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Conserved domains on  [gi|2316062970|ref|WP_263059458|]
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MBL fold metallo-hydrolase [Pectobacterium sp. F1-1]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 12958315)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 3-192 1.23e-128

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: 360.33  E-value: 1.23e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   3 YQIVPVTAFSQNCTLLWCEKTNEAAIVDPGGDAEKIKRAVADAGISVKQILLTHGHLDHVGAAAELAEHYQVAIIGPQIE 82
Cdd:cd07737     1 YQIIPVTPFQQNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  83 DAFWLEGLPAQSRMFGLEECAPLTPSRWLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAQVGDVIFNGGVGRTD 162
Cdd:cd07737    81 DKFLLENLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTD 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 2316062970 163 FPQGNHQALIASIKNKLLPLGDDVTFIPGH 192
Cdd:cd07737   161 FPGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
HAGH_C super family cl38483
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 196-214 8.79e-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).


The actual alignment was detected with superfamily member pfam16123:

Pssm-ID: 465030 [Multi-domain]  Cd Length: 82  Bit Score: 37.03  E-value: 8.79e-04
                          10        20
                  ....*....|....*....|
gi 2316062970 196 STLGHERKTNPFLR-EDAAI 214
Cdd:pfam16123  40 STLGDEKATNPFLRvDDPAV 59
 
Name Accession Description Interval E-value
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 3-192 1.23e-128

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: 360.33  E-value: 1.23e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   3 YQIVPVTAFSQNCTLLWCEKTNEAAIVDPGGDAEKIKRAVADAGISVKQILLTHGHLDHVGAAAELAEHYQVAIIGPQIE 82
Cdd:cd07737     1 YQIIPVTPFQQNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  83 DAFWLEGLPAQSRMFGLEECAPLTPSRWLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAQVGDVIFNGGVGRTD 162
Cdd:cd07737    81 DKFLLENLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTD 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 2316062970 163 FPQGNHQALIASIKNKLLPLGDDVTFIPGH 192
Cdd:cd07737   161 FPGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 7-208 4.43e-57

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: 179.89  E-value: 4.43e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   7 PVTAFSQNCTLLWCekTNEAAIVDPGGD---AEKIKRAVADAGISVKQILLTHGHLDHVGAAAELAEHYQVAIIGPQIED 83
Cdd:COG0491     9 PGAGLGVNSYLIVG--GDGAVLIDTGLGpadAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  84 AFWLEglPAQSRMFGLEecaPLTPSRWLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAQVGDVIFNGGVGRTDF 163
Cdd:COG0491    87 EALEA--PAAGALFGRE---PVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2316062970 164 PQGNHQALIASIKnKLLPLGDDVtFIPGHGPMSTLGH-----------ERKTNPFL 208
Cdd:COG0491   162 PDGDLAQWLASLE-RLLALPPDL-VIPGHGPPTTAEAidyleellaalGERANPFL 215
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 14-192 1.70e-40

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: 136.14  E-value: 1.70e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   14 NCTLLWCEKtnEAAIVDPG-GDAEKIKRAVADAGIS-VKQILLTHGHLDHVGAAAELAEHYQVAIIGPQIEDAFWLEGLP 91
Cdd:smart00849   1 NSYLVRDDG--GAILIDTGpGEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   92 AQSRMFGLEECAPLTpsRWLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAQVGDVIFNGGVGRTDFPQGNHQAL 171
Cdd:smart00849  79 LLGELGAEAEPAPPD--RTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAAS 156

                          170       180
                   ....*....|....*....|.
gi 2316062970  172 IASIKNKLLPLGDDVTFIPGH 192
Cdd:smart00849 157 DALESLLKLLKLLPKLVVPGH 177
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 5-214 1.25e-37

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


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 131.12  E-value: 1.25e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   5 IVPVTAFSQNCTLLWCEKTNEAAIVDPGgDAEKIKRAVADAGISVKQILLTHGHLDHVGAAAELAEHYQVAIIGPQIEDa 84
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPDGQAAVVDPG-EAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAFPAPVYGPAEER- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  85 fwlegLPAQSRmfgleecapltpsrWLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAQVGDVIFNGGVGRTdFp 164
Cdd:TIGR03413  79 -----IPGITH--------------PVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRL-F- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970 165 QGNHQALIASIKnKLLPLGDDVTFIPGH---------------------------------GPM---STLGHERKTNPFL 208
Cdd:TIGR03413 138 EGTPEQMYDSLQ-RLAALPDDTLVYCAHeytlsnlrfaltvepdnpalqerlkevealraqGQPtlpSTLGLERATNPFL 216


