQRAELEYATGPDplaagyyeDVLALDDDLPGGRVRLVDGD 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 156 REVAPGVQIFSTPGHSPGHQSVLVTTEHsGPILLTIDVAYTRENFDNGVPF-LSYDSESTVRSIKRMKGLIEKVqPSKVF 234
Cdd:cd07729  156 YDLFPGVTLIPTPGHTPGHQSVLVRLPE-GTVLLAGDAAYTYENLEEGRPPgINYDPEAALASLERLKALAERE-GARVI 233


                 ....
gi 489419388 235 FGHD 238
Cdd:cd07729  234 PGHD 237
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 12-224 2.28e-29

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: 110.82  E-value: 2.28e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  12 GSCYLDQSAVNKNlAPGRLLEMPVWSFLLE-TTDGPILIDTGMPDAFVNNPEyfKGTKREGRVVPKMTANDKIVNILKSA 90
Cdd:cd07730    1 GSCTLPERLVLRG-GPLKRVTFPALAFLIEhPTGGKILFDLGYRKDFEEYTP--RVPERLYRTPVPLEVEEDVAEQLAAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  91 GYRAGDIQAVISSHLHLDHAGGNGHFPKTPIFIQQAEFDAAMGN------------DDYSPEEcrlpDLQYQIIEGDREV 158
Cdd:cd07730   78 GIDPEDIDAVILSHLHWDHIGGLSDFPNARLIVGPGAKEALRPPgypsgflpellpSDFEGRL----VRWEEDDFLWVPL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 159 APGVQ-----------IFSTPGHSPGHQSVLVTTEHSGPILLTIDVAYTRENFDNGVPFL-------SYDSESTVRSIKR 220
Cdd:cd07730  154 GPFPRaldlfgdgslyLVDLPGHAPGHLGLLARTTSGTWVFLAGDACHHRIGLLRPSPLLplpdlddGADREAARETLAR 233


                 ....
gi 489419388 221 MKGL 224
Cdd:cd07730  234 LREL 237
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 39-221 9.62e-27

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: 102.28  E-value: 9.62e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  39 LLETTDGPILIDTGMPdafvnnpeyfkgtkrEGRvvpkmtanDKIVNILKSAGYRAGDIQAVISSHLHLDHAGGNGHFPK 118
Cdd:cd07711   26 LIKDGGKNILVDTGTP---------------WDR--------DLLLKALAEHGLSPEDIDYVVLTHGHPDHIGNLNLFPN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 119 TPIFIQQAEFDAAMGNDDYSPEEcrlpdlqyqiiegDREVAPGVQIFSTPGHSPGHQSVLVTTEHSGPILLTIDVAYTRE 198
Cdd:cd07711   83 ATVIVGWDICGDSYDDHSLEEGD-------------GYEIDENVEVIPTPGHTPEDVSVLVETEKKGTVAVAGDLFEREE 149

                        170       180
                 ....*....|....*....|....*
gi 489419388 199 NFDNGV--PFLSYDSESTVRSIKRM 221
Cdd:cd07711  150 DLEDPIlwDPLSEDPELQEESRKRI 174
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 26-245 4.70e-25

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: 98.61  E-value: 4.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  26 APGRLLEMPVWSFLLETTDGPILIDTGMPDAFVnnpeyfkgtkregrvvpkmtanDKIVNILKSAGyraGDIQAVISSHL 105
Cdd:COG0491    6 GGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADA----------------------EALLAALAALG---LDIKAVLLTHL 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 106 HLDHAGGNGHFPK---TPIFIQQAEFDAAMGNDDYSPEECRLPDLQYQIIEGDR-EVA-PGVQIFSTPGHSPGHQSVLVT 180
Cdd:COG0491   61 HPDHVGGLAALAEafgAPVYAHAAEAEALEAPAAGALFGREPVPPDRTLEDGDTlELGgPGLEVIHTPGHTPGHVSFYVP 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489419388 181 TEhsgPILLTIDVAYTRenfDNGVPFLSY-DSESTVRSIKRMKGLiekvQPSKVFFGHDRVQAREA 245
Cdd:COG0491  141 DE---KVLFTGDALFSG---GVGRPDLPDgDLAQWLASLERLLAL----PPDLVIPGHGPPTTAEA 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 37-237 4.34e-24

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: 94.93  E-value: 4.34e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388    37 SFLLETTDGPILIDTGMPDAfvnnpeyfkgtkregrvvpkmtanDKIVNILKSAGYRagDIQAVISSHLHLDHAGGNGHF 116
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEA------------------------EDLLAELKKLGPK--KIDAIILTHGHPDHIGGLPEL 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388   117 ---PKTPIFIQQAEFDAAMGNDDYSPEECRLPDLQYQII---EGDREV--APGVQIFSTPGHSPGHQSVLVtteHSGPIL 188
Cdd:smart00849  56 leaPGAPVYAPEGTAELLKDLLALLGELGAEAEPAPPDRtlkDGDELDlgGGELEVIHTPGHTPGSIVLYL---PEGKIL 132

