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Conserved domains on  [gi|510023053|emb|CCW35093|]
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Zn-dependent hydrolases, including glyoxylases [Chthonomonas calidirosea T49]

Protein Classification

MBL fold metallo-hydrolase; INTS11 family MBL fold metallo-hydrolase( domain architecture ID 10888885)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme| INTS11 family MBL fold metallo-hydrolase similar to metazoan Integrator complex subunit 11, which is part of the complex that is 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 3-205 7.01e-102

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: 293.10  E-value: 7.01e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053   3 IYRHLLGPMDNNTYLIVDEVTGEAALVDPSFDSEQLLPEIEQLGYSLRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDD 82
Cdd:cd16322    1 VRPFTLGPLQENTYLVADEGGGEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  83 LGLLHAVPEQAKAFQVEVEPSPEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTFLVED--AALVGDCLFQGSIGRVDL 160
Cdd:cd16322   81 LPLYEAADLGAKAFGLGIEPLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEegLLFSGDLLFQGSIGRTDL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 510023053 161 PGGsAEQLMASLHNRLLTLPDETRVLPGHGEPTTIGAEKRHNPFL 205
Cdd:cd16322  161 PGG-DPKAMAASLRRLLTLPDETRVFPGHGPPTTLGEERRTNPFL 204
 
Name Accession Description Interval E-value
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 3-205 7.01e-102

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: 293.10  E-value: 7.01e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053   3 IYRHLLGPMDNNTYLIVDEVTGEAALVDPSFDSEQLLPEIEQLGYSLRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDD 82
Cdd:cd16322    1 VRPFTLGPLQENTYLVADEGGGEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  83 LGLLHAVPEQAKAFQVEVEPSPEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTFLVED--AALVGDCLFQGSIGRVDL 160
Cdd:cd16322   81 LPLYEAADLGAKAFGLGIEPLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEegLLFSGDLLFQGSIGRTDL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 510023053 161 PGGsAEQLMASLHNRLLTLPDETRVLPGHGEPTTIGAEKRHNPFL 205
Cdd:cd16322  161 PGG-DPKAMAASLRRLLTLPDETRVFPGHGPPTTLGEERRTNPFL 204
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 10-205 1.41e-55

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: 176.03  E-value: 1.41e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  10 PMDNNTYLIVDevTGEAALVDPSFDS---EQLLPEIEQLGYSLRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDDLGLL 86
Cdd:COG0491   12 GLGVNSYLIVG--GDGAVLIDTGLGPadaEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEAL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  87 havpEQAKAFQVEVEPSPEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTFLVED--AALVGDCLFQGSIGRVDLPGGS 164
Cdd:COG0491   90 ----EAPAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDekVLFTGDALFSGGVGRPDLPDGD 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 510023053 165 AEQLMASLHnRLLTLPDEtRVLPGHGEPTTIGA-----------EKRHNPFL 205
Cdd:COG0491  166 LAQWLASLE-RLLALPPD-LVIPGHGPPTTAEAidyleellaalGERANPFL 215
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 14-189 1.88e-36

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: 125.74  E-value: 1.88e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053    14 NTYLIVDEvtGEAALVDPSF-DSEQLLPEIEQLGYS-LRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDDLGLLhAVPE 91
Cdd:smart00849   1 NSYLVRDD--GGAILIDTGPgEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELL-KDLL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053    92 QAKAFQVEVEPSPEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTFLVED--AALVGDCLFQGSIGRVDLPGGSAEQLM 169
Cdd:smart00849  78 ALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEgkILFTGDLLFAGGDGRTLVDGGDAAASD 157

                          170       180
                   ....*....|....*....|
gi 510023053   170 ASLHNRLLTLPDETRVLPGH 189
Cdd:smart00849 158 ALESLLKLLKLLPKLVVPGH 177
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 12-208 3.60e-27

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 105.70  E-value: 3.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  12 DNNTYLIVDEVTGEAALVDPSfDSEQLLPEIEQLGYSLRYILNTHAHLDHVVGNAFFAAWTGAPI---ALHKDDLgllha 88
Cdd:PLN02398  86 DNYAYLLHDEDTGTVGVVDPS-EAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVigsAVDKDRI----- 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  89 vpeqakafqvevepsPEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTFLVEDAALV--GDCLFQGSIGRvdLPGGSAE 166
Cdd:PLN02398 160 ---------------PGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIftGDTLFSLSCGK--LFEGTPE 222

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510023053 167 QLMASLHnRLLTLPDETRVLPGHGE------------------------------------PTTIGAEKRHNPFLRSS 208
Cdd:PLN02398 223 QMLSSLQ-KIISLPDDTNIYCGHEYtlsnskfalsiepnnevlqsyaahvahlrskglptiPTTVKMEKACNPFLRTS 299
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
8-189 2.87e-23

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 92.43  E-value: 2.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053    8 LGPMDNNTYLIVDEvtGEAALVDP----SFDSEQLLPEIEQLGYSLRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDD- 82
Cdd:pfam00753   1 LGPGQVNSYLIEGG--GGAVLIDTggsaEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEa 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053   83 ---LGLLHAVPEQAKAFQVEVEPSPEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTFLVEDA--ALVGDCLFQGSIGR 157
Cdd:pfam00753  79 relLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGkvLFTGDLLFAGEIGR 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 510023053  158 VDLPGGSAEQLMASLHN------RLLTLPDETRVLPGH 189
Cdd:pfam00753 159 LDLPLGGLLVLHPSSAEssleslLKLAKLKAAVIVPGH 196
SoxH_rel_PQQ_2 TIGR04559
quinoprotein relay system zinc metallohydrolase 2; By homology, members are Zn ...
 36-200 1.69e-08

quinoprotein relay system zinc metallohydrolase 2; By homology, members are Zn metallohydrolases in the same family as the SoxH protein associated with sulfate metabolism, Bacillus cereus beta-lactamase II (see PDB:1bc2), and, more distantly, hydroxyacylglutathione hydrolase (glyoxalase II). All members occur in genomes with both PQQ biosynthesis and a PQQ-dependent (quinoprotein) dehydrogenase that has a motif of two consecutive Cys residues (see TIGR03075). The Cys-Cys motif is associated with electron transfer by specialized cytochromes such as c551. All these genomes also include a fusion protein (TIGR04557) whose domains resemble SoxY and SoxZ from thiosulfate oxidation. A conserved Cys in this fusion protein aligns to the Cys residue in SoxY that carries sulfur cycle intermediates. In many genomes, the genes for PQQ biosynthesis enzymes, PQQ-dependent enzymes, their associated cytochromes, and members of this family are clustered. Note that one to three closely related Zn metallohydrolases may occur; this family represents a specific clade among them. Some members of this family have a short additional N-terminal domain with four conserved Cys residues. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275352  Cd Length: 283  Bit Score: 53.35  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053   36 EQLLPEIEQL-GYSLRYILNTHAHLDHVVGNAFFAAwTGAPIALHK---DDLGL-----LHAVPEQAKAFQVEVEPSPeP 106
Cdd:TIGR04559  54 EALLAAIRQRtDLPIRYVINTHVHPDHIFGNAAFRE-DGAEFVGHAklpRALAArgefyLASFARLLGEAFLGTEIVP-P 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  107 EILLEDGQELPLGElsiKVLHTPGHAPGH----VTFLVEDAALV--GDCLFQGSIGRVD--LPGGSA--EQLMAslhnrl 176
Cdd:TIGR04559 132 TRLVADPLELDLGG---RVLELTAWPTAHtdndLTVFDEKTGTLftGDLLFVEHIPVLDgsLLGWLAvlDRLKA------ 202