                  ....*..
gi 2316062970 209 R-EDAAI 214
Cdd:TIGR03413 217 RaDDPAV 223
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
8-192 7.31e-34

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 119.78  E-value: 7.31e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   8 VTAFSQNCTLLwcEKTNEAAIVDPGGDAEKIK----RAVADAGISVKQILLTHGHLDHVGAAAELAEHYQVAIIGPQIED 83
Cdd:pfam00753   1 LGPGQVNSYLI--EGGGGAVLIDTGGSAEAALllllAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  84 AFWLEGLPAQSRMFGLEECAPLTPS---RWLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAQVGDVIFNGGVGR 160
Cdd:pfam00753  79 RELLDEELGLAASRLGLPGPPVVPLppdVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGR 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2316062970 161 TDFPQGNHQALIASIKNKLLPLGDDV------TFIPGH 192
Cdd:pfam00753 159 LDLPLGGLLVLHPSSAESSLESLLKLaklkaaVIVPGH 196
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 8-210 1.17e-17

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 78.71  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   8 VTAFSQNCTLLWCEKTNEAAIVDPGgDAEKIKRAVADAGISVKQILLTHGHLDHVGAAAELAEHYqvaiigPQIEdafwl 87
Cdd:PRK10241    6 IPAFDDNYIWVLNDEAGRCLIVDPG-EAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKF------PQIV----- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  88 eglpaqsrMFGLEECAPLTPSRWLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAqvGDVIFNGGVGRtdFPQGN 167
Cdd:PRK10241   74 --------VYGPQETQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYFSKPYLFC--GDTLFSGGCGR--LFEGT 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2316062970 168 HQALIASIKnKLLPLGDDVTFIPGHG--------PMSTLGHERKTNPFLRE 210
Cdd:PRK10241  142 ASQMYQSLK-KINALPDDTLICCAHEytlsnmkfALSILPHDLSINDYYRK 191
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 196-214 8.79e-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: 37.03  E-value: 8.79e-04
                          10        20
                  ....*....|....*....|
gi 2316062970 196 STLGHERKTNPFLR-EDAAI 214
Cdd:pfam16123  40 STLGDEKATNPFLRvDDPAV 59
 
Name Accession Description Interval E-value
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 3-192 1.23e-128

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: 360.33  E-value: 1.23e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   3 YQIVPVTAFSQNCTLLWCEKTNEAAIVDPGGDAEKIKRAVADAGISVKQILLTHGHLDHVGAAAELAEHYQVAIIGPQIE 82
Cdd:cd07737     1 YQIIPVTPFQQNCSLIWCEETKEAAVIDPGGDADKILQAIEDLGLTLKKILLTHGHLDHVGGAAELAEHYGVPIIGPHKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  83 DAFWLEGLPAQSRMFGLEECAPLTPSRWLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAQVGDVIFNGGVGRTD 162
Cdd:cd07737    81 DKFLLENLPEQSQMFGFPPAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNRESKLAIVGDVLFKGSIGRTD 160

                         170       180       190
                  ....*....|....*....|....*....|
gi 2316062970 163 FPQGNHQALIASIKNKLLPLGDDVTFIPGH 192
Cdd:cd07737   161 FPGGNHAQLIASIKEKLLPLGDDVTFIPGH 190
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 4-208 1.61e-67

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: 206.05  E-value: 1.61e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   4 QIVPVTAFSQNCTLLWCEKTNEAAIVDPGGDAEKIKRAVADAGISVKQILLTHGHLDHVGAAAELAEHYQVAI-IGPQie 82
Cdd:cd16322     2 RPFTLGPLQENTYLVADEGGGEAVLVDPGDESEKLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVyLHPD-- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  83 DAFWLEGLPAQSRMFGLEECAPLTPSRWLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAQVGDVIFNGGVGRTD 162
Cdd:cd16322    80 DLPLYEAADLGAKAFGLGIEPLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRTD 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2316062970 163 FPQGNHQALIASIKnKLLPLGDDVTFIPGHGPMSTLGHERKTNPFL 208
Cdd:cd16322   160 LPGGDPKAMAASLR-RLLTLPDETRVFPGHGPPTTLGEERRTNPFL 204
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 5-192 6.36e-66

