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Conserved domains on  [gi|1729628664|ref|WP_148129252|]
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MBL fold metallo-hydrolase, partial [Dulcicalothrix desertica]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869928)

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
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 41-224 2.08e-76

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: 230.51  E-value: 2.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  41 FKLGDFAITVLSDGTLPQDLHTLLSNTNPTETDRLLQKNFLTNPVEASINAFLIDTGDQQVLVDTGAGNFFGPKlGGKLQ 120
Cdd:cd07720     1 FKVGDFEVTALSDGTLPLPLDLLLGGAAPEAEAALLAAFLPPDPVETSVNAFLVRTGGRLILVDTGAGGLFGPT-AGKLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664 121 TSLKAAGYTPNEIDAILLTHIHTDHSGGLVEQGKR-VFPAATLYVGKPDIDFWFDRANAKRFNVAEK-YFDEAAKTVKPY 198
Cdd:cd07720    80 ANLAAAGIDPEDIDDVLLTHLHPDHIGGLVDAGGKpVFPNAEVHVSEAEWDFWLDDANAAKAPEGAKrFFDAARDRLRPY 159

                         170       180
                  ....*....|....*....|....*.
gi 1729628664 199 LDAGKvksFSGKTVLLPGITAHPTPG 224
Cdd:cd07720   160 AAAGR---FEDGDEVLPGITAVPAPG 182
 
Name Accession Description Interval E-value
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 41-224 2.08e-76

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: 230.51  E-value: 2.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  41 FKLGDFAITVLSDGTLPQDLHTLLSNTNPTETDRLLQKNFLTNPVEASINAFLIDTGDQQVLVDTGAGNFFGPKlGGKLQ 120
Cdd:cd07720     1 FKVGDFEVTALSDGTLPLPLDLLLGGAAPEAEAALLAAFLPPDPVETSVNAFLVRTGGRLILVDTGAGGLFGPT-AGKLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664 121 TSLKAAGYTPNEIDAILLTHIHTDHSGGLVEQGKR-VFPAATLYVGKPDIDFWFDRANAKRFNVAEK-YFDEAAKTVKPY 198
Cdd:cd07720    80 ANLAAAGIDPEDIDDVLLTHLHPDHIGGLVDAGGKpVFPNAEVHVSEAEWDFWLDDANAAKAPEGAKrFFDAARDRLRPY 159

                         170       180
                  ....*....|....*....|....*.
gi 1729628664 199 LDAGKvksFSGKTVLLPGITAHPTPG 224
Cdd:cd07720   160 AAAGR---FEDGDEVLPGITAVPAPG 182
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 88-224 7.05e-15

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: 70.49  E-value: 7.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  88 SINAFLIDTGDQQVLVDTGagnfFGPKLGGKLQTSLKAAGYTpneIDAILLTHIHTDHSGGLVEQGKRVfpAATLYVGKP 167
Cdd:COG0491    14 GVNSYLIVGGDGAVLIDTG----LGPADAEALLAALAALGLD---IKAVLLTHLHPDHVGGLAALAEAF--GAPVYAHAA 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1729628664 168 DIDFWFDRANAKRFNVAEKYFDEAaktvkpyLDAGKVKSFSGktvllPGITAHPTPG 224
Cdd:COG0491    85 EAEALEAPAAGALFGREPVPPDRT-------LEDGDTLELGG-----PGLEVIHTPG 129
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 90-224 8.78e-15

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 69.50  E-value: 8.78e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664   90 NAFLIDTGDQQVLVDTGAGNffgpklGGKLQTSLKAAGytPNEIDAILLTHIHTDHSGGLVEQGKRvfPAATLYVGKPDI 169
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGE------AEDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1729628664  170 DFWfdrANAKRFNVAEKYFDEAAKTVKPyLDAGKVKSFSGktvllPGITAHPTPG 224
Cdd:smart00849  71 ELL---KDLLALLGELGAEAEPAPPDRT-LKDGDELDLGG-----GELEVIHTPG 116
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
88-224 4.78e-13

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 65.47  E-value: 4.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  88 SINAFLIDTGDQQVLVDTGAGNFFGpklggkLQTSLKAAGYTPNEIDAILLTHIHTDHSGGLVEqGKRVFPAATlYVGKP 167
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTGGSAEAA------LLLLLAALGLGPKDIDAVILTHGHFDHIGGLGE-LAEATDVPV-IVVAE 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1729628664 168 DIDFWFDRAnAKRFNVAEKYFDEAAKTVKPYLDAGKVKSFSGKTVLLpGITAHPTPG 224
Cdd:pfam00753  77 EARELLDEE-LGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGL-LVTHGPGHG 131
PRK00055 PRK00055
ribonuclease Z; Reviewed
 90-149 9.17e-06

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 45.17  E-value: 9.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  90 NAFLIDTGDQQVLVDTGAGNffgpklggklQTSLKAAGYTPNEIDAILLTHIHTDHSGGL 149
Cdd:PRK00055   21 SSILLRLGGELFLFDCGEGT----------QRQLLKTGIKPRKIDKIFITHLHGDHIFGL 70
 
Name Accession Description Interval E-value
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 41-224 2.08e-76