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 489419388   189 LTIDVAYTRENFDNGVPFLSYDSESTVRSIKRMKGLIEKVqpskVFFGH 237
Cdd:smart00849 133 FTGDLLFAGGDGRTLVDGGDAAASDALESLLKLLKLLPKL----VVPGH 177
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 31-237 6.32e-24

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: 94.98  E-value: 6.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  31 LEMPVWSFLLETTDGPILIDTGMPDAFvnnpeyfkgtkregrvvpkmtanDKIVNILKSAGYRAGDIQAVISSHLHLDHA 110
Cdd:cd07721    7 LLPPVNAYLIEDDDGLTLIDTGLPGSA-----------------------KRILKALRELGLSPKDIRRILLTHGHIDHI 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 111 GGNGHF---PKTPIFIQQAEFDAAMGNDDY---------------SPEECRLPDLQYQiiEGDR-EVAPGVQIFSTPGHS 171
Cdd:cd07721   64 GSLAALkeaPGAPVYAHEREAPYLEGEKPYpppvrlgllgllsplLPVKPVPVDRTLE--DGDTlDLAGGLRVIHTPGHT 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489419388 172 PGHQSVLVttEHSGpILLTIDVAYTRE-NFDNGVPFLSYDSESTVRSIKRMKGLiekvQPSKVFFGH 237
Cdd:cd07721  142 PGHISLYL--EEDG-VLIAGDALVTVGgELVPPPPPFTWDMEEALESLRKLAEL----DPEVLAPGH 201
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 31-180 1.67e-23

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: 95.31  E-value: 1.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  31 LEMPVWSFLLETTDGPILIDTGMPDAFvnnpeyfkgtkreGRVVPKMTANdkivniLKSAGYRAGDIQAVISSHLHLDHA 110
Cdd:cd07720   45 VETSVNAFLVRTGGRLILVDTGAGGLF-------------GPTAGKLLAN------LAAAGIDPEDIDDVLLTHLHPDHI 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 111 GG------NGHFPKTPIFIQQAEFDA--AMGNDDYSPEECRLPDLQYQ----------IIEGDREVAPGVQIFSTPGHSP 172
Cdd:cd07720  106 GGlvdaggKPVFPNAEVHVSEAEWDFwlDDANAAKAPEGAKRFFDAARdrlrpyaaagRFEDGDEVLPGITAVPAPGHTP 185


                 ....*...
gi 489419388 173 GHQSVLVT 180
Cdd:cd07720  186 GHTGYRIE 193
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 29-183 2.73e-19

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: 83.34  E-value: 2.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  29 RLLEMpVWSFLLETTDGPILIDTGM-PDAFVNNPEYFkgtkregrvvpkMTANDKIVNILKSAGYRAGDIQAVISSHLHL 107
Cdd:cd16277    8 RIVEL-IHSWLVRTPGRTILVDTGIgNDKPRPGPPAF------------HNLNTPYLERLAAAGVRPEDVDYVLCTHLHV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 108 DHAGGNGH---------FPKTPIFIQQAEFDAAMGNDDYSP------EECRLPDL---QYQIIEGDREVAPGVQIFSTPG 169
Cdd:cd16277   75 DHVGWNTRlvdgrwvptFPNARYLFSRAEYDHWSSPDAGGPpnrgvfEDSVLPVIeagLADLVDDDHEILDGIRLEPTPG 154

                        170
                 ....*....|....
gi 489419388 170 HSPGHQSVLVTTEH 183
Cdd:cd16277  155 HTPGHVSVELESGG 168
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
34-237 1.06e-18

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 81.26  E-value: 1.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388   34 PVWSFLLETTDGPILIDTGMPDAFvnnpeyfkgtkregrvvpkmtandKIVNILKSAGYRAGDIQAVISSHLHLDHAGGN 113
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTGGSAEA------------------------ALLLLLAALGLGPKDIDAVILTHGHFDHIGGL 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  114 GHFPKT---PIFIQQAEFDAAMGNDDYS--------PEECRLPDLQYQIIEGDREVAPGVQIFSTPGHSPGHQSVLVTTE 182
Cdd:pfam00753  61 GELAEAtdvPVIVVAEEARELLDEELGLaasrlglpGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYG 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489419388  183 hSGPILLTIDVAYTREN------FDNGVPFLSYDSESTVRSIKRMKGLiekvQPSKVFFGH 237
Cdd:pfam00753 141 -GGKVLFTGDLLFAGEIgrldlpLGGLLVLHPSSAESSLESLLKLAKL----KAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 37-237 4.52e-17

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: 76.56  E-value: 4.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  37 SFLLETTDGP-ILIDTGMPdafvnnpeyfkgtkregrvvpkmtANDKIVNILKSAGYragDIQAVISSHLHLDHAGGNGH 115
Cdd:cd06262   12 CYLVSDEEGEaILIDPGAG------------------------ALEKILEAIEELGL---KIKAILLTHGHFDHIGGLAE 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 116 F---PKTPIFIQQAE---FDAAMGNDDYSPEECRLPDLQYQIIEGDREVAPG---VQIFSTPGHSPGHQSVLVTTEHsgp 186
Cdd:cd06262   65 LkeaPGAPVYIHEADaelLEDPELNLAFFGGGPLPPPEPDILLEDGDTIELGgleLEVIHTPGHTPGSVCFYIEEEG--- 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489419388 187 ILLTIDVAytrenFDNGV---PFLSYDSESTVRSIKR-MKGLIEKVqpsKVFFGH 237
Cdd:cd06262  142 VLFTGDTL-----FAGSIgrtDLPGGDPEQLIESIKKlLLLLPDDT---VVYPGH 188
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 27-195 3.79e-16

