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Conserved domains on  [gi|748266646|gb|AJE49187|]
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hypothetical protein P73_4472 (plasmid) [Celeribacter indicus]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 7-241 9.21e-62

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: 194.36  E-value: 9.21e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646   7 ELFAVCYARQpERRPAHLTYVDGREAESTTgFDYFFWYAVQGERVVVIDTGFSEEA---------CRRLGRAWAGDPATL 77
Cdd:cd07729    1 KLYALDYGTV-TVDKSSLFYYGRGPGEPID-LPVYAYLIEHPEGTILVDTGFHPDAaddpgglelAFPPGVTEEQTLEEQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  78 LARAGIDAGAVRDVILTHAHPDHVGNLDQFPNATFWIHAEEMRALTGEEMSFDFFRHsyhgeDVCALVRLLHAGRLRIIA 157
Cdd:cd07729   79 LARLGLDPEDIDYVILSHLHFDHAGGLDLFPNATIIVQRAELEYATGPDPLAAGYYE-----DVLALDDDLPGGRVRLVD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646 158 EDGAFAEGLDHILIGGHAPGQMALRIETRRGPVLLASDAVHLFEEMEGERPFFVFHDMRRMLRGLRTCRRLAGS-DDRLV 236
Cdd:cd07729  154 GDYDLFPGVTLIPTPGHTPGHQSVLVRLPEGTVLLAGDAAYTYENLEEGRPPGINYDPEAALASLERLKALAEReGARVI 233


                 ....*
gi 748266646 237 PGHDP 241
Cdd:cd07729  234 PGHDP 238
 
Name Accession Description Interval E-value
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 7-241 9.21e-62

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: 194.36  E-value: 9.21e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646   7 ELFAVCYARQpERRPAHLTYVDGREAESTTgFDYFFWYAVQGERVVVIDTGFSEEA---------CRRLGRAWAGDPATL 77
Cdd:cd07729    1 KLYALDYGTV-TVDKSSLFYYGRGPGEPID-LPVYAYLIEHPEGTILVDTGFHPDAaddpgglelAFPPGVTEEQTLEEQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  78 LARAGIDAGAVRDVILTHAHPDHVGNLDQFPNATFWIHAEEMRALTGEEMSFDFFRHsyhgeDVCALVRLLHAGRLRIIA 157
Cdd:cd07729   79 LARLGLDPEDIDYVILSHLHFDHAGGLDLFPNATIIVQRAELEYATGPDPLAAGYYE-----DVLALDDDLPGGRVRLVD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646 158 EDGAFAEGLDHILIGGHAPGQMALRIETRRGPVLLASDAVHLFEEMEGERPFFVFHDMRRMLRGLRTCRRLAGS-DDRLV 236
Cdd:cd07729  154 GDYDLFPGVTLIPTPGHTPGHQSVLVRLPEGTVLLAGDAAYTYENLEEGRPPGINYDPEAALASLERLKALAEReGARVI 233


                 ....*
gi 748266646 237 PGHDP 241
Cdd:cd07729  234 PGHDP 238
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 30-244 1.02e-21

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 90.13  E-value: 1.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  30 REAESTTGFDYFFWYAVQGERVVVIDTGFSEEACRRLgrawagdpATLLARAGIDagaVRDVILTHAHPDHVGNLDQFP- 108
Cdd:COG0491    5 PGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEAL--------LAALAALGLD---IKAVLLTHLHPDHVGGLAALAe 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646 109 --NATFWIHAEEMRALTGEEMSFDFfrhsyhGEDVCALVRLLHAG-RLRIiaedgaFAEGLDHILIGGHAPGQMALRIET 185
Cdd:COG0491   74 afGAPVYAHAAEAEALEAPAAGALF------GREPVPPDRTLEDGdTLEL------GGPGLEVIHTPGHTPGHVSFYVPD 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 748266646 186 RRgpVLLASDAVHlfeEMEGERPFFVFHDMRRMLRGLRTCRRLagSDDRLVPGHDPRVT 244
Cdd:COG0491  142 EK--VLFTGDALF---SGGVGRPDLPDGDLAQWLASLERLLAL--PPDLVIPGHGPPTT 193
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
43-239 4.87e-19