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: 230.51  E-value: 2.08e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  41 FKLGDFAITVLSDGTLPQDLHTLLSNTNPTETDRLLQKNFLTNPVEASINAFLIDTGDQQVLVDTGAGNFFGPKlGGKLQ 120
Cdd:cd07720     1 FKVGDFEVTALSDGTLPLPLDLLLGGAAPEAEAALLAAFLPPDPVETSVNAFLVRTGGRLILVDTGAGGLFGPT-AGKLL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664 121 TSLKAAGYTPNEIDAILLTHIHTDHSGGLVEQGKR-VFPAATLYVGKPDIDFWFDRANAKRFNVAEK-YFDEAAKTVKPY 198
Cdd:cd07720    80 ANLAAAGIDPEDIDDVLLTHLHPDHIGGLVDAGGKpVFPNAEVHVSEAEWDFWLDDANAAKAPEGAKrFFDAARDRLRPY 159

                         170       180
                  ....*....|....*....|....*.
gi 1729628664 199 LDAGKvksFSGKTVLLPGITAHPTPG 224
Cdd:cd07720   160 AAAGR---FEDGDEVLPGITAVPAPG 182
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 85-224 4.24e-29

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 108.38  E-value: 4.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  85 VEASINAFLIDTGDQQVLVDTGAGNFF---GPKLGGKLQT----SLKAAGYTPNEIDAILLTHIHTDHSGG---LVEqGK 154
Cdd:cd16277     9 IVELIHSWLVRTPGRTILVDTGIGNDKprpGPPAFHNLNTpyleRLAAAGVRPEDVDYVLCTHLHVDHVGWntrLVD-GR 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729628664 155 RV--FPAATLYVGKPDIDFWFDRANAKRFNVAekYFDEaakTVKPYLDAGKVKSFSGKTVLLPGITAHPTPG 224
Cdd:cd16277    88 WVptFPNARYLFSRAEYDHWSSPDAGGPPNRG--VFED---SVLPVIEAGLADLVDDDHEILDGIRLEPTPG 154
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 48-224 3.53e-25

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: 98.44  E-value: 3.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  48 ITVLSDGTLPQDLHTLLSNTNPTETdrllqknfltnPVEASINAFLIDTGDQQVLVDTG-----AGNFFGPKLGGKLQTS 122
Cdd:cd07729     2 LYALDYGTVTVDKSSLFYYGRGPGE-----------PIDLPVYAYLIEHPEGTILVDTGfhpdaADDPGGLELAFPPGVT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664 123 --------LKAAGYTPNEIDAILLTHIHTDHSGGLveqgkRVFPAATLYVGKPDIDFWFDRANakrfnvAEKYFDEAAKT 194
Cdd:cd07729    71 eeqtleeqLARLGLDPEDIDYVILSHLHFDHAGGL-----DLFPNATIIVQRAELEYATGPDP------LAAGYYEDVLA 139

                         170       180       190
                  ....*....|....*....|....*....|
gi 1729628664 195 VKPYLDAGKVKSFSGKTVLLPGITAHPTPG 224
Cdd:cd07729   140 LDDDLPGGRVRLVDGDYDLFPGVTLIPTPG 169
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 93-224 1.67e-24

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: 97.18  E-value: 1.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  93 LIDTGDQQVLVDTGAGNFFGPKLGGK--------LQTSLKAAGYTPNEIDAILLTHIHTDHSGGLV--EQGKRV---FPA 159
Cdd:cd16281    47 LIETGGRNILIDTGIGDKQDPKFRSIyvqhsehsLLKSLARLGLSPEDITDVILTHLHFDHCGGATraDDDGLVellFPN 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729628664 160 ATLYVGKpdiDFWfdrANAKRFNVAEK--YFDEaakTVKPYLDAGKVKSFSGK-TVLLPGITAHP----TPG 224
Cdd:cd16281   127 ATYWVQK---RHW---EWALNPNPRERasFLPE---NIEPLEESGRLKLIDGSdAELGPGIRFHLsdghTPG 189
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 83-224 4.87e-17

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: 76.91  E-value: 4.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  83 NPVEASINAFLIDTGDQQVLVDTGAGN---------FFGPKLGGKLQTSLKAAGYTPNEIDAILLTHIHTDHSGGLV--- 150
Cdd:cd07728    37 NQIELRTDPILIQYQGKNYLIDAGIGNgkltekqkrNFGVTEESSIEESLAELGLTPEDIDYVLMTHLHFDHASGLTkvk 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729628664 151 -EQGKRVFPAATLYVGKPDidfWFDRANAkrfNVAEK--YFDEAAKTVkpyldAGKVKSFSGKTVLLPGITAHPTPG 224
Cdd:cd07728   117 gEQLVSVFPNATIYVSEIE---WEEMRNP---NIRSKntYWKENWEPI-----EDQVKTFSDEIEIVPGITMIHTGG 182
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 84-224 2.18e-16