                         170       180
                  ....*....|....*....|....*....
gi 510023053  177 ltlPDETRVLPGHGEPTT-----IGAEKR 200
Cdd:TIGR04559 203 ---RPAARVVPGHGPVSLdwpaaLAPQRR 228
 
Name Accession Description Interval E-value
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 3-205 7.01e-102

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: 293.10  E-value: 7.01e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053   3 IYRHLLGPMDNNTYLIVDEVTGEAALVDPSFDSEQLLPEIEQLGYSLRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDD 82
Cdd:cd16322    1 VRPFTLGPLQENTYLVADEGGGEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  83 LGLLHAVPEQAKAFQVEVEPSPEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTFLVED--AALVGDCLFQGSIGRVDL 160
Cdd:cd16322   81 LPLYEAADLGAKAFGLGIEPLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEegLLFSGDLLFQGSIGRTDL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 510023053 161 PGGsAEQLMASLHNRLLTLPDETRVLPGHGEPTTIGAEKRHNPFL 205
Cdd:cd16322  161 PGG-DPKAMAASLRRLLTLPDETRVFPGHGPPTTLGEERRTNPFL 204
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 4-189 8.14e-71

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: 213.69  E-value: 8.14e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053   4 YRHLLGPMDNNTYLIVDEvTGEAALVDPSFDS-EQLLPEIEQLGYSLRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDD 82
Cdd:cd06262    1 KRLPVGPLQTNCYLVSDE-EGEAILIDPGAGAlEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEAD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  83 LGLLHAVPEQAKAFQVEVEPSPEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTFLVED--AALVGDCLFQGSIGRVDL 160
Cdd:cd06262   80 AELLEDPELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEegVLFTGDTLFAGSIGRTDL 159

                        170       180
                 ....*....|....*....|....*....
gi 510023053 161 PGGSAEQLMASLHNRLLTLPDETRVLPGH 189
Cdd:cd06262  160 PGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 14-189 3.30e-61

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


Pssm-ID: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 189.30  E-value: 3.30e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  14 NTYLIVDEVTGEAALVDPSFDSEQLLPEIEQLGYSLRYILNTHAHLDHVVGNAFFAAWTGAPIA-LHKDDLGLLHAVPEQ 92
Cdd:cd07737   12 NCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIgPHKEDKFLLENLPEQ 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  93 AKAFQVEVEPSPEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTFLVEDA--ALVGDCLFQGSIGRVDLPGGSAEQLMA 170
Cdd:cd07737   92 SQMFGFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESklAIVGDVLFKGSIGRTDFPGGNHAQLIA 171

                        170
                 ....*....|....*....
gi 510023053 171 SLHNRLLTLPDETRVLPGH 189
Cdd:cd07737  172 SIKEKLLPLGDDVTFIPGH 190
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 15-190 1.07e-59

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


Pssm-ID: 293810 [Multi-domain]  Cd Length: 177  Bit Score: 184.91  E-value: 1.07e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  15 TYLIVDEVTGEAALVDPSFDS-EQLLPEIEQLGYSLRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDDlgllhavpeqa 93
Cdd:cd07724   14 SYLVGDPETGEAAVIDPVRDSvDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIVIGEGA----------- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  94 kafqvevePSPEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTFLVED--AALVGDCLFQGSIGRVDLPG---GSAEQL 168
Cdd:cd07724   83 --------PASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDpdAVFTGDTLFVGDVGRPDLPGeaeGLARQL 154

                        170       180
                 ....*....|....*....|..
gi 510023053 169 MASLHNRLLTLPDETRVLPGHG 190
Cdd:cd07724  155 YDSLQRKLLLLPDETLVYPGHD 176
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 10-205 1.41e-55

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: 176.03  E-value: 1.41e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  10 PMDNNTYLIVDevTGEAALVDPSFDS---EQLLPEIEQLGYSLRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDDLGLL 86
Cdd:COG0491   12 GLGVNSYLIVG--GDGAVLIDTGLGPadaEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEAL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  87 havpEQAKAFQVEVEPSPEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTFLVED--AALVGDCLFQGSIGRVDLPGGS 164
Cdd:COG0491   90 ----EAPAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDekVLFTGDALFSGGVGRPDLPDGD 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 510023053 165 AEQLMASLHnRLLTLPDEtRVLPGHGEPTTIGA-----------EKRHNPFL 205
Cdd:COG0491  166 LAQWLASLE-RLLALPPD-LVIPGHGPPTTAEAidyleellaalGERANPFL 215
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 11-189 1.80e-48

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: 156.08  E-value: 1.80e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  11 MDNNTYLIVDEVTGEAALVDPSfDSEQLLPEIEQLGYSLRYILNTHAHLDHVVGNA-FFAAWTGAPIALHKDDlgllhav 89
Cdd:cd07723    7 SDNYIYLIVDEATGEAAVVDPG-EAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAeLKALFPDAPVYGPAED------- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  90 peqakafqvevePSPEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTFLVEDAALV--GDCLFQGSIGRVDLpgGSAEQ 167
Cdd:cd07723   79 ------------RIPGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALftGDTLFSGGCGRFFE--GTAEQ 144

                        170       180
                 ....*....|....*....|..
gi 510023053 168 LMASLhNRLLTLPDETRVLPGH 189
Cdd:cd07723  145 MYASL-QKLLALPDDTLVYCGH 165
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 8-189 1.09e-46

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: 151.92  E-value: 1.09e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053   8 LGPMDNNTYLIVDEVTGEAALVDPSFDSEQLLPEIEQLGYSLRYILNTHAHLDHVVGNAFFAAWTGAPIALHKddlgllh 87
Cdd:cd16275    7 AGPMINYSYIIIDKATREAAVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSK------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  88 avpEQAKAFQVevepSPEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTFLVEDAALVGDCLFQGSIGRVDLPGGSAEQ 167
Cdd:cd16275   80 ---EEIDYYGF----RCPNLIPLEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGDSLFTGDTLFIEGCGRCDLPGGDPEE 152