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 82.42  E-value: 4.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646   43 WYAVQGERVVVIDTGFSEEAcrrlgrawagDPATLLARAGIDAGAVRDVILTHAHPDHVGNLDQFPNATF---WIHAEEM 119
Cdd:pfam00753   9 YLIEGGGGAVLIDTGGSAEA----------ALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDvpvIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  120 RALTGEEMSFDFFRHSYHGedvcALVRLLHAGRLRIIAEDGAFaEGLDHILIGGHAPGQMALRIETRRGPVLLASDAVHL 199
Cdd:pfam00753  79 RELLDEELGLAASRLGLPG----PPVVPLPPDVVLEEGDGILG-GGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 748266646  200 FEEMEGERPFFVFHDMRRMLRG--LRTCRRLAGSD-DRLVPGH 239
Cdd:pfam00753 154 GEIGRLDLPLGGLLVLHPSSAEssLESLLKLAKLKaAVIVPGH 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 43-239 1.88e-15

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: 72.20  E-value: 1.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646    43 WYAVQGE-RVVVIDTGFSeeacrrlgraWAGDPATLLARAGIDAgaVRDVILTHAHPDHVGNLDQF---PNATFWIHAEE 118
Cdd:smart00849   2 SYLVRDDgGAILIDTGPG----------EAEDLLAELKKLGPKK--IDAIILTHGHPDHIGGLPELleaPGAPVYAPEGT 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646   119 MRALTGEEMSFDFFRHSYHGEDVcalVRLLHAGRLRIIAEdgafaEGLDHILIGGHAPGQMALRIETRRgpVLLASDAVH 198
Cdd:smart00849  70 AELLKDLLALLGELGAEAEPAPP---DRTLKDGDELDLGG-----GELEVIHTPGHTPGSIVLYLPEGK--ILFTGDLLF 139

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 748266646   199 lFEEMEGERPFFVFHDMRRMLRGLRtcRRLAGSDDRLVPGH 239
Cdd:smart00849 140 -AGGDGRTLVDGGDAAASDALESLL--KLLKLLPKLVVPGH 177
 
Name Accession Description Interval E-value
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 7-241 9.21e-62

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: 194.36  E-value: 9.21e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646   7 ELFAVCYARQpERRPAHLTYVDGREAESTTgFDYFFWYAVQGERVVVIDTGFSEEA---------CRRLGRAWAGDPATL 77
Cdd:cd07729    1 KLYALDYGTV-TVDKSSLFYYGRGPGEPID-LPVYAYLIEHPEGTILVDTGFHPDAaddpgglelAFPPGVTEEQTLEEQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  78 LARAGIDAGAVRDVILTHAHPDHVGNLDQFPNATFWIHAEEMRALTGEEMSFDFFRHsyhgeDVCALVRLLHAGRLRIIA 157
Cdd:cd07729   79 LARLGLDPEDIDYVILSHLHFDHAGGLDLFPNATIIVQRAELEYATGPDPLAAGYYE-----DVLALDDDLPGGRVRLVD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646 158 EDGAFAEGLDHILIGGHAPGQMALRIETRRGPVLLASDAVHLFEEMEGERPFFVFHDMRRMLRGLRTCRRLAGS-DDRLV 236
Cdd:cd07729  154 GDYDLFPGVTLIPTPGHTPGHQSVLVRLPEGTVLLAGDAAYTYENLEEGRPPGINYDPEAALASLERLKALAEReGARVI 233


                 ....*
gi 748266646 237 PGHDP 241
Cdd:cd07729  234 PGHDP 238
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 43-239 6.20e-22

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: 90.36  E-value: 6.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  43 WYAVQGER-VVVIDTGFSEEAcRRLGRAwagdpatlLARAGIDAGAVRDVILTHAHPDHVGNLDQF---PNATFWIHAEE 118
Cdd:cd07721   13 AYLIEDDDgLTLIDTGLPGSA-KRILKA--------LRELGLSPKDIRRILLTHGHIDHIGSLAALkeaPGAPVYAHERE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646 119 MRALTGEEMSFDFFRHSYHG-------EDVCALVRLLHAGrlriiaEDGAFAEGLDHILIGGHAPGQMALRIETRRgpVL 191
Cdd:cd07721   84 APYLEGEKPYPPPVRLGLLGllspllpVKPVPVDRTLEDG------DTLDLAGGLRVIHTPGHTPGHISLYLEEDG--VL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 748266646 192 LASDAVHLFE-EMEGERPFFvFHDMRRMlrgLRTCRRLAGSD-DRLVPGH 239
Cdd:cd07721  156 IAGDALVTVGgELVPPPPPF-TWDMEEA---LESLRKLAELDpEVLAPGH 201
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 30-244 1.02e-21