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 75.35  E-value: 3.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  27 PGRLLEMPVWSFLLETTDGPILIDTGMPDAFVNNPEyfkgtKREG---------RVVPKMTAndkiVNILKSAGYRAGDI 97
Cdd:cd07742   11 PGGDLRLVCHCLLVETDDGLVLVDTGFGLADVADPK-----RRLGgpfrrllrpRLDEDETA----VRQIEALGFDPSDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  98 QAVISSHLHLDHAGGNGHFPKTPIFIQQAEFDAAM-GNDDYSPEECRL------PDLQYQIIEGDR----EVAPGVQIFS 166
Cdd:cd07742   82 RHIVLTHLDLDHAGGLADFPHATVHVHAAELDAATsPRTRYERRRYRPqqlahgPWWVTYAAGGERwfgfEAVRPLDGLP 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489419388 167 T-------PGHSPGHQSVLVTTEHSGpiLLTIDVAY 195
Cdd:cd07742  162 PeillvplPGHTRGHCGVAVRTGDRW--LLHAGDAY 195
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 37-237 3.89e-15

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: 71.75  E-value: 3.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  37 SFLLETTDGPILIDTGmpdafvnnpeyfkgtkregrvvPKMTAnDKIVNILKSAGYRAGDIQAVISSHLHLDHAGGNG-- 114
Cdd:cd07726   18 SYLLDGEGRPALIDTG----------------------PSSSV-PRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGll 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 115 --HFPKTPIF---------------IQQAEfdAAMGNDDYS--------PEEcRL--PDLQYQIIEGDREvapgVQIFST 167
Cdd:cd07726   75 aeALPNAKVYvhprgarhlidpsklWASAR--AVYGDEADRlggeilpvPEE-RVivLEDGETLDLGGRT----LEVIDT 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489419388 168 PGHSPGHQSVLVttEHSGpILLTIDVA--YTRENFDNGVPFLS---YDSESTVRSIKRMKGLiekvQPSKVFFGH 237
Cdd:cd07726  148 PGHAPHHLSFLD--EESD-GLFTGDAAgvRYPELDVVGPPSTPppdFDPEAWLESLDRLLSL----KPERIYLTH 215
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 39-190 9.98e-14

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: 68.44  E-value: 9.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  39 LLETTDGPILIDTGMpdafvNNPEYFKGTKREGRVvpkmTANDKIVNILKSAGYRAGDIQAVISSHLHLDHAGG-----N 113
Cdd:cd07728   47 LIQYQGKNYLIDAGI-----GNGKLTEKQKRNFGV----TEESSIEESLAELGLTPEDIDYVLMTHLHFDHASGltkvkG 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 114 GH----FPKTPIFIQQAEFDaAMGNDD----YSPEECRLPDLQYQII--EGDREVAPGVQIFSTPGHSPGHQSVLVTTE- 182
Cdd:cd07728  118 EQlvsvFPNATIYVSEIEWE-EMRNPNirskNTYWKENWEPIEDQVKtfSDEIEIVPGITMIHTGGHSDGHSIIEIEQGg 196

                        170
                 ....*....|..
gi 489419388 183 ----HSGPILLT 190
Cdd:cd07728  197 etaiHMADLMPT 208
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 4-193 3.08e-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.


Pssm-ID: 293839  Cd Length: 252  Bit Score: 64.44  E-value: 3.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388   4 KKLYFLLAGSCYLDQSAV---------NK-------NLAPgrlLEMPVWsfLLETTDGPILIDTGMPDAFvnNPEYFKGT 67
Cdd:cd16281    1 MQLHSIEGGYFKLDGGAMfgvvpkplwQKwypadedNRIT---LAMRCL--LIETGGRNILIDTGIGDKQ--DPKFRSIY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  68 KREGRVVpkmtandkIVNILKSAGYRAGDIQAVISSHLHLDHAGG-----NGH-----FPKTPIFIQQAEFDAAMgN--- 134
Cdd:cd16281   74 VQHSEHS--------LLKSLARLGLSPEDITDVILTHLHFDHCGGatradDDGlvellFPNATYWVQKRHWEWAL-Npnp 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 135 ---DDYSPE-------ECRLpdlqyQIIEG-DREVAPGVQIFSTPGHSPGHQSVLVTTEHsGPILLTIDV 193
Cdd:cd16281  145 rerASFLPEniepleeSGRL-----KLIDGsDAELGPGIRFHLSDGHTPGQMLPEISTPG-GTVVFAADL 208
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 30-237 3.95e-12