                        170       180
                 ....*....|....*....|...
gi 510023053 168 LMASLHnRLLTLPDE-TRVLPGH 189
Cdd:cd16275  153 MYESLQ-RLKKLPPPnTRVYPGH 174
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 14-189 1.88e-36

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: 125.74  E-value: 1.88e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053    14 NTYLIVDEvtGEAALVDPSF-DSEQLLPEIEQLGYS-LRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDDLGLLhAVPE 91
Cdd:smart00849   1 NSYLVRDD--GGAILIDTGPgEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELL-KDLL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053    92 QAKAFQVEVEPSPEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTFLVED--AALVGDCLFQGSIGRVDLPGGSAEQLM 169
Cdd:smart00849  78 ALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEgkILFTGDLLFAGGDGRTLVDGGDAAASD 157

                          170       180
                   ....*....|....*....|
gi 510023053   170 ASLHNRLLTLPDETRVLPGH 189
Cdd:smart00849 158 ALESLLKLLKLLPKLVVPGH 177
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 14-190 4.33e-30

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: 110.00  E-value: 4.33e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  14 NTYLIVDEvtGEAALVD--PSFDSEQLLPEIEQLGYS---LRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDDLGLL-- 86
Cdd:cd07721   12 NAYLIEDD--DGLTLIDtgLPGSAKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEREAPYLeg 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  87 -----HAVPEQAKAFQVEVEP--SPEPEILLEDGQELPLGElSIKVLHTPGHAPGHVTFLVE--DAALVGDcLFQGSIGR 157
Cdd:cd07721   90 ekpypPPVRLGLLGLLSPLLPvkPVPVDRTLEDGDTLDLAG-GLRVIHTPGHTPGHISLYLEedGVLIAGD-ALVTVGGE 167

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 510023053 158 VDLPGGSA----EQLMASLHnRLLTLpDETRVLPGHG 190
Cdd:cd07721  168 LVPPPPPFtwdmEEALESLR-KLAEL-DPEVLAPGHG 202
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-192 9.32e-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: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 106.04  E-value: 9.32e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  14 NTYLIVDEvtGEAALVDPSFDSEQ----LLPEIEqlGYSLRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDdlgllHAV 89
Cdd:cd16278   19 NTYLLGAP--DGVVVIDPGPDDPAhldaLLAALG--GGRVSAILVTHTHRDHSPGAARLAERTGAPVRAFGP-----HRA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  90 PEQAKAFQvevepspePEILLEDGQELPLGELSIKVLHTPGHAPGHVTFLV--EDAALVGDCLFQGSIGRVDLPGGSAEQ 167
Cdd:cd16278   90 GGQDTDFA--------PDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALedEGALFTGDHVMGWSTTVIAPPDGDLGD 161

                        170       180
                 ....*....|....*....|....*
gi 510023053 168 LMASLHnRLLTLPDEtRVLPGHGEP 192
Cdd:cd16278  162 YLASLE-RLLALDDR-LLLPGHGPP 184
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 12-208 3.60e-27

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 105.70  E-value: 3.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  12 DNNTYLIVDEVTGEAALVDPSfDSEQLLPEIEQLGYSLRYILNTHAHLDHVVGNAFFAAWTGAPI---ALHKDDLgllha 88
Cdd:PLN02398  86 DNYAYLLHDEDTGTVGVVDPS-EAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVigsAVDKDRI----- 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  89 vpeqakafqvevepsPEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTFLVEDAALV--GDCLFQGSIGRvdLPGGSAE 166
Cdd:PLN02398 160 ---------------PGIDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYFPGSGAIftGDTLFSLSCGK--LFEGTPE 222

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510023053 167 QLMASLHnRLLTLPDETRVLPGHGE------------------------------------PTTIGAEKRHNPFLRSS 208
Cdd:PLN02398 223 QMLSSLQ-KIISLPDDTNIYCGHEYtlsnskfalsiepnnevlqsyaahvahlrskglptiPTTVKMEKACNPFLRTS 299
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 15-205 9.21e-26

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 100.26  E-value: 9.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  15 TYLIVDEVTGE--AALVDPSFDS-EQLLPEIEQLGYSLRYILNTHAHLDHVVGNAFFAawTGAPialhkddlGLLHAVPE 91
Cdd:PLN02962  25 TYLLADVSHPDkpALLIDPVDKTvDRDLSLVKELGLKLIYAMNTHVHADHVTGTGLLK--TKLP--------GVKSIISK 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  92 QAKAfqvevepspEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTFLVEDA--------ALVGDCLFQGSIGRVDLPGG 163
Cdd:PLN02962  95 ASGS---------KADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGpdqpqprmAFTGDALLIRGCGRTDFQGG 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 510023053 164 SAEQLMASLHNRLLTLPDETRVLPGHG----EPTTIGAEKRHNPFL 205
Cdd:PLN02962 166 SSDQLYKSVHSQIFTLPKDTLIYPAHDykgfTVSTVGEEMLYNPRL 211
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 12-206 5.31e-25

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 98.29  E-value: 5.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  12 DNNTYLIVDEVTGEAALVDPsFDSEQLLPEIEQLGYSLRYILNTHAHLDHVVGNaffaawtgapialhkddlgllHAVPE 91
Cdd:PLN02469  11 DNYAYLIIDESTKDAAVVDP-VDPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGN---------------------EKIKK 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  92 QAKAFQV------EVEPSPEPeilLEDGQELPLG-ELSIKVLHTPGHAPGHVTFLV-----EDAAL-VGDCLFQGSIGRV 158
Cdd:PLN02469  69 LVPGIKVyggsldNVKGCTHP---VENGDKLSLGkDVNILALHTPCHTKGHISYYVtgkegEDPAVfTGDTLFIAGCGKF 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053 159 DlpGGSAEQLMASLHNRLLTLPDETRVLPGH---------------------------------GEPT---TIGAEKRHN 202
Cdd:PLN02469 146 F--EGTAEQMYQSLCVTLGSLPKPTQVYCGHeytvknlkfaltvepdneklkqklewaekqrqaGLPTvpsTIEEELETN 223


                 ....
gi 510023053 203 PFLR 206
Cdd:PLN02469 224 PFMR 227
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
8-189 2.87e-23

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 92.43  E-value: 2.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053    8 LGPMDNNTYLIVDEvtGEAALVDP----SFDSEQLLPEIEQLGYSLRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDD- 82
Cdd:pfam00753   1 LGPGQVNSYLIEGG--GGAVLIDTggsaEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEa 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053   83 ---LGLLHAVPEQAKAFQVEVEPSPEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTFLVEDA--ALVGDCLFQGSIGR 157
Cdd:pfam00753  79 relLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGkvLFTGDLLFAGEIGR 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 510023053  158 VDLPGGSAEQLMASLHN------RLLTLPDETRVLPGH 189
Cdd:pfam00753 159 LDLPLGGLLVLHPSSAEssleslLKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 9-194 3.69e-22