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 74.57  E-value: 2.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  84 PVEASINAFLIDTGDQQVLVDTGAgnffgPKLGGKLQTSLKAAGYTPNEIDAILLTHIHTDHSGGLVEQGKRvfPAATLY 163
Cdd:cd07721     6 PLLPPVNAYLIEDDDGLTLIDTGL-----PGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEA--PGAPVY 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1729628664 164 VGKPDIDF-------WFDRANAKRFNVAEKYFDEAAKTVKPYLDAGKVKsfsgktvLLPGITAHPTPG 224
Cdd:cd07721    79 AHEREAPYlegekpyPPPVRLGLLGLLSPLLPVKPVPVDRTLEDGDTLD-------LAGGLRVIHTPG 139
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 91-224 5.73e-15

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


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 70.60  E-value: 5.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  91 AFLIDTGDQQVLVDTGAGNFFGPKLGGklqtsLKAAGYTPNEIDAILLTHIHTDHSGG---LVEQgkrvFPAATLYV--- 164
Cdd:cd07726    18 SYLLDGEGRPALIDTGPSSSVPRLLAA-----LEALGIAPEDVDYIILTHIHLDHAGGaglLAEA----LPNAKVYVhpr 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1729628664 165 GKPD-ID---FWfdrANAKRF--NVAEKYFDEaaktVKPyLDAGKVKSFSGKTVLLPG---ITAHPTPG 224
Cdd:cd07726    89 GARHlIDpskLW---ASARAVygDEADRLGGE----ILP-VPEERVIVLEDGETLDLGgrtLEVIDTPG 149
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 88-224 7.05e-15

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: 70.49  E-value: 7.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  88 SINAFLIDTGDQQVLVDTGagnfFGPKLGGKLQTSLKAAGYTpneIDAILLTHIHTDHSGGLVEQGKRVfpAATLYVGKP 167
Cdd:COG0491    14 GVNSYLIVGGDGAVLIDTG----LGPADAEALLAALAALGLD---IKAVLLTHLHPDHVGGLAALAEAF--GAPVYAHAA 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1729628664 168 DIDFWFDRANAKRFNVAEKYFDEAaktvkpyLDAGKVKSFSGktvllPGITAHPTPG 224
Cdd:COG0491    85 EAEALEAPAAGALFGREPVPPDRT-------LEDGDTLELGG-----PGLEVIHTPG 129
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 90-224 8.78e-15

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 69.50  E-value: 8.78e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664   90 NAFLIDTGDQQVLVDTGAGNffgpklGGKLQTSLKAAGytPNEIDAILLTHIHTDHSGGLVEQGKRvfPAATLYVGKPDI 169
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGE------AEDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPELLEA--PGAPVYAPEGTA 70

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1729628664  170 DFWfdrANAKRFNVAEKYFDEAAKTVKPyLDAGKVKSFSGktvllPGITAHPTPG 224
Cdd:smart00849  71 ELL---KDLLALLGELGAEAEPAPPDRT-LKDGDELDLGG-----GELEVIHTPG 116
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
88-224 4.78e-13

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 65.47  E-value: 4.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  88 SINAFLIDTGDQQVLVDTGAGNFFGpklggkLQTSLKAAGYTPNEIDAILLTHIHTDHSGGLVEqGKRVFPAATlYVGKP 167
Cdd:pfam00753   5 QVNSYLIEGGGGAVLIDTGGSAEAA------LLLLLAALGLGPKDIDAVILTHGHFDHIGGLGE-LAEATDVPV-IVVAE 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1729628664 168 DIDFWFDRAnAKRFNVAEKYFDEAAKTVKPYLDAGKVKSFSGKTVLLpGITAHPTPG 224
Cdd:pfam00753  77 EARELLDEE-LGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGL-LVTHGPGHG 131
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 90-149 5.72e-11

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: 58.43  E-value: 5.72e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  90 NAFLIDTGDQQVLVDTGAGnffgpklGGKLQTSLKAAGYTPNEIDAILLTHIHTDHSGGL 149
Cdd:cd07733    10 NCTYLETEDGKLLIDAGLS-------GRKITGRLAEIGRDPEDIDAILVTHEHADHIKGL 62
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 93-165 1.16e-10

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: 58.37  E-value: 1.16e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1729628664  93 LIDTGDQQVLVDTGagnffGPKLGGKLQTSLKAAGYTPNEIDAILLTHIHTDHSGGLveqgkRVFPAATLYVG 165
Cdd:cd07711    26 LIKDGGKNILVDTG-----TPWDRDLLLKALAEHGLSPEDIDYVVLTHGHPDHIGNL-----NLFPNATVIVG 88
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 81-149 2.32e-10

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: 57.69  E-value: 2.32e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  81 LTNPV-EASINAFLIDTGDQQVLVDTGagnFFGPKLGGKLQTSLKAAGYTPNEIDAILLTHIHTDHSGGL 149
Cdd:cd07725     6 LPLPGpLGHVNVYLLRDGDETTLIDTG---LATEEDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLA 72
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 89-224 2.88e-10

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: 58.33  E-value: 2.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  89 INAFLIDTGDQQVLVDTGAgnffgPKLGGKLQTSLKAAGYTPNEIDAILLTHIHTDHSGGLVEQGKRVfpAATLYVGKPD 168
Cdd:cd07708    22 LAAYLIVTPQGNILIDGDM-----EQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAEIKKQT--GAKVMAGAED 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1729628664 169 IDFwFDRANAK---RFNVAEKYFdEAAKTVKPYLDAGKVKsfSGKTVLlpgiTAHPTPG 224
Cdd:cd07708    95 VSL-LLSGGSSdfhYANDSSTYF-PQSTVDRAVHDGERVT--LGGTVL----TAHATPG 145
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 91-218 3.97e-10