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: 63.03  E-value: 3.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  30 LLEMPVWSFLLETTDGPILIDTGMPDafVNNPEYfkgtkregrvVPKMTanDKIVnilksagyragdiqAVISSHLHLDH 109
Cdd:cd07712    4 EEDDRVNIYLLRGRDRALLIDTGLGI--GDLKEY----------VRTLT--DLPL--------------LVVATHGHFDH 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 110 AGGNGHFPKtpIFIQQAEFDAAMGNDDYSPEECR------------LPDLQYQIIE-GDREvapgVQIFSTPGHSPGHQS 176
Cdd:cd07712   56 IGGLHEFEE--VYVHPADAEILAAPDNFETLTWDaatysvppagptLPLRDGDVIDlGDRQ----LEVIHTPGHTPGSIA 129

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489419388 177 VLvttEHSGPILLTIDVAYTRENFDNGVpflSYDSESTVRSIKRMKGLieKVQPSKVFFGH 237
Cdd:cd07712  130 LL---DRANRLLFSGDVVYDGPLIMDLP---HSDLDDYLASLEKLSKL--PDEFDKVLPGH 182
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-173 1.76e-11

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: 62.22  E-value: 1.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  35 VWSFLLETTDGPILIDTGmpdafvNNPEyfkgtkregrvvpkmtANDKIVNILKSAGYRAGDIQAVISSHLHLDHAGGNG 114
Cdd:cd16280   22 VSAWAIDTGDGLILIDAL------NNNE----------------AADLIVDGLEKLGLDPADIKYILITHGHGDHYGGAA 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489419388 115 HF---PKTPIFIQQAEFDaAMGNDDYSPEECRLPDLqyqiIEGDREVAPG---------VQIFSTPGHSPG 173
Cdd:cd16280   80 YLkdlYGAKVVMSEADWD-MMEEPPEEGDNPRWGPP----PERDIVIKDGdtltlgdttITVYLTPGHTPG 145
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-185 2.56e-10

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: 58.87  E-value: 2.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  37 SFLLETTDGPILIDTGMPDAfvnnpeyfkgtkregrvVPKMTANdkivniLKSAGYRAGDIQAVISSHLHLDHAGGNGHF 116
Cdd:cd16288   24 SYLITTPQGLILIDTGLESS-----------------APMIKAN------IRKLGFKPSDIKILLNSHAHLDHAGGLAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 117 PK-TPIFIQQAEFDAAM----GNDDYSPEEcrlPDLQYQIIEGDREVAPGVQI---------FSTPGHSPGHQSVLVTTE 182
Cdd:cd16288   81 KKlTGAKLMASAEDAALlasgGKSDFHYGD---DSLAFPPVKVDRVLKDGDRVtlggttltaHLTPGHTRGCTTWTMTVK 157


                 ...
gi 489419388 183 HSG 185
Cdd:cd16288  158 DDG 160
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 39-176 6.41e-10

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: 57.74  E-value: 6.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  39 LLETTDGPILIDTGMPDAfvnnpeyfkgtkregrvVPKMTANdkivniLKSAGYRAGDIQAVISSHLHLDHAGGNGHfpk 118
Cdd:cd16315   26 LITGDDGHVLIDSGTEEA-----------------APLVLAN------IRKLGFDPKDVRWLLSSHEHFDHVGGLAA--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 119 tpifIQQ---------AEFDAAMGNDDYSPEecrlpDLQYQIIEG------DREVAPGVQI---------FSTPGHSPGH 174
Cdd:cd16315   80 ----LQRatgarvaasAAAAPVLESGKPAPD-----DPQAGLHEPfppvrvDRIVEDGDTValgslrltaHATPGHTPGA 150


                 ..
gi 489419388 175 QS 176
Cdd:cd16315  151 LS 152
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-173 8.14e-10

Bradyrhizobium diazoefficiens BJP-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 BJP-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: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 57.49  E-value: 8.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  37 SFLLETTDGPILIDTGMPDAfvnnpeyfkgtkregrvVPKMTANdkivniLKSAGYRAGDIQAVISSHLHLDHAGGNGHF 116
Cdd:cd16309   24 VFLITTPEGHILIDGAMPQS-----------------TPLIKDN------IKKLGFDVKDVKYLLNTHAHFDHAGGLAEL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 117 PK-TPIFIQQAEFDAAM---GNDDYSPEEcrlpDLQYQIIEGDREVAPGVQI---------FSTPGHSPG 173
Cdd:cd16309   81 KKaTGAQLVASAADKPLlesGYVGSGDTK----NLQFPPVRVDRVIGDGDKVtlggttltaHLTPGHSPG 146
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-176 8.63e-10

Janthinobacterium lividum THIN-B2 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 THIN-B2-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: 293869  Cd Length: 257  Bit Score: 57.69  E-value: 8.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  37 SFLLETTDGPILIDTGMPDAfvnnpeyfkgtkregrvVPKMTANdkivniLKSAGYRAGDIQAVISSHLHLDHAGGNGHF 116
Cdd:cd16311   24 SVLVTSPQGHVLVDGGLPES-----------------APKIIAN------IEALGFRIEDVKLILNSHGHIDHAGGLAEL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489419388 117 PKTPIFIQQAEFDAAM-------GNDD----YSPEECRLPDLQYQIIEGDREVAP-GVQIFSTPGHSPGHQS 176
Cdd:cd16311   81 QRRSGALVAASPSAALdlasgevGPDDpqyhALPKYPPVKDMRLARDGGQFNVGPvSLTAHATPGHTPGGLS 152
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 81-174 4.95e-09

