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Conserved domains on  [gi|516959197|ref|WP_018184857|]
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N-acyl homoserine lactonase family protein [Kaistia granuli]

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 ...
 5-260 1.75e-52

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: 171.63  E-value: 1.75e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197   5 SIWVLEYAYIPEMPLSALVYGEHNKGTCKLPYAYTLLKSDEHTILIDCGHDDAAH----GKFLADRSGVVNFAAPRDVLA 80
Cdd:cd07729    1 KLYALDYGTVTVDKSSLFYYGRGPGEPIDLPVYAYLIEHPEGTILVDTGFHPDAAddpgGLELAFPPGVTEEQTLEEQLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  81 EIGMTPGDIDHVIITHAHFDHMGGLALFLNAKFYIQEAELSRWIWAMSLDRRFRWlmrttdpaDIIRCVELARDGRLVAV 160
Cdd:cd07729   81 RLGLDPEDIDYVILSHLHFDHAGGLDLFPNATIIVQRAELEYATGPDPLAAGYYE--------DVLALDDDLPGGRVRLV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 161 NGDMeDVFPGIDLRLAAdTHTPGSQFVVIrndgqRTSEDSFVITGDLVYRMENLNGGEPADPFYRPVgmgigsqtNMVFA 240
Cdd:cd07729  153 DGDY-DLFPGVTLIPTP-GHTPGHQSVLV-----RLPEGTVLLAGDAAYTYENLEEGRPPGINYDPE--------AALAS 217

                        250       260
                 ....*....|....*....|
gi 516959197 241 LDAIVKAAGDDPGRVVPPHE 260
Cdd:cd07729  218 LERLKALAEREGARVIPGHD 237
 
Name Accession Description Interval E-value
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 5-260 1.75e-52

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: 171.63  E-value: 1.75e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197   5 SIWVLEYAYIPEMPLSALVYGEHNKGTCKLPYAYTLLKSDEHTILIDCGHDDAAH----GKFLADRSGVVNFAAPRDVLA 80
Cdd:cd07729    1 KLYALDYGTVTVDKSSLFYYGRGPGEPIDLPVYAYLIEHPEGTILVDTGFHPDAAddpgGLELAFPPGVTEEQTLEEQLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  81 EIGMTPGDIDHVIITHAHFDHMGGLALFLNAKFYIQEAELSRWIWAMSLDRRFRWlmrttdpaDIIRCVELARDGRLVAV 160
Cdd:cd07729   81 RLGLDPEDIDYVILSHLHFDHAGGLDLFPNATIIVQRAELEYATGPDPLAAGYYE--------DVLALDDDLPGGRVRLV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 161 NGDMeDVFPGIDLRLAAdTHTPGSQFVVIrndgqRTSEDSFVITGDLVYRMENLNGGEPADPFYRPVgmgigsqtNMVFA 240
Cdd:cd07729  153 DGDY-DLFPGVTLIPTP-GHTPGHQSVLV-----RLPEGTVLLAGDAAYTYENLEEGRPPGINYDPE--------AALAS 217

                        250       260
                 ....*....|....*....|
gi 516959197 241 LDAIVKAAGDDPGRVVPPHE 260
Cdd:cd07729  218 LERLKALAEREGARVIPGHD 237
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
39-259 4.22e-19

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 83.19  E-value: 4.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197   39 TLLKSDEHTILIDCGHDDAAHGKFLadrsgvvnfaaprdvLAEIGMTPGDIDHVIITHAHFDHMGGLALFLNAKFYIQEA 118
Cdd:pfam00753   9 YLIEGGGGAVLIDTGGSAEAALLLL---------------LAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  119 ElsrWIWAMSLDRRFRWLMRTTDPADIIRCVELARDgrlVAVNGDMEDVFPGIDLRLAAdTHTPGSQFVVIRNDGQRtse 198
Cdd:pfam00753  74 V---AEEARELLDEELGLAASRLGLPGPPVVPLPPD---VVLEEGDGILGGGLGLLVTH-GPGHGPGHVVVYYGGGK--- 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516959197  199 dsFVITGDLVYRMENLNGGEPADPFYRPVGMGIGSqtnmvfALDAIVKAAGDDPGRVVPPH 259
Cdd:pfam00753 144 --VLFTGDLLFAGEIGRLDLPLGGLLVLHPSSAES------SLESLLKLAKLKAAVIVPGH 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 39-259 3.82e-18

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 79.90  E-value: 3.82e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197    39 TLLKSDEHTILIDCGHDDAAHgkfladrsgvvnfaaPRDVLAEIGmtPGDIDHVIITHAHFDHMGGLALFL---NAKFYI 115
Cdd:smart00849   3 YLVRDDGGAILIDTGPGEAED---------------LLAELKKLG--PKKIDAIILTHGHPDHIGGLPELLeapGAPVYA 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197   116 QEAElsrWIWAMSLDRRFRWLMRTTDPADIIRCVElardgrlvavNGDMEDvFPGIDLR-LAADTHTPGSQFVVIRndgq 194
Cdd:smart00849  66 PEGT---AELLKDLLALLGELGAEAEPAPPDRTLK----------DGDELD-LGGGELEvIHTPGHTPGSIVLYLP---- 127

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516959197   195 rtsEDSFVITGDLVYrmenlnGGEPADPFYRPVGMgigsqtNMVFALDAIVKAAGDDPGRVVPPH 259
Cdd:smart00849 128 ---EGKILFTGDLLF------AGGDGRTLVDGGDA------AASDALESLLKLLKLLPKLVVPGH 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 36-273 9.66e-17

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 77.04  E-value: 9.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  36 YAYtLLKSDEHTILIDCGHDDAAHGKFLAdrsgvvnfaaprdVLAEIGMtpgDIDHVIITHAHFDHMGGLALF---LNAK 112
Cdd:COG0491   16 NSY-LIVGGDGAVLIDTGLGPADAEALLA-------------ALAALGL---DIKAVLLTHLHPDHVGGLAALaeaFGAP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 113 FYIQEAELSRWiwamSLDRRFRWLMRTTDPADiircvELARDGRLVAVNGdmedvfPGIDLrLAADTHTPGSQFVVIRND 192
Cdd:COG0491   79 VYAHAAEAEAL----EAPAAGALFGREPVPPD-----RTLEDGDTLELGG------PGLEV-IHTPGHTPGHVSFYVPDE 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 193 GqrtsedsFVITGDLVyrmenlnggepadpFYRPVGMGIGSQTNMVFALDAIVKAAGDDPGRVVPPHEARLPEMFPSRLT 272
Cdd:COG0491  143 K-------VLFTGDAL--------------FSGGVGRPDLPDGDLAQWLASLERLLALPPDLVIPGHGPPTTAEAIDYLE 201


                 .
gi 516959197 273 E 273
Cdd:COG0491  202 E 202
 
Name Accession Description Interval E-value
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 5-260 1.75e-52

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: 171.63  E-value: 1.75e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197   5 SIWVLEYAYIPEMPLSALVYGEHNKGTCKLPYAYTLLKSDEHTILIDCGHDDAAH----GKFLADRSGVVNFAAPRDVLA 80
Cdd:cd07729    1 KLYALDYGTVTVDKSSLFYYGRGPGEPIDLPVYAYLIEHPEGTILVDTGFHPDAAddpgGLELAFPPGVTEEQTLEEQLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  81 EIGMTPGDIDHVIITHAHFDHMGGLALFLNAKFYIQEAELSRWIWAMSLDRRFRWlmrttdpaDIIRCVELARDGRLVAV 160
Cdd:cd07729   81 RLGLDPEDIDYVILSHLHFDHAGGLDLFPNATIIVQRAELEYATGPDPLAAGYYE--------DVLALDDDLPGGRVRLV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 161 NGDMeDVFPGIDLRLAAdTHTPGSQFVVIrndgqRTSEDSFVITGDLVYRMENLNGGEPADPFYRPVgmgigsqtNMVFA 240
Cdd:cd07729  153 DGDY-DLFPGVTLIPTP-GHTPGHQSVLV-----RLPEGTVLLAGDAAYTYENLEEGRPPGINYDPE--------AALAS 217

                        250       260
                 ....*....|....*....|
gi 516959197 241 LDAIVKAAGDDPGRVVPPHE 260
Cdd:cd07729  218 LERLKALAEREGARVIPGHD 237
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 40-208 2.35e-21

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: 90.63  E-value: 2.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  40 LLKSDEHTILIDCG----HDDaahgKFLaDRSGVVNFAAPRDVLAEIGMTPGDIDHVIITHAHFDHMGGL---------- 105
Cdd:cd16281   47 LIETGGRNILIDTGigdkQDP----KFR-SIYVQHSEHSLLKSLARLGLSPEDITDVILTHLHFDHCGGAtradddglve 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 106 ALFLNAKFYIQEAElsrWIWAMSLDRR-----FRWLMrttDPadiircveLARDGRLVAVNGDMEDVFPGIDLRLaADTH 180
Cdd:cd16281  122 LLFPNATYWVQKRH---WEWALNPNPRerasfLPENI---EP--------LEESGRLKLIDGSDAELGPGIRFHL-SDGH 186

                        170       180
                 ....*....|....*....|....*...
gi 516959197 181 TPGSQFVVIRNDGQrtsedSFVITGDLV 208
Cdd:cd16281  187 TPGQMLPEISTPGG-----TVVFAADLI 209
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 39-223 4.66e-21

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: 88.03  E-value: 4.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  39 TLLKSDEHTILIDCGHddaahgkfLADRSGVVnfaaprDVLAEIGMTPGDIDHVIITHAHFDHMGGLALFLNAKFYIQea 118
Cdd:cd07711   25 TLIKDGGKNILVDTGT--------PWDRDLLL------KALAEHGLSPEDIDYVVLTHGHPDHIGNLNLFPNATVIVG-- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 119 elsrwiWAMSLDRRFRWLMRTTDPADIIRCVELARDgrlvavngdmedvfPGidlrlaadtHTPGSQFVVIRNDGQRTse 198
Cdd:cd07711   89 ------WDICGDSYDDHSLEEGDGYEIDENVEVIPT--------------PG---------HTPEDVSVLVETEKKGT-- 137

                        170       180
                 ....*....|....*....|....*
gi 516959197 199 dsFVITGDLVYRMENLNGGEPADPF 223
Cdd:cd07711  138 --VAVAGDLFEREEDLEDPILWDPL 160
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 39-209 5.72e-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: 86.83  E-value: 5.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  39 TLLKSDEHTILIDCGHddaahGKFLADRSGVVnfaapRDVLAEIGMTPGDIDHVIITHAHFDHMGGL------ALFLNAK 112
Cdd:cd07720   52 FLVRTGGRLILVDTGA-----GGLFGPTAGKL-----LANLAAAGIDPEDIDDVLLTHLHPDHIGGLvdaggkPVFPNAE 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 113 FYIQEAELSRWiwaMSLDrrfrwlMRTTDPADIIRCVELARD------GRLVAVNGDmeDVFPGIDLRLAADtHTPGSQF 186
Cdd:cd07720  122 VHVSEAEWDFW---LDDA------NAAKAPEGAKRFFDAARDrlrpyaAAGRFEDGD--EVLPGITAVPAPG-HTPGHTG 189

                        170       180
                 ....*....|....*....|...
gi 516959197 187 VVIRNDGQRtsedsFVITGDLVY 209
Cdd:cd07720  190 YRIESGGER-----LLIWGDIVH 207
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
39-259 4.22e-19

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 83.19  E-value: 4.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197   39 TLLKSDEHTILIDCGHDDAAHGKFLadrsgvvnfaaprdvLAEIGMTPGDIDHVIITHAHFDHMGGLALFLNAKFYIQEA 118
Cdd:pfam00753   9 YLIEGGGGAVLIDTGGSAEAALLLL---------------LAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  119 ElsrWIWAMSLDRRFRWLMRTTDPADIIRCVELARDgrlVAVNGDMEDVFPGIDLRLAAdTHTPGSQFVVIRNDGQRtse 198
Cdd:pfam00753  74 V---AEEARELLDEELGLAASRLGLPGPPVVPLPPD---VVLEEGDGILGGGLGLLVTH-GPGHGPGHVVVYYGGGK--- 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 516959197  199 dsFVITGDLVYRMENLNGGEPADPFYRPVGMGIGSqtnmvfALDAIVKAAGDDPGRVVPPH 259
Cdd:pfam00753 144 --VLFTGDLLFAGEIGRLDLPLGGLLVLHPSSAES------SLESLLKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 44-210 1.52e-18

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: 81.18  E-value: 1.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  44 DEHTILIDCGHDDAAhgkfladrsgvvnfaaprDVLAEIGMTPGDIDHVIITHAHFDHMGGLALFL---NAKFYIQEAEL 120
Cdd:cd06262   19 EGEAILIDPGAGALE------------------KILEAIEELGLKIKAILLTHGHFDHIGGLAELKeapGAPVYIHEADA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 121 SRWIWAMSLDRRFRWLMRTTDPADIIrcvelardgrlvaVNGDMEDVFPGIDLR-LAADTHTPGSQFVVIRNDGqrtsed 199
Cdd:cd06262   81 ELLEDPELNLAFFGGGPLPPPEPDIL-------------LEDGDTIELGGLELEvIHTPGHTPGSVCFYIEEEG------ 141

                        170
                 ....*....|.
gi 516959197 200 sFVITGDLVYR 210
Cdd:cd06262  142 -VLFTGDTLFA 151
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 39-259 3.82e-18

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 79.90  E-value: 3.82e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197    39 TLLKSDEHTILIDCGHDDAAHgkfladrsgvvnfaaPRDVLAEIGmtPGDIDHVIITHAHFDHMGGLALFL---NAKFYI 115
Cdd:smart00849   3 YLVRDDGGAILIDTGPGEAED---------------LLAELKKLG--PKKIDAIILTHGHPDHIGGLPELLeapGAPVYA 65

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197   116 QEAElsrWIWAMSLDRRFRWLMRTTDPADIIRCVElardgrlvavNGDMEDvFPGIDLR-LAADTHTPGSQFVVIRndgq 194
Cdd:smart00849  66 PEGT---AELLKDLLALLGELGAEAEPAPPDRTLK----------DGDELD-LGGGELEvIHTPGHTPGSIVLYLP---- 127

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516959197   195 rtsEDSFVITGDLVYrmenlnGGEPADPFYRPVGMgigsqtNMVFALDAIVKAAGDDPGRVVPPH 259
Cdd:smart00849 128 ---EGKILFTGDLLF------AGGDGRTLVDGGDA------AASDALESLLKLLKLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 40-207 6.84e-18

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 80.26  E-value: 6.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  40 LLKSDEHTILIDCG---HDDAAHGKFLADRSGVVnfaapRDVLAEIGMTPGDIDHVIITHAHFDHMGG---------LAL 107
Cdd:cd16277   17 LVRTPGRTILVDTGignDKPRPGPPAFHNLNTPY-----LERLAAAGVRPEDVDYVLCTHLHVDHVGWntrlvdgrwVPT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 108 FLNAKFYIQEAELSRWIWAMSLDRRFRWLMrttdpADIIRCVELArdGRLVAVNGDmEDVFPGIDLRLAADtHTPGSQFV 187
Cdd:cd16277   92 FPNARYLFSRAEYDHWSSPDAGGPPNRGVF-----EDSVLPVIEA--GLADLVDDD-HEILDGIRLEPTPG-HTPGHVSV 162

                        170       180
                 ....*....|....*....|
gi 516959197 188 VIRNDGQRtsedsFVITGDL 207
Cdd:cd16277  163 ELESGGER-----ALFTGDV 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 36-273 9.66e-17

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


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 77.04  E-value: 9.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  36 YAYtLLKSDEHTILIDCGHDDAAHGKFLAdrsgvvnfaaprdVLAEIGMtpgDIDHVIITHAHFDHMGGLALF---LNAK 112
Cdd:COG0491   16 NSY-LIVGGDGAVLIDTGLGPADAEALLA-------------ALAALGL---DIKAVLLTHLHPDHVGGLAALaeaFGAP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 113 FYIQEAELSRWiwamSLDRRFRWLMRTTDPADiircvELARDGRLVAVNGdmedvfPGIDLrLAADTHTPGSQFVVIRND 192
Cdd:COG0491   79 VYAHAAEAEAL----EAPAAGALFGREPVPPD-----RTLEDGDTLELGG------PGLEV-IHTPGHTPGHVSFYVPDE 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 193 GqrtsedsFVITGDLVyrmenlnggepadpFYRPVGMGIGSQTNMVFALDAIVKAAGDDPGRVVPPHEARLPEMFPSRLT 272
Cdd:COG0491  143 K-------VLFTGDAL--------------FSGGVGRPDLPDGDLAQWLASLERLLALPPDLVIPGHGPPTTAEAIDYLE 201


                 .
gi 516959197 273 E 273
Cdd:COG0491  202 E 202
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 36-259 2.54e-16

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: 75.72  E-value: 2.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  36 YAYtLLKSDEHTILIDCGHddAAHGKFLadrsgvvnfaapRDVLAEIGMTPGDIDHVIITHAHFDHMGGLALFL---NAK 112
Cdd:cd07721   12 NAY-LIEDDDGLTLIDTGL--PGSAKRI------------LKALRELGLSPKDIRRILLTHGHIDHIGSLAALKeapGAP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 113 FYIQEAEL--------SRWIWAMSLDRRFRWLMrttdPADIIRCVELARDGRLVAVNGDMEDVF-PGidlrlaadtHTPG 183
Cdd:cd07721   77 VYAHEREApylegekpYPPPVRLGLLGLLSPLL----PVKPVPVDRTLEDGDTLDLAGGLRVIHtPG---------HTPG 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516959197 184 SQfVVIRNdgqrtsEDSFVITGDLVYRMENLNGGEPAdPFYrpvgmgigsqTNMVFALDAIVKAAGDDPGRVVPPH 259
Cdd:cd07721  144 HI-SLYLE------EDGVLIAGDALVTVGGELVPPPP-PFT----------WDMEEALESLRKLAELDPEVLAPGH 201
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 40-119 1.14e-13

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: 69.21  E-value: 1.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  40 LLKSDEHTILIDCGHDDaahGKFlaDRSGVVNFAAPRDV-----LAEIGMTPGDIDHVIITHAHFDHMGGLA-------- 106
Cdd:cd07728   47 LIQYQGKNYLIDAGIGN---GKL--TEKQKRNFGVTEESsieesLAELGLTPEDIDYVLMTHLHFDHASGLTkvkgeqlv 121

                         90
                 ....*....|....
gi 516959197 107 -LFLNAKFYIQEAE 119
Cdd:cd07728  122 sVFPNATIYVSEIE 135
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 17-260 6.62e-13

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: 66.91  E-value: 6.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  17 MPLSALVYGEHNKgTCKLPYAYTLLK-SDEHTILIDCG----HDDAAHGKFLADRSGVVNFAAPRDV---LAEIGMTPGD 88
Cdd:cd07730    5 LPERLVLRGGPLK-RVTFPALAFLIEhPTGGKILFDLGyrkdFEEYTPRVPERLYRTPVPLEVEEDVaeqLAAGGIDPED 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  89 IDHVIITHAHFDHMGGLALFLNAKFYIQEAELS--------RWIWAMSLDRRF-----RWLMRTTDPADII---RCVELA 152
Cdd:cd07730   84 IDAVILSHLHWDHIGGLSDFPNARLIVGPGAKEalrppgypSGFLPELLPSDFegrlvRWEEDDFLWVPLGpfpRALDLF 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 153 RDGRLVAVNgdmedvFPGidlrlaadtHTPGSQFVVIrndgqRTSEDSFV-ITGDLVYRMENLNGGEPADPFYRPVGMGI 231
Cdd:cd07730  164 GDGSLYLVD------LPG---------HAPGHLGLLA-----RTTSGTWVfLAGDACHHRIGLLRPSPLLPLPDLDDGAD 223

                        250       260
                 ....*....|....*....|....*....
gi 516959197 232 GSQTNMvfALDAIVKAAGDDPGRVVPPHE 260
Cdd:cd07730  224 REAARE--TLARLRELDAAPDVRVVLAHD 250
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 40-171 2.00e-11

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293799  Cd Length: 269  Bit Score: 63.02  E-value: 2.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  40 LLKSDEHTILIDCGHDDAahgkFL--ADRSGVvnfaaprDvlaeigmtPGDIDHVIITHAHFDHMGGLALFL----NAKF 113
Cdd:cd07713   24 LIETEGKKILFDTGQSGV----LLhnAKKLGI-------D--------LSDIDAVVLSHGHYDHTGGLKALLelnpKAPV 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 516959197 114 YIQEAelsrwiwamSLDRRFRWLMRTTDPADIIRCVELARDGRLVAVNGDMEdVFPGI 171
Cdd:cd07713   85 YAHPD---------AFEPRYSKRGGGKKGIGIGREELEKAGARLVLVEEPTE-IAPGV 132
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 40-207 3.30e-10

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: 58.24  E-value: 3.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  40 LLKSDEHTILIDCGhddaahgKFLADRSGVVNFAAPrdvlaeIGMTPGDIDHVIITHAHFDHMGGL----ALFLNAKFYI 115
Cdd:cd16295   16 LLETGGKRILLDCG-------LFQGGKELEELNNEP------FPFDPKEIDAVILTHAHLDHSGRLpllvKEGFRGPIYA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 116 QEA--ELSRWIWA-----MSLDRRFRWLMRTTDPADIIRCVElardgRLVAVN-GDMEDVFPGIDLRL--AAdtHTPGSQ 185
Cdd:cd16295   83 TPAtkDLAELLLLdsakiQEEEAEHPPAEPLYTEEDVEKALK-----HFRPVEyGEPFEIGPGVKVTFydAG--HILGSA 155

                        170       180
                 ....*....|....*....|..
gi 516959197 186 FVVIRNDGQRTsedsFVITGDL 207
Cdd:cd16295  156 SVELEIGGGKR----ILFSGDL 173
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 39-206 5.95e-10

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


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 57.27  E-value: 5.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  39 TLLKSDEHTILIDCGhddaahgkfladrSGVVNFaaprdvLAEIGMTPGDIDHVIITHAHFDHMGGLALFLNAKFYIQE- 117
Cdd:cd16272   20 YLLETGGTRILLDCG-------------EGTVYR------LLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYGGRk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 118 --------AELSRWIwaMSLDRRFRWLMRTTDPADIIrcvELARDGRlvavngdmedVFPGIDLRL-AADT-HTPGSQFV 187
Cdd:cd16272   81 kpltiygpKGIKEFL--EKLLNFPVEILPLGFPLEIE---ELEEGGE----------VLELGDLKVeAFPVkHSVESLGY 145

                        170
                 ....*....|....*....
gi 516959197 188 VIRNDGQrtsedSFVITGD 206
Cdd:cd16272  146 RIEAEGK-----SIVYSGD 159
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 40-207 8.49e-10

Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; CPSF3 (cleavage and polyadenylation specificity factor subunit 3; also known as cleavage and polyadenylation specificity factor 73 kDa subunit, CPSF-73) and CPSF2 (also known as cleavage and polyadenylation specificity factor 100 kDa subunit /CPSF-100) are components of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. CPSF3 functions as a 3' endonuclease. Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)), and Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74) are subunits of Integrator, a metazoan-specific multifunctional protein complex composed of 14 subunits. Integrator has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 56.96  E-value: 8.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  40 LLKSDEHTILIDCGHDdaaHGKfladrsgvVNFAAPrdvLAEIGMTPGDIDHVIITHAHFDHMGGLA-LFLNAKF----Y 114
Cdd:cd07734   15 LVEFKGRTVLLDCGMN---PGK--------EDPEAC---LPQFELLPPEIDAILISHFHLDHCGALPyLFRGFIFrgpiY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 115 IQEAELSRWIWAMSLDRRFR----WLMRTTDPADIIRCVelardGRLVAVN-GDMEDVFPGIDLRLAADTHTPGSQFVVI 189
Cdd:cd07734   81 ATHPTVALGRLLLEDYVKSAerigQDQSLYTPEDIEEAL-----KHIVPLGyGQSIDLFPALSLTAYNAGHVLGAAMWEI 155

                        170
                 ....*....|....*...
gi 516959197 190 RNDGQrtsedSFVITGDL 207
Cdd:cd07734  156 QIYGE-----KLVYTGDF 168
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 40-207 1.13e-09

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 58.66  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  40 LLKSDEHTILIDCGhddaahgkfladrsgvVNFAAPRDVLAEIGMTPGDIDHVIITHAHFDHMGGL----ALFLNAKFYI 115
Cdd:COG1236   18 LLETGGTRILIDCG----------------LFQGGKERNWPPFPFRPSDVDAVVLTHAHLDHSGALpllvKEGFRGPIYA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 116 QEA--ELSRWIW--AMSLDRRFRWLMRTTDPADIIRCVElardgRLVAVNGDMEDVFPGIDLRL--AAdtHTPGSQFVVI 189
Cdd:COG1236   82 TPAtaDLARILLgdSAKIQEEEAEAEPLYTEEDAERALE-----LFQTVDYGEPFEIGGVRVTFhpAG--HILGSAQVEL 154

                        170
                 ....*....|....*...
gi 516959197 190 RNDGQRtsedsFVITGDL 207
Cdd:COG1236  155 EVGGKR-----IVFSGDY 167
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 40-115 2.81e-09

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 55.96  E-value: 2.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  40 LLKSDEHTILIDCGHDdaahgkfladrsgvVNFAAPRDVLAEIGMTPGDIDHVIITHAHFDHMGGLALFL----NAKFYI 115
Cdd:cd07726   20 LLDGEGRPALIDTGPS--------------SSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLAealpNAKVYV 85
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
40-111 9.48e-09

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 54.82  E-value: 9.48e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516959197  40 LLKSDEHTILIDCGhddaahgkfladrSGVVnfaaprDVLAEIGMTPGDIDHVIITHAHFDHMGGLALFLNA 111
Cdd:COG1234   23 LLEAGGERLLIDCG-------------EGTQ------RQLLRAGLDPRDIDAIFITHLHGDHIAGLPGLLST 75
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 40-119 1.08e-08

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 54.90  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  40 LLKSDEHTILIDCGHDDAAhGKFLADRsgvvnfaaprdvLAEIGMTPGDIDHVIITHAHFDHMGGLALF---LNAKFYIQ 116
Cdd:cd16280   26 AIDTGDGLILIDALNNNEA-ADLIVDG------------LEKLGLDPADIKYILITHGHGDHYGGAAYLkdlYGAKVVMS 92


                 ...
gi 516959197 117 EAE 119
Cdd:cd16280   93 EAD 95
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 39-111 2.41e-08

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: 52.52  E-value: 2.41e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516959197  39 TLLKSDEHTILIDCGhddaahGKFLADRSGVVNFAAPRDVLaeigmtpgDIDHVIITHAHFDHMGGLALFLNA 111
Cdd:cd07731   13 ILIQTPGKTILIDTG------PRDSFGEDVVVPYLKARGIK--------KLDYLILTHPDADHIGGLDAVLKN 71
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 39-111 3.73e-08

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


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 52.52  E-value: 3.73e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516959197  39 TLLKSDEHTILIDCGhddaahgkfladrSGVVNfaapRdvLAEIGMTPGDIDHVIITHAHFDHMGGL-ALFLNA 111
Cdd:cd07719   21 TLVVVGGRVYLVDAG-------------SGVVR----R--LAQAGLPLGDLDAVFLTHLHSDHVADLpALLLTA 75
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 39-116 5.15e-08

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 52.98  E-value: 5.15e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516959197  39 TLLKSDEHTILIDCGHDdaahgkfladrsgvvnfaaPRDVLAEIGMTPGDIDHVIITHAHFDHMGGLALFlnAKFYIQ 116
Cdd:COG1235   38 ILVEADGTRLLIDAGPD-------------------LREQLLRLGLDPSKIDAILLTHEHADHIAGLDDL--RPRYGP 94
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 40-117 7.25e-08

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: 51.53  E-value: 7.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  40 LLKSDEHTILIDCGHDDAAHGKFLADRsgvvnfaaprdvLAEIGMTPGDIDHVIITHAHFDHMGGLALF---LNAKFYIQ 116
Cdd:cd07725   19 LLRDGDETTLIDTGLATEEDAEALWEG------------LKELGLKPSDIDRVLLTHHHPDHIGLAGKLqekSGATVYIL 86


                 .
gi 516959197 117 E 117
Cdd:cd07725   87 D 87
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 76-259 1.37e-07

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 51.03  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  76 RDVLAEI-GMTPGDIDHVIITHAHFDHMGGLALFLNakfyiQEAElsrwIWAMSLDRRfrwLMRTTDPADIIRCVELARD 154
Cdd:cd16282   39 RALLAAIrKVTDKPVRYVVNTHYHGDHTLGNAAFAD-----AGAP----IIAHENTRE---ELAARGEAYLELMRRLGGD 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 155 G----RLVA----VNGDMEDVFPGIDLRLAA--DTHTPGSQFVVIRNDGqrtsedsFVITGDLVYrmenlNGgepadpfy 224
Cdd:cd16282  107 AmagtELVLpdrtFDDGLTLDLGGRTVELIHlgPAHTPGDLVVWLPEEG-------VLFAGDLVF-----NG-------- 166

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 516959197 225 RPVGMGIGSQTNMVFALDAIVKAagdDPGRVVPPH 259
Cdd:cd16282  167 RIPFLPDGSLAGWIAALDRLLAL---DATVVVPGH 198
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
40-112 1.60e-07

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 51.42  E-value: 1.60e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516959197  40 LLKSDEHTILIDCGHDDAahgkFLAdrsgvvNFAAprdvlaeIGMTPGDIDHVIITHAHFDHMGGLALFLNAK 112
Cdd:COG1237   26 LIETEGKRILFDTGQSDV----LLK------NAEK-------LGIDLSDIDAVVLSHGHYDHTGGLPALLELN 81
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 73-210 4.58e-07

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: 49.27  E-value: 4.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  73 AAPRDVLAEIGMTPGDIDHVIITHAHFDHMGGLALF---LNAKFYIQEAELSRWIWAMSLDRRFRWLMRTTDPADIircv 149
Cdd:cd16322   31 DESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLrrhPGAPVYLHPDDLPLYEAADLGAKAFGLGIEPLPPPDR---- 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516959197 150 eLARDGRLVAVNGDMEDVF--PGidlrlaadtHTPGS-QFVVirndgqrtSEDSFVITGDLVYR 210
Cdd:cd16322  107 -LLEDGQTLTLGGLEFKVLhtPG---------HSPGHvCFYV--------EEEGLLFSGDLLFQ 152
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 39-106 7.43e-07

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: 49.47  E-value: 7.43e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516959197  39 TLLKS-DEHTILIDCGHDDAahgkFLADRSGVVNFaaprdvLAEIGMTpgDIDHVIITHAHFDHMGGLA 106
Cdd:COG2333   14 ILIRTpDGKTILIDTGPRPS----FDAGERVVLPY------LRALGIR--RLDLLVLTHPDADHIGGLA 70
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 40-120 2.44e-06

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


Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 47.62  E-value: 2.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  40 LLKSDEHTILIDCG--HDDAAH-----GKFLADRSGVV---NFAAPRDVLAeIGMTPGDIDHVIITHAHFDHMGGLALFL 109
Cdd:cd07742   23 LVETDDGLVLVDTGfgLADVADpkrrlGGPFRRLLRPRldeDETAVRQIEA-LGFDPSDVRHIVLTHLDLDHAGGLADFP 101

                         90
                 ....*....|.
gi 516959197 110 NAKFYIQEAEL 120
Cdd:cd07742  102 HATVHVHAAEL 112
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 40-105 1.45e-05

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: 44.77  E-value: 1.45e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516959197  40 LLKSDEHTILIDCGHD--DAAHgkfladRSGVvnfaaprdvlaeigmtpGDIDHVIITHAHFDHMGGL 105
Cdd:cd16279   39 LIETGGKNILIDTGPDfrQQAL------RAGI-----------------RKLDAVLLTHAHADHIHGL 83
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 29-108 1.86e-05

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: 43.79  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  29 KGTCklpyayTLLKSDEHTILIDCGhddaahgkfladrsgvVNFAAPRDVLAEIGMTPGDIDHVIITHAHFDHMGGLALF 108
Cdd:cd07733    8 KGNC------TYLETEDGKLLIDAG----------------LSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVL 65
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 38-113 2.27e-05

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 44.17  E-value: 2.27e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516959197  38 YTLLKSDEHTILIDCGhddaahgkfladRSGVVNfaaprdvLAEIGMTPGDIDHVIITHAHFDHMGGLALF-LNAKF 113
Cdd:cd07740   18 CFHVASEAGRFLIDCG------------ASSLIA-------LKRAGIDPNAIDAIFITHLHGDHFGGLPFFlLDAQF 75
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 76-224 3.12e-05

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: 43.68  E-value: 3.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  76 RDVLAEIGMTPGDIDHVIITHAHFDHMGGLALFL---NAKFYIQEAELSrwIWAMSLDRrfrwlMRTTDPADIIRCvela 152
Cdd:cd16275   35 EKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLakyDAPVYMSKEEID--YYGFRCPN-----LIPLEDGDTIKI---- 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 153 rdgrlvavnGDMEDVF---PGidlrlaadtHTPGSQ-FVVirndgqrtseDSFVITGDLVYrME-----NLNGGEPADPF 223
Cdd:cd16275  104 ---------GDTEITClltPG---------HTPGSMcYLL----------GDSLFTGDTLF-IEgcgrcDLPGGDPEEMY 154


                 .
gi 516959197 224 Y 224
Cdd:cd16275  155 E 155
CPSF2-like_MBL-fold cd16293
cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; ...
 39-114 4.68e-05

cleavage and polyadenylation specificity factor (CPSF) subunit 2 and related proteins; MBL-fold metallo-hydrolase domain; CPSF2, also known as cleavage and polyadenylation specificity factor 100 kDa subunit (CPSF-100), is a component of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. This subgroup includes Ydh1p, the yeast homolog of CPSF2. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain. 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: 293851  Cd Length: 199  Bit Score: 43.28  E-value: 4.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  39 TLLKSDEHTILIDCGHDDAAHGKFLadrsgvvnfaaprDVLAEIGMTpgdIDHVIITHAHFDHMGGLA-----LFLNAKF 113
Cdd:cd16293   15 YLLEIDDVTILLDCGWDESFDMEYL-------------ESLKRIAPT---IDAVLLSHPDLEHLGALPylvgkLGLTCPV 78


                 .
gi 516959197 114 Y 114
Cdd:cd16293   79 Y 79
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 40-102 5.40e-05

uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. Members of this bacterial subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 42.81  E-value: 5.40e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516959197  40 LLKSDEHTILIDCGhddaahgkfladrSGVvnFAAprdvLAEIgMTPGDIDHVIITHAHFDHM 102
Cdd:cd07716   22 LLEADGFRILLDCG-------------SGV--LSR----LQRY-IDPEDLDAVVLSHLHPDHC 64
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 48-106 6.42e-05

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: 42.91  E-value: 6.42e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  48 ILIDCGhddaahgkfladrSGVVNF-AAPRDVLAEIGMTPgdIDHVIITHAHFDHMGGLA 106
Cdd:cd07722   30 ILIDTG-------------EGRPSYiPLLKSVLDSEGNAT--ISDILLTHWHHDHVGGLP 74
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 76-209 7.99e-05

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: 42.62  E-value: 7.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  76 RDVLAEIGMTPGDIDH-----------VIITHAHFDHMGGLALFlnAKFYIQEAELSrWIWAMSLDRRFRWLMRTT--DP 142
Cdd:cd07712   19 RALLIDTGLGIGDLKEyvrtltdlpllVVATHGHFDHIGGLHEF--EEVYVHPADAE-ILAAPDNFETLTWDAATYsvPP 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516959197 143 ADIIRCVelaRDGRLVAVNGDMEDVF--PGidlrlaadtHTPGSQFVVIRNDGqrtsedsFVITGDLVY 209
Cdd:cd07712   96 AGPTLPL---RDGDVIDLGDRQLEVIhtPG---------HTPGSIALLDRANR-------LLFSGDVVY 145
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 40-103 1.58e-04

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 42.21  E-value: 1.58e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516959197  40 LLKSDEHTILIDcghddaahgKFLADRSGVVNfaaPRDVLAEigmTPGDIDHVIITHAHFDHMG 103
Cdd:COG2220   15 LIETGGKRILID---------PVFSGRASPVN---PLPLDPE---DLPKIDAVLVTHDHYDHLD 63
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 46-105 1.92e-04

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: 41.53  E-value: 1.92e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197   46 HTILIDCGHDDAAHgkfladrsgvvnfAAPRDVLAEIGMTPgdIDHVIITHAHFDHMGGL 105
Cdd:pfam12706   1 RRILIDPGPDLRQQ-------------ALPALQPGRLRDDP--IDAVLLTHDHYDHLAGL 45
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 40-119 2.22e-04

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: 41.92  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  40 LLKSDEHTILIDCGHDDAAhgkfladrsgvvnfaaP--RDVLAEIGMTPGDIDHVIITHAHFDHMGGLALF---LNAKFY 114
Cdd:cd16288   26 LITTPQGLILIDTGLESSA----------------PmiKANIRKLGFKPSDIKILLNSHAHLDHAGGLAALkklTGAKLM 89


                 ....*
gi 516959197 115 IQEAE 119
Cdd:cd16288   90 ASAED 94
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 30-184 2.57e-04

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: 41.57  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  30 GTCKLpyAYTLLKSDEHTILIDCGHDDAAhgkfladrsgvvnfaapRDVLAEI---GMTPGDIDHVIITHAHFDHMGGLA 106
Cdd:cd16315   18 GTCGI--SAILITGDDGHVLIDSGTEEAA-----------------PLVLANIrklGFDPKDVRWLLSSHEHFDHVGGLA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197 107 LflnakfyIQEAELSRwIWAMSLDRRfrwLMRT--TDPAD----IIRCVELARDGRLVAvngDMEDVFPGiDLRLAADT- 179
Cdd:cd16315   79 A-------LQRATGAR-VAASAAAAP---VLESgkPAPDDpqagLHEPFPPVRVDRIVE---DGDTVALG-SLRLTAHAt 143


                 ....*..
gi 516959197 180 --HTPGS 184
Cdd:cd16315  144 pgHTPGA 150
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 40-108 4.42e-04

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 40.17  E-value: 4.42e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516959197  40 LLKSDEHTILIDCGHDDAAHgkfLadrsgvvnfaapRDVLAEIGmtPGDIDHVIITHAHFDHMGGLALF 108
Cdd:cd16278   22 LLGAPDGVVVIDPGPDDPAH---L------------DALLAALG--GGRVSAILVTHTHRDHSPGAARL 73
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 41-108 5.40e-04

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 40.21  E-value: 5.40e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516959197  41 LKSDEHTILIDCGHDDAAHGKfladrsgvvnfaaPRDVLAEIGMTPgdiDHVIITHAHFDHMGGLALF 108
Cdd:cd07743   14 VFGDKEALLIDSGLDEDAGRK-------------IRKILEELGWKL---KAIINTHSHADHIGGNAYL 65
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 40-106 7.28e-04

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


Pssm-ID: 293868  Cd Length: 252  Bit Score: 40.13  E-value: 7.28e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516959197  40 LLKSDEHTILIDCGHDDAAHgkfladrsgvvnfAAPRDVLAeIGMTPGDIDHVIITHAHFDHMGGLA 106
Cdd:cd16310   26 LITSNHGAILLDGGLEENAA-------------LIEQNIKA-LGFKLSDIKIIINTHAHYDHAGGLA 78
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 76-107 8.57e-04

