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Conserved domains on  [gi|446613782|ref|WP_000691128|]
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MULTISPECIES: MBL fold metallo-hydrolase [Bacillus]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869930)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme that may have substrate towards phosphotriesters, esters, and/or lactones

CATH:  3.60.15.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  17597585|12177301|11471246|11513844
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 2-223 3.27e-58

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: 182.81  E-value: 3.27e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782   2 KIIELPIEFecngrkqWIYPSLIVLNNELTLVDTGYKNFLPLIENEILKHGYEMKNLKNIIITHYDDDHIGSLYDFKvKY 81
Cdd:cd07721    1 GVYQLPLLP-------PVNAYLIEDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALK-EA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  82 PQLHVIASEIESNYINGEIKSERLVQAEEMLehmpieekefsewFIQQLKNIRHISVDEKVYDGQMI-LNDKCQIVATPG 160
Cdd:cd07721   73 PGAPVYAHEREAPYLEGEKPYPPPVRLGLLG-------------LLSPLLPVKPVPVDRTLEDGDTLdLAGGLRVIHTPG 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446613782 161 HTSGHISLYFPDLDCVITGDAAVQDNNELVIANPNFCLDIEKAEESLKRIKNLKAASYYCYHG 223
Cdd:cd07721  140 HTPGHISLYLEEDGVLIAGDALVTVGGELVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
 
Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 2-223 3.27e-58

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: 182.81  E-value: 3.27e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782   2 KIIELPIEFecngrkqWIYPSLIVLNNELTLVDTGYKNFLPLIENEILKHGYEMKNLKNIIITHYDDDHIGSLYDFKvKY 81
Cdd:cd07721    1 GVYQLPLLP-------PVNAYLIEDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALK-EA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  82 PQLHVIASEIESNYINGEIKSERLVQAEEMLehmpieekefsewFIQQLKNIRHISVDEKVYDGQMI-LNDKCQIVATPG 160
Cdd:cd07721   73 PGAPVYAHEREAPYLEGEKPYPPPVRLGLLG-------------LLSPLLPVKPVPVDRTLEDGDTLdLAGGLRVIHTPG 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446613782 161 HTSGHISLYFPDLDCVITGDAAVQDNNELVIANPNFCLDIEKAEESLKRIKNLKAASYYCYHG 223
Cdd:cd07721  140 HTPGHISLYLEEDGVLIAGDALVTVGGELVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 19-224 2.31e-26

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: 101.31  E-value: 2.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  19 IYPSLIVLNNELTLVDTGYKN-FLPLIENEILKHGyemKNLKNIIITHYDDDHIGSLYDFKVKYpQLHVIASEIESNYIN 97
Cdd:COG0491   15 VNSYLIVGGDGAVLIDTGLGPaDAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAF-GAPVYAHAAEAEALE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  98 GEIKSERLVQaeemlehmpieekefsewfiqqlkniRHISVDEKVYDGQMI--LNDKCQIVATPGHTSGHISLYFPDLDC 175
Cdd:COG0491   91 APAAGALFGR--------------------------EPVPPDRTLEDGDTLelGGPGLEVIHTPGHTPGHVSFYVPDEKV 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446613782 176 VITGDAAVQDNnelvIANPN-FCLDIEKAEESLKRIKNLKAASYYCYHGG 224
Cdd:COG0491  145 LFTGDALFSGG----VGRPDlPDGDLAQWLASLERLLALPPDLVIPGHGP 190
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 23-222 5.65e-22

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: 88.76  E-value: 5.65e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782    23 LIVLNNELTLVDTGYKNFLPLIEnEILKHGyeMKNLKNIIITHYDDDHIGSLYDFKvKYPQLHVIASEIESNYINGEIKS 102
Cdd:smart00849   4 LVRDDGGAILIDTGPGEAEDLLA-ELKKLG--PKKIDAIILTHGHPDHIGGLPELL-EAPGAPVYAPEGTAELLKDLLAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782   103 erlvqaeemlehmpieekefsewFIQQLKNIRHISVDEKVYDGQM--ILNDKCQIVATPGHTSGHISLYFPDLDCVITGD 180
Cdd:smart00849  80 -----------------------LGELGAEAEPAPPDRTLKDGDEldLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGD 136

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 446613782   181 AAVQDNNELVIANPNFClDIEKAEESLKRIKNLKAASYYCYH 222
Cdd:smart00849 137 LLFAGGDGRTLVDGGDA-AASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
23-222 2.83e-21