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: 54.00  E-value: 4.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  81 DKIVNILKSAGYRagdIQAVISSHLHLDHAGGNG----HFPKTPIfiqqaefdaamgnddYSPEECRLPDLQYQIIEGDr 156
Cdd:cd07723   31 EPVLAALEKNGLT---LTAILTTHHHWDHTGGNAelkaLFPDAPV---------------YGPAEDRIPGLDHPVKDGD- 91

                         90       100
                 ....*....|....*....|.
gi 489419388 157 EVAPG---VQIFSTPGHSPGH 174
Cdd:cd07723   92 EIKLGgleVKVLHTPGHTLGH 112
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 36-166 5.32e-08

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: 52.24  E-value: 5.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  36 WSFLLETTDGPILIDTGMPDAFVNNpeyfkgtkregrvvpkmtandkivniLKSAGYRAGDIQAVISSHLHLDHAGG--- 112
Cdd:cd07713   21 LSLLIETEGKKILFDTGQSGVLLHN--------------------------AKKLGIDLSDIDAVVLSHGHYDHTGGlka 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489419388 113 -NGHFPKTPIFIQQAEF-------DAAMGNDDYSPEECRLPDLQYQIIEGDREVAPGVQIFS 166
Cdd:cd07713   75 lLELNPKAPVYAHPDAFepryskrGGGKKGIGIGREELEKAGARLVLVEEPTEIAPGVYLTG 136
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 37-173 1.24e-07

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: 51.01  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  37 SFLLETTDGPILIDTGMPdafvnnpeyfkgtkregRVVPKMTANdkivniLKSAGYRAGDIQAVISSHLHLDHAGGNGHF 116
Cdd:cd07708   24 AYLIVTPQGNILIDGDME-----------------QNAPMIKAN------IKKLGFKFSDTKLILISHAHFDHAGGSAEI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 117 PK-TPIFIQQAEFDA---AMGNDDYSPEEcRLPDLQYQIIEGDREVAPG---------VQIFSTPGHSPG 173
Cdd:cd07708   81 KKqTGAKVMAGAEDVsllLSGGSSDFHYA-NDSSTYFPQSTVDRAVHDGervtlggtvLTAHATPGHTPG 149
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 47-224 3.50e-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) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 49.07  E-value: 3.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  47 ILIDTGMPDafvnnpeyfkgtkregrvvpkmTANDKIVNILKSAGYRagdIQAVISSHLHLDHAGGNGHFPKTP------ 120
Cdd:cd07743   21 LLIDSGLDE----------------------DAGRKIRKILEELGWK---LKAIINTHSHADHIGGNAYLQKKTgckvya 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 121 -----IFIQQAEFDAAMGNDDYSPEECRLPDLQYQIIEGDREVAPG--------VQIFSTPGHSPGHQSVLVTTEhsgpI 187
Cdd:cd07743   76 pkiekAFIENPLLEPSYLGGAYPPKELRNKFLMAKPSKVDDIIEEGelelggvgLEIIPLPGHSFGQIGILTPDG----V 151

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 489419388 188 LLTIDVAYTRENFDN-GVPFLsYDSESTVRSIKRMKGL 224
Cdd:cd07743  152 LFAGDALFGEEVLEKyGIPFL-YDVEEQLETLEKLEEL 188
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-176 5.79e-07

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: 49.12  E-value: 5.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  37 SFLLETTD-GPILIDTGMPDAfvnnpeyfkgtkregrvVPKMTANdkivniLKSAGYRAGDIQAVISSHLHLDHAGGNGH 115
Cdd:cd16314   23 SALLVTSDaGHILIDGGTDKA-----------------APLIEAN------IRALGFRPEDVRYIVSSHEHFDHAGGIAR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 116 FPK---TPIFIQQAEFDA-AMGNDDYSpeecrlpDLQYQIIEgdrEVAP--GVQIF----------------STPGHSPG 173
Cdd:cd16314   80 LQRatgAPVVAREPAATTlERGRSDRS-------DPQFLVVE---KFPPvaSVQRIgdgevlrvgplaltahATPGHTPG 149


                 ...
gi 489419388 174 HQS 176
Cdd:cd16314  150 GTS 152
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 37-174 1.64e-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: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  37 SFLLETTDGPILIDTGMPdafvnnpeyfkgTKREGRVVpkmtandkiVNILKSAGYRAGDIQAVISSHLHLDHAGGNGHF 116
Cdd:cd07725   17 VYLLRDGDETTLIDTGLA------------TEEDAEAL---------WEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKL 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489419388 117 pktpifiqQAEFDAamgnDDYSPEECRLPDLQyQIIEGDREvapgVQIFSTPGHSPGH 174
Cdd:cd07725   76 --------QEKSGA----TVYILDVTPVKDGD-KIDLGGLR----LKVIETPGHTPGH 116
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 37-130 2.73e-06

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: 46.10  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  37 SFLLETTDGPILIDTGMPdafvnnpeyfkgtkreGRvvpkmtandKIVNILKSAGYRAGDIQAVISSHLHLDHAGGNGHF 116
Cdd:cd07733   11 CTYLETEDGKLLIDAGLS----------------GR---------KITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVL 65