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 90.13  E-value: 1.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  30 REAESTTGFDYFFWYAVQGERVVVIDTGFSEEACRRLgrawagdpATLLARAGIDagaVRDVILTHAHPDHVGNLDQFP- 108
Cdd:COG0491    5 PGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEAL--------LAALAALGLD---IKAVLLTHLHPDHVGGLAALAe 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646 109 --NATFWIHAEEMRALTGEEMSFDFfrhsyhGEDVCALVRLLHAG-RLRIiaedgaFAEGLDHILIGGHAPGQMALRIET 185
Cdd:COG0491   74 afGAPVYAHAAEAEALEAPAAGALF------GREPVPPDRTLEDGdTLEL------GGPGLEVIHTPGHTPGHVSFYVPD 141

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 748266646 186 RRgpVLLASDAVHlfeEMEGERPFFVFHDMRRMLRGLRTCRRLagSDDRLVPGHDPRVT 244
Cdd:COG0491  142 EK--VLFTGDALF---SGGVGRPDLPDGDLAQWLASLERLLAL--PPDLVIPGHGPPTT 193
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 48-198 1.13e-20

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: 87.99  E-value: 1.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  48 GERVVVIDTGFSEEACRRLGRAwagdpATLLARAGIDAGAVRDVILTHAHPDHVGNL------DQFPNATFWIHAEEMRA 121
Cdd:cd07720   57 GGRLILVDTGAGGLFGPTAGKL-----LANLAAAGIDPEDIDDVLLTHLHPDHIGGLvdaggkPVFPNAEVHVSEAEWDF 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 748266646 122 LTGEEM--SFDFFRHSYHGEDVCALVRLLHAGRlriIAEDGAFAEGLDHILIGGHAPGQMALRIETRRGPVLLASDAVH 198
Cdd:cd07720  132 WLDDANaaKAPEGAKRFFDAARDRLRPYAAAGR---FEDGDEVLPGITAVPAPGHTPGHTGYRIESGGERLLIWGDIVH 207
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 21-240 5.20e-20

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: 86.17  E-value: 5.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  21 PAHLTYVDGREAESTTGFDYFFWYAVQGERVVvIDTGFS---EEACRRLGRAWAGDPATL---------LARAGIDAGAV 88
Cdd:cd07730    6 PERLVLRGGPLKRVTFPALAFLIEHPTGGKIL-FDLGYRkdfEEYTPRVPERLYRTPVPLeveedvaeqLAAGGIDPEDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  89 RDVILTHAHPDHVGNLDQFPNATFWIHAEEMRALTGEEMSFDFFrHSYHGEDVcalvrllhAGRLRIIAED-------GA 161
Cdd:cd07730   85 DAVILSHLHWDHIGGLSDFPNARLIVGPGAKEALRPPGYPSGFL-PELLPSDF--------EGRLVRWEEDdflwvplGP 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646 162 FAEGLDhiLIG----------GHAPGQMALRIETRRG-PVLLASDAVH-LFEEMEGERPFFVFH-----DMRRMLRGLRT 224
Cdd:cd07730  156 FPRALD--LFGdgslylvdlpGHAPGHLGLLARTTSGtWVFLAGDACHhRIGLLRPSPLLPLPDlddgaDREAARETLAR 233

                        250
                 ....*....|....*..
gi 748266646 225 CRRLAGSDD-RLVPGHD 240
Cdd:cd07730  234 LRELDAAPDvRVVLAHD 250
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
43-239 4.87e-19

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 82.42  E-value: 4.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646   43 WYAVQGERVVVIDTGFSEEAcrrlgrawagDPATLLARAGIDAGAVRDVILTHAHPDHVGNLDQFPNATF---WIHAEEM 119
Cdd:pfam00753   9 YLIEGGGGAVLIDTGGSAEA----------ALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDvpvIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  120 RALTGEEMSFDFFRHSYHGedvcALVRLLHAGRLRIIAEDGAFaEGLDHILIGGHAPGQMALRIETRRGPVLLASDAVHL 199
Cdd:pfam00753  79 RELLDEELGLAASRLGLPG----PPVVPLPPDVVLEEGDGILG-GGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 748266646  200 FEEMEGERPFFVFHDMRRMLRG--LRTCRRLAGSD-DRLVPGH 239
Cdd:pfam00753 154 GEIGRLDLPLGGLLVLHPSSAEssLESLLKLAKLKaAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-198 2.16e-18