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: 89.55  E-value: 3.69e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053   9 GPMDNNTYLIVDEvtGEAALVDPSFD---SEQLLPEIEQL-GYSLRYILNTHAHLDHVVGNAFFAAwTGAPIALHKDDLG 84
Cdd:cd16282   11 GGFISNIGFIVGD--DGVVVIDTGASprlARALLAAIRKVtDKPVRYVVNTHYHGDHTLGNAAFAD-AGAPIIAHENTRE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  85 LLHAVPEQAKAFQVEVEPSPE-------PEILLEDGQELPLGELSIKVLHT-PGHAPGHVTFLVEDAALV--GDCLFQGS 154
Cdd:cd16282   88 ELAARGEAYLELMRRLGGDAMagtelvlPDRTFDDGLTLDLGGRTVELIHLgPAHTPGDLVVWLPEEGVLfaGDLVFNGR 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 510023053 155 IGRVdlPGGSAEQLMASLhNRLLTLPDETrVLPGHGEPTT 194
Cdd:cd16282  168 IPFL--PDGSLAGWIAAL-DRLLALDATV-VVPGHGPVGD 203
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 27-147 1.49e-20

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 86.48  E-value: 1.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  27 ALVDPSFdSEQLLPEIEQLGYS---LRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDDLGLLHAVPEQAKAFqVEVEPs 103
Cdd:cd16280   38 ALNNNEA-ADLIVDGLEKLGLDpadIKYILITHGHGDHYGGAAYLKDLYGAKVVMSEADWDMMEEPPEEGDNP-RWGPP- 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 510023053 104 PEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTFL--VED------AALVG 147
Cdd:cd16280  115 PERDIVIKDGDTLTLGDTTITVYLTPGHTPGTLSLIfpVKDggkthrAGLWG 166
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 15-189 1.32e-17

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


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 77.53  E-value: 1.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  15 TYLIVDEvtGEAALVD--PSFDSEQLLPEIEQLGYS---LRYILNTHAHLDHVVGNAFFA-AWTGAPIALHKddLGLLH- 87
Cdd:cd07726   18 SYLLDGE--GRPALIDtgPSSSVPRLLAALEALGIApedVDYIILTHIHLDHAGGAGLLAeALPNAKVYVHP--RGARHl 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  88 ------------AVPEQAKAFQVEVEPSPEPEIL-LEDGQELPLGELSIKVLHTPGHAPGHVTFLVEDAalvgDCLFQG- 153
Cdd:cd07726   94 idpsklwasaraVYGDEADRLGGEILPVPEERVIvLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEES----DGLFTGd 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 510023053 154 ----SIGRVDLPGGSA--------EQLMASLhNRLLTLPDEtRVLPGH 189
Cdd:cd07726  170 aagvRYPELDVVGPPStpppdfdpEAWLESL-DRLLSLKPE-RIYLTH 215
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 14-189 5.84e-17

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: 75.36  E-value: 5.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  14 NTYLIVDEVTG-------EAALVDPSFDSEQLLPEIEQLGYSLRYILNTHAHLDHVVGNAFFAAwtgapIALHKDDLGLL 86
Cdd:cd07712    1 LFIEEDDRVNIyllrgrdRALLIDTGLGIGDLKEYVRTLTDLPLLVVATHGHFDHIGGLHEFEE-----VYVHPADAEIL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  87 HA---VPEQAKAFQVEVEPSPEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTFLVEDAAL--VGDCLFQGSIgRVDLP 161
Cdd:cd07712   76 AApdnFETLTWDAATYSVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLlfSGDVVYDGPL-IMDLP 154

                        170       180
                 ....*....|....*....|....*....
gi 510023053 162 GGSAEQLMASLHnRLLTLPDETR-VLPGH 189
Cdd:cd07712  155 HSDLDDYLASLE-KLSKLPDEFDkVLPGH 182
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 14-151 2.06e-16

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: 74.10  E-value: 2.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  14 NTYLIVDEvTGEAALVDPSFDSE---QLLPEIEQLGYSLRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDD-------- 82
Cdd:cd07743    9 NIGVYVFG-DKEALLIDSGLDEDagrKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEkafienpl 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  83 -----LGLLHAVPE------QAKAFQVEVEPSPEpeilledgqELPLGELSIKVLHTPGHAPGHVTFLVEDAAL-VGDCL 150
Cdd:cd07743   88 lepsyLGGAYPPKElrnkflMAKPSKVDDIIEEG---------ELELGGVGLEIIPLPGHSFGQIGILTPDGVLfAGDAL 158


                 .
gi 510023053 151 F 151
Cdd:cd07743  159 F 159
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 16-156 4.83e-16

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: 74.28  E-value: 4.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  16 YLIVdevTGEAA-LVDPSFDSE--QLLPEIEQLGYS---LRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDDLGLL--- 86
Cdd:cd16288   25 YLIT---TPQGLiLIDTGLESSapMIKANIRKLGFKpsdIKILLNSHAHLDHAGGLAALKKLTGAKLMASAEDAALLasg 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510023053  87 ----HAVPEQAKAFqvevePSPEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTFL--VEDAALVGDCLFQGSIG 156
Cdd:cd16288  102 gksdFHYGDDSLAF-----PPVKVDRVLKDGDRVTLGGTTLTAHLTPGHTRGCTTWTmtVKDDGKVYQVVFADSLT 172
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 14-191 1.36e-15

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: 71.80  E-value: 1.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  14 NTYLI--------VDevTGEAalvDPSFDS--EQLLPEIEQLgySLRYILNTHAHLDHVVG-NAFFAAWTGAPIALHKDd 82
Cdd:cd07722   19 NTYLVgtgkrrilID--TGEG---RPSYIPllKSVLDSEGNA--TISDILLTHWHHDHVGGlPDVLDLLRGPSPRVYKF- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  83 lgLLHAVPEQAKAFQVEVEPspepeilLEDGQELPLGELSIKVLHTPGHAPGHVTF-LVEDAAL-VGDCLfqgsigrvdL 160
Cdd:cd07722   91 --PRPEEDEDPDEDGGDIHD-------LQDGQVFKVEGATLRVIHTPGHTTDHVCFlLEEENALfTGDCV---------L 152

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 510023053 161 PGGSA--EQL---MASLHnRLLTLPdETRVLPGHGE 191
Cdd:cd07722  153 GHGTAvfEDLaayMASLK-KLLSLG-PGRIYPGHGP 186
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 28-192 8.72e-15

uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YmaE and Nostoc all1228 proteins.Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 69.53  E-value: 8.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  28 LVD-PSFdSEQLLPEIEQLGySLRYILNTHAhlDHVVGNAFFAAWTGAPIALHKDDLgllHAVPEqakafqvevepsPEP 106
Cdd:cd07727   28 LVDsPRY-SPPLAKRIEALG-GIRYIFLTHR--DDVADHAKWAERFGAKRIIHEDDV---NAVTR------------PDE 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053 107 EILLEDGQELPLGElSIKVLHTPGHAPGHVTFLVED--AALVGDCLFqGSIGRVDLPG------GSAEQLMASLHnRLLT 178
Cdd:cd07727   89 VIVLWGGDPWELDP-DLTLIPVPGHTRGSVVLLYKEkgVLFTGDHLA-WSRRRGWLSAfryvcwYSWPEQAESVE-RLAD 165