                         90
                 ....*....|....*..
gi 489419388 117 P---KTPIFIQQAEFDA 130
Cdd:cd07733   66 ArkyNVPIYATAGTLRA 82
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 81-220 4.69e-06

Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Salmonella enterica serovar typhimurium YcbL which has type II hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as glyoxalase II) activity, and has a single metal ion binding site, and Thermus thermophilus TTHA1623 which does not have GLX2 activity and has two metal ion binding sites with a glyoxalase II-type metal coordination. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 46.01  E-value: 4.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  81 DKIVNILKSAGYRagdIQAVISSHLHLDHAGGNGHFPKT---PIF---------IQQAEFDAAMGNddYSPEECRLPD-- 146
Cdd:cd07737   34 DKILQAIEDLGLT---LKKILLTHGHLDHVGGAAELAEHygvPIIgphkedkflLENLPEQSQMFG--FPPAEAFTPDrw 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 147 LQyqiiEGDrEVAPG---VQIFSTPGHSPGHqsvLVTTEHSGPILLTIDVAytrenFDNGV---PFLSYDSESTVRSIKR 220
Cdd:cd07737  109 LE----EGD-TVTVGnltLEVLHCPGHTPGH---VVFFNRESKLAIVGDVL-----FKGSIgrtDFPGGNHAQLIASIKE 175
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 97-237 7.66e-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) 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: 45.63  E-value: 7.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  97 IQAVISSHLHLDHAGGNGHFP--KTPIF-------------IQQAEFDAAMGNDDYSPEECRLPDL----QYQIIEGDRE 157
Cdd:cd16282   53 VRYVVNTHYHGDHTLGNAAFAdaGAPIIahentreelaargEAYLELMRRLGGDAMAGTELVLPDRtfddGLTLDLGGRT 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 158 V---APGvqifstPGHSPGHQSVLVTTEHsgpILLTIDVAytrenFDNGVPFLSY-DSESTVRSIKRMKGLIEKVqpskV 233
Cdd:cd16282  133 VeliHLG------PAHTPGDLVVWLPEEG---VLFAGDLV-----FNGRIPFLPDgSLAGWIAALDRLLALDATV----V 194


                 ....
gi 489419388 234 FFGH 237
Cdd:cd16282  195 VPGH 198
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 37-112 1.67e-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: 44.05  E-value: 1.67e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489419388  37 SFLLETTDGPILIDTGMPDAFvnnpeyfkgtkregrvvpkmtANDKIVNILKSAGYRagDIQAVISSHLHLDHAGG 112
Cdd:cd07731   12 AILIQTPGKTILIDTGPRDSF---------------------GEDVVVPYLKARGIK--KLDYLILTHPDADHIGG 64
AIM-1_SMB-1-like_MBL-B3 cd16290
AIM-1, SMB-1, EVM-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-112 3.61e-05

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


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 43.88  E-value: 3.61e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489419388  37 SFLLETTDGPILIDTGMPDAfvnnpeyfkgtkregrvVPKMTANdkivniLKSAGYRAGDIQAVISSHLHLDHAGG 112
Cdd:cd16290   24 AVLITSPQGLILIDGALPQS-----------------APQIEAN------IRALGFRLEDVKLILNSHAHFDHAGG 76
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 39-195 4.61e-05

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: 43.27  E-value: 4.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  39 LLETTDGPILIDTGMPDAfvnnpeyfkgtkregrvvpkmtaNDKIVNILKSAGYRAGDIQAVISSHLHLDHAGGNGHFPK 118
Cdd:cd16289   26 LVKTPDGAVLLDGGMPQA-----------------------ADMLLDNMRALGVAPGDLKLILHSHAHADHAGPLAALKR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 119 TPIFIQQAEFDAAM-----GNDDYSPEEcrlpDLQYQIIEGDREVAPGVQI------FS---TPGHSPGHQSVLVTTEHS 184
Cdd:cd16289   83 ATGARVAANAESAVllargGSDDIHFGD----GITFPPVQADRIVMDGEVVtlggvtFTahfTPGHTPGSTSWTWTDTRD 158

                        170
                 ....*....|.
gi 489419388 185 GPillTIDVAY 195
Cdd:cd16289  159 GK---PVRIAY 166
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 37-112 5.01e-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: 43.31  E-value: 5.01e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489419388  37 SFLLETTDGP-ILIDTGMPDAFvnnpeyfkgtkregrvvpkMTANDKIVNILKSAGYRagDIQAVISSHLHLDHAGG 112
Cdd:COG2333   13 AILIRTPDGKtILIDTGPRPSF-------------------DAGERVVLPYLRALGIR--RLDLLVLTHPDADHIGG 68
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 86-237 5.04e-05