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 81.03  E-value: 2.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  48 GERVVVIDTGFSEEACRRLGRAWAGDPATL---LARAGIDAGAVRDVILTHAHPDHVG---NLDQ------FPNATFWIH 115
Cdd:cd16277   21 PGRTILVDTGIGNDKPRPGPPAFHNLNTPYlerLAAAGVRPEDVDYVLCTHLHVDHVGwntRLVDgrwvptFPNARYLFS 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646 116 AEEMRALTGEEMSFDFFRHSYhgEDVCALVRLlhAGRLRIIAEDGAFAEGLDHILIGGHAPGQMALRIETRRGPVLLASD 195
Cdd:cd16277  101 RAEYDHWSSPDAGGPPNRGVF--EDSVLPVIE--AGLADLVDDDHEILDGIRLEPTPGHTPGHVSVELESGGERALFTGD 176


                 ...
gi 748266646 196 AVH 198
Cdd:cd16277  177 VMH 179
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 47-195 2.78e-17

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: 78.69  E-value: 2.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  47 QGERVVVIDTG----FSEeacRRLGRAWAGDPATL---LARAGIDAGAVRDVILTHAHPDHVGNLDQ----------FPN 109
Cdd:cd16281   50 TGGRNILIDTGigdkQDP---KFRSIYVQHSEHSLlksLARLGLSPEDITDVILTHLHFDHCGGATRadddglvellFPN 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646 110 ATFWIHAEEmraltgeemsFDFFRH-------SYHGEDvcaLVRLLHAGRLRII-AEDGAFAEGLDHILIGGHAPGQMAL 181
Cdd:cd16281  127 ATYWVQKRH----------WEWALNpnpreraSFLPEN---IEPLEESGRLKLIdGSDAELGPGIRFHLSDGHTPGQMLP 193

                        170
                 ....*....|....
gi 748266646 182 RIETRRGPVLLASD 195
Cdd:cd16281  194 EISTPGGTVVFAAD 207
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 44-239 1.24e-15

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: 73.09  E-value: 1.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  44 YAVQGE--RVVVIDTGfseeacrrlgrawaGDPATLLARAGIDAGA-VRDVILTHAHPDHVGNLDQF---PNATFWIHAE 117
Cdd:cd06262   13 YLVSDEegEAILIDPG--------------AGALEKILEAIEELGLkIKAILLTHGHFDHIGGLAELkeaPGAPVYIHEA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646 118 EMRALTGEEMSFDFFRhSYHGEDVCALVRLlhagrlriiaEDGAFAEGLDH----ILIGGHAPGQMALRIETRRgpVLLA 193
Cdd:cd06262   79 DAELLEDPELNLAFFG-GGPLPPPEPDILL----------EDGDTIELGGLelevIHTPGHTPGSVCFYIEEEG--VLFT 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 748266646 194 SDAvhLFEEMEGeRPFFVFHDMRRMLRGLRTCRRLAGSDDRLVPGH 239
Cdd:cd06262  146 GDT--LFAGSIG-RTDLPGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 43-239 1.88e-15

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: 72.20  E-value: 1.88e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646    43 WYAVQGE-RVVVIDTGFSeeacrrlgraWAGDPATLLARAGIDAgaVRDVILTHAHPDHVGNLDQF---PNATFWIHAEE 118
Cdd:smart00849   2 SYLVRDDgGAILIDTGPG----------EAEDLLAELKKLGPKK--IDAIILTHGHPDHIGGLPELleaPGAPVYAPEGT 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646   119 MRALTGEEMSFDFFRHSYHGEDVcalVRLLHAGRLRIIAEdgafaEGLDHILIGGHAPGQMALRIETRRgpVLLASDAVH 198
Cdd:smart00849  70 AELLKDLLALLGELGAEAEPAPP---DRTLKDGDELDLGG-----GELEVIHTPGHTPGSIVLYLPEGK--ILFTGDLLF 139

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 748266646   199 lFEEMEGERPFFVFHDMRRMLRGLRtcRRLAGSDDRLVPGH 239
Cdd:smart00849 140 -AGGDGRTLVDGGDAAASDALESLL--KLLKLLPKLVVPGH 177
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 48-241 2.55e-13