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 87.42  E-value: 2.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782   23 LIVLNNELTLVDTGYKNFLPLIEnEILKHGYEMKNLKNIIITHYDDDHIGSLYDFKVKYPQLHVIASEIESNYIngeiks 102
Cdd:pfam00753  10 LIEGGGGAVLIDTGGSAEAALLL-LLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELL------ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  103 erlvqaeeMLEHMPIEEKEFSEWFIQQLKNIRHISVDEKVYDGQMILNdkcQIVATPGHTSGHISLYFPDLDCVITGDAA 182
Cdd:pfam00753  83 --------DEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGL---LVTHGPGHGPGHVVVYYGGGKVLFTGDLL 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 446613782  183 VQDNNELVIANPNFCLDI-----EKAEESLKRIKNLKAASYYCYH 222
Cdd:pfam00753 152 FAGEIGRLDLPLGGLLVLhpssaESSLESLLKLAKLKAAVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 56-180 5.79e-09

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 55.23  E-value: 5.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  56 KNLKNIIITHYDDDHIGSLYDFKVKYPQlHVIASEIESNYINGeikserlvqaeemlehMPIEEKEFSEWfiqqlknirh 135
Cdd:PLN02398 120 RNLTYILNTHHHYDHTGGNLELKARYGA-KVIGSAVDKDRIPG----------------IDIVLKDGDKW---------- 172

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446613782 136 isvdekvydgqMILNDKCQIVATPGHTSGHISLYFPDLDCVITGD 180
Cdd:PLN02398 173 -----------MFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGD 206
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 61-180 2.69e-06

hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione hydrolase, a detoxification enzyme known as glyoxalase II. It follows lactoylglutathione lyase, or glyoxalase I, and acts to remove the toxic metabolite methylglyoxal and related compounds. This protein belongs to the broader metallo-beta-lactamase family (pfam00753). [Cellular processes, Detoxification]


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 46.76  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782   61 IIITHYDDDHIGSLYDFKVKYPqLHVIAseiesnyingeikserlvqaeemlehmPIEEKefsewfiqqLKNIRHIsvde 140
Cdd:TIGR03413  47 ILLTHHHHDHVGGVAELLEAFP-APVYG---------------------------PAEER---------IPGITHP---- 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 446613782  141 kVYDGQ--MILNDKCQIVATPGHTSGHISLYFPDLDCVITGD 180
Cdd:TIGR03413  86 -VKDGDtvTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGD 126
 
Name Accession Description Interval E-value
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 2-223 3.27e-58

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: 182.81  E-value: 3.27e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782   2 KIIELPIEFecngrkqWIYPSLIVLNNELTLVDTGYKNFLPLIENEILKHGYEMKNLKNIIITHYDDDHIGSLYDFKvKY 81
Cdd:cd07721    1 GVYQLPLLP-------PVNAYLIEDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALK-EA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  82 PQLHVIASEIESNYINGEIKSERLVQAEEMLehmpieekefsewFIQQLKNIRHISVDEKVYDGQMI-LNDKCQIVATPG 160
Cdd:cd07721   73 PGAPVYAHEREAPYLEGEKPYPPPVRLGLLG-------------LLSPLLPVKPVPVDRTLEDGDTLdLAGGLRVIHTPG 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446613782 161 HTSGHISLYFPDLDCVITGDAAVQDNNELVIANPNFCLDIEKAEESLKRIKNLKAASYYCYHG 223
Cdd:cd07721  140 HTPGHISLYLEEDGVLIAGDALVTVGGELVPPPPPFTWDMEEALESLRKLAELDPEVLAPGHG 202
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 19-224 2.31e-26

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: 101.31  E-value: 2.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  19 IYPSLIVLNNELTLVDTGYKN-FLPLIENEILKHGyemKNLKNIIITHYDDDHIGSLYDFKVKYpQLHVIASEIESNYIN 97
Cdd:COG0491   15 VNSYLIVGGDGAVLIDTGLGPaDAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAF-GAPVYAHAAEAEALE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  98 GEIKSERLVQaeemlehmpieekefsewfiqqlkniRHISVDEKVYDGQMI--LNDKCQIVATPGHTSGHISLYFPDLDC 175
Cdd:COG0491   91 APAAGALFGR--------------------------EPVPPDRTLEDGDTLelGGPGLEVIHTPGHTPGHVSFYVPDEKV 144

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446613782 176 VITGDAAVQDNnelvIANPN-FCLDIEKAEESLKRIKNLKAASYYCYHGG 224
Cdd:COG0491  145 LFTGDALFSGG----VGRPDlPDGDLAQWLASLERLLALPPDLVIPGHGP 190
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 23-222 5.65e-22