                        170
                 ....*....|....
gi 510023053 179 LpDETRVLPGHGEP 192
Cdd:cd07727  166 L-DFEWVLPGHGRR 178
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 18-189 3.58e-14

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 68.78  E-value: 3.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  18 IVDEVTGEAALVDPSFDSEQLLPE-IEQLGYS---LRYILNTHAHLDHVVGNAFFaawTGAPIALHKDDL----GLLHAV 89
Cdd:cd07729   54 AADDPGGLELAFPPGVTEEQTLEEqLARLGLDpedIDYVILSHLHFDHAGGLDLF---PNATIIVQRAELeyatGPDPLA 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  90 PEQAKAFQVEVEPSPEPEI-LLEDGQELpLGelSIKVLHTPGHAPGHVTFLVE----DAALVGDCL-FQGSI--GRVDLP 161
Cdd:cd07729  131 AGYYEDVLALDDDLPGGRVrLVDGDYDL-FP--GVTLIPTPGHTPGHQSVLVRlpegTVLLAGDAAyTYENLeeGRPPGI 207

                        170       180       190
                 ....*....|....*....|....*....|
gi 510023053 162 GGSAEQLMASLHnRLLTLPDET--RVLPGH 189
Cdd:cd07729  208 NYDPEAALASLE-RLKALAEREgaRVIPGH 236
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 12-199 4.11e-14

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: 67.71  E-value: 4.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  12 DNNTYLIVDEvtGEAALVDPSF----DSEQLLPEIEQLGYSLR---YILNTHAHLDHVVGNAFFAAWTGAPIALhkddlg 84
Cdd:cd07725   14 HVNVYLLRDG--DETTLIDTGLateeDAEALWEGLKELGLKPSdidRVLLTHHHPDHIGLAGKLQEKSGATVYI------ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  85 llhavpeqakafqVEVEPspepeilLEDGQELPLGELSIKVLHTPGHAPGHVTFLVEDA--ALVGDCLFQGS----IGRV 158
Cdd:cd07725   86 -------------LDVTP-------VKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRreLFVGDAVLPKItpnvSLWA 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 510023053 159 DLPGGSAEQLMASLhNRLLTLPDEtRVLPGHGEPTTIGAEK 199
Cdd:cd07725  146 VRVEDPLGAYLESL-DKLEKLDVD-LAYPGHGGPIKDPKAR 184
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 15-138 1.33e-13

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: 67.48  E-value: 1.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  15 TYLIVDevTGEAALVDPSFDSEQLLPE--IEQLGYSLR---YILNTHAHLDHVVGNAFFAAWTGAP-IALHKDDLGLLHA 88
Cdd:cd16310   24 SYLITS--NHGAILLDGGLEENAALIEqnIKALGFKLSdikIIINTHAHYDHAGGLAQLKADTGAKlWASRGDRPALEAG 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 510023053  89 VPEQAKAFQVEVEPSPEPEILLEDGQELPLGELSIKVLHTPGHAPGHVTF 138
Cdd:cd16310  102 KHIGDNITQPAPFPAVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTW 151
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 ...
 36-137 5.90e-13

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: 65.83  E-value: 5.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  36 EQLLPEIEQLGYSL---RYILNTHAHLDHVVGNAFFAAWTGAPIA---LHKDDLGLLHAVPEQAKAFQVEVEPSPEPEIL 109
Cdd:cd16290   45 PQIEANIRALGFRLedvKLILNSHAHFDHAGGIAALQRDSGATVAaspAGAAALRSGGVDPDDPQAGAADPFPPVAKVRV 124

                         90       100
                 ....*....|....*....|....*...
gi 510023053 110 LEDGQELPLGELSIKVLHTPGHAPGHVT 137
Cdd:cd16290  125 VADGEVVKLGPLAVTAHATPGHTPGGTS 152
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 28-192 2.38e-12

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: 62.99  E-value: 2.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  28 LVDP--SFDSEQLLPEIEQLGYSLR---YILNTHAHLDHVVGNAFFaawTGAPIALHKD---DLGLLHavpeqakafqve 99
Cdd:cd07711   35 LVDTgtPWDRDLLLKALAEHGLSPEdidYVVLTHGHPDHIGNLNLF---PNATVIVGWDicgDSYDDH------------ 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053 100 vepspepeiLLEDGQELPLGElSIKVLHTPGHAPGHVTFLVEDA-----ALVGDcLFQGSIG---RVDLPGGSA--EQLM 169
Cdd:cd07711  100 ---------SLEEGDGYEIDE-NVEVIPTPGHTPEDVSVLVETEkkgtvAVAGD-LFEREEDledPILWDPLSEdpELQE 168

                        170       180
                 ....*....|....*....|...
gi 510023053 170 ASLhNRLLTLPDetRVLPGHGEP 192
Cdd:cd07711  169 ESR-KRILALAD--WIIPGHGPP 188
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 12-189 9.69e-12

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 62.15  E-value: 9.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  12 DNNTYLIVDEvTGEAALVDPSfDSEQLLPEIEQLGYSLRYILNTHAHLDHVVGnaffaawtgapialhkddlgllhaVPE 91
Cdd:PRK10241  11 DNYIWVLNDE-AGRCLIVDPG-EAEPVLNAIAENNWQPEAIFLTHHHHDHVGG------------------------VKE 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  92 QAKAF-QVEVEPSPEPE-----ILLEDGQELPLGELSIKVLHTPGHAPGHVTFLVEDAALVGDCLFQGSIGRvdLPGGSA 165
Cdd:PRK10241  65 LVEKFpQIVVYGPQETQdkgttQVVKDGETAFVLGHEFSVFATPGHTLGHICYFSKPYLFCGDTLFSGGCGR--LFEGTA 142

                        170       180
                 ....*....|....*....|....
gi 510023053 166 EQLMASLHnRLLTLPDETRVLPGH 189
Cdd:PRK10241 143 SQMYQSLK-KINALPDDTLICCAH 165
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 42-141 1.28e-11

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


Pssm-ID: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 62.10  E-value: 1.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  42 IEQLGYS---LRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDDLGLLH---AVPEQAKAFQVEVEPSpEPEILLEDGQE 115
Cdd:cd16308   51 IQALGFKfkdIKILLTTQAHYDHVGAMAAIKQQTGAKMMVDEKDAKVLAdggKSDYEMGGYGSTFAPV-KADKLLHDGDT 129