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: 66.84  E-value: 2.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  48 GERVVVIDTGFseeacrrlgrAWAGDpaTL---LARAGIDAGAVRDVILTHAHPDHVGNLDQFPNATFWIHaeemraltg 124
Cdd:cd07711   30 GGKNILVDTGT----------PWDRD--LLlkaLAEHGLSPEDIDYVVLTHGHPDHIGNLNLFPNATVIVG--------- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646 125 eemsFDFFRHSYHGEDvcalvrLLHAGRLRIiaedgafAEGLDHILIGGHAPGQMALRIET-RRGPVLLASDavhLFEEM 203
Cdd:cd07711   89 ----WDICGDSYDDHS------LEEGDGYEI-------DENVEVIPTPGHTPEDVSVLVETeKKGTVAVAGD---LFERE 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 748266646 204 E----GERPFFVFHDMRRMLRGLRTCRRLAgsdDRLVPGHDP 241
Cdd:cd07711  149 EdledPILWDPLSEDPELQEESRKRILALA---DWIIPGHGP 187
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-244 2.54e-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) 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: 61.87  E-value: 2.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  48 GERVVVIDTGFSEEAC----RRLGRAWAG------DPA-TLLA---RAGIDAGAVRDVILTHAHPDHVGNLDQFPNATFW 113
Cdd:cd07742   27 DDGLVLVDTGFGLADVadpkRRLGGPFRRllrprlDEDeTAVRqieALGFDPSDVRHIVLTHLDLDHAGGLADFPHATVH 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646 114 IHAEEMRALTGEEMSFDffRHSYHgedvcalVRLLHAGRLRIIAEDG-----------AFAEGLDHILI---GGHAPGQM 179
Cdd:cd07742  107 VHAAELDAATSPRTRYE--RRRYR-------PQQLAHGPWWVTYAAGgerwfgfeavrPLDGLPPEILLvplPGHTRGHC 177

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 748266646 180 ALRIETRRGPVLLASDAVHLFEEMEGE-RPFFVFHDMRRML-----RGLRTCRRLAgsddRLVPGHDPRVT 244
Cdd:cd07742  178 GVAVRTGDRWLLHAGDAYFHHGELDPLpPPPPPLRLFQRLLavdrsARLANLARLR----ELARDHGDEVE 244
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-239 1.11e-10

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 59.50  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  48 GERVVVIDTGFSEEACRRLGRAwagdpatllARAgIDAGAVRDVILTHAHPDHVGNLDQFPN--ATFWIHAEEMRALTGE 125
Cdd:cd16282   23 DDGVVVIDTGASPRLARALLAA---------IRK-VTDKPVRYVVNTHYHGDHTLGNAAFADagAPIIAHENTREELAAR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646 126 EMSFDFFRHSYHGEDvcalvrllhAGRLRIIAEDGAFAEGLDhILIGG-----------HAPGQMALRIETRRgpVLLAS 194
Cdd:cd16282   93 GEAYLELMRRLGGDA---------MAGTELVLPDRTFDDGLT-LDLGGrtvelihlgpaHTPGDLVVWLPEEG--VLFAG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 748266646 195 DAVhlfeeMEGERPFFVFHDMRRMlrgLRTCRRLAGSDDR-LVPGH 239
Cdd:cd16282  161 DLV-----FNGRIPFLPDGSLAGW---IAALDRLLALDATvVVPGH 198
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 44-239 1.14e-09

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


Pssm-ID: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 56.10  E-value: 1.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  44 YAVQG-ERVVVIDTGFSEEACRRLGRAWAGDPATllaragidagavrdVILTHAHPDHVGNLDQFPNatFWIHAEEMRAL 122
Cdd:cd07712   12 YLLRGrDRALLIDTGLGIGDLKEYVRTLTDLPLL--------------VVATHGHFDHIGGLHEFEE--VYVHPADAEIL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646 123 TGEEMSFDFFRHSYHGEDVcalvrllHAGRLRIIAEDGAFAEG---LDHILIGGHAPGQMALRIETRRgpVLLASDAVhl 199
Cdd:cd07712   76 AAPDNFETLTWDAATYSVP-------PAGPTLPLRDGDVIDLGdrqLEVIHTPGHTPGSIALLDRANR--LLFSGDVV-- 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 748266646 200 feemeGERPFFVFHDMRRMLRGLRTCRRLAGSD---DRLVPGH 239
Cdd:cd07712  145 -----YDGPLIMDLPHSDLDDYLASLEKLSKLPdefDKVLPGH 182
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 48-239 3.52e-09