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: 88.76  E-value: 5.65e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782    23 LIVLNNELTLVDTGYKNFLPLIEnEILKHGyeMKNLKNIIITHYDDDHIGSLYDFKvKYPQLHVIASEIESNYINGEIKS 102
Cdd:smart00849   4 LVRDDGGAILIDTGPGEAEDLLA-ELKKLG--PKKIDAIILTHGHPDHIGGLPELL-EAPGAPVYAPEGTAELLKDLLAL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782   103 erlvqaeemlehmpieekefsewFIQQLKNIRHISVDEKVYDGQM--ILNDKCQIVATPGHTSGHISLYFPDLDCVITGD 180
Cdd:smart00849  80 -----------------------LGELGAEAEPAPPDRTLKDGDEldLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGD 136

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 446613782   181 AAVQDNNELVIANPNFClDIEKAEESLKRIKNLKAASYYCYH 222
Cdd:smart00849 137 LLFAGGDGRTLVDGGDA-AASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
23-222 2.83e-21

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 87.42  E-value: 2.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782   23 LIVLNNELTLVDTGYKNFLPLIEnEILKHGYEMKNLKNIIITHYDDDHIGSLYDFKVKYPQLHVIASEIESNYIngeiks 102
Cdd:pfam00753  10 LIEGGGGAVLIDTGGSAEAALLL-LLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELL------ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  103 erlvqaeeMLEHMPIEEKEFSEWFIQQLKNIRHISVDEKVYDGQMILNdkcQIVATPGHTSGHISLYFPDLDCVITGDAA 182
Cdd:pfam00753  83 --------DEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGL---LVTHGPGHGPGHVVVYYGGGKVLFTGDLL 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 446613782  183 VQDNNELVIANPNFCLDI-----EKAEESLKRIKNLKAASYYCYH 222
Cdd:pfam00753 152 FAGEIGRLDLPLGGLLVLhpssaESSLESLLKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 27-223 2.52e-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: 79.25  E-value: 2.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  27 NNELTLVDTGYkNFLPLIENEILKHGyemKNLKNIIITHYDDDHIGSLYDFKvKYPQLHVIASEIEsnyingeikserlv 106
Cdd:cd06262   19 EGEAILIDPGA-GALEKILEAIEELG---LKIKAILLTHGHFDHIGGLAELK-EAPGAPVYIHEAD-------------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782 107 qaEEMLEHMpieEKEFSEWFiqqLKNIRHISVDEKVYDGQMIL--NDKCQIVATPGHTSGHISLYFPDLDCVITGDAAVQ 184
Cdd:cd06262   80 --AELLEDP---ELNLAFFG---GGPLPPPEPDILLEDGDTIElgGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFA 151

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446613782 185 dnnELVIANPNFCLDIEKAEESLKRIKNLKAASYYCYHG 223
Cdd:cd06262  152 ---GSIGRTDLPGGDPEQLIESIKKLLLLLPDDTVVYPG 187
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 23-219 6.11e-17

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: 76.38  E-value: 6.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  23 LIVLNNELTLVDTGYKNFLPLIENEILKHGYEMKNLKNIIITHYDDDHIGSLYDFKVKYPQLHVIASEIesnyinGE--- 99
Cdd:cd07726   20 LLDGEGRPALIDTGPSSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLAEALPNAKVYVHPR------GArhl 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782 100 IKSERLVQA------EEMLEH----MPIEEKefsewfiqqlkniRHISVDekvyDGQM--ILNDKCQIVATPGHTSGHIS 167
Cdd:cd07726   94 IDPSKLWASaravygDEADRLggeiLPVPEE-------------RVIVLE----DGETldLGGRTLEVIDTPGHAPHHLS 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446613782 168 LYFPDLDCVITGDAAVQDNNELVIANPNFC----LDIEKAEESLKRIKNLKAASYY 219
Cdd:cd07726  157 FLDEESDGLFTGDAAGVRYPELDVVGPPSTpppdFDPEAWLESLDRLLSLKPERIY 212
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 23-216 1.22e-14

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: 70.32  E-value: 1.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  23 LIVLNNELTLVDTGY-----KNFLPL-------------IENEILKHGYEMKNLKNIIITHYDDDHIGSLYDFkvkyPQL 84
Cdd:cd07729   36 LIEHPEGTILVDTGFhpdaaDDPGGLelafppgvteeqtLEEQLARLGLDPEDIDYVILSHLHFDHAGGLDLF----PNA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  85 HVIASEIESNYINGEIkserlvqaeeMLEHMPIEEKEFSEWFIQQLkNIRHISVDEKVYDGqmilndkCQIVATPGHTSG 164
Cdd:cd07729  112 TIIVQRAELEYATGPD----------PLAAGYYEDVLALDDDLPGG-RVRLVDGDYDLFPG-------VTLIPTPGHTPG 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446613782 165 HISLYF--PDLDCVITGDAA-VQDNNELVIAnPNFCLDIEKAEESLKRIKNLKAA 216
Cdd:cd07729  174 HQSVLVrlPEGTVLLAGDAAyTYENLEEGRP-PGINYDPEAALASLERLKALAER 227
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 44-180 1.06e-13

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 66.33  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  44 IENEILKHGYEmknLKNIIITHYDDDHIGSLYDFKVKYPQLHVIASeiesnyingeikserlvqaeemlehmpieekefs 123
Cdd:cd07723   33 VLAALEKNGLT---LTAILTTHHHWDHTGGNAELKALFPDAPVYGP---------------------------------- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446613782 124 ewfiqqlKNIRHISVDEKVYDGQMI--LNDKCQIVATPGHTSGHISLYFPDLDCVITGD 180
Cdd:cd07723   76 -------AEDRIPGLDHPVKDGDEIklGGLEVKVLHTPGHTLGHICYYVPDEPALFTGD 127
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 30-216 1.73e-12

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 64.53  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  30 LTLVDTGYKN-FLPLIENEILKHGYEMKNLKNIIITHYDDDHIGSLYDFKVKY-PQlhVIASEIEsnyingeikserlvq 107
Cdd:cd16280   33 LILIDALNNNeAADLIVDGLEKLGLDPADIKYILITHGHGDHYGGAAYLKDLYgAK--VVMSEAD--------------- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782 108 AEEMLEHmpiEEKEFSEWFIQqlknirHISVDEKVYDGQMI-LND-KCQIVATPGHTSGHISLYFPdldcvitgdaaVQD 185
Cdd:cd16280   96 WDMMEEP---PEEGDNPRWGP------PPERDIVIKDGDTLtLGDtTITVYLTPGHTPGTLSLIFP-----------VKD 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446613782 186 NNELVIA------NPNFCLDIEKAEE---SLKRIKNLKAA 216
Cdd:cd16280  156 GGKTHRAglwggtGLNTGPNLERREQyiaSLERFKKIAEE 195
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 27-218 2.70e-11

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 60.62  E-value: 2.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  27 NNELTLVDTGYKNFLPLIENEILKHGYEmkNLKNIIITHYDDDHIGSLYDFKvKYPQLHVIASEIESNYINgeikserlv 106
Cdd:cd07743   17 DKEALLIDSGLDEDAGRKIRKILEELGW--KLKAIINTHSHADHIGGNAYLQ-KKTGCKVYAPKIEKAFIE--------- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782 107 qaEEMLEHMPIEEKEFSEWFIQQLKNIRHISVDEKVYDGQMILNDKC-QIVATPGHTSGHISLYFPDlDCVITGDAAVQD 185
Cdd:cd07743   85 --NPLLEPSYLGGAYPPKELRNKFLMAKPSKVDDIIEEGELELGGVGlEIIPLPGHSFGQIGILTPD-GVLFAGDALFGE 161

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446613782 186 NnelVIAN--PNFCLDIEKAEESLKRIKNLKAASY 218
Cdd:cd07743  162 E---VLEKygIPFLYDVEEQLETLEKLEELDADYY 193
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 23-227 4.81e-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: 53.84  E-value: 4.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  23 LIVLNNELTLVDTGYKNFL--PLIENEILKHGYEMKNLKNIIITHYDDDHIGslydfkvkypqlhvIASEIESnyingei 100
Cdd:cd07725   19 LLRDGDETTLIDTGLATEEdaEALWEGLKELGLKPSDIDRVLLTHHHPDHIG--------------LAGKLQE------- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782 101 KSERLVqaeemlehmpieekefsewFIQQLKNIRHisvDEKVYDGQMILndkcQIVATPGHTSGHISLYFPDLDCVITGD 180
Cdd:cd07725   78 KSGATV-------------------YILDVTPVKD---GDKIDLGGLRL----KVIETPGHTPGHIVLYDEDRRELFVGD 131

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446613782 181 AAVQDNNELVIANPNFCLDIEKA-EESLKRIKNLKAASYYCYHGGKLI 227
Cdd:cd07725  132 AVLPKITPNVSLWAVRVEDPLGAyLESLDKLEKLDVDLAYPGHGGPIK 179
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 56-180 5.79e-09

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 55.23  E-value: 5.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  56 KNLKNIIITHYDDDHIGSLYDFKVKYPQlHVIASEIESNYINGeikserlvqaeemlehMPIEEKEFSEWfiqqlknirh 135
Cdd:PLN02398 120 RNLTYILNTHHHYDHTGGNLELKARYGA-KVIGSAVDKDRIPG----------------IDIVLKDGDKW---------- 172

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446613782 136 isvdekvydgqMILNDKCQIVATPGHTSGHISLYFPDLDCVITGD 180
Cdd:PLN02398 173 -----------MFAGHEVLVMETPGHTRGHISFYFPGSGAIFTGD 206
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 32-210 9.41e-09

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: 53.36  E-value: 9.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  32 LVDTGYKNFLPLIENEILKHGYEMKNLKNIIITHYDDDHIGSLYDFKvkypqlhviaseiesnyingeiKSERLVqaeem 111
Cdd:cd07711   35 LVDTGTPWDRDLLLKALAEHGLSPEDIDYVVLTHGHPDHIGNLNLFP----------------------NATVIV----- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782 112 leHMPIEEKEFSEWfiqqlknirhisvDEKVYDGqMILNDKCQIVATPGHTSGHISLYFPDLD---CVITGDAAVQDNN- 187
Cdd:cd07711   88 --GWDICGDSYDDH-------------SLEEGDG-YEIDENVEVIPTPGHTPEDVSVLVETEKkgtVAVAGDLFEREEDl 151

                        170       180
                 ....*....|....*....|...
gi 446613782 188 ELVIANPNFCLDIEKAEESLKRI 210
Cdd:cd07711  152 EDPILWDPLSEDPELQEESRKRI 174
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 32-223 3.31e-08

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: 51.77  E-value: 3.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  32 LVDTG--YKNFLPLIENEILKHGYEMknLKNIIITHYDDDHIGSLydfkvkypqlhviaSEIESNYINGEIKserlvqae 109
Cdd:cd07722   31 LIDTGegRPSYIPLLKSVLDSEGNAT--ISDILLTHWHHDHVGGL--------------PDVLDLLRGPSPR-------- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782 110 eMLEHMPIEEKEFSEWFIQQLKNIRhisvdekvyDGQMI------LndkcQIVATPGHTSGHISLYFPDLDCVITGD--- 180
Cdd:cd07722   87 -VYKFPRPEEDEDPDEDGGDIHDLQ---------DGQVFkvegatL----RVIHTPGHTTDHVCFLLEEENALFTGDcvl 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446613782 181 ----AAVQDNNELVianpnfcldiekaeESLKRIKNLKAASYYCYHG 223
Cdd:cd07722  153 ghgtAVFEDLAAYM--------------ASLKKLLSLGPGRIYPGHG 185
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 23-165 1.81e-07

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


Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 50.32  E-value: 1.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  23 LIVLNNELTLVDTGY-------------KNFLPLI-----ENE-----ILKHGYEMKNLKNIIITHYDDDHIGSLYDFkv 79
Cdd:cd07742   23 LVETDDGLVLVDTGFgladvadpkrrlgGPFRRLLrprldEDEtavrqIEALGFDPSDVRHIVLTHLDLDHAGGLADF-- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  80 kyP--QLHVIASEIESnYINGEIKSERLVQAEEMLEHMP--IEEKEFSE-WF----IQQLKNIrhisvdekvyDGQMILn 150
Cdd:cd07742  101 --PhaTVHVHAAELDA-ATSPRTRYERRRYRPQQLAHGPwwVTYAAGGErWFgfeaVRPLDGL----------PPEILL- 166

                        170
                 ....*....|....*
gi 446613782 151 dkcqiVATPGHTSGH 165
Cdd:cd07742  167 -----VPLPGHTRGH 176
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 138-181 2.69e-07

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: 48.94  E-value: 2.69e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 446613782 138 VDEKVYDGQMIL--NDKCQIVATPGHTSGHISLYFPDLDCVITGDA 181
Cdd:cd07724   87 FDRLLKDGDVLElgNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDT 132
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 32-213 1.88e-06

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: 46.47  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  32 LVDTGYKNFlPLIEneilkhgyEMKNLKN----IIITHYDDDHIGSLYDFkvkyPQLHVIASEIEsnyingeikserLVQ 107
Cdd:cd07712   22 LIDTGLGIG-DLKE--------YVRTLTDlpllVVATHGHFDHIGGLHEF----EEVYVHPADAE------------ILA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782 108 AEEMLEHMPIEEKEFSEWFIQQLKNIRhisvdekvyDGQMI-LNDKC-QIVATPGHTSGHISLYFPDLDCVITGDaAVQD 185
Cdd:cd07712   77 APDNFETLTWDAATYSVPPAGPTLPLR---------DGDVIdLGDRQlEVIHTPGHTPGSIALLDRANRLLFSGD-VVYD 146

                        170       180
                 ....*....|....*....|....*...
gi 446613782 186 NNelVIANPNfCLDIEKAEESLKRIKNL 213
Cdd:cd07712  147 GP--LIMDLP-HSDLDDYLASLEKLSKL 171
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 61-180 2.69e-06

hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione hydrolase, a detoxification enzyme known as glyoxalase II. It follows lactoylglutathione lyase, or glyoxalase I, and acts to remove the toxic metabolite methylglyoxal and related compounds. This protein belongs to the broader metallo-beta-lactamase family (pfam00753). [Cellular processes, Detoxification]


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 46.76  E-value: 2.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782   61 IIITHYDDDHIGSLYDFKVKYPqLHVIAseiesnyingeikserlvqaeemlehmPIEEKefsewfiqqLKNIRHIsvde 140
Cdd:TIGR03413  47 ILLTHHHHDHVGGVAELLEAFP-APVYG---------------------------PAEER---------IPGITHP---- 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 446613782  141 kVYDGQ--MILNDKCQIVATPGHTSGHISLYFPDLDCVITGD 180
Cdd:TIGR03413  86 -VKDGDtvTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGD 126
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 32-180 3.04e-06

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: 46.19  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  32 LVDTGYKNfLPLIENEILKHgyemKNLKNIIITHYDDDHIGSLYDFKvKYPQLHVIASEIESnyingeikserlvqaeEM 111
Cdd:cd16322   26 LVDPGDES-EKLLARFGTTG----LTLLYILLTHAHFDHVGGVADLR-RHPGAPVYLHPDDL----------------PL 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446613782 112 LEHMPIEEKEFsewfiqQLKNIRHISVDEKVYDGQMI-LND-KCQIVATPGHTSGHISLYFPDLDCVITGD 180
Cdd:cd16322   84 YEAADLGAKAF------GLGIEPLPPPDRLLEDGQTLtLGGlEFKVLHTPGHSPGHVCFYVEEEGLLFSGD 148
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 23-210 3.91e-06

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: 46.39  E-value: 3.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  23 LIVLNNELTLVDTGY-KNFLP----LIENeiLKH-GYEMKNLKNIIITHYDDDHIGSLYD-FKVK-YPQLHVIASEIESN 94
Cdd:cd07720   53 LVRTGGRLILVDTGAgGLFGPtagkLLAN--LAAaGIDPEDIDDVLLTHLHPDHIGGLVDaGGKPvFPNAEVHVSEAEWD 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  95 YIngeikserlvQAEEMLEHMPIEEKEFSEWFIQQLK---NIRHISVDEKVYDGqmIlndkcQIVATPGHTSGHISLYF- 170
Cdd:cd07720  131 FW----------LDDANAAKAPEGAKRFFDAARDRLRpyaAAGRFEDGDEVLPG--I-----TAVPAPGHTPGHTGYRIe 193

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 446613782 171 -PDLDCVITGD----AAVQdnnelvIANPNFCL----DIEKAEESLKRI 210
Cdd:cd07720  194 sGGERLLIWGDivhhPALQ------FAHPDWTIafdvDPEQAAATRRRL 236
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 23-164 6.38e-06

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: 45.90  E-value: 6.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  23 LIVLNNELTLVDTGYKNFLPLIENEILKHGYEMKNLKNIIITHYDDDHIGSLYDFKvKYPQLHVIASEiesnyinGEIKS 102
Cdd:cd16310   26 LITSNHGAILLDGGLEENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQLK-ADTGAKLWASR-------GDRPA 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446613782 103 erlvqaeemLEH-MPIEEKEFSEWFIQQLKnirhisVDEKVYDGQMILNDKCQIVA--TPGHTSG 164
Cdd:cd16310   98 ---------LEAgKHIGDNITQPAPFPAVK------VDRILGDGEKIKLGDITLTAtlTPGHTKG 147
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 139-180 1.09e-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: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 44.40  E-value: 1.09e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446613782 139 DEKVYDGQMILNDKCQI--VATPGHTSGHISLYFPDLDCVITGD 180
Cdd:cd16278   99 DRPLADGEVIEGGGLRLtvLHTPGHTSDHLCFALEDEGALFTGD 142
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 23-94 2.57e-05

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 43.28  E-value: 2.57e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446613782  23 LIVLNNELTLVDTG--YKNFLPLIENEILKHGYemKNLKNIIITHYDDDHIGSLYDFKVKYPQLHVIASEIESN 94
Cdd:cd07731   14 LIQTPGKTILIDTGprDSFGEDVVVPYLKARGI--KKLDYLILTHPDADHIGGLDAVLKNFPVKEVYMPGVTHT 85
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 154-224 4.01e-05

uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YmaE and Nostoc all1228 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. 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: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 42.95  E-value: 4.01e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446613782 154 QIVATPGHTSGHISLYFPDLDCVITGD--AAVQDNNELVIANPNFCLDIEKAEESLKRIKNLKAASYYCYHGG 224
Cdd:cd07727  105 TLIPVPGHTRGSVVLLYKEKGVLFTGDhlAWSRRRGWLSAFRYVCWYSWPEQAESVERLADLDFEWVLPGHGR 177
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 23-164 4.18e-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: 43.24  E-value: 4.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  23 LIVLNNELTLVDTGYKNFLPLIENEILKHGYEMKNLKNIIITHYDDDHIGSLYDFKvKYPQLHVIASE-----IESNYIN 97
Cdd:cd16309   26 LITTPEGHILIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAELK-KATGAQLVASAadkplLESGYVG 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446613782  98 GEIKSERLVQAeemlehmpieekefsewfiqqlknirhISVDEKVYDGQMILNDKCQIVA--TPGHTSG 164
Cdd:cd16309  105 SGDTKNLQFPP---------------------------VRVDRVIGDGDKVTLGGTTLTAhlTPGHSPG 146
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 24-91 4.49e-05

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: 43.24  E-value: 4.49e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446613782  24 IVLNNELTLVDTGYKNFLPLIENEILKHGyEMKNLKNIIITHYDDDHIGSLYDFKVKYPQLHVIASEI 91
Cdd:cd07709   36 LIKDEKTALIDTVKEPFFDEFLENLEEVI-DPRKIDYIVVNHQEPDHSGSLPELLELAPNAKIVCSKK 102
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 23-211 1.17e-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: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  23 LIVLNNELTLVDTGYKNFLPLIENEILKHGYEMKNLKNIIITHYDDDHIGSLYDFKvKYPQLHVIASEIESnyingeiks 102
Cdd:cd16288   26 LITTPQGLILIDTGLESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAALK-KLTGAKLMASAEDA--------- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782 103 erlvqaeEMLEHMpiEEKEF---SEWFIQQlknirHISVDEKVYDGQMILNDKCQIVA--TPGHTSGHISLYFP------ 171
Cdd:cd16288   96 -------ALLASG--GKSDFhygDDSLAFP-----PVKVDRVLKDGDRVTLGGTTLTAhlTPGHTRGCTTWTMTvkddgk 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446613782 172 DLDCVITGDAAVQDNNELV--IANPNFCLDIEKAEESLKRIK 211
Cdd:cd16288  162 VYQVVFADSLTVNPGYKLVgnPTYPGIAEDYRHSFATLRALQ 203
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 44-180 1.60e-04

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


Pssm-ID: 293833 [Multi-domain]  Cd Length: 174  Bit Score: 40.98  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  44 IENEILKHGYEMKNLKNIIITHYDDDHIGsLYDFKVKYPQLHViaseiesnyingeikserlvqaeemleHMPIEEKEFS 123
Cdd:cd16275   34 IEKILAKLNELGLTLTGILLTHSHFDHVN-LVEPLLAKYDAPV---------------------------YMSKEEIDYY 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446613782 124 EwfiQQLKNIRHISVDEKVydgqMILNDKCQIVATPGHTSGHISLYFPdlDCVITGD 180
Cdd:cd16275   86 G---FRCPNLIPLEDGDTI----KIGDTEITCLLTPGHTPGSMCYLLG--DSLFTGD 133
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 41-180 1.97e-04

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


Pssm-ID: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 41.00  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  41 LPLIENEILKHGYEmknLKNIIITHYDDDHIGSLYDFKVKYpQLHVIASEIESNYingeikserlvqaeeMLEHMPIEEK 120
Cdd:cd07737   33 ADKILQAIEDLGLT---LKKILLTHGHLDHVGGAAELAEHY-GVPIIGPHKEDKF---------------LLENLPEQSQ 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446613782 121 EFSewfiqqLKNIRHISVDEKVYDGQMIL--NDKCQIVATPGHTSGHISLYFPDLDCVITGD 180
Cdd:cd07737   94 MFG------FPPAEAFTPDRWLEEGDTVTvgNLTLEVLHCPGHTPGHVVFFNRESKLAIVGD 149
NorV COG0426
Flavorubredoxin [Energy production and conversion];
20-115 2.77e-04

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 41.36  E-value: 2.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  20 YPSLIVLNNELTLVDTGYKNFLP-LIENeiLKHGYEMKNLKNIIITHYDDDHIGSLYDFKVKYPQLHVIASEIesnying 98
Cdd:COG0426   34 YNSYLIVDEKTALIDTVGESFFEeFLEN--LSKVIDPKKIDYIIVNHQEPDHSGSLPELLELAPNAKIVCSKK------- 104

                         90
                 ....*....|....*..
gi 446613782  99 eikserlvqAEEMLEHM 115
Cdd:COG0426  105 ---------AARFLPHF 112
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-181 3.33e-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: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 40.18  E-value: 3.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  22 SLIVLNNELTLVDTGY--KNFLPLIEnEILKHGyemKNLKNIIITHYDDDHIGSLYDFKVKYPQLHVIAseiesnyinge 99
Cdd:cd07739   19 TLIYGETEAVLVDAQFtrADAERLAD-WIKASG---KTLTTIYITHGHPDHYFGLEVLLEAFPDAKVVA----------- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782 100 ikserlvqAEEMLEHMPIE-EKEFSEWFIQQLKNI-RHISVDEKVYDGQMIL-NDKCQIVATPGHTSGHIS-LYFPDLDC 175
Cdd:cd07739   84 --------TPAVVAHIKAQlEPKLAFWGPLLGGNApARLVVPEPLDGDTLTLeGHPLEIVGVGGGDTDDTTyLWIPSLKT 155


                 ....*.
gi 446613782 176 VITGDA 181
Cdd:cd07739  156 VVAGDV 161
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 22-77 1.03e-03

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


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 38.65  E-value: 1.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446613782  22 SLIVLNNELTLVDTG---YKNFLplieneilKHGYEMKNLKNIIITHYDDDHIGSLYDF 77
Cdd:cd07719   21 TLVVVGGRVYLVDAGsgvVRRLA--------QAGLPLGDLDAVFLTHLHSDHVADLPAL 71
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 61-175 1.05e-03

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 39.04  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  61 IIITHYDDDHIGSLYDFKVKYPQLHViaseiesnyingeikserlvqaeemleHMPIEEKEfsewfiqqlKNIRHIsvde 140
Cdd:PRK10241  49 IFLTHHHHDHVGGVKELVEKFPQIVV---------------------------YGPQETQD---------KGTTQV---- 88

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446613782 141 kVYDGQ--MILNDKCQIVATPGHTSGHISLY-FPDLDC 175
Cdd:PRK10241  89 -VKDGEtaFVLGHEFSVFATPGHTLGHICYFsKPYLFC 125
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 23-171 1.51e-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: 38.60  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  23 LIVLNNELTLVDTGYKNFLPLIENEILKHGYEMKNLKNIIITHYDDDHIGSLYDFKvKYPQLHVIASEIESNYINGEIKS 102
Cdd:cd16308   26 LIVTPKGNILINTGLAESVPLIKKNIQALGFKFKDIKILLTTQAHYDHVGAMAAIK-QQTGAKMMVDEKDAKVLADGGKS 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446613782 103 ERlvqaeemleHMPIEEKEFSEwfiqqlknirhISVDEKVYDGQMIL--NDKCQIVATPGHTSGHISLYFP 171
Cdd:cd16308  105 DY---------EMGGYGSTFAP-----------VKADKLLHDGDTIKlgGTKLTLLHHPGHTKGSCSFLFD 155
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 23-94 1.54e-03

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 38.69  E-value: 1.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446613782  23 LIVL-NNELTLVDTGYKNFLPLIENEIL----KHGyeMKNLKNIIITHYDDDHIGSLYDFKVKYPQLHVIASEIESN 94
Cdd:COG2333   15 LIRTpDGKTILIDTGPRPSFDAGERVVLpylrALG--IRRLDLLVLTHPDADHIGGLAAVLEAFPVGRVLVSGPPDT 89
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 47-216 2.00e-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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 38.40  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782  47 EIL-KHGYEMKNLKNIIITHYDDDHIGSLYDFkvkyPQLHVIASE------IESNYINGEIKSerlVQAEEMLEHMPIEE 119
Cdd:cd07730   72 EQLaAGGIDPEDIDAVILSHLHWDHIGGLSDF----PNARLIVGPgakealRPPGYPSGFLPE---LLPSDFEGRLVRWE 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446613782 120 KEFSEWfiqqlkniRHISVDEKVYD----GQMIlndkcqIVATPGHTSGHISLYFPDL---------DCVITGDAAVQDN 186
Cdd:cd07730  145 EDDFLW--------VPLGPFPRALDlfgdGSLY------LVDLPGHAPGHLGLLARTTsgtwvflagDACHHRIGLLRPS 210

                        170       180       190
                 ....*....|....*....|....*....|
gi 446613782 187 NELVIANPNFCLDIEKAEESLKRIKNLKAA 216
Cdd:cd07730  211 PLLPLPDLDDGADREAARETLARLRELDAA 240
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 154-210 8.47e-03

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 36.35  E-value: 8.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446613782 154 QIVATPGHTSGHISLYF--PDLDCVITGDAA---VQdnnelvIANPN----FCLDIEKAEESLKRI 210
Cdd:cd16277  148 RLEPTPGHTPGHVSVELesGGERALFTGDVMhhpIQ------VARPDwssvFDEDPAQAAATRRRL 207
 
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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