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: 58.02  E-value: 3.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  91 AFLIDTGDQQVLVDTGAGnffgpklgGKLQTSLKAAGYTPNEIDAILLTHIHTDHSGGLVEQGKRvFPAATLYVGKpdiD 170
Cdd:cd07713    22 SLLIETEGKKILFDTGQS--------GVLLHNAKKLGIDLSDIDAVVLSHGHYDHTGGLKALLEL-NPKAPVYAHP---D 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1729628664 171 FWFDRANAKRFNVAEKYFDEAAKtvkpYLDAGKVKSFSGKTVLLPGIT 218
Cdd:cd07713    90 AFEPRYSKRGGGKKGIGIGREEL----EKAGARLVLVEEPTEIAPGVY 133
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 90-223 4.37e-10

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 57.98  E-value: 4.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  90 NAFLIDTGDQQVLVDTGagnffgpkLGGKLQtsLKAAGYTPNEIDAILLTHIHTDHSGGLveqgkrvFPAATLYVGKPdI 169
Cdd:COG1235    36 SSILVEADGTRLLIDAG--------PDLREQ--LLRLGLDPSKIDAILLTHEHADHIAGL-------DDLRPRYGPNP-I 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1729628664 170 DFWfdrANAKRFNVAEKYFDEAAKTVKPYLDAGKVKsfSGKTVLLPGITAHPTP 223
Cdd:COG1235    98 PVY---ATPGTLEALERRFPYLFAPYPGKLEFHEIE--PGEPFEIGGLTVTPFP 146
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
91-149 8.43e-10

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 57.13  E-value: 8.43e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1729628664  91 AFLIDTGDQQVLVDTGAGnffgpklggkLQTSLKAAGYTPNEIDAILLTHIHTDHSGGL 149
Cdd:COG1234    21 SYLLEAGGERLLIDCGEG----------TQRQLLRAGLDPRDIDAIFITHLHGDHIAGL 69
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 93-170 8.63e-10

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 56.86  E-value: 8.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  93 LIDTGDQQVLVDTG------------AGNFFGPKLGGKLQTS------LKAAGYTPNEIDAILLTHIHTDHSGGLVEqgk 154
Cdd:cd07742    23 LVETDDGLVLVDTGfgladvadpkrrLGGPFRRLLRPRLDEDetavrqIEALGFDPSDVRHIVLTHLDLDHAGGLAD--- 99

                          90
                  ....*....|....*.
gi 1729628664 155 rvFPAATLYVGKPDID 170
Cdd:cd07742   100 --FPHATVHVHAAELD 113
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 91-168 1.09e-09

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: 55.60  E-value: 1.09e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1729628664  91 AFLIDTGDQQVLVDTGAGNFFGpklGGKLQTSLKAAGYTpnEIDAILLTHIHTDHSGGLVEQGKRvFPAATLYVGKPD 168
Cdd:cd07731    12 AILIQTPGKTILIDTGPRDSFG---EDVVVPYLKARGIK--KLDYLILTHPDADHIGGLDAVLKN-FPVKEVYMPGVT 83
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 78-224 1.31e-09

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: 55.75  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  78 KNFLTNPVEAsiNAFLIDTGDQQ-VLVDTGAGNFfgpklgGKLQTSLKAAGYTpneIDAILLTHIHTDHSGGLVEqgKRV 156
Cdd:cd06262     1 KRLPVGPLQT--NCYLVSDEEGEaILIDPGAGAL------EKILEAIEELGLK---IKAILLTHGHFDHIGGLAE--LKE 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1729628664 157 FPAATLYVGKPDIDFWFD-RANAKRFNVAEKYFDEAAKTVKPyldaGKVKSFSGKTvllpgITAHPTPG 224
Cdd:cd06262    68 APGAPVYIHEADAELLEDpELNLAFFGGGPLPPPEPDILLED----GDTIELGGLE-----LEVIHTPG 127
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 91-153 1.43e-09

Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General function prediction only];


Pssm-ID: 441388 [Multi-domain]  Cd Length: 460  Bit Score: 57.06  E-value: 1.43e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1729628664  91 AFLIDTGDQQVLVDtgAGNFFGPKlgGKLQTSLKAAGYTPNEIDAILLTHIHTDHSG---GLVEQG 153
Cdd:COG1782    16 CHLLETGESRILLD--CGLFQGGR--EERERNNDAFPFDPEELDAVVLTHAHLDHSGllpLLVKYG 77
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 91-149 4.05e-09

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: 54.39  E-value: 4.05e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1729628664  91 AFLIDTGDQQVLVDtgAGNFFGPKLGGKLqtSLKAAGYTPNEIDAILLTHIHTDHSGGL 149
Cdd:cd16295    14 CYLLETGGKRILLD--CGLFQGGKELEEL--NNEPFPFDPKEIDAVILTHAHLDHSGRL 68
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 91-166 6.13e-09