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


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 55.00  E-value: 3.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  48 GERVVVIDTGFSEEACRRLgrAWAGdpatlLARAGIDAGAVRDVILTHAHPDHVGNLDQFpnatfwihaeemRALTGEEM 127
Cdd:cd07725   23 GDETTLIDTGLATEEDAEA--LWEG-----LKELGLKPSDIDRVLLTHHHPDHIGLAGKL------------QEKSGATV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646 128 SFDFFRHSYHGEdvcaLVRLLHaGRLRIiaedgafaegldhILIGGHAPGQMALRIETRRgpVLLASDavHLFEEME--- 204
Cdd:cd07725   84 YILDVTPVKDGD----KIDLGG-LRLKV-------------IETPGHTPGHIVLYDEDRR--ELFVGD--AVLPKITpnv 141

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 748266646 205 GERPFFVFHDMRRMLRGLRTCRRLagSDDRLVPGH 239
Cdd:cd07725  142 SLWAVRVEDPLGAYLESLDKLEKL--DVDLAYPGH 174
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 51-239 4.31e-08

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 52.15  E-value: 4.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  51 VVVIDTGFSEEACRRLGRawagdpatLLARAGIdagAVRDVILTHAHPDHVGNLDQF---PNATFWIHAEEMRALTGEEM 127
Cdd:cd07743   20 ALLIDSGLDEDAGRKIRK--------ILEELGW---KLKAIINTHSHADHIGGNAYLqkkTGCKVYAPKIEKAFIENPLL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646 128 SFDFFRHSYHGEDVCALVRLLHAGRLRIIAEDGAFA---EGLDHILIGGHAPGQMALRIETRrgpVLLASDAvhLFEEME 204
Cdd:cd07743   89 EPSYLGGAYPPKELRNKFLMAKPSKVDDIIEEGELElggVGLEIIPLPGHSFGQIGILTPDG---VLFAGDA--LFGEEV 163

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 748266646 205 GER-PFFVFHDMRRMLRGLrtcRRLAGSDDRL-VPGH 239
Cdd:cd07743  164 LEKyGIPFLYDVEEQLETL---EKLEELDADYyVPGH 197
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
71-239 3.53e-07

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 50.27  E-value: 3.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  71 AGDPATLLARA---GIDAGAVRDVILTHAHPDHVGNLDQF----PNATFWIHAeemraltgeemsfDFFRHSYHGEDVCA 143
Cdd:COG1237   38 TGQSDVLLKNAeklGIDLSDIDAVVLSHGHYDHTGGLPALlelnPKAPVYAHP-------------DAFEKRYSKRPGGK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646 144 LVRLL--------HAGRLRIIAEDGAFAEGL-----------------------DHILIGGHAPGQMALRIETRRGPVLL 192
Cdd:COG1237  105 YIGIPfsreelekLGARLILVKEPTEIAPGVyltgeiprvtdfekgdpglyvkeDGGLVPDPFLDEQALVIKTDKGLVVI 184

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646 193 ASDAV--------HLFEEMEGERPFFV---FHDMRRMLRGL-RTCRRLAGSD-DRLVPGH 239
Cdd:COG1237  185 TGCSHagivnileYAKEVTGGKRIYAViggFHLLGASEERIeKTIEALKELGvEKIYPGH 244
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 73-186 1.20e-06

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: 47.53  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  73 DPA----TLLARAGIDAGAVRDVILTHAHPDHVGNLDQFP---NATFWIHAEEmraltgeemsFDFFRhsyhgedvcalv 145
Cdd:cd16275   29 DPAwdieKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLakyDAPVYMSKEE----------IDYYG------------ 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 748266646 146 rlLHAGRLRIIaEDGafaeglDHILIG----------GHAPGQMALRIETR 186
Cdd:cd16275   87 --FRCPNLIPL-EDG------DTIKIGdteitclltpGHTPGSMCYLLGDS 128
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 48-204 2.01e-05

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 44.89  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  48 GERVVVIDTGFSeeaCRRLGRawagdpatllaRAGIDAGAVRDVILTHAHPDHVGNLDQF------PNATFWIHAEEMRA 121
Cdd:COG1235   43 DGTRLLIDAGPD---LREQLL-----------RLGLDPSKIDAILLTHEHADHIAGLDDLrprygpNPIPVYATPGTLEA 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646 122 LtgeEMSFDFFRHSYHGEDvcalvrllhagRLRIIAEDGAFAegldhilIGG---------HAPGQ-MALRIETRRGPVL 191
Cdd:COG1235  109 L---ERRFPYLFAPYPGKL-----------EFHEIEPGEPFE-------IGGltvtpfpvpHDAGDpVGYRIEDGGKKLA 167