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: 201.36  E-value: 6.36e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   5 IVPVTAFSQNCTLLWCEKtNEAAIVDPGGDA-EKIKRAVADAGISVKQILLTHGHLDHVGAAAELAEHYQVAIIGPQiED 83
Cdd:cd06262     2 RLPVGPLQTNCYLVSDEE-GEAILIDPGAGAlEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHE-AD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  84 AFWLEGLPAQSRMFGLEECAPLTPSRWLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAQVGDVIFNGGVGRTDF 163
Cdd:cd06262    80 AELLEDPELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEGVLFTGDTLFAGSIGRTDL 159

                         170       180
                  ....*....|....*....|....*....
gi 2316062970 164 PQGNHQALIASIKNKLLPLGDDVTFIPGH 192
Cdd:cd06262   160 PGGDPEQLIESIKKLLLLLPDDTVVYPGH 188
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 7-208 4.43e-57

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: 179.89  E-value: 4.43e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   7 PVTAFSQNCTLLWCekTNEAAIVDPGGD---AEKIKRAVADAGISVKQILLTHGHLDHVGAAAELAEHYQVAIIGPQIED 83
Cdd:COG0491     9 PGAGLGVNSYLIVG--GDGAVLIDTGLGpadAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  84 AFWLEglPAQSRMFGLEecaPLTPSRWLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAQVGDVIFNGGVGRTDF 163
Cdd:COG0491    87 EALEA--PAAGALFGRE---PVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGVGRPDL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2316062970 164 PQGNHQALIASIKnKLLPLGDDVtFIPGHGPMSTLGH-----------ERKTNPFL 208
Cdd:COG0491   162 PDGDLAQWLASLE-RLLALPPDL-VIPGHGPPTTAEAidyleellaalGERANPFL 215
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 6-192 2.41e-42

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: 140.29  E-value: 2.41e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   6 VPVTAFSQN-CTLLWCEKTNEAAIVDPGgDAEKIKRAVADAGISVKQILLTHGHLDHVGAAAELAEHY-QVAIIGPQIED 83
Cdd:cd07723     1 VPIPALSDNyIYLIVDEATGEAAVVDPG-EAEPVLAALEKNGLTLTAILTTHHHWDHTGGNAELKALFpDAPVYGPAEDR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  84 AFWLeglpaqsrmfgleecapltpSRWLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAQVGDVIFNGGVGRTDf 163
Cdd:cd07723    80 IPGL--------------------DHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEPALFTGDTLFSGGCGRFF- 138

                         170       180
                  ....*....|....*....|....*....
gi 2316062970 164 pQGNHQALIASIkNKLLPLGDDVTFIPGH 192
Cdd:cd07723   139 -EGTAEQMYASL-QKLLALPDDTLVYCGH 165
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 14-192 1.70e-40

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: 136.14  E-value: 1.70e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   14 NCTLLWCEKtnEAAIVDPG-GDAEKIKRAVADAGIS-VKQILLTHGHLDHVGAAAELAEHYQVAIIGPQIEDAFWLEGLP 91
Cdd:smart00849   1 NSYLVRDDG--GAILIDTGpGEAEDLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   92 AQSRMFGLEECAPLTpsRWLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAQVGDVIFNGGVGRTDFPQGNHQAL 171
Cdd:smart00849  79 LLGELGAEAEPAPPD--RTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGGDAAAS 156

                          170       180
                   ....*....|....*....|.
gi 2316062970  172 IASIKNKLLPLGDDVTFIPGH 192
Cdd:smart00849 157 DALESLLKLLKLLPKLVVPGH 177
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 17-193 1.79e-38

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: 130.98  E-value: 1.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  17 LLWCEKTNEAAIVDPGGD-AEKIKRAVADAGISVKQILLTHGHLDHVGAAAELAEHYQVAI-IGPQIEDAFwleglpaqs 94
Cdd:cd07724    16 LVGDPETGEAAVIDPVRDsVDRYLDLAAELGLKITYVLETHVHADHVSGARELAERTGAPIvIGEGAPASF--------- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  95 rmfgleecapltPSRWLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAQVGDVIFNGGVGRTDFPQGNHQ---AL 171
Cdd:cd07724    87 ------------FDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPDAVFTGDTLFVGDVGRPDLPGEAEGlarQL 154

                         170       180
                  ....*....|....*....|..
gi 2316062970 172 IASIKNKLLPLGDDVTFIPGHG 193
Cdd:cd07724   155 YDSLQRKLLLLPDETLVYPGHD 176
GSH_gloB TIGR03413
hydroxyacylglutathione hydrolase; Members of this protein family are hydroxyacylglutathione ...
 5-214 1.25e-37