                         90       100
                 ....*....|....*....|....*.
gi 510023053 116 LPLGELSIKVLHTPGHAPGHVTFLVE 141
Cdd:cd16308  130 IKLGGTKLTLLHHPGHTKGSCSFLFD 155
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 18-134 8.38e-11

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: 59.67  E-value: 8.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  18 IVDEVTGEAAlvdpsfdsEQLLPEIEQLGYSL---RYILNTHAHLDHVVGNAFFAAWTGAPIAlhkddlgllhAVPEQAK 94
Cdd:cd16315   35 LIDSGTEEAA--------PLVLANIRKLGFDPkdvRWLLSSHEHFDHVGGLAALQRATGARVA----------ASAAAAP 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 510023053  95 AF----------QVEVEPSPEP---EILLEDGQELPLGELSIKVLHTPGHAPG 134
Cdd:cd16315   97 VLesgkpapddpQAGLHEPFPPvrvDRIVEDGDTVALGSLRLTAHATPGHTPG 149
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-134 1.86e-10

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: 58.65  E-value: 1.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  37 QLLPEIEQLGYS---LRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDDLGLL---HAVPEQAKAFQVevePSPEPEILL 110
Cdd:cd16309   46 LIKDNIKKLGFDvkdVKYLLNTHAHFDHAGGLAELKKATGAQLVASAADKPLLesgYVGSGDTKNLQF---PPVRVDRVI 122

                         90       100
                 ....*....|....*....|....
gi 510023053 111 EDGQELPLGELSIKVLHTPGHAPG 134
Cdd:cd16309  123 GDGDKVTLGGTTLTAHLTPGHSPG 146
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 28-138 9.68e-10

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: 56.79  E-value: 9.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  28 LVDPSFD--SEQLLPEIEQLGYSL---RYILNTHAHLDHVVGNAFFAAWTGAPIALHKDDLGLLHA--VPEQAKAFQVEV 100
Cdd:cd16313   35 LIDGGFPksPEQIAASIRQLGFKLedvKYILSSHDHWDHAGGIAALQKLTGAQVLASPATVAVLRSgsMGKDDPQFGGLT 114

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 510023053 101 EPSPEPEI-LLEDGQELPLGELSIKVLHTPGHAPGHVTF 138
Cdd:cd16313  115 PMPPVASVrAVRDGEVVKLGPLAVTAHATPGHTTGGTSW 153
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 38-156 3.55e-09

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: 54.86  E-value: 3.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  38 LLPEIEQLGYS---LRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDDLGLL----HAVPEQAKAFQVEVEPSPEPEIlL 110
Cdd:cd07708   47 IKANIKKLGFKfsdTKLILISHAHFDHAGGSAEIKKQTGAKVMAGAEDVSLLlsggSSDFHYANDSSTYFPQSTVDRA-V 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 510023053 111 EDGQELPLGELSIKVLHTPGHAPGHV--TFLVEDAALVGDCLFQGSIG 156
Cdd:cd07708  126 HDGERVTLGGTVLTAHATPGHTPGCTtwTMTLKDHGKQYQVVFADSLT 173
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 42-138 9.18e-09

Janthinobacterium lividum 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 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: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 53.84  E-value: 9.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  42 IEQLGYSL---RYILNTHAHLDHVVGNAFFAAWTGAPIALHKDD-LGLLHAVP----EQAKAFQVEVEPSPEPEILLEDG 113
Cdd:cd16312   51 IEALGFRIedvKLILNSHAHWDHAGGIAALQKASGATVAASAHGaQVLQSGTNgkddPQYQAKPVVHVAKVAKVKEVGEG 130

                         90       100
                 ....*....|....*....|....*
gi 510023053 114 QELPLGELSIKVLHTPGHAPGHVTF 138
Cdd:cd16312  131 DTLKVGPLRLTAHMTPGHTPGGTTW 155
SoxH_rel_PQQ_2 TIGR04559
quinoprotein relay system zinc metallohydrolase 2; By homology, members are Zn ...
 36-200 1.69e-08

quinoprotein relay system zinc metallohydrolase 2; By homology, members are Zn metallohydrolases in the same family as the SoxH protein associated with sulfate metabolism, Bacillus cereus beta-lactamase II (see PDB:1bc2), and, more distantly, hydroxyacylglutathione hydrolase (glyoxalase II). All members occur in genomes with both PQQ biosynthesis and a PQQ-dependent (quinoprotein) dehydrogenase that has a motif of two consecutive Cys residues (see TIGR03075). The Cys-Cys motif is associated with electron transfer by specialized cytochromes such as c551. All these genomes also include a fusion protein (TIGR04557) whose domains resemble SoxY and SoxZ from thiosulfate oxidation. A conserved Cys in this fusion protein aligns to the Cys residue in SoxY that carries sulfur cycle intermediates. In many genomes, the genes for PQQ biosynthesis enzymes, PQQ-dependent enzymes, their associated cytochromes, and members of this family are clustered. Note that one to three closely related Zn metallohydrolases may occur; this family represents a specific clade among them. Some members of this family have a short additional N-terminal domain with four conserved Cys residues. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275352  Cd Length: 283  Bit Score: 53.35  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053   36 EQLLPEIEQL-GYSLRYILNTHAHLDHVVGNAFFAAwTGAPIALHK---DDLGL-----LHAVPEQAKAFQVEVEPSPeP 106
Cdd:TIGR04559  54 EALLAAIRQRtDLPIRYVINTHVHPDHIFGNAAFRE-DGAEFVGHAklpRALAArgefyLASFARLLGEAFLGTEIVP-P 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  107 EILLEDGQELPLGElsiKVLHTPGHAPGH----VTFLVEDAALV--GDCLFQGSIGRVD--LPGGSA--EQLMAslhnrl 176
Cdd:TIGR04559 132 TRLVADPLELDLGG---RVLELTAWPTAHtdndLTVFDEKTGTLftGDLLFVEHIPVLDgsLLGWLAvlDRLKA------ 202

                         170       180
                  ....*....|....*....|....*....
gi 510023053  177 ltlPDETRVLPGHGEPTT-----IGAEKR 200
Cdd:TIGR04559 203 ---RPAARVVPGHGPVSLdwpaaLAPQRR 228
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 17-192 2.70e-08

metallo-beta-lactamases, subclass B1; 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 B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. Includes chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1.


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 51.90  E-value: 2.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  17 LIVDEvTGEAALVDPSF---DSEQLLPEIEQ-LGYSLRYILNTHAHLDHVVGNAFFAAwTGAPIALHKDDLGLLhavpeq 92
Cdd:cd16285   29 LIVID-GKGLVLIDTPWteaQTATLLDWIEKkLGKPVTAAISTHSHDDRTGGIKALNA-RGIPTYATALTNELA------ 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  93 akafqvEVEPSPEPEILLEDGQELPLGELSIKVLhTPGHAPGHVT-FLVEDAALVGDCLFQG----SIGRVDlpGGSAEQ 167
Cdd:cd16285  101 ------KKEGKPVPTHSLKGALTLGFGPLEVFYP-GPGHTPDNIVvWLPKSKILFGGCLVKSasatSLGNVG--DADVEA 171

                        170       180
                 ....*....|....*....|....*
gi 510023053 168 LMASLHNRLLTLPDETRVLPGHGEP 192
Cdd:cd16285  172 WPKSIENLKAKYPEARMVVPGHGAP 196
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 10-142 1.22e-07

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: 50.62  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  10 PMDNNTYLI--------VDevTGEAALVDPSFdsEQLLPEIEQLGYSLR---YILNTHAHLDHVVG-------NAF---- 67
Cdd:cd07720   46 ETSVNAFLVrtggrlilVD--TGAGGLFGPTA--GKLLANLAAAGIDPEdidDVLLTHLHPDHIGGlvdaggkPVFpnae 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  68 -------FAAWTGAPIAlhkddlgllHAVPEQAKAFQVEVEPSPEP---EILLEDGQELPLGelsIKVLHTPGHAPGHVT 137
Cdd:cd07720  122 vhvseaeWDFWLDDANA---------AKAPEGAKRFFDAARDRLRPyaaAGRFEDGDEVLPG---ITAVPAPGHTPGHTG 189


                 ....*
gi 510023053 138 FLVED 142
Cdd:cd07720  190 YRIES 194
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 16-134 1.78e-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: 1.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  16 YLIVDEVTGEAAlvdpsfdsEQLLPEIEQLGY---SLRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDDLGLLH-AVPE 91
Cdd:cd16314   33 HILIDGGTDKAA--------PLIEANIRALGFrpeDVRYIVSSHEHFDHAGGIARLQRATGAPVVAREPAATTLErGRSD 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 510023053  92 QAKAFQVEVEPSPEPE--ILLEDGQELPLGELSIKVLHTPGHAPG 134
Cdd:cd16314  105 RSDPQFLVVEKFPPVAsvQRIGDGEVLRVGPLALTAHATPGHTPG 149
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-153 1.63e-06

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


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 46.73  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  22 VTG--EAALVDPSF---DSEQLLPEIEQLGYSLRYILNTHAHLDHVVG-NAFFAAWTGAPI------------ALHKDDL 83
Cdd:cd07739   21 IYGetEAVLVDAQFtraDAERLADWIKASGKTLTTIYITHGHPDHYFGlEVLLEAFPDAKVvatpavvahikaQLEPKLA 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510023053  84 GLLHAVPEQAKAFQVEVEPSPEPEILLEdGQElplgelsIKVLHTPGHAPGHVTFL---VEDAALVGDCLFQG 153
Cdd:cd07739  101 FWGPLLGGNAPARLVVPEPLDGDTLTLE-GHP-------LEIVGVGGGDTDDTTYLwipSLKTVVAGDVVYNG 165
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 37-134 1.90e-06

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: 47.29  E-value: 1.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  37 QLLPEIEQLGY---SLRYILNTHAHLDHVVG--------NAFFAAWTGAPIALHKDDLG----LLHAVPEQAKAFQVEve 101
Cdd:cd16311   46 KIIANIEALGFrieDVKLILNSHGHIDHAGGlaelqrrsGALVAASPSAALDLASGEVGpddpQYHALPKYPPVKDMR-- 123

                         90       100       110
                 ....*....|....*....|....*....|...
gi 510023053 102 pspepeiLLEDGQELPLGELSIKVLHTPGHAPG 134
Cdd:cd16311  124 -------LARDGGQFNVGPVSLTAHATPGHTPG 149
NorV COG0426
Flavorubredoxin [Energy production and conversion];
14-145 2.43e-06

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 47.13  E-value: 2.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  14 NTYLIVDEvtgEAALVDP---SFdSEQLLPEIEQL--GYSLRYILNTHAHLDHVVG-NAFFAAWTGAPIALHKDDLGLLh 87
Cdd:COG0426   35 NSYLIVDE---KTALIDTvgeSF-FEEFLENLSKVidPKKIDYIIVNHQEPDHSGSlPELLELAPNAKIVCSKKAARFL- 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  88 avpeqaKAFqveVEPSPEPEILLEDGQELPLGELSIKVLHTPG-HAPGH-VTFLVEDAAL 145
Cdd:COG0426  110 ------PHF---YGIPDFRFIVVKEGDTLDLGGHTLQFIPAPMlHWPDTmFTYDPEDKIL 160
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 14-145 2.60e-06

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: 46.71  E-value: 2.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  14 NTYLIVDEvtgEAALVDP---SFdSEQLLPEIEQL--GYSLRYILNTHAHLDHVVG-NAFFAAWTGAPIALHKDDLGLL- 86
Cdd:cd07709   33 NSYLIKDE---KTALIDTvkePF-FDEFLENLEEVidPRKIDYIVVNHQEPDHSGSlPELLELAPNAKIVCSKKAARFLk 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510023053  87 HAVPEQAKAFQVevepspepeilLEDGQELPLGELSIKVLHTPG-HAPGH-VTFLVEDAAL 145
Cdd:cd07709  109 HFYPGIDERFVV-----------VKDGDTLDLGKHTLKFIPAPMlHWPDTmVTYDPEDKIL 158
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 35-134 4.19e-05

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: 43.27  E-value: 4.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  35 SEQLLPEIEQLGYS---LRYILNTHAHLDHVVGNAFFAAWTGAPIALHKDDLGLLHAVPEQAKAFQVEVE-PSPEPEILL 110
Cdd:cd16289   44 ADMLLDNMRALGVApgdLKLILHSHAHADHAGPLAALKRATGARVAANAESAVLLARGGSDDIHFGDGITfPPVQADRIV 123

                         90       100
                 ....*....|....*....|....
gi 510023053 111 EDGQELPLGELSIKVLHTPGHAPG 134
Cdd:cd16289  124 MDGEVVTLGGVTFTAHFTPGHTPG 147
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 36-189 5.90e-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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 42.64  E-value: 5.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  36 EQLlpeiEQLGYSL---RYILNTHAHLDHV------------VGNAFFAAwTGAPIALHKDDLGLLHAVPEQAKAFQVEV 100
Cdd:cd07730   72 EQL----AAGGIDPediDAVILSHLHWDHIgglsdfpnarliVGPGAKEA-LRPPGYPSGFLPELLPSDFEGRLVRWEED 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053 101 EPSPEPEILLEDGQELpLGELSIKVLHTPGHAPGHVTFLVEDAA-----LVGDC------LFQGS---IGRVDLPGGSAE 166
Cdd:cd07730  147 DFLWVPLGPFPRALDL-FGDGSLYLVDLPGHAPGHLGLLARTTSgtwvfLAGDAchhrigLLRPSpllPLPDLDDGADRE 225

                        170       180
                 ....*....|....*....|....
gi 510023053 167 QLMASLHN-RLLTLPDETRVLPGH 189
Cdd:cd07730  226 AARETLARlRELDAAPDVRVVLAH 249
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 23-192 9.62e-05

metallo-beta-lactamases; subclasses B1 and B2 and related proteins; 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 B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B1 MBls include chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1. B2 MBLs have a narrow substrate profile that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis. B2 MBLs include Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I.


Pssm-ID: 293793 [Multi-domain]  Cd Length: 219  Bit Score: 41.76  E-value: 9.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  23 TGEAALVDPSFD---SEQLLPEIE-QLGYSLRYILNTHAHLDHVVGNAFF-----AAWTGAPIA-LHKDDLGLLHAVPEQ 92
Cdd:cd07707   29 SKGLVLVDSTWTpktTKELIKEIEkVSQKPVTEVINTHFHTDRAGGNAYLkergaKTVSTALTRdLAKSEWAEIVAFTRK 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  93 AKAFQVEVEPSPePEILLEDGQElpLGELSIKVLHT-PGHAP-GHVTFLVEDAALVGDCLFQ----GSIGRVDLPGGSae 166
Cdd:cd07707  109 GLPEYPDLGYEL-PDGVLDGDFN--LQFGKVEAFYPgPAHTPdNIVVYFPQENVLYGGCIIKetdlGNVADADVKEWP-- 183

                        170       180
                 ....*....|....*....|....*.
gi 510023053 167 qlmASLHNRLLTLPDETRVLPGHGEP 192
Cdd:cd07707  184 ---TSIERLKKRYRNIKAVIPGHGEV 206
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-192 4.11e-04

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 39.88  E-value: 4.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  22 VTGEAALV-D-PSFDSEQLLPEIEQL-GYSLRYILNTHAHLDHVVGNAFFAAwTGAPIALHKDDLGLLHAVPEQAKafqv 98
Cdd:cd16276   16 VTDKGVIVvDaPPSLGENLLAAIRKVtDKPVTHVVYSHNHADHIGGASIFKD-EGATIIAHEATAELLKRNPDPKR---- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  99 evepsPEPEILLEDGQELPLGELSIKvLHTPG--HAPGHVTFLVED--AALVGDCLFQGSIGRVDLPGGSAEQLMASLHN 174
Cdd:cd16276   91 -----PVPTVTFDDEYTLEVGGQTLE-LSYFGpnHGPGNIVIYLPKqkVLMAVDLINPGWVPFFNFAGSEDIPGYIEALD 164

                        170
                 ....*....|....*...
gi 510023053 175 RLLTLPDETrVLPGHGEP 192
Cdd:cd16276  165 ELLEYDFDT-FVGGHGNR 181
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-156 5.43e-04

Fluoribacter gormanii FEZ-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 FEZ-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: 293865  Cd Length: 255  Bit Score: 39.74  E-value: 5.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  28 LVDPSFDSE--QLLPEIEQLGYSL---RYILNTHAHLDHVVGNAFFAAWTGAPIALHKDDLGLLHAvpEQAKAFQVEVEP 102
Cdd:cd16307   35 LINSNLESSvpQIKASIEKLGFKFsdtKILLISHAHFDHAAGSALIKRETHAKYMVMDGDVDVVES--GGKSDFFYGNDP 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510023053 103 S---PEPEI--LLEDGQELPLGELSIKVLHTPGHAPGHVT--FLVEDAALVGDCLFQGSIG 156
Cdd:cd16307  113 StyfPPAHVdkVLHDGEQVELGGTVLTAHLTAGHTKGCTTwtMKVKDHGKTYDVVIVGSPN 173
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 192-206 6.72e-04

Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of hydroxyacylglutathione hydrolase enzymes. Substrate binding occurs at the interface between this domain and the catalytic domain (pfam00753).


Pssm-ID: 465030 [Multi-domain]  Cd Length: 82  Bit Score: 37.42  E-value: 6.72e-04
                          10
                  ....*....|....*
gi 510023053  192 PTTIGAEKRHNPFLR 206
Cdd:pfam16123  39 PSTLGDEKATNPFLR 53
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 24-134 1.19e-03

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 38.69  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  24 GEAALVD----PSFDSEQ--LLPEIEQLGYS-LRYILNTHAHLDHV-----------VGNAFFAAWTgapialhkDDLGL 85
Cdd:COG2333   21 GKTILIDtgprPSFDAGErvVLPYLRALGIRrLDLLVLTHPDADHIgglaavleafpVGRVLVSGPP--------DTSET 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 510023053  86 LHAVPEQAKAFQVEVEPspepeilLEDGQELPLGELSIKVLHTPGHAPG 134
Cdd:COG2333   93 YERLLEALKEKGIPVRP-------CRAGDTWQLGGVRFEVLWPPEDLLE 134
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 51-150 2.73e-03

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 37.50  E-value: 2.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  51 YILNTHAHLDHV---------------------VGNAFFAAWTGAPialhkddlgllHAVPEQAKAFQVEVEPSPE--PE 107
Cdd:cd16277   66 YVLCTHLHVDHVgwntrlvdgrwvptfpnarylFSRAEYDHWSSPD-----------AGGPPNRGVFEDSVLPVIEagLA 134

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 510023053 108 ILLEDGQELpLGELSIkvLHTPGHAPGHVTFLV----EDAALVGDCL 150
Cdd:cd16277  135 DLVDDDHEI-LDGIRL--EPTPGHTPGHVSVELesggERALFTGDVM 178
PDE1 COG5212
cAMP phosphodiesterase [Signal transduction mechanisms];
7-69 6.52e-03

cAMP phosphodiesterase [Signal transduction mechanisms];


Pssm-ID: 444071 [Multi-domain]  Cd Length: 300  Bit Score: 36.86  E-value: 6.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053   7 LLGPMDNNTYLIVDEVTG----EAALVDPSFDSEQllpeieqlGYSLRYI---LNTHAHLDHVVGNAFFA 69
Cdd:COG5212   32 LLRPLGSDDYVLLDAGTVvsglELAEQKGAFKGRQ--------GYVLEHIkgyLISHAHLDHIAGLPILS 93
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 21-142 7.93e-03

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 36.41  E-value: 7.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510023053  21 EVTGEAALVDPSFDSEQLLPEIEQLGYSLRYILNTHAHLDHVVGNAFFA-AWTGAPIALHKDDlGLLHAVPEQAKAFQVE 99
Cdd:COG1235   41 EADGTRLLIDAGPDLREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRpRYGPNPIPVYATP-GTLEALERRFPYLFAP 119

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 510023053 100 VEPSPEPEIlLEDGQELPLGELSIKVLHTPgHAPGHVT-FLVED 142
Cdd:COG1235  120 YPGKLEFHE-IEPGEPFEIGGLTVTPFPVP-HDAGDPVgYRIED 161
 
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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