                        170
                 ....*....|...
gi 748266646 192 LASDAVHLFEEME 204
Cdd:COG1235  168 YATDTGYIPEEVL 180
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 44-115 5.40e-05

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: 43.25  E-value: 5.40e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 748266646  44 YAVQGE-RVVVIDTGFSEEACRRLgrawagdpaTLLARAGIDAGAVRDVILTHAHPDHVGN----LDQFPNATFWIH 115
Cdd:cd07726   19 YLLDGEgRPALIDTGPSSSVPRLL---------AALEALGIAPEDVDYIILTHIHLDHAGGagllAEALPNAKVYVH 86
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 78-166 7.83e-05

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: 42.99  E-value: 7.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  78 LARAGIDAGAVRDVILTHAHPDHVGNLDQF----PNATFWIHAEEMRALtgeemsFDFFRHSYHGEDVCALVRLLHAGRL 153
Cdd:cd07713   46 AKKLGIDLSDIDAVVLSHGHYDHTGGLKALlelnPKAPVYAHPDAFEPR------YSKRGGGKKGIGIGREELEKAGARL 119

                         90
                 ....*....|...
gi 748266646 154 RIIAEDGAFAEGL 166
Cdd:cd07713  120 VLVEEPTEIAPGV 132
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 48-120 1.06e-04

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: 42.34  E-value: 1.06e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 748266646  48 GERVVVIDTGFSEEacrrlgrawagdpaTLLARAGIDAGAVRDVILTHAHPDHVGNLDQF---PNATFWIHAEEMR 120
Cdd:cd16322   21 GGEAVLVDPGDESE--------------KLLARFGTTGLTLLYILLTHAHFDHVGGVADLrrhPGAPVYLHPDDLP 82
NorV COG0426
Flavorubredoxin [Energy production and conversion];
44-174 2.71e-04

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 41.74  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  44 YAVQGERVVVIDTG---FSEEACRRLGRawAGDPATllaragIDAgavrdVILTHAHPDHVGNLDQ----FPNATFWIHa 116
Cdd:COG0426   37 YLIVDEKTALIDTVgesFFEEFLENLSK--VIDPKK------IDY-----IIVNHQEPDHSGSLPEllelAPNAKIVCS- 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 748266646 117 eemraltgeEMSFDFFRHSYHGEDvcalvrllhaGRLRIIaEDGafaeglDHILIGGH 174
Cdd:COG0426  103 ---------KKAARFLPHFYGIPD----------FRFIVV-KEG------DTLDLGGH 134
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 46-121 5.38e-04

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: 40.32  E-value: 5.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  46 VQGERVVvIDTG-----FSEEACRRLGrawAGDPATL---LARAGIDAGAVRDVILTHAHPDHVGNL-----DQ----FP 108
Cdd:cd07728   50 YQGKNYL-IDAGigngkLTEKQKRNFG---VTEESSIeesLAELGLTPEDIDYVLMTHLHFDHASGLtkvkgEQlvsvFP 125

                         90
                 ....*....|....*.
gi 748266646 109 NATFWIHA---EEMRA 121
Cdd:cd07728  126 NATIYVSEiewEEMRN 141
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 44-111 7.38e-04

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


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 39.78  E-value: 7.38e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 748266646  44 YAVQGERVVVIDTG---FSEEACRRLGRAwagdpatllaragIDAGAVRDVILTHAHPDHVGNL----DQFPNAT 111
Cdd:cd07709   35 YLIKDEKTALIDTVkepFFDEFLENLEEV-------------IDPRKIDYIVVNHQEPDHSGSLpellELAPNAK 96
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 44-107 7.50e-04

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


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 39.42  E-value: 7.50e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 748266646  44 YAVQ-GERVVVIDTGFSeeACRRLgrawagdpatllARAGIDAGAVRDVILTHAHPDHVGNLDQF 107
Cdd:cd07719   21 TLVVvGGRVYLVDAGSG--VVRRL------------AQAGLPLGDLDAVFLTHLHSDHVADLPAL 71
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 50-113 1.23e-03