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


Pssm-ID: 274569 [Multi-domain]  Cd Length: 248  Bit Score: 131.12  E-value: 1.25e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   5 IVPVTAFSQNCTLLWCEKTNEAAIVDPGgDAEKIKRAVADAGISVKQILLTHGHLDHVGAAAELAEHYQVAIIGPQIEDa 84
Cdd:TIGR03413   1 IIPIPALSDNYIWLLHDPDGQAAVVDPG-EAEPVLDALEARGLTLTAILLTHHHHDHVGGVAELLEAFPAPVYGPAEER- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  85 fwlegLPAQSRmfgleecapltpsrWLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAQVGDVIFNGGVGRTdFp 164
Cdd:TIGR03413  79 -----IPGITH--------------PVKDGDTVTLGGLEFEVLAVPGHTLGHIAYYLPDSPALFCGDTLFSAGCGRL-F- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970 165 QGNHQALIASIKnKLLPLGDDVTFIPGH---------------------------------GPM---STLGHERKTNPFL 208
Cdd:TIGR03413 138 EGTPEQMYDSLQ-RLAALPDDTLVYCAHeytlsnlrfaltvepdnpalqerlkevealraqGQPtlpSTLGLERATNPFL 216


                  ....*..
gi 2316062970 209 R-EDAAI 214
Cdd:TIGR03413 217 RaDDPAV 223
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
8-192 7.31e-34

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 119.78  E-value: 7.31e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   8 VTAFSQNCTLLwcEKTNEAAIVDPGGDAEKIK----RAVADAGISVKQILLTHGHLDHVGAAAELAEHYQVAIIGPQIED 83
Cdd:pfam00753   1 LGPGQVNSYLI--EGGGGAVLIDTGGSAEAALllllAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  84 AFWLEGLPAQSRMFGLEECAPLTPS---RWLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAQVGDVIFNGGVGR 160
Cdd:pfam00753  79 RELLDEELGLAASRLGLPGPPVVPLppdVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGR 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2316062970 161 TDFPQGNHQALIASIKNKLLPLGDDV------TFIPGH 192
Cdd:pfam00753 159 LDLPLGGLLVLHPSSAESSLESLLKLaklkaaVIVPGH 196
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 14-193 6.04e-32

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: 115.01  E-value: 6.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  14 NCTLLWCEktNEAAIVDPG--GDAEKIKRAVADAGIS---VKQILLTHGHLDHVGAAAELAEHYQVAI-IGPqiEDAFWL 87
Cdd:cd07721    12 NAYLIEDD--DGLTLIDTGlpGSAKRILKALRELGLSpkdIRRILLTHGHIDHIGSLAALKEAPGAPVyAHE--REAPYL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  88 EG---------LPAQSRMFGLEECAPLTPSRWLQEGDEVTVGEtTLAVFHCPGHTPGHIVFFDAESRLAQVGDVIFNGGv 158
Cdd:cd07721    88 EGekpypppvrLGLLGLLSPLLPVKPVPVDRTLEDGDTLDLAG-GLRVIHTPGHTPGHISLYLEEDGVLIAGDALVTVG- 165

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2316062970 159 GRTDFPQG----NHQALIASIKnKLLPLGDDVtFIPGHG 193
Cdd:cd07721   166 GELVPPPPpftwDMEEALESLR-KLAELDPEV-LAPGHG 202
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 21-192 1.77e-31

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: 113.02  E-value: 1.77e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  21 EKTNEAAIVDPGGDAEKIKRAVADAGISVKQILLTHGHLDHVGAAAELAEHYQVAIIGPQIEDAFWleGLPaqsrmfgle 100
Cdd:cd16275    20 KATREAAVVDPAWDIEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDYY--GFR--------- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970 101 eCAPLTPsrwLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAqvGDVIFNGGVGRTDFPQGNHQALIASIK--NK 178
Cdd:cd16275    89 -CPNLIP---LEDGDTIKIGDTEITCLLTPGHTPGSMCYLLGDSLFT--GDTLFIEGCGRCDLPGGDPEEMYESLQrlKK 162

                         170
                  ....*....|....
gi 2316062970 179 LLPlgDDVTFIPGH 192
Cdd:cd16275   163 LPP--PNTRVYPGH 174
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 24-194 5.54e-24

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 93.71  E-value: 5.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  24 NEAAIVDPGGDAEKIKRAVADA--GISVKQILLTHGHLDHVGAAAELAEHYQVAIIGPQIEDAFWLEGLPAqsrmfglee 101
Cdd:cd16278    27 DGVVVIDPGPDDPAHLDALLAAlgGGRVSAILVTHTHRDHSPGAARLAERTGAPVRAFGPHRAGGQDTDFA--------- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970 102 capltPSRWLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAQVGDVIFNGGVGRTDFPQGNHQALIASIKnKLLP 181
Cdd:cd16278    98 -----PDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCFALEDEGALFTGDHVMGWSTTVIAPPDGDLGDYLASLE-RLLA 171

                         170
                  ....*....|...
gi 2316062970 182 LGDDVtFIPGHGP 194
Cdd:cd16278   172 LDDRL-LLPGHGP 183
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 26-197 2.18e-21

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 87.62  E-value: 2.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  26 AAIVDPGGD---AEKIKRAVAD-AGISVKQILLTHGHLDHVGAAAELAEHyQVAIIG-PQIEDAFWLEGLPAQSRM---- 96
Cdd:cd16282    26 VVVIDTGASprlARALLAAIRKvTDKPVRYVVNTHYHGDHTLGNAAFADA-GAPIIAhENTREELAARGEAYLELMrrlg 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  97 -FGLEECAPLTPSRWLQEGDEVTVGETTLAVFH-CPGHTPGHIVFFDAESRLAQVGDVIFNGGVgrTDFPQGNHQALIAS 174
Cdd:cd16282   105 gDAMAGTELVLPDRTFDDGLTLDLGGRTVELIHlGPAHTPGDLVVWLPEEGVLFAGDLVFNGRI--PFLPDGSLAGWIAA 182

                         170       180
                  ....*....|....*....|...
gi 2316062970 175 IKnKLLPLGDDVtFIPGHGPMST 197
Cdd:cd16282   183 LD-RLLALDATV-VVPGHGPVGD 203
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 23-192 6.03e-21

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: 85.76  E-value: 6.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  23 TNEAAIVDPG---GDAEKIKRAVADAGISVkqiLLTHGHLDHVGAAAELAEHYQVAIIGPQIEDAFWLEGLPAQSRMFGL 99
Cdd:cd07712    17 RDRALLIDTGlgiGDLKEYVRTLTDLPLLV---VATHGHFDHIGGLHEFEEVYVHPADAEILAAPDNFETLTWDAATYSV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970 100 EecaPLTPSRWLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAQVGDVIFNGGVgRTDFPQGNHQALIASIKnKL 179
Cdd:cd07712    94 P---PAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALLDRANRLLFSGDVVYDGPL-IMDLPHSDLDDYLASLE-KL 168

                         170
                  ....*....|....
gi 2316062970 180 LPLGDDVTFI-PGH 192
Cdd:cd07712   169 SKLPDEFDKVlPGH 182
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 6-193 9.95e-19

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: 80.04  E-value: 9.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   6 VPVTAF--SQNCTLLWCEktNEAAIVDPG----GDAEKIKRAVADAGIS---VKQILLTHGHLDHVGAAAELAEHYQVAI 76
Cdd:cd07725     6 LPLPGPlgHVNVYLLRDG--DETTLIDTGlateEDAEALWEGLKELGLKpsdIDRVLLTHHHPDHIGLAGKLQEKSGATV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  77 IgpqiedafwleglpaqsrmfgleeCAPLTPsrwLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAQVGDVIF-- 154
Cdd:cd07725    84 Y------------------------ILDVTP---VKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRRELFVGDAVLpk 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2316062970 155 ---NGGV--GRTDFPQGNHQALIASIKNKllplgDDVTFIPGHG 193
Cdd:cd07725   137 itpNVSLwaVRVEDPLGAYLESLDKLEKL-----DVDLAYPGHG 175
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 24-176 7.60e-18

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: 78.30  E-value: 7.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  24 NEAAIVDPGGD--AEKIKRAVADAGIS---VKQILLTHGHLDHVGAAAELAEHY---QV--------------------- 74
Cdd:cd07726    25 GRPALIDTGPSssVPRLLAALEALGIApedVDYIILTHIHLDHAGGAGLLAEALpnaKVyvhprgarhlidpsklwasar 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  75 AIIGPQIeDAFWLEGLP-AQSRMFGLEecapltpsrwlqEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAQVGD-- 151
Cdd:cd07726   105 AVYGDEA-DRLGGEILPvPEERVIVLE------------DGETLDLGGRTLEVIDTPGHAPHHLSFLDEESDGLFTGDaa 171