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: 54.58  E-value: 6.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  91 AFLIDTGDQ-QVLVDTG----------------AGNFFGPKLGGKLQTSLKAAGYTPNEIDAILLTHIHTDHSGGLveqg 153
Cdd:cd07730    25 AFLIEHPTGgKILFDLGyrkdfeeytprvperlYRTPVPLEVEEDVAEQLAAGGIDPEDIDAVILSHLHWDHIGGL---- 100

                          90
                  ....*....|...
gi 1729628664 154 kRVFPAATLYVGK 166
Cdd:cd07730   101 -SDFPNARLIVGP 112
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 91-168 6.72e-09

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: 54.48  E-value: 6.72e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1729628664  91 AFLIDTGDQQ-VLVDTGaGNFFGPKLGGKLQTSLKAAGYtpNEIDAILLTHIHTDHSGGLVEQGKRvFPAATLYVGKPD 168
Cdd:COG2333    13 AILIRTPDGKtILIDTG-PRPSFDAGERVVLPYLRALGI--RRLDLLVLTHPDADHIGGLAAVLEA-FPVGRVLVSGPP 87
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 90-155 7.21e-09

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 54.81  E-value: 7.21e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1729628664  90 NAFLIDTGDQQVLVDtgAGNFFGPKLGgklqtSLKAAGYTPNEIDAILLTHIHTDHSGG---LVEQGKR 155
Cdd:COG1236    15 SCYLLETGGTRILID--CGLFQGGKER-----NWPPFPFRPSDVDAVVLTHAHLDHSGAlplLVKEGFR 76
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 91-151 7.40e-09

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: 53.42  E-value: 7.40e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1729628664  91 AFLIDTGDQQVLVDTGAGNFFgpklggklqtSLKAAGYTPNEIDAILLTHIHTDHSGGLVE 151
Cdd:cd16272    19 SYLLETGGTRILLDCGEGTVY----------RLLKAGVDPDKLDAIFLSHFHLDHIGGLPT 69
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 90-149 1.43e-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: 52.54  E-value: 1.43e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  90 NAFLIDTGDQQVLVDTGAGNffgPKLGGKLQTSLKAAGytPNEIDAILLTHIHTDHSGGL 149
Cdd:cd07722    19 NTYLVGTGKRRILIDTGEGR---PSYIPLLKSVLDSEG--NATISDILLTHWHHDHVGGL 73
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 91-149 2.95e-08

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


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 51.75  E-value: 2.95e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1729628664  91 AFLIDTGDQQVLVDTGAGNFfgpklggklqTSLKAAGYTPNEIDAILLTHIHTDHSGGL 149
Cdd:cd07719    20 STLVVVGGRVYLVDAGSGVV----------RRLAQAGLPLGDLDAVFLTHLHSDHVADL 68
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
91-166 5.62e-08

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 51.81  E-value: 5.62e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1729628664  91 AFLIDTGDQQVLVDTGAGNFFgpklggklQTSLKAAGYTPNEIDAILLTHIHTDHSGGLVEQGKRvFPAATLYVGK 166
Cdd:COG1237    24 SALIETEGKRILFDTGQSDVL--------LKNAEKLGIDLSDIDAVVLSHGHYDHTGGLPALLEL-NPKAPVYAHP 90
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 92-150 7.94e-08

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 50.72  E-value: 7.94e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1729628664  92 FLIDTGDQQVLVDTGAGNFfgpklggklqTSLKAAGYTPNEIDAILLTHIHTDHSGGLV 150
Cdd:cd07740    19 FHVASEAGRFLIDCGASSL----------IALKRAGIDPNAIDAIFITHLHGDHFGGLP 67
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 89-224 1.74e-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: 50.40  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  89 INAFLIDTGDQQVLVDTGAgnffgPKLGGKLQTSLKAAGYTPNEIDAILLTHIHTDHSGGLVEQGKrvFPAATLYVGKPD 168
Cdd:cd16288    22 LASYLITTPQGLILIDTGL-----ESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAALKK--LTGAKLMASAED 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1729628664 169 IDFWFDRANAKRFNVAEKYFDEAAKTVKPYLDAGKVKsfSGKTVLlpgiTAHPTPG 224
Cdd:cd16288    95 AALLASGGKSDFHYGDDSLAFPPVKVDRVLKDGDRVT--LGGTTL----TAHLTPG 144
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 89-224 1.88e-07

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


Pssm-ID: 293872 [Multi-domain]  Cd Length: 255  Bit Score: 50.28  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  89 INAFLIDTGDQQVLVDTGAgnffgPKLGGKLQTSLKAAGYTPNEIDAILLTHIHTDHSGGLVEQGKRVfpAATLYVGKPD 168
Cdd:cd16314    22 ISALLVTSDAGHILIDGGT-----DKAAPLIEANIRALGFRPEDVRYIVSSHEHFDHAGGIARLQRAT--GAPVVAREPA 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1729628664 169 IDFwFDRANAKRfnvAEKYFDEAAKtVKPYLDagkVKSFSGKTVLLPG---ITAHPTPG 224
Cdd:cd16314    95 ATT-LERGRSDR---SDPQFLVVEK-FPPVAS---VQRIGDGEVLRVGplaLTAHATPG 145
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 87-155 8.08e-07

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: 48.27  E-value: 8.08e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1729628664  87 ASINAFLIDTGDQQVLVDTGAgnffgPKLGGKLQTSLKAAGYTPNEIDAILLTHIHTDHSGGLVEQGKR 155
Cdd:cd16289    20 ESLTALLVKTPDGAVLLDGGM-----PQAADMLLDNMRALGVAPGDLKLILHSHAHADHAGPLAALKRA 83
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 87-148 1.03e-06

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 47.96  E-value: 1.03e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729628664  87 ASINAFLIDTGDQQVLVDTGAGNFFGPKLGGklqtSLKAAGYTPNEIDAILLTHIHTDHSGG 148
Cdd:cd16280    20 KWVSAWAIDTGDGLILIDALNNNEAADLIVD----GLEKLGLDPADIKYILITHGHGDHYGG 77
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 87-224 1.79e-06

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: 47.48  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  87 ASINAFLIDTGDQQVLVDTGAgnffgPKLGGKLQTSLKAAGYTPNEIDAILLTHIHTDHSGGLVEQGKRVfpAATLYVGK 166
Cdd:cd16309    20 AGLGVFLITTPEGHILIDGAM-----PQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAELKKAT--GAQLVASA 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1729628664 167 PDidfwfdranakrfnvaekyfdeaaktvKPYLDAGKVKSFSGKTVLLPGI-------------------TAHPTPG 224
Cdd:cd16309    93 AD---------------------------KPLLESGYVGSGDTKNLQFPPVrvdrvigdgdkvtlggttlTAHLTPG 142
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 ...
 87-224 3.06e-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: 46.57  E-value: 3.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  87 ASINAFLIDTGDQQVLVDTGAgnffgPKLGGKLQTSLKAAGYTPNEIDAILLTHIHTDHSGGLVE----QGKRVFP---- 158
Cdd:cd16290    20 GGLSAVLITSPQGLILIDGAL-----PQSAPQIEANIRALGFRLEDVKLILNSHAHFDHAGGIAAlqrdSGATVAAspag 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1729628664 159 AATLYVGKPDIDfwfdranakrfnvaekyfDEAAKTVKPYLDAGKVKSFS-GKTVLLPG--ITAHPTPG 224
Cdd:cd16290    95 AAALRSGGVDPD------------------DPQAGAADPFPPVAKVRVVAdGEVVKLGPlaVTAHATPG 145
PRK00055 PRK00055
ribonuclease Z; Reviewed
 90-149 9.17e-06

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 45.17  E-value: 9.17e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  90 NAFLIDTGDQQVLVDTGAGNffgpklggklQTSLKAAGYTPNEIDAILLTHIHTDHSGGL 149
Cdd:PRK00055   21 SSILLRLGGELFLFDCGEGT----------QRQLLKTGIKPRKIDKIFITHLHGDHIFGL 70
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 90-145 1.05e-05

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 44.91  E-value: 1.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1729628664  90 NAFLIDTGDQQVLVDTgagnFFGPKLGGKLQTSLKAAGYTPneIDAILLTHIHTDH 145
Cdd:COG2220    12 ATFLIETGGKRILIDP----VFSGRASPVNPLPLDPEDLPK--IDAVLVTHDHYDH 61
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 90-176 1.84e-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: 43.63  E-value: 1.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  90 NAFLIDTGDQQVLVDTGagnffgPKLGGKLQTSLKAAGytPNEIDAILLTHIHTDHSGG---LVEQ-GKRVFPAATLYVG 165
Cdd:cd16278    19 NTYLLGAPDGVVVIDPG------PDDPAHLDALLAALG--GGRVSAILVTHTHRDHSPGaarLAERtGAPVRAFGPHRAG 90

                          90
                  ....*....|.
gi 1729628664 166 KPDIDFWFDRA 176
Cdd:cd16278    91 GQDTDFAPDRP 101
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 91-155 2.39e-05

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 43.65  E-value: 2.39e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1729628664  91 AFLIDTGDQQVLVDtgagnffgPKLGGKLQTSLKAAGYtpnEIDAILLTHIHTDHSGGLVEQGKR 155
Cdd:PRK00685   10 AFLIETGGKKILID--------PFITGNPLADLKPEDV---KVDYILLTHGHGDHLGDTVEIAKR 63
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 89-224 2.62e-05

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: 43.88  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  89 INAFLIDTGDQQVLVDTGAgnffgPKLGGKLQTSLKAAGYTPNEIDAILLTHIHTDHSGGLVE----QGKRVF--PAA-- 160
Cdd:cd16315    22 ISAILITGDDGHVLIDSGT-----EEAAPLVLANIRKLGFDPKDVRWLLSSHEHFDHVGGLAAlqraTGARVAasAAAap 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1729628664 161 TLYVGKPDidfwfdrANAKRFNVAEkyfDEAAKTVKPYLDAGKVKSFsGKTVLlpgiTAHPTPG 224
Cdd:cd16315    97 VLESGKPA-------PDDPQAGLHE---PFPPVRVDRIVEDGDTVAL-GSLRL----TAHATPG 145
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 93-149 3.66e-05

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


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 42.85  E-value: 3.66e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1729628664  93 LIDTGDQQVLVDTGagnffgPKLggKLQtsLKAAGytPNEIDAILLTHIHTDHSGGL 149
Cdd:cd16279    39 LIETGGKNILIDTG------PDF--RQQ--ALRAG--IRKLDAVLLTHAHADHIHGL 83
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 86-168 7.09e-05

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: 41.68  E-value: 7.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  86 EASINAFLIDTGDQQVLVDTgagnffgpklggklqtsLKAAGYTpneIDAILLTHIHTDHSGGlVEQGKRVFPAATLYVG 165
Cdd:cd07723    17 EATGEAAVVDPGEAEPVLAA-----------------LEKNGLT---LTAILTTHHHWDHTGG-NAELKALFPDAPVYGP 75


                  ...
gi 1729628664 166 KPD 168
Cdd:cd07723    76 AED 78
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 90-148 7.46e-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: 42.17  E-value: 7.46e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1729628664  90 NAFLIDTGDQQVLVDTGagnfFGPKLGGKLQTSLKAAgyTPNEIDAILLTHIHTDHSGG 148
Cdd:cd16282    16 NIGFIVGDDGVVVIDTG----ASPRLARALLAAIRKV--TDKPVRYVVNTHYHGDHTLG 68
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 89-224 1.05e-04

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


Pssm-ID: 293869  Cd Length: 257  Bit Score: 42.28  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  89 INAFLIDTGDQQVLVDTGAgnffgPKLGGKLQTSLKAAGYTPNEIDAILLTHIHTDHSGGLVEQGKRvfpAATLYVGKPD 168
Cdd:cd16311    22 LSSVLVTSPQGHVLVDGGL-----PESAPKIIANIEALGFRIEDVKLILNSHGHIDHAGGLAELQRR---SGALVAASPS 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664 169 IDFWFDRANAK----RFNVAEKYfdEAAKTVKPYLDAGKVKsfsgktVLLPGITAHPTPG 224
Cdd:cd16311    94 AALDLASGEVGpddpQYHALPKY--PPVKDMRLARDGGQFN------VGPVSLTAHATPG 145
NorV COG0426
Flavorubredoxin [Energy production and conversion];
90-171 1.39e-04

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 42.13  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  90 NAFLIDtGDQQVLVDTGaGNFFGPKLGGKLQTSLKaagytPNEIDAILLTHIHTDHSGGLveqgKRV---FPAATLYVGK 166
Cdd:COG0426    35 NSYLIV-DEKTALIDTV-GESFFEEFLENLSKVID-----PKKIDYIIVNHQEPDHSGSL----PELlelAPNAKIVCSK 103


                  ....*
gi 1729628664 167 PDIDF 171
Cdd:COG0426   104 KAARF 108
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 90-149 1.71e-04

Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; 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. 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. 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; this subgroup includes the short form (ELAC1). Only the short form exists in bacteria. 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: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 41.28  E-value: 1.71e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  90 NAFLIDTGDQQVLVDTGAGnffgpklggkLQTSLKAAGYTPNEIDAILLTHIHTDHSGGL 149
Cdd:cd07717    18 SSIALRLEGELWLFDCGEG----------TQRQLLRAGLSPSKIDRIFITHLHGDHILGL 67
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 88-167 2.14e-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: 40.93  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  88 SINAFLIDtGDQQVLVDTGAGNFFgPKLGGKLQTSLKaagytPNEIDAILLTHIHTDHSGGLVEQgKRVFPAATLYVGKP 167
Cdd:cd07709    31 SYNSYLIK-DEKTALIDTVKEPFF-DEFLENLEEVID-----PRKIDYIVVNHQEPDHSGSLPEL-LELAPNAKIVCSKK 102
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 87-224 2.30e-04

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


Pssm-ID: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 41.00  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  87 ASINAFLIDTGDQQVLVDTGAgnffgPKLGGKLQTSLKAAGYTPNEIDAILLTHIHTDHSGGLVEQGKrvFPAATLYVGK 166
Cdd:cd16313    20 GGISAVLITSPQGHILIDGGF-----PKSPEQIAASIRQLGFKLEDVKYILSSHDHWDHAGGIAALQK--LTGAQVLASP 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1729628664 167 PDIDfwfdranAKRFNVAEKYfDEAAKTVKPYLDAGKVKSFS-GKTVLL-P-GITAHPTPG 224
Cdd:cd16313    93 ATVA-------VLRSGSMGKD-DPQFGGLTPMPPVASVRAVRdGEVVKLgPlAVTAHATPG 145
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 123-172 2.82e-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: 40.21  E-value: 2.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1729628664 123 LKAAGYTPNEIDAILLTHIHTDHSgGLVEQGKRVFPaATLYVGKPDIDFW 172
Cdd:cd16275    38 LAKLNELGLTLTGILLTHSHFDHV-NLVEPLLAKYD-APVYMSKEEIDYY 85
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 92-145 4.01e-04

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


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 39.73  E-value: 4.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1729628664  92 FLIDTGDQQVLVDTGAGNFfgpklgGKLQTSLkaagyTPNEIDAILLTHIHTDH 145
Cdd:cd07716    21 YLLEADGFRILLDCGSGVL------SRLQRYI-----DPEDLDAVVLSHLHPDH 63
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 85-148 9.20e-04

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 39.05  E-value: 9.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1729628664  85 VEASINAFLIDTGDQQV-LVDTGAGNffgpKLGGKLQTSLKAAGYTPneiDAILLTHIHTDHSGG 148
Cdd:cd07743     4 IPGPTNIGVYVFGDKEAlLIDSGLDE----DAGRKIRKILEELGWKL---KAIINTHSHADHIGG 61
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 90-149 1.19e-03

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: 38.48  E-value: 1.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729628664  90 NAFLI--DTGDQQVLVDTGAGNffgpklggklQTSLKAAGYTPNEIDAILLTHIHTDHSGGL 149
Cdd:cd16322    12 NTYLVadEGGGEAVLVDPGDES----------EKLLARFGTTGLTLLYILLTHAHFDHVGGV 63
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 91-149 1.41e-03

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


Pssm-ID: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 38.47  E-value: 1.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1729628664  91 AFLIDTGDQQVLVDTGAgnFFGPKLGGKLqtsLKAAGYTPNEIDAILLTHIHTDHSGGL 149
Cdd:cd07734    13 CFLVEFKGRTVLLDCGM--NPGKEDPEAC---LPQFELLPPEIDAILISHFHLDHCGAL 66
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 89-149 1.76e-03

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: 38.59  E-value: 1.76e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1729628664  89 INAFLIDTGDQQVLVDTGagnffgPKLGGKL-QTSLKAAGYTPNEIDAILLTHIHTDHSGGL 149
Cdd:cd16310    22 IGSYLITSNHGAILLDGG------LEENAALiEQNIKALGFKLSDIKIIINTHAHYDHAGGL 77
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 92-147 3.02e-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: 37.55  E-value: 3.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1729628664  92 FLIDTGDQQVLVDTGAG---NFFGPKLggklqtslkaagyTPNEIDAILLTHIHTDHSG 147
Cdd:cd07741    23 IWIELNGKNIHIDPGPGalvRMCRPKL-------------DPTKLDAIILSHRHLDHSN 68
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 90-187 4.04e-03

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: 36.84  E-value: 4.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  90 NAFLIDTGDQQVLVDTGAGnffgpklggklQTSLKAAGYTPNEIDAI-LLTHIHTDHSGGLVEQGKR-VFPA-ATLYVGK 166
Cdd:cd07712    10 NIYLLRGRDRALLIDTGLG-----------IGDLKEYVRTLTDLPLLvVATHGHFDHIGGLHEFEEVyVHPAdAEILAAP 78

                          90       100
                  ....*....|....*....|.
gi 1729628664 167 PDIDFWFDRANAKRFNVAEKY 187
Cdd:cd07712    79 DNFETLTWDAATYSVPPAGPT 99
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 101-149 6.33e-03

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 36.52  E-value: 6.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1729628664 101 VLVDTGAGnFFGPKLggkLQTSLKAAGYTPneIDAILLTHIHTDHSGGL 149
Cdd:pfam12706   3 ILIDPGPD-LRQQAL---PALQPGRLRDDP--IDAVLLTHDHYDHLAGL 45
PhnP-like_MBL-fold cd07736
phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase ...
 126-149 7.90e-03

phosphodiesterase Escherichia coli PhnP and related proteins; MBL-fold metallo hydrolase domain; Escherichia coli PhnP catalyzes the hydrolysis of 5-phospho-D-ribose-1,2-cyclic phosphate to D-ribose-1,5-bisphosphate, a step in the C-P lyase pathway. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily. 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: 293822 [Multi-domain]  Cd Length: 186  Bit Score: 36.06  E-value: 7.90e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1729628664 126 AGYT-------PNEIDAILLTHIHTDHSGGL 149
Cdd:cd07736    53 AGLTdlaerfpPGSIDAILLTHFHMDHVQGL 83
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 92-156 8.04e-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: 36.12  E-value: 8.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1729628664  92 FLIDTGDQQVLVDTGAGNffgpklggklQTSLKAAGYTPNEIDAILLTHIHTDHSGGLVE---QGKRV 156
Cdd:cd07738    18 FIIWINGRGIMVDPPVNS----------TSYLRQNGISPRLVDHVILTHCHADHDAGTFQkilEEEKI 75
class_II_PDE_MBL-fold cd07735
class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium ...
 91-150 8.33e-03

class II cyclic nucleotide phosphodiesterases Saccharomyces cerevisiae PDE1, Dictyostelium discoideum PDE1 and PDE7, and related proteins; MBL-fold metallo-hydrolase domain; Cyclic nucleotide phosphodiesterases (PDEs) decompose the second messengers cyclic adenosine and guanosine 3',5'-monophosphate (cAMP and cGMP, respectively). Saccharomyces cerevisiae PDE1 and Dictyostelium discoideum PDE1 and PDE7, have dual cAMP/cGMP specificity. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293821  Cd Length: 259  Bit Score: 36.42  E-value: 8.33e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1729628664  91 AFLIDTGDQQ--VLVDTGAG--------NFfgpklGGKLQTSLKAAGYTPNEIDAILLTHIHTDHSGGLV 150
Cdd:cd07735    19 SFLLDPAGSDgdILLDAGTGvgalsleeMF-----NDILFPSQKAAYELYQRIRHYLITHAHLDHIAGLP 83
 
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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