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: 43.11  E-value: 5.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  86 ILKSAGYRAGDIQAVISSHLHLDHAGGNGHFPKTPifiqQAEFdaAMGNDDysPEECRLPDLQYQI--------IEGDRE 157
Cdd:cd16322   36 LLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHP----GAPV--YLHPDD--LPLYEAADLGAKAfglgieplPPPDRL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 158 VAPG---------VQIFSTPGHSPGHQSVLVtteHSGPILLTIDVAYT----RENFDNGVPFLSYdsestvRSIKRmkgL 224
Cdd:cd16322  108 LEDGqtltlggleFKVLHTPGHSPGHVCFYV---EEEGLLFSGDLLFQgsigRTDLPGGDPKAMA------ASLRR---L 175

                        170
                 ....*....|...
gi 489419388 225 IEKVQPSKVFFGH 237
Cdd:cd16322  176 LTLPDETRVFPGH 188
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 37-181 5.67e-05

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


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 43.23  E-value: 5.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  37 SFLLETTDGPILIDTGMPDAfvnnpeyfkgtkregrvVPKMTANdkivniLKSAGYRAGDIQAVISSHLHLDHAGGNGHF 116
Cdd:cd16308   24 CYLIVTPKGNILINTGLAES-----------------VPLIKKN------IQALGFKFKDIKILLTTQAHYDHVGAMAAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 117 PKTP---IFIQQAefDAAM----GNDDYspeECRLPDLQYQIIEGDREVAPG---------VQIFSTPGHSPGHQSVLVT 180
Cdd:cd16308   81 KQQTgakMMVDEK--DAKVladgGKSDY---EMGGYGSTFAPVKADKLLHDGdtiklggtkLTLLHHPGHTKGSCSFLFD 155


                 .
gi 489419388 181 T 181
Cdd:cd16308  156 V 156
metallo-hydrolase-like_MBL-fold cd07732
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 39-123 5.88e-05

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: 42.60  E-value: 5.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  39 LLETTDGPILIDTGMPdaFVNNPEYF--KGTKREGRVVPKMTANDKIVNILKSaGYRAGDIQ--AVISSHLHLDHAGGNG 114
Cdd:cd07732   17 EVETGGTRILLDFGLP--LDPESKYFdeVLDFLELGLLPDIVGLYRDPLLLGG-LRSEEDPSvdAVLLSHAHLDHYGLLN 93

                         90
                 ....*....|
gi 489419388 115 HF-PKTPIFI 123
Cdd:cd07732   94 YLrPDIPVYM 103
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-173 7.62e-05

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


Pssm-ID: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 43.05  E-value: 7.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  37 SFLLETTDGPILIDTGMPDAfvnnpeyfkgtkregrvVPKMTANdkivniLKSAGYRAGDIQAVISSHLHLDHAGGNGHF 116
Cdd:cd16312   24 AVLVTSPQGHVLLDGALPQS-----------------APLIIAN------IEALGFRIEDVKLILNSHAHWDHAGGIAAL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489419388 117 PKTPIFIQQAEFDAAMGNDDYSPEEcrlPDLQYQI--------IEGDREVAPG---------VQIFSTPGHSPG 173
Cdd:cd16312   81 QKASGATVAASAHGAQVLQSGTNGK---DDPQYQAkpvvhvakVAKVKEVGEGdtlkvgplrLTAHMTPGHTPG 151
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 37-193 7.72e-05

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: 42.45  E-value: 7.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  37 SFLLETTDGPILIDTGMpdafvnnpeyFKGtKREGRVVPKmtandkivnilKSAGYRAGDIQAVISSHLHLDHAGG---- 112
Cdd:cd16295   14 CYLLETGGKRILLDCGL----------FQG-GKELEELNN-----------EPFPFDPKEIDAVILTHAHLDHSGRlpll 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 113 --NGhfPKTPIF------------------IQQAEFDAAMGNDDYSPEECRLPDLQYQIIEGDR--EVAPGVQIFSTP-G 169
Cdd:cd16295   72 vkEG--FRGPIYatpatkdlaelllldsakIQEEEAEHPPAEPLYTEEDVEKALKHFRPVEYGEpfEIGPGVKVTFYDaG 149

                        170       180
                 ....*....|....*....|....
gi 489419388 170 HSPGHQSVLVTTEHSGPILLTIDV 193
Cdd:cd16295  150 HILGSASVELEIGGGKRILFSGDL 173
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 86-238 9.16e-05

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 42.83  E-value: 9.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  86 ILKSAGYRAGDIQAVISSHLHLDHAGGNGHFPKTPIFIQQaeFDAAMGNddyspeecrLPDLQYQIIEGDR-EVAPGVQI 164
Cdd:PLN02469  36 VLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLVPGIKV--YGGSLDN---------VKGCTHPVENGDKlSLGKDVNI 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489419388 165 FS--TPGHSPGHQSVLVT-TEHSGPILLTIDVAYTR--ENFDNGVPFLSYDSEStvrsikrmKGLIEKVQPSKVFFGHD 238
Cdd:PLN02469 105 LAlhTPCHTKGHISYYVTgKEGEDPAVFTGDTLFIAgcGKFFEGTAEQMYQSLC--------VTLGSLPKPTQVYCGHE 175
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 85-237 1.12e-04

Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; Bacillus amyloliquefaciens BaeB may play a role in the synthesis of the antibiotic polyketide bacillaene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293833 [Multi-domain]  Cd Length: 174  Bit Score: 41.75  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  85 NILKSAGYRAGDIQAVISSHLHLDHAGGNGHFPKT---PIFIQQAEFDaamgnddYSPEECrlPDLQyqIIEGDREVAPG 161
Cdd:cd16275   36 KILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKydaPVYMSKEEID-------YYGFRC--PNLI--PLEDGDTIKIG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388 162 ---VQIFSTPGHSPGHQSVLVttehsGPILLTIDVAYT----RENFDNGvpflsyDSESTVRSIKRMKGLIEKvqPSKVF 234
Cdd:cd16275  105 dteITCLLTPGHTPGSMCYLL-----GDSLFTGDTLFIegcgRCDLPGG------DPEEMYESLQRLKKLPPP--NTRVY 171


                 ...
gi 489419388 235 FGH 237
Cdd:cd16275  172 PGH 174
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-173 1.32e-04

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


Pssm-ID: 293868  Cd Length: 252  Bit Score: 42.05  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  37 SFLLETTDGPILIDTGMPDAfvnnpeyfkgtkregrvVPKMTANdkivniLKSAGYRAGDIQAVISSHLHLDHAGGNGHF 116
Cdd:cd16310   24 SYLITSNHGAILLDGGLEEN-----------------AALIEQN------IKALGFKLSDIKIIINTHAHYDHAGGLAQL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489419388 117 PKT---PIFIQQAEFDA-----AMGNDDYSPeeCRLPDLQYQIIEGDREVAP--GVQIFS--TPGHSPG 173
Cdd:cd16310   81 KADtgaKLWASRGDRPAleagkHIGDNITQP--APFPAVKVDRILGDGEKIKlgDITLTAtlTPGHTKG 147
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 37-173 5.36e-04

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 40.26  E-value: 5.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  37 SFLLETTDGPILIDTGmPDAfvnnpeyfkgtkREgrvvpkmtandkivnILKSAGYRAGDIQAVISSHLHLDHAGGNGHF 116
Cdd:COG1235   37 SILVEADGTRLLIDAG-PDL------------RE---------------QLLRLGLDPSKIDAILLTHEHADHIAGLDDL 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489419388 117 ------PKTPIFIQQAEFDAAMGNDDYSPEECRlPDLQYQIIEGDREVAPG---VQIFSTPgHSPG 173
Cdd:COG1235   89 rprygpNPIPVYATPGTLEALERRFPYLFAPYP-GKLEFHEIEPGEPFEIGgltVTPFPVP-HDAG 152
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 37-176 1.61e-03

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


Pssm-ID: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 38.69  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  37 SFLLETTDGPILIDTGMPDAfvnnPEYFKGTKREgrvvpkmtandkivnilksAGYRAGDIQAVISSHLHLDHAGGNGHF 116
Cdd:cd16313   24 AVLITSPQGHILIDGGFPKS----PEQIAASIRQ-------------------LGFKLEDVKYILSSHDHWDHAGGIAAL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489419388 117 PK---TPIFIQQAEFDA----AMGNDDysPEECRLPdlQYQIIEGDREVAPG---------VQIFSTPGHSPGHQS 176
Cdd:cd16313   81 QKltgAQVLASPATVAVlrsgSMGKDD--PQFGGLT--PMPPVASVRAVRDGevvklgplaVTAHATPGHTTGGTS 152
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 37-122 1.65e-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: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  37 SFLLETTDGPILIDTGM-PDAFVNNPEYFkgtkregrvvpkmtandkivnilksaGYRAGDIQAVISSHLHLDHAgGNGH 115
Cdd:COG1236   16 CYLLETGGTRILIDCGLfQGGKERNWPPF--------------------------PFRPSDVDAVVLTHAHLDHS-GALP 68

                         90
                 ....*....|..
gi 489419388 116 -----FPKTPIF 122
Cdd:COG1236   69 llvkeGFRGPIY 80
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 39-183 2.52e-03

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: 37.90  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  39 LLETTDGPILIDTGmpdafvnnpeyfkgtkrEGRVVPKmtanDKIVNILKSAGyrAGDIQAVISSHLHLDHAGG------ 112
Cdd:cd07722   22 LVGTGKRRILIDTG-----------------EGRPSYI----PLLKSVLDSEG--NATISDILLTHWHHDHVGGlpdvld 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489419388 113 NGHFPKTPIFIQQaefdaamgnDDYSPEECRLPDLQYQIIEGDrevapgvQIFSTPG------HSPGHqsvlvTTEH 183
Cdd:cd07722   79 LLRGPSPRVYKFP---------RPEEDEDPDEDGGDIHDLQDG-------QVFKVEGatlrviHTPGH-----TTDH 134
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 98-174 4.08e-03

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 37.50  E-value: 4.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489419388  98 QAVISSHLHLDHAGG----NGHFPKTPIfiqqaefdaamgnddYSPEECRLPDLQYQIIEGDREVAPGVQ--IFSTPGHS 171
Cdd:PRK10241  47 EAIFLTHHHHDHVGGvkelVEKFPQIVV---------------YGPQETQDKGTTQVVKDGETAFVLGHEfsVFATPGHT 111


                 ...
gi 489419388 172 PGH 174
Cdd:PRK10241 112 LGH 114
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH