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Conserved domains on  [gi|520903000|ref|WP_020325045|]
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MULTISPECIES: N-acyl homoserine lactonase AttM [Klebsiella]

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 ...
 6-250 2.13e-76

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: 231.72  E-value: 2.13e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000   6 KLFMFQSGTQHCRYQHI-RMNQGVGEHYEIPVPWFLLTHPDGFTLIDGGLAVEGLKDpsgyWGSAVEQFKPVMSEEQGCV 84
Cdd:cd07729    1 KLYALDYGTVTVDKSSLfYYGRGPGEPIDLPVYAYLIEHPEGTILVDTGFHPDAADD----PGGLELAFPPGVTEEQTLE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  85 EQLKRIGIAPEDIRYVVLSHLHSDHTGAIGRFPHATHVVQRQEYEYAFAPDWFTSGAY---CRRDFDRPQLNWLFLNGls 161
Cdd:cd07729   77 EQLARLGLDPEDIDYVILSHLHFDHAGGLDLFPNATIIVQRAELEYATGPDPLAAGYYedvLALDDDLPGGRVRLVDG-- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 162 ddHYDLYgdGTLQCIFTPGHSPGHQSFIIRLPGGTnFTLAIDAAYTLDHYHEKALPGLMTSATDVAQSVRKLRQLTERYH 241
Cdd:cd07729  155 --DYDLF--PGVTLIPTPGHTPGHQSVLVRLPEGT-VLLAGDAAYTYENLEEGRPPGINYDPEAALASLERLKALAEREG 229


                 ....*....
gi 520903000 242 AVFIPGHDP 250
Cdd:cd07729  230 ARVIPGHDP 238
 
Name Accession Description Interval E-value
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 6-250 2.13e-76

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: 231.72  E-value: 2.13e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000   6 KLFMFQSGTQHCRYQHI-RMNQGVGEHYEIPVPWFLLTHPDGFTLIDGGLAVEGLKDpsgyWGSAVEQFKPVMSEEQGCV 84
Cdd:cd07729    1 KLYALDYGTVTVDKSSLfYYGRGPGEPIDLPVYAYLIEHPEGTILVDTGFHPDAADD----PGGLELAFPPGVTEEQTLE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  85 EQLKRIGIAPEDIRYVVLSHLHSDHTGAIGRFPHATHVVQRQEYEYAFAPDWFTSGAY---CRRDFDRPQLNWLFLNGls 161
Cdd:cd07729   77 EQLARLGLDPEDIDYVILSHLHFDHAGGLDLFPNATIIVQRAELEYATGPDPLAAGYYedvLALDDDLPGGRVRLVDG-- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 162 ddHYDLYgdGTLQCIFTPGHSPGHQSFIIRLPGGTnFTLAIDAAYTLDHYHEKALPGLMTSATDVAQSVRKLRQLTERYH 241
Cdd:cd07729  155 --DYDLF--PGVTLIPTPGHTPGHQSVLVRLPEGT-VLLAGDAAYTYENLEEGRPPGINYDPEAALASLERLKALAEREG 229


                 ....*....
gi 520903000 242 AVFIPGHDP 250
Cdd:cd07729  230 ARVIPGHDP 238
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 38-248 6.67e-19

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: 81.45  E-value: 6.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000    38 WFLLTHPDGFTLIDgglaveglkdpsgywgsaveqfkPVMSEEQGCVEQLKRIGiaPEDIRYVVLSHLHSDHTGAIGRFP 117
Cdd:smart00849   2 SYLVRDDGGAILID-----------------------TGPGEAEDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPELL 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000   118 HATHV---VQRQEYEYAFAPDWFTSGAYcrrDFDRPQLNWLFLNglSDDHYDLyGDGTLQCIFTPGHSPGHQSFIIRlpg 194
Cdd:smart00849  57 EAPGApvyAPEGTAELLKDLLALLGELG---AEAEPAPPDRTLK--DGDELDL-GGGELEVIHTPGHTPGSIVLYLP--- 127

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 520903000   195 GTNFTLAIDAAYTldhyHEKALPGLMTSATDVAQSVRKLRQLTERYHAVFIPGH 248
Cdd:smart00849 128 EGKILFTGDLLFA----GGDGRTLVDGGDAAASDALESLLKLLKLLPKLVVPGH 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 39-250 2.47e-18

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: 80.89  E-value: 2.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  39 FLLTHPDGFTLIDGGLAVEGLKDPsgywgsaveqfkpvmseeqgcVEQLKRIGiapEDIRYVVLSHLHSDHTGAIGRFP- 117
Cdd:COG0491   18 YLIVGGDGAVLIDTGLGPADAEAL---------------------LAALAALG---LDIKAVLLTHLHPDHVGGLAALAe 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 118 --HATHVVQRQEYEYAFAPDWFTSGAYCRRDFDRPqlnwlflngLSD-DHYDLyGDGTLQCIFTPGHSPGHQSFIIRlpg 194
Cdd:COG0491   74 afGAPVYAHAAEAEALEAPAAGALFGREPVPPDRT---------LEDgDTLEL-GGPGLEVIHTPGHTPGHVSFYVP--- 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 520903000 195 GTNFTLAIDAAYTLDHYHEKALPGlmtSATDVAQSVRKLRQLTERyhaVFIPGHDP 250
Cdd:COG0491  141 DEKVLFTGDALFSGGVGRPDLPDG---DLAQWLASLERLLALPPD---LVIPGHGP 190
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
35-248 4.49e-18

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 79.72  E-value: 4.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000   35 PVPWFLLTHPDGFTLIDGGlaveglkdpsgywgsaveqfkpvMSEEQGCVEQLKRIGIAPEDIRYVVLSHLHSDHTGAIG 114
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTG-----------------------GSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLG 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  115 RFPHATHVVQRQEYEYAFAPDWFTSGAYCRRDFDRPQLNWLFLNGLSDDHYDLYGDGTLQCIFTPGHSPGHQSFIIRLPG 194
Cdd:pfam00753  62 ELAEATDVPVIVVAEEARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGG 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 520903000  195 GtNFTLAIDAAYTLDHYHEKALPGLMT--SATDVAQSVRKLRQLTERYHAVFIPGH 248
Cdd:pfam00753 142 G-KVLFTGDLLFAGEIGRLDLPLGGLLvlHPSSAESSLESLLKLAKLKAAVIVPGH 196
 
Name Accession Description Interval E-value
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 6-250 2.13e-76

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: 231.72  E-value: 2.13e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000   6 KLFMFQSGTQHCRYQHI-RMNQGVGEHYEIPVPWFLLTHPDGFTLIDGGLAVEGLKDpsgyWGSAVEQFKPVMSEEQGCV 84
Cdd:cd07729    1 KLYALDYGTVTVDKSSLfYYGRGPGEPIDLPVYAYLIEHPEGTILVDTGFHPDAADD----PGGLELAFPPGVTEEQTLE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  85 EQLKRIGIAPEDIRYVVLSHLHSDHTGAIGRFPHATHVVQRQEYEYAFAPDWFTSGAY---CRRDFDRPQLNWLFLNGls 161
Cdd:cd07729   77 EQLARLGLDPEDIDYVILSHLHFDHAGGLDLFPNATIIVQRAELEYATGPDPLAAGYYedvLALDDDLPGGRVRLVDG-- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 162 ddHYDLYgdGTLQCIFTPGHSPGHQSFIIRLPGGTnFTLAIDAAYTLDHYHEKALPGLMTSATDVAQSVRKLRQLTERYH 241
Cdd:cd07729  155 --DYDLF--PGVTLIPTPGHTPGHQSVLVRLPEGT-VLLAGDAAYTYENLEEGRPPGINYDPEAALASLERLKALAEREG 229


                 ....*....
gi 520903000 242 AVFIPGHDP 250
Cdd:cd07729  230 ARVIPGHDP 238
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 27-249 1.10e-31

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: 116.98  E-value: 1.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  27 GVGEHYEIPVPWFLLTHPDGFT-LIDGGLAveglKDPSGYWGSAVEQFK---PVMSEEQGCVEQLKRIGIAPEDIRYVVL 102
Cdd:cd07730   14 GPLKRVTFPALAFLIEHPTGGKiLFDLGYR----KDFEEYTPRVPERLYrtpVPLEVEEDVAEQLAAGGIDPEDIDAVIL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 103 SHLHSDHTGAIGRFPHATHVVQRQEYEYAFAPDWFT--SGAYCRRDFDRPQLNWLFLNGLS------DDHYDLYGDGTLQ 174
Cdd:cd07730   90 SHLHWDHIGGLSDFPNARLIVGPGAKEALRPPGYPSgfLPELLPSDFEGRLVRWEEDDFLWvplgpfPRALDLFGDGSLY 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 175 CIFTPGHSPGHQSFIIRLPGGTNFTLAIDAAYTLDH-YHEKALPGLMTSATDV-----AQSVRKLRQLTERYHAVFIPGH 248
Cdd:cd07730  170 LVDLPGHAPGHLGLLARTTSGTWVFLAGDACHHRIGlLRPSPLLPLPDLDDGAdreaaRETLARLRELDAAPDVRVVLAH 249


                 .
gi 520903000 249 D 249
Cdd:cd07730  250 D 250
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 38-248 6.67e-19

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: 81.45  E-value: 6.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000    38 WFLLTHPDGFTLIDgglaveglkdpsgywgsaveqfkPVMSEEQGCVEQLKRIGiaPEDIRYVVLSHLHSDHTGAIGRFP 117
Cdd:smart00849   2 SYLVRDDGGAILID-----------------------TGPGEAEDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPELL 56

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000   118 HATHV---VQRQEYEYAFAPDWFTSGAYcrrDFDRPQLNWLFLNglSDDHYDLyGDGTLQCIFTPGHSPGHQSFIIRlpg 194
Cdd:smart00849  57 EAPGApvyAPEGTAELLKDLLALLGELG---AEAEPAPPDRTLK--DGDELDL-GGGELEVIHTPGHTPGSIVLYLP--- 127

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 520903000   195 GTNFTLAIDAAYTldhyHEKALPGLMTSATDVAQSVRKLRQLTERYHAVFIPGH 248
Cdd:smart00849 128 EGKILFTGDLLFA----GGDGRTLVDGGDAAASDALESLLKLLKLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 40-242 1.35e-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) 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: 82.29  E-value: 1.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  40 LLTHPDGFTLIDGGLAVEGLKDP-SGYWGSAVEQFKPVMSEEQGCVEQLKRIGIAPEDIRYVVLSHLHSDHTGAIGRFPH 118
Cdd:cd07742   23 LVETDDGLVLVDTGFGLADVADPkRRLGGPFRRLLRPRLDEDETAVRQIEALGFDPSDVRHIVLTHLDLDHAGGLADFPH 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 119 AT-HVVQRqEYEYAFAP-DWFTSGAYCRRDFDRPQL---------NWLF------LNGLSDDhydlygdgtLQCIFTPGH 181
Cdd:cd07742  103 ATvHVHAA-ELDAATSPrTRYERRRYRPQQLAHGPWwvtyaaggeRWFGfeavrpLDGLPPE---------ILLVPLPGH 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 182 SPGHQSFIIRLPGGTNFtLAIDAAY---TLDHYHEKALPGLM---TSATDVAQ---SVRKLRQLTERYHA 242
Cdd:cd07742  173 TRGHCGVAVRTGDRWLL-HAGDAYFhhgELDPLPPPPPPLRLfqrLLAVDRSArlaNLARLRELARDHGD 241
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 39-250 2.47e-18

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: 80.89  E-value: 2.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  39 FLLTHPDGFTLIDGGLAVEGLKDPsgywgsaveqfkpvmseeqgcVEQLKRIGiapEDIRYVVLSHLHSDHTGAIGRFP- 117
Cdd:COG0491   18 YLIVGGDGAVLIDTGLGPADAEAL---------------------LAALAALG---LDIKAVLLTHLHPDHVGGLAALAe 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 118 --HATHVVQRQEYEYAFAPDWFTSGAYCRRDFDRPqlnwlflngLSD-DHYDLyGDGTLQCIFTPGHSPGHQSFIIRlpg 194
Cdd:COG0491   74 afGAPVYAHAAEAEALEAPAAGALFGREPVPPDRT---------LEDgDTLEL-GGPGLEVIHTPGHTPGHVSFYVP--- 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 520903000 195 GTNFTLAIDAAYTLDHYHEKALPGlmtSATDVAQSVRKLRQLTERyhaVFIPGHDP 250
Cdd:COG0491  141 DEKVLFTGDALFSGGVGRPDLPDG---DLAQWLASLERLLALPPD---LVIPGHGP 190
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 35-248 2.68e-18

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: 80.34  E-value: 2.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  35 PVPWFLLTHPDGFTLIDGGLAveglkdpsGYWGSAVEQfkpvmseeqgcveqLKRIGIAPEDIRYVVLSHLHSDHTGAIG 114
Cdd:cd07721   10 PVNAYLIEDDDGLTLIDTGLP--------GSAKRILKA--------------LRELGLSPKDIRRILLTHGHIDHIGSLA 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 115 RFPHATHV---VQRQEYEYA---FAPDWFTSGAYCRRDFD-RPQLNWLFLNGLSD-DHYDLYGDgtLQCIFTPGHSPGHQ 186
Cdd:cd07721   68 ALKEAPGApvyAHEREAPYLegeKPYPPPVRLGLLGLLSPlLPVKPVPVDRTLEDgDTLDLAGG--LRVIHTPGHTPGHI 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520903000 187 SFIIRLPGgtnftLAI--DAAYTLDHYHeKALPGLMTSATDVA-QSVRKLRQLterYHAVFIPGH 248
Cdd:cd07721  146 SLYLEEDG-----VLIagDALVTVGGEL-VPPPPPFTWDMEEAlESLRKLAEL---DPEVLAPGH 201
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
35-248 4.49e-18

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 79.72  E-value: 4.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000   35 PVPWFLLTHPDGFTLIDGGlaveglkdpsgywgsaveqfkpvMSEEQGCVEQLKRIGIAPEDIRYVVLSHLHSDHTGAIG 114
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTG-----------------------GSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLG 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  115 RFPHATHVVQRQEYEYAFAPDWFTSGAYCRRDFDRPQLNWLFLNGLSDDHYDLYGDGTLQCIFTPGHSPGHQSFIIRLPG 194
Cdd:pfam00753  62 ELAEATDVPVIVVAEEARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGG 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 520903000  195 GtNFTLAIDAAYTLDHYHEKALPGLMT--SATDVAQSVRKLRQLTERYHAVFIPGH 248
Cdd:pfam00753 142 G-KVLFTGDLLFAGEIGRLDLPLGGLLvlHPSSAESSLESLLKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 85-248 1.03e-17

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 79.10  E-value: 1.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  85 EQLKRIGIAPEDIRYVVLSHLHSDHTG-----AIGR----FPHATHVVQRQEYEYAFAPDwfTSGAYCRRDFDRPQLnWL 155
Cdd:cd16277   52 ERLAAAGVRPEDVDYVLCTHLHVDHVGwntrlVDGRwvptFPNARYLFSRAEYDHWSSPD--AGGPPNRGVFEDSVL-PV 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 156 FLNGL---SDDHYDLygDGTLQCIFTPGHSPGHQSFIIRLPGGTnftlAIDAAYTLDHYHEKALPGLMTSA-TDVAQSVR 231
Cdd:cd16277  129 IEAGLadlVDDDHEI--LDGIRLEPTPGHTPGHVSVELESGGER----ALFTGDVMHHPIQVARPDWSSVFdEDPAQAAA 202

                        170       180
                 ....*....|....*....|
gi 520903000 232 KLRQLTERY---HAVFIPGH 248
Cdd:cd16277  203 TRRRLLERAadtDTLLFPAH 222
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 48-250 9.09e-15

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: 70.69  E-value: 9.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  48 TLIDGGLAVEgLKDPSGYWGsaveqfkpvmseEQGCVEQLKRIGIAPEDIRYVVLSHLHSDHTGAIGRFPHATHVVQRQE 127
Cdd:cd07711   25 TLIKDGGKNI-LVDTGTPWD------------RDLLLKALAEHGLSPEDIDYVVLTHGHPDHIGNLNLFPNATVIVGWDI 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 128 YEYAFAP-DWFTSGAYcrrdfdrpqlnwlflnGLSDDhydlygdgtLQCIFTPGHSPGHQSFIIRlpgGTNF-TLAI--D 203
Cdd:cd07711   92 CGDSYDDhSLEEGDGY----------------EIDEN---------VEVIPTPGHTPEDVSVLVE---TEKKgTVAVagD 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 520903000 204 A-AYTLDHYHEKALPGLMTSATDVAQSVRKLRQLTEryhaVFIPGHDP 250
Cdd:cd07711  144 LfEREEDLEDPILWDPLSEDPELQEESRKRILALAD----WIIPGHGP 187
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 25-190 3.17e-14

Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold metallo hydrolase domain; Pseudomonas pseudoalcaligenes OPHC2 is a thermostable organophosphorus hydrolase which a broad substrate activity spectrum: it hydrolyzes various phosphotriesters, esters, and a lactone. This subgroup also includes Pseudomonas oleovorans PoOPH which exhibits high lactonase and esterase activities, and latent PTE activity. However, double mutations His250Ile/Ile263Trp switch PoOPH into an efficient and thermostable PTE. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293806 [Multi-domain]  Cd Length: 251  Bit Score: 70.27  E-value: 3.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  25 NQGVGEHYEIPVPWFLLTHPDGFTLIDGGLAveglkdpsGYWGSAVEQFkpvmseeqgcVEQLKRIGIAPEDIRYVVLSH 104
Cdd:cd07720   38 AFLPPDPVETSVNAFLVRTGGRLILVDTGAG--------GLFGPTAGKL----------LANLAAAGIDPEDIDDVLLTH 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 105 LHSDHTGAI------GRFPHATHVVQRQEYEYafapdWFTSGAYCRRDFDRPQLNWLFLNGLS--DDHYDLYGDGTL--- 173
Cdd:cd07720  100 LHPDHIGGLvdaggkPVFPNAEVHVSEAEWDF-----WLDDANAAKAPEGAKRFFDAARDRLRpyAAAGRFEDGDEVlpg 174

                        170
                 ....*....|....*...
gi 520903000 174 -QCIFTPGHSPGHQSFII 190
Cdd:cd07720  175 iTAVPAPGHTPGHTGYRI 192
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 87-190 3.54e-14

mainly hydrolytic enzymes and related proteins which carry out various biological functions; MBL-fold metallohydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) for which this fold was named perform only a small fraction of the activities included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases which can catalyze the hydrolysis of a wide range of beta-lactam antibiotics, hydroxyacylglutathione hydrolases (also called glyoxalase II) which hydrolyze S-d-lactoylglutathione to d-lactate in the second step of the glycoxlase system, AHL lactonases which catalyze the hydrolysis and opening of the homoserine lactone rings of acyl homoserine lactones (AHLs), persulfide dioxygenase which catalyze the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria, flavodiiron proteins which catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J which has both 5'-3' exoribonucleolytic and endonucleolytic activity and ribonuclease Z which catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors, cyclic nucleotide phosphodiesterases which decompose cyclic adenosine and guanosine 3', 5'-monophosphate (cAMP and cGMP) respectively, insecticide hydrolases, and proteins required for natural transformation competence. The diversity of biological roles is reflected in variations in the active site metallo-chemistry, for example classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, human persulfide dioxygenase ETHE1 is a mono-iron binding member of the superfamily; Arabidopsis thaliana hydroxyacylglutathione hydrolases incorporates iron, manganese, and zinc in its dinuclear metal binding site, and flavodiiron proteins contains a diiron site.


Pssm-ID: 293792 [Multi-domain]  Cd Length: 188  Bit Score: 68.85  E-value: 3.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  87 LKRIGIAPEDIRYVVLSHLHSDHTGAIGRF---PHATHVVQRQEYEYAFAPDWftSGAYCRRDFDRPQLNWLFLNGlsDD 163
Cdd:cd06262   36 LEAIEELGLKIKAILLTHGHFDHIGGLAELkeaPGAPVYIHEADAELLEDPEL--NLAFFGGGPLPPPEPDILLED--GD 111

                         90       100
                 ....*....|....*....|....*..
gi 520903000 164 HYDLyGDGTLQCIFTPGHSPGHQSFII 190
Cdd:cd06262  112 TIEL-GGLELEVIHTPGHTPGSVCFYI 137
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 84-196 2.81e-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.


Pssm-ID: 293839  Cd Length: 252  Bit Score: 67.52  E-value: 2.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  84 VEQLKRIGIAPEDIRYVVLSHLHSDHTGAIGR----------FPHATHVVQRQEYEYAFAPDwftsgaycRRD---FDRP 150
Cdd:cd16281   82 LKSLARLGLSPEDITDVILTHLHFDHCGGATRadddglvellFPNATYWVQKRHWEWALNPN--------PRErasFLPE 153

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 520903000 151 QLNWLFLNG---LSDDHYDLYGDGtLQCIFTPGHSPGHQSFIIRLPGGT 196
Cdd:cd16281  154 NIEPLEESGrlkLIDGSDAELGPG-IRFHLSDGHTPGQMLPEISTPGGT 201
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 79-192 4.10e-11

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: 61.51  E-value: 4.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  79 EEQGCVEQLKRIGIAPEDIRYVVLSHLHSDHTGAIGR---------FPHATHVVQRQEYEYAFAPDWFTSGAYcrrdfdr 149
Cdd:cd07728   78 EESSIEESLAELGLTPEDIDYVLMTHLHFDHASGLTKvkgeqlvsvFPNATIYVSEIEWEEMRNPNIRSKNTY------- 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 520903000 150 PQLNWLFLNGL----SDDHYDLYGdgtLQCIFTPGHSPGHQsfIIRL 192
Cdd:cd07728  151 WKENWEPIEDQvktfSDEIEIVPG---ITMIHTGGHSDGHS--IIEI 192
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 35-188 3.17e-09

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


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 55.00  E-value: 3.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  35 PVPWFLLTHPDGFTLIDGGLAVEGlkdpsgywgsaveqfkpvmsEEQGCVEQLKRIGIAPEDIRYVVLSHLHSDHTGAIG 114
Cdd:cd07725   14 HVNVYLLRDGDETTLIDTGLATEE--------------------DAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAG 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520903000 115 RFphathvvqrqeyeyafapdwftsgaycrRDFDRPQLNWLFLNGLSDDHYDLYGDGTLQCIFTPGHSPGHQSF 188
Cdd:cd07725   74 KL----------------------------QEKSGATVYILDVTPVKDGDKIDLGGLRLKVIETPGHTPGHIVL 119
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 39-195 7.91e-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: 54.42  E-value: 7.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  39 FLLTHPDGFTLIDGGLAveglkdpsgywgSAVEQFKpvmseeqgcvEQLKRIGIAPEDIRYVVLSHLHSDHTGAIG---- 114
Cdd:cd07726   19 YLLDGEGRPALIDTGPS------------SSVPRLL----------AALEALGIAPEDVDYIILTHIHLDHAGGAGllae 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 115 RFPHATHVVQRQEYEYAFAPDWFTSGAycRR----DFDR--------PQLNWLFLnglsDDHYDLY-GDGTLQCIFTPGH 181
Cdd:cd07726   77 ALPNAKVYVHPRGARHLIDPSKLWASA--RAvygdEADRlggeilpvPEERVIVL----EDGETLDlGGRTLEVIDTPGH 150

                        170
                 ....*....|....
gi 520903000 182 SPGHQSFIIRLPGG 195
Cdd:cd07726  151 APHHLSFLDEESDG 164
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 85-251 1.29e-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: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 53.26  E-value: 1.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  85 EQLKRI--GIAPEDIRYVVLSHLHSDHTGAIGRFPHATHV-VqrqeyeYAFAPDWFTSGAYCRRdFDRPqlnwlflngLS 161
Cdd:cd16278   40 AHLDALlaALGGGRVSAILVTHTHRDHSPGAARLAERTGApV------RAFGPHRAGGQDTDFA-PDRP---------LA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 162 DDHYDLYGDGTLQCIFTPGHSPGHQSFIIRlpggtnftlAIDAAYTLDHyhekalpgLMTSAT--------DVA---QSV 230
Cdd:cd16278  104 DGEVIEGGGLRLTVLHTPGHTSDHLCFALE---------DEGALFTGDH--------VMGWSTtviappdgDLGdylASL 166

                        170       180
                 ....*....|....*....|.
gi 520903000 231 RKLRQLTERyhaVFIPGHDPE 251
Cdd:cd16278  167 ERLLALDDR---LLLPGHGPP 184
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 84-190 2.34e-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: 53.36  E-value: 2.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  84 VEQLKRIGIAPEDIRYVVLSHLHSDHTGAIGRF---PHATHVVQRQEYEYAFAPDWFTSGaycRRDFDRPQLNwLFLNgl 160
Cdd:cd16280   49 VDGLEKLGLDPADIKYILITHGHGDHYGGAAYLkdlYGAKVVMSEADWDMMEEPPEEGDN---PRWGPPPERD-IVIK-- 122

                         90       100       110
                 ....*....|....*....|....*....|
gi 520903000 161 sDDHYDLYGDGTLQCIFTPGHSPGHQSFII 190
Cdd:cd16280  123 -DGDTLTLGDTTITVYLTPGHTPGTLSLIF 151
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 87-190 3.36e-08

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: 51.77  E-value: 3.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  87 LKRIGIAPEDIRYVVLSHLHSDHTGAIGRFPHATHV---VQRQEYEYafapdwftSGAYCRRdfdrpqlnwlfLNGLSD- 162
Cdd:cd16275   38 LAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDApvyMSKEEIDY--------YGFRCPN-----------LIPLEDg 98

                         90       100
                 ....*....|....*....|....*...
gi 520903000 163 DHYDLyGDGTLQCIFTPGHSPGHQSFII 190
Cdd:cd16275   99 DTIKI-GDTEITCLLTPGHTPGSMCYLL 125
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 40-191 5.98e-08

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: 52.20  E-value: 5.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  40 LLTHPDGFTLIDGGLAVEGlkdpsgywgsaveqfkPVMSEeqgcveQLKRIGIAPEDIRYVVLSHLHSDHTGAIGRFPHA 119
Cdd:cd16314   26 LVTSDAGHILIDGGTDKAA----------------PLIEA------NIRALGFRPEDVRYIVSSHEHFDHAGGIARLQRA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 120 T--HVVQRqeyeyAFAPDWFTSGaycRRDFDRPQlnwlFLNG-----------LSDDHYDLYGDGTLQCIFTPGHSPGHQ 186
Cdd:cd16314   84 TgaPVVAR-----EPAATTLERG---RSDRSDPQ----FLVVekfppvasvqrIGDGEVLRVGPLALTAHATPGHTPGGT 151


                 ....*
gi 520903000 187 SFIIR 191
Cdd:cd16314  152 SWTWR 156
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 100-248 1.02e-07

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: 50.70  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 100 VVLSHLHSDHTGAIGRFPHAthVVQRQEYEYAFAPDWFTSGAYCRRDFDRPQ---LNWLflngLSDDHYDLyGDGTLQCI 176
Cdd:cd07712   46 VVATHGHFDHIGGLHEFEEV--YVHPADAEILAAPDNFETLTWDAATYSVPPagpTLPL----RDGDVIDL-GDRQLEVI 118

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520903000 177 FTPGHSPGHQSFIIRlpgGTNFTLAIDAAYT---LDHYHekalpglMTSATDVAQSVRKLRQLTERYHAVFiPGH 248
Cdd:cd07712  119 HTPGHTPGSIALLDR---ANRLLFSGDVVYDgplIMDLP-------HSDLDDYLASLEKLSKLPDEFDKVL-PGH 182
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 39-236 2.07e-07

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: 50.78  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  39 FLLTHPDGFTLIDGGLAveglkdpsgywgSAVEQFKpvmseeqgcvEQLKRIGIAPEDIRYVVLSHLHSDHTGAIGRFPH 118
Cdd:cd16288   25 YLITTPQGLILIDTGLE------------SSAPMIK----------ANIRKLGFKPSDIKILLNSHAHLDHAGGLAALKK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 119 ATHVvqrqEYeYAFAPD--WFTSGAycRRDFDrPQLNWLFLNG------LSDDHYDLYGDGTLQCIFTPGHSPGHQSFII 190
Cdd:cd16288   83 LTGA----KL-MASAEDaaLLASGG--KSDFH-YGDDSLAFPPvkvdrvLKDGDRVTLGGTTLTAHLTPGHTRGCTTWTM 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 520903000 191 RL--PGGTNFTLAIDAAYTLDHYH---EKALPGLmtsATDVAQSVRKLRQL 236
Cdd:cd16288  155 TVkdDGKVYQVVFADSLTVNPGYKlvgNPTYPGI---AEDYRHSFATLRAL 202
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 82-119 2.80e-06

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: 46.74  E-value: 2.80e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 520903000  82 GCVEQLKRIGIAPEDIRYVVLSHLHSDHTGAIGRFPHA 119
Cdd:cd07719   37 GVVRRLAQAGLPLGDLDAVFLTHLHSDHVADLPALLLT 74
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 ...
 40-184 4.01e-06

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: 46.96  E-value: 4.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  40 LLTHPDGFTLIDGGLaveglkdpsgywgsavEQFKPVMseeqgcVEQLKRIGIAPEDIRYVVLSHLHSDHTGAIGRFPHA 119
Cdd:cd16290   26 LITSPQGLILIDGAL----------------PQSAPQI------EANIRALGFRLEDVKLILNSHAHFDHAGGIAALQRD 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520903000 120 T--HVVQRqeyeyAFAPDWFTSGaycRRDFDRPQLNWLF-------LNGLSDDHYDLYGDGTLQCIFTPGHSPG 184
Cdd:cd16290   84 SgaTVAAS-----PAGAAALRSG---GVDPDDPQAGAADpfppvakVRVVADGEVVKLGPLAVTAHATPGHTPG 149
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 39-184 4.38e-06

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: 46.77  E-value: 4.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  39 FLLTHPDGFTLIDGGLaveglkdpsgywgsavEQFKPVMSEeqgcveQLKRIGIAPEDIRYVVLSHLHSDHTG---AIGR 115
Cdd:cd07708   25 YLIVTPQGNILIDGDM----------------EQNAPMIKA------NIKKLGFKFSDTKLILISHAHFDHAGgsaEIKK 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520903000 116 FPHATHVVQRQEyeyafAPDWFTSGAYCRRDFDRPQLNWLFLN---GLSDDHYDLYGDGTLQCIFTPGHSPG 184
Cdd:cd07708   83 QTGAKVMAGAED-----VSLLLSGGSSDFHYANDSSTYFPQSTvdrAVHDGERVTLGGTVLTAHATPGHTPG 149
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 40-120 7.87e-06

Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of L1- and Pom-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293847  Cd Length: 239  Bit Score: 45.96  E-value: 7.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  40 LLTHPDGFTLIDGGLaveglkdpsgywgsaveqfkPVMSEEqgCVEQLKRIGIAPEDIRYVVLSHLHSDHTGAIGRFPHA 119
Cdd:cd16289   26 LVKTPDGAVLLDGGM--------------------PQAADM--LLDNMRALGVAPGDLKLILHSHAHADHAGPLAALKRA 83


                 .
gi 520903000 120 T 120
Cdd:cd16289   84 T 84
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 87-121 1.16e-05

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


Pssm-ID: 293799  Cd Length: 269  Bit Score: 45.69  E-value: 1.16e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 520903000  87 LKRIGIAPEDIRYVVLSHLHSDHTGAIGRFPHATH 121
Cdd:cd07713   46 AKKLGIDLSDIDAVVLSHGHYDHTGGLKALLELNP 80
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 39-196 1.18e-05

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: 45.55  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  39 FLLTHPDGFTLIDGGLAveglkdpsgywgSAVEQFKpvmseeqgcvEQLKRIGIAPEDIRYVVLSHLHSDHTGAIGRFPH 118
Cdd:cd16309   25 FLITTPEGHILIDGAMP------------QSTPLIK----------DNIKKLGFDVKDVKYLLNTHAHFDHAGGLAELKK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 119 AT--HVVQRQEYEYAFAPDWFTSGAYCRRDFDRPQLNWLFLNGlsdDHYDLyGDGTLQCIFTPGHSPGHQSFIIRLPGGT 196
Cdd:cd16309   83 ATgaQLVASAADKPLLESGYVGSGDTKNLQFPPVRVDRVIGDG---DKVTL-GGTTLTAHLTPGHSPGCTSWTTTVKDTA 158
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
82-109 1.33e-05

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 45.19  E-value: 1.33e-05
                         10        20
                 ....*....|....*....|....*...
gi 520903000  82 GCVEQLKRIGIAPEDIRYVVLSHLHSDH 109
Cdd:COG1234   38 GTQRQLLRAGLDPRDIDAIFITHLHGDH 65
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 87-127 5.64e-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: 43.02  E-value: 5.64e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 520903000  87 LKRIGIAPEDIRYVVLSHLHSDHTGAIGRFP-HATHVVQRQE 127
Cdd:cd07740   40 LKRAGIDPNAIDAIFITHLHGDHFGGLPFFLlDAQFVAKRTR 81
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
87-113 7.33e-05

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 42.95  E-value: 7.33e-05
                         10        20
                 ....*....|....*....|....*..
gi 520903000  87 LKRIGIAPEDIRYVVLSHLHSDHTGAI 113
Cdd:COG1237   48 AEKLGIDLSDIDAVVLSHGHYDHTGGL 74
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 85-248 7.82e-05

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 42.55  E-value: 7.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  85 EQLKRIGIAPedIRYVVLSHLHSDHTGAIGRFP--HAT---HVVQRQEYEYAFAPDWFTSGAYCRRDFDRPQLNW---LF 156
Cdd:cd16282   43 AAIRKVTDKP--VRYVVNTHYHGDHTLGNAAFAdaGAPiiaHENTREELAARGEAYLELMRRLGGDAMAGTELVLpdrTF 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 157 lnglsDDHYDLY-GDGTLQCI-FTPGHSPGHQsfIIRLPgGTNFTLAIDAAYtldhyhEKALPglMTSATDVAQSVRKLR 234
Cdd:cd16282  121 -----DDGLTLDlGGRTVELIhLGPAHTPGDL--VVWLP-EEGVLFAGDLVF------NGRIP--FLPDGSLAGWIAALD 184

                        170
                 ....*....|....
gi 520903000 235 QLTERYHAVFIPGH 248
Cdd:cd16282  185 RLLALDATVVVPGH 198
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 40-191 1.10e-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: 42.34  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  40 LLTHPDGFTLIDGGlaveglkdpsgywgsaVEQFKPVMseeqgcVEQLKRIGIAPEDIRYVVLSHLHSDHTGAIGRFPHA 119
Cdd:cd16315   26 LITGDDGHVLIDSG----------------TEEAAPLV------LANIRKLGFDPKDVRWLLSSHEHFDHVGGLAALQRA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000 120 T--HVVQRQEyeyafAPDWFTSGaycRRDFDRPQlnwlflNGLSD--------------DHYDLyGDGTLQCIFTPGHSP 183
Cdd:cd16315   84 TgaRVAASAA-----AAPVLESG---KPAPDDPQ------AGLHEpfppvrvdrivedgDTVAL-GSLRLTAHATPGHTP 148


                 ....*...
gi 520903000 184 GHQSFIIR 191
Cdd:cd16315  149 GALSWTWR 156
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 84-184 1.12e-04

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


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 42.47  E-value: 1.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  84 VEQLKRIgIAPEDIRYVVLSHLHSDHTGAIG----RFPHATHVVQRQeyeyafapdWFtsgAYCRRDFDRPQLNWLFLNg 159
Cdd:cd07709   57 LENLEEV-IDPRKIDYIVVNHQEPDHSGSLPelleLAPNAKIVCSKK---------AA---RFLKHFYPGIDERFVVVK- 122

                         90       100
                 ....*....|....*....|....*.
gi 520903000 160 lSDDHYDLyGDGTLQCIFTPG-HSPG 184
Cdd:cd07709  123 -DGDTLDL-GKHTLKFIPAPMlHWPD 146
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 82-111 1.71e-04

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: 41.09  E-value: 1.71e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 520903000  82 GCVEQLKRIGIAPEDIRYVVLSHLHSDHTG 111
Cdd:cd16272   36 GTVYRLLKAGVDPDKLDAIFLSHFHLDHIG 65
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 82-135 2.90e-04

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 41.42  E-value: 2.90e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520903000  82 GCVEQLKRIGIAPEDIRYVVLSHLHSDHTGAIGRF-------------PHATHVVQRQEYEYAFAPD 135
Cdd:COG1235   54 DLREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLrprygpnpipvyaTPGTLEALERRFPYLFAPY 120
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 39-113 7.74e-04

DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 39.84  E-value: 7.74e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520903000  39 FLLTHPDGFT-LIDGGLaveglKDPSGYWGSAVEQFkpvmseeqgcveqLKRIGIapEDIRYVVLSHLHSDHTGAI 113
Cdd:COG2333   14 ILIRTPDGKTiLIDTGP-----RPSFDAGERVVLPY-------------LRALGI--RRLDLLVLTHPDADHIGGL 69
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 39-190 1.13e-03

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


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 39.38  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  39 FLLTHPDGFTLIDGGLAveglkdpsgywgSAVeqfkPVMSEEqgcVEQLkriGIAPEDIRYVVLSHLHSDHTGAIGRFPH 118
Cdd:cd16308   25 YLIVTPKGNILINTGLA------------ESV----PLIKKN---IQAL---GFKFKDIKILLTTQAHYDHVGAMAAIKQ 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 520903000 119 ATHV-VQRQEYEYAFAPDWFTSgaycrrDFDRPQLNWLFL-----NGLSDDHYDLYGDGTLQCIFTPGHSPGHQSFII 190
Cdd:cd16308   83 QTGAkMMVDEKDAKVLADGGKS------DYEMGGYGSTFApvkadKLLHDGDTIKLGGTKLTLLHHPGHTKGSCSFLF 154
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 40-111 1.30e-03

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 38.65  E-value: 1.30e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520903000  40 LLTHPDGFTLIDGGlaveglkdPSGYWGSAVEqfkpvmseeqgcVEQLKRIGIapEDIRYVVLSHLHSDHTG 111
Cdd:cd07731   14 LIQTPGKTILIDTG--------PRDSFGEDVV------------VPYLKARGI--KKLDYLILTHPDADHIG 63
NorV COG0426
Flavorubredoxin [Energy production and conversion];
84-185 1.39e-03

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 39.43  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  84 VEQLKRIgIAPEDIRYVVLSHLHSDHTGAIG----RFPHATHVVqrqeyeyafAPDWFTS--GAYCRRDFDrpqlnwlfL 157
Cdd:COG0426   59 LENLSKV-IDPKKIDYIIVNHQEPDHSGSLPelleLAPNAKIVC---------SKKAARFlpHFYGIPDFR--------F 120

                         90       100       110
                 ....*....|....*....|....*....|
gi 520903000 158 NGLSD-DHYDLyGDGTLQCIFTPG-HSPGH 185
Cdd:COG0426  121 IVVKEgDTLDL-GGHTLQFIPAPMlHWPDT 149
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 96-194 2.47e-03

ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; MBL-fold metallo-hydrolase domain; Persulfide dioxygenase (PDO, also known as sulfur dioxygenase, SDO, EC 1.13.11.18) is a non-heme iron-dependent oxygenase which catalyzes the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria. Mutations in ethe1 (the human PDO gene) are responsible for a rare autosomal recessive metabolic disorder called ethylmalonic encephalopathy. Arabidopsis thaliana ETHE1 is essential for embryo and endosperm development. Bacterial ETHE1-type PDOs are also called Type 1 PDOs. Type II PDOs (also called PDOAs), are mainly proteobacterial. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293810 [Multi-domain]  Cd Length: 177  Bit Score: 37.76  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520903000  96 DIRYVVLSHLHSDH-TGA--IGRFPHATHVVqrqeyeyafapdwftSGAYCRRDFDRPqlnwlflngLSDDHYDLYGDGT 172
Cdd:cd07724   48 KITYVLETHVHADHvSGAreLAERTGAPIVI---------------GEGAPASFFDRL---------LKDGDVLELGNLT 103

                         90       100
                 ....*....|....*....|..
gi 520903000 173 LQCIFTPGHSPGHQSFIIRLPG 194
Cdd:cd07724  104 LEVLHTPGHTPESVSYLVGDPD 125
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 39-113 4.26e-03

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: 37.44  E-value: 4.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520903000  39 FLLTHPDGFTLIDGGLAVEGLKDPSGYWgsavEQFkpvmseeqgcveqlkriGIAPEDIRYVVLSHLHSDHTGAI 113
Cdd:cd16295   15 YLLETGGKRILLDCGLFQGGKELEELNN----EPF-----------------PFDPKEIDAVILTHAHLDHSGRL 68
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 87-109 5.25e-03

Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase domain; Includes Dictyostelium discoideum cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A (also known as cyclic GMP-binding protein A, phosphodiesterase 5, phosphodiesterase D, and PDE5) and cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B (also known as cyclic GMP-binding protein B, phosphodiesterase 6, phosphodiesterase E, and PDE6. 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: 293824  Cd Length: 189  Bit Score: 36.89  E-value: 5.25e-03
                         10        20
                 ....*....|....*....|...
gi 520903000  87 LKRIGIAPEDIRYVVLSHLHSDH 109
Cdd:cd07738   39 LRQNGISPRLVDHVILTHCHADH 61
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 39-114 8.44e-03

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


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 36.09  E-value: 8.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520903000  39 FLLTHPDGFTLIDGGLAveglkdpsgywGSAVEqfkpvmseeqgcvEQLKRIGIAPEDIRYVVLSHLHSDHTGAIG 114
Cdd:cd07733   12 TYLETEDGKLLIDAGLS-----------GRKIT-------------GRLAEIGRDPEDIDAILVTHEHADHIKGLG 63
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 82-109 9.62e-03

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


Pssm-ID: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 36.40  E-value: 9.62e-03
                         10        20
                 ....*....|....*....|....*...
gi 520903000  82 GCVEQLKRIGIAPEDIRYVVLSHLHSDH 109
Cdd:cd07741   39 GALVRMCRPKLDPTKLDAIILSHRHLDH 66
 
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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