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: 40.22  E-value: 8.57e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 516959197  76 RDVLAEIGMTPGDIDHVIITHAHFDHMGGLAL 107
Cdd:cd07708   48 KANIKKLGFKFSDTKLILISHAHFDHAGGSAE 79
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 89-107 1.04e-03

class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. 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: 293821  Cd Length: 259  Bit Score: 39.89  E-value: 1.04e-03
                         10
                 ....*....|....*....
gi 516959197  89 IDHVIITHAHFDHMGGLAL 107
Cdd:cd07735   66 IRHYLITHAHLDHIAGLPL 84
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 15-106 1.11e-03

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: 39.87  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  15 PEMPLSalVYGEH-NKGTCKLpyAYTLLKSDEHTILIDcghddaahgkfladrsGVVNFAAPRdVLAEI---GMTPGDID 90
Cdd:cd16314    4 PAPPRR--IYGNTwYVGTCGI--SALLVTSDAGHILID----------------GGTDKAAPL-IEANIralGFRPEDVR 62

                         90
                 ....*....|....*.
gi 516959197  91 HVIITHAHFDHMGGLA 106
Cdd:cd16314   63 YIVSSHEHFDHAGGIA 78
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 ...
 15-106 1.47e-03

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: 39.25  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516959197  15 PEMPLSalVYGE-HNKGTCKLPYAytLLKSDEHTILIDcghddaahgkfladrsGVVNFAAPRdVLAEI---GMTPGDID 90
Cdd:cd16290    4 PQAPFR--IHGNtYYVGTGGLSAV--LITSPQGLILID----------------GALPQSAPQ-IEANIralGFRLEDVK 62

                         90
                 ....*....|....*.
gi 516959197  91 HVIITHAHFDHMGGLA 106
Cdd:cd16290   63 LILNSHAHFDHAGGIA 78
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
42-107 1.88e-03

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 39.17  E-value: 1.88e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516959197  42 KSDEHTILIDCGhdDAAHGKFLADRSGVvnFAAPRDVLAEigmtpgDIDHVIITHAHFDHMGGLAL 107
Cdd:COG5212   36 LGSDDYVLLDAG--TVVSGLELAEQKGA--FKGRQGYVLE------HIKGYLISHAHLDHIAGLPI 91
NorV COG0426
Flavorubredoxin [Energy production and conversion];
44-115 2.11e-03

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 39.43  E-value: 2.11e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 516959197  44 DEHTILIDCGHDDAAHgKFLADRSGVVNfaaprdvlaeigmtPGDIDHVIITHAHFDHMGGLALFL----NAKFYI 115
Cdd:COG0426   41 DEKTALIDTVGESFFE-EFLENLSKVID--------------PKKIDYIIVNHQEPDHSGSLPELLelapNAKIVC 101
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 62-108 2.42e-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: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 38.33  E-value: 2.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516959197  62 FLADRSGVVNFAAPRD----VLAEIGM-TPGDIDHVIITHAHFDHMGGLALF 108
Cdd:cd16276   14 FLVTDKGVIVVDAPPSlgenLLAAIRKvTDKPVTHVVYSHNHADHIGGASIF 65
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 77-106 3.16e-03

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: 38.23  E-value: 3.16e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 516959197  77 DVLAEIGMTPGDIDHVIITHAHFDHMGGLA 106
Cdd:cd16309   49 DNIKKLGFDVKDVKYLLNTHAHFDHAGGLA 78
INTS11-like_MBL-fold cd16291
Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; ...
 47-108 3.79e-03

Integrator complex subunit 11, and related proteins; MBL-fold metallo-hydrolase domain; Integrator is a metazoan-specific multisubunit, multifunctional protein complex composed of 14 subunits named Int1-Int14 (Integrator subunits). This subgroup includes Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)). Integrator complex has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293849  Cd Length: 199  Bit Score: 37.63  E-value: 3.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516959197  47 TILIDCGhddaAHGKFLADRSgVVNFaaprDVLAEIGMTPGDIDHVIITHAHFDHMGGLALF 108
Cdd:cd16291   23 NIMFDCG----MHMGYNDERR-FPDF----SYISQNGPFTEHIDCVIISHFHLDHCGALPYF 75
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 39-110 4.82e-03

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. 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: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 37.77  E-value: 4.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516959197  39 TLLKSDEHTILIDCGHddaahgKFLADRSGVVNFAAPR-DVLAEIGmtpGDIDHVIITHAHFDHMGGLALFLN 110
Cdd:cd07714   14 YVVEYDDDIIIIDCGL------KFPDEDMPGVDYIIPDfSYLEENK---DKIKGIFITHGHEDHIGALPYLLP 77
Lactamase_B_6 pfam16661
Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase ...
 40-111 4.87e-03

Metallo-beta-lactamase superfamily domain; This family is part of the metallo-beta-lactamase superfamily.


Pssm-ID: 406948  Cd Length: 192  Bit Score: 37.19  E-value: 4.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516959197   40 LLKSDEHTILIDCGHDDaahgkfladrsgvvnFAAPRDVLAEIGMTPGDIDHVIITHAHFDHMGGLALFLNA 111
Cdd:pfam16661   1 LLEFDNVRILLDPGWDG---------------SFSYESDLKYLEKILPEVDLILLSHPTLEHLGAYPLLYYK 57
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
88-109 6.44e-03

mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 37.73  E-value: 6.44e-03
                         10        20
                 ....*....|....*....|..
gi 516959197  88 DIDHVIITHAHFDHMGGLALFL 109
Cdd:COG0595   63 KIKGIVLTHGHEDHIGALPYLL 84
 
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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