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: 39.46  E-value: 1.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 748266646  50 RVVVIDTGfseeacrrlgRAWAGDPAT-----LLARAGI---DAgavrdVILTHAHPDHVGNL----DQFPNATFW 113
Cdd:COG2333   22 KTILIDTG----------PRPSFDAGErvvlpYLRALGIrrlDL-----LVLTHPDADHIGGLaavlEAFPVGRVL 82
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 48-104 1.41e-03

Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 38.78  E-value: 1.41e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 748266646  48 GERVVVIDTGfsEEACRRLgrawagdpatllARAGIDAGAVRDVILTHAHPDHVGNL 104
Cdd:cd16272   25 GGTRILLDCG--EGTVYRL------------LKAGVDPDKLDAIFLSHFHLDHIGGL 67
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 44-102 1.47e-03

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 39.11  E-value: 1.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 748266646  44 YAVQ-GERVVVIDTGFSEEAcrrlgRAW--AGdpatlLARAGIDAGAVRDVILTHAHPDHVG 102
Cdd:cd16280   25 WAIDtGDGLILIDALNNNEA-----ADLivDG-----LEKLGLDPADIKYILITHGHGDHYG 76
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 49-102 3.64e-03

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. 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: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 37.87  E-value: 3.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 748266646  49 ERVVVIDTGFSEEACRRlgrAWAgdpatlLARAGIDAGAVRDVILTHAHPDHVG 102
Cdd:cd07710   27 TGLIIIDTLESAEAAKA---ALE------LFRKHTGDKPVKAIIYTHSHPDHFG 71
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 52-207 3.79e-03

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 37.67  E-value: 3.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646   52 VVIDTGFSeeacRRLGRAWAGDPATLLARaGIDAgavrdVILTHAHPDHVGNLD---QFPNATFWIHAEEMRALTGEEMS 128
Cdd:pfam12706   3 ILIDPGPD----LRQQALPALQPGRLRDD-PIDA-----VLLTHDHYDHLAGLLdlrEGRPRPLYAPLGVLAHLRRNFPY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  129 FDFFRHSYHgedvcalvrllhagRLRIIAEDGAFAEGLDHILI------GGHAPGQ-------MALRIETRRGPVLLASD 195
Cdd:pfam12706  73 LFLLEHYGV--------------RVHEIDWGESFTVGDGGLTVtatparHGSPRGLdpnpgdtLGFRIEGPGKRVYYAGD 138

                         170
                  ....*....|..
gi 748266646  196 aVHLFEEMEGER 207
Cdd:pfam12706 139 -TGYFPDEIGER 149
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 47-114 4.36e-03

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: 37.11  E-value: 4.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 748266646  47 QGERVVVIDTGfseeacrrlGRAWAGDPATL--LARAGI---DAgavrdVILTHAHPDHVGNLD----QFPNATFWI 114
Cdd:cd07731   17 TPGKTILIDTG---------PRDSFGEDVVVpyLKARGIkklDY-----LILTHPDADHIGGLDavlkNFPVKEVYM 79
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 48-106 5.91e-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: 36.74  E-value: 5.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 748266646  48 GERVVVIDTGfsEEacrrlGRAWAGDPATLLARAGIDAgaVRDVILTHAHPDHVGNLDQ 106
Cdd:cd07722   26 GKRRILIDTG--EG-----RPSYIPLLKSVLDSEGNAT--ISDILLTHWHHDHVGGLPD 75
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
44-102 7.66e-03

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 37.10  E-value: 7.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  44 YAVQ-GERVVVIDTGfseEACRRLgrawagdpatlLARAGIDAGAVRDVILTHAHPDHVG 102
Cdd:COG1234   22 YLLEaGGERLLIDCG---EGTQRQ-----------LLRAGLDPRDIDAIFITHLHGDHIA 67
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 80-162 7.69e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; 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 named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 36.68  E-value: 7.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 748266646  80 RAGIDAgaVRDVILTHAHPDHVGNLDQFPNATFW------IHAEEmRALTGEEMSFDFFRHSYHGEDVCALvrllhagRL 153
Cdd:cd16279   61 RAGIRK--LDAVLLTHAHADHIHGLDDLRPFNRLqqrpipVYASE-ETLDDLKRRFPYFFAATGGGGVPKL-------DL 130


                 ....*....
gi 748266646 154 RIIAEDGAF 162
Cdd:cd16279  131 HIIEPDEPF 139
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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