                         170       180       190
                  ....*....|....*....|....*....|
gi 2316062970 152 -VIFNGGVGRTDF----PQGNHQALIASIK 176
Cdd:cd07726   172 gVRYPELDVVGPPstppPDFDPEAWLESLD 201
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 8-210 1.17e-17

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 78.71  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   8 VTAFSQNCTLLWCEKTNEAAIVDPGgDAEKIKRAVADAGISVKQILLTHGHLDHVGAAAELAEHYqvaiigPQIEdafwl 87
Cdd:PRK10241    6 IPAFDDNYIWVLNDEAGRCLIVDPG-EAEPVLNAIAENNWQPEAIFLTHHHHDHVGGVKELVEKF------PQIV----- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  88 eglpaqsrMFGLEECAPLTPSRWLQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAESRLAqvGDVIFNGGVGRtdFPQGN 167
Cdd:PRK10241   74 --------VYGPQETQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLGHICYFSKPYLFC--GDTLFSGGCGR--LFEGT 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2316062970 168 HQALIASIKnKLLPLGDDVTFIPGHG--------PMSTLGHERKTNPFLRE 210
Cdd:PRK10241  142 ASQMYQSLK-KINALPDDTLICCAHEytlsnmkfALSILPHDLSINDYYRK 191
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 4-211 7.12e-16

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 74.03  E-value: 7.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   4 QIVPVTAFSQNCT-LLWCEKTNEAAIVDPGgDAEKIKRAVADAGISVKQILLTHGHLDHVGAAAELAEHYqvaiigPQIe 82
Cdd:PLN02469    2 KIIPVPCLEDNYAyLIIDESTKDAAVVDPV-DPEKVLQAAHEHGAKIKLVLTTHHHWDHAGGNEKIKKLV------PGI- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  83 dafwleglpaqsRMFG-----LEECapltpSRWLQEGDEVTVGETT-LAVFHCPGHTPGHIVFF--DAESRLAQV--GDV 152
Cdd:PLN02469   74 ------------KVYGgsldnVKGC-----THPVENGDKLSLGKDVnILALHTPCHTKGHISYYvtGKEGEDPAVftGDT 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970 153 IFNGGVGRtdFPQGNHQALIASIKNKLLPLGDDVTFIPGH---------------------GPM---------------S 196
Cdd:PLN02469  137 LFIAGCGK--FFEGTAEQMYQSLCVTLGSLPKPTQVYCGHeytvknlkfaltvepdneklkQKLewaekqrqaglptvpS 214

                         250
                  ....*....|....*
gi 2316062970 197 TLGHERKTNPFLRED 211
Cdd:PLN02469  215 TIEEELETNPFMRVD 229
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 49-140 1.13e-15

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: 73.00  E-value: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  49 VKQILLTHGHLDHVGAAAELAEHYqvaiiGPQI----EDAFWLEGLPAQSRmfglEECAPLTPSR--WLQEGDEVTVGET 122
Cdd:cd16280    62 IKYILITHGHGDHYGGAAYLKDLY-----GAKVvmseADWDMMEEPPEEGD----NPRWGPPPERdiVIKDGDTLTLGDT 132

                          90
                  ....*....|....*...
gi 2316062970 123 TLAVFHCPGHTPGHIVFF 140
Cdd:cd16280   133 TITVYLTPGHTPGTLSLI 150
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 17-192 4.64e-15

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 72.57  E-value: 4.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  17 LLWCEKTNEAAIVDPGgDAEKIKRAVADAGISVKQILLTHGHLDHVGAAAELAEHYQVAIIGPQIEdafwleglpaQSRM 96
Cdd:PLN02398   91 LLHDEDTGTVGVVDPS-EAVPVIDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVD----------KDRI 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  97 FGLEeCAPLTPSRWLQEGDEVTVGETtlavfhcPGHTPGHIVFFDAESRLAQVGDVIFNGGVGRtdFPQGNHQALIASIK 176
Cdd:PLN02398  160 PGID-IVLKDGDKWMFAGHEVLVMET-------PGHTRGHISFYFPGSGAIFTGDTLFSLSCGK--LFEGTPEQMLSSLQ 229

                         170
                  ....*....|....*.
gi 2316062970 177 nKLLPLGDDVTFIPGH 192
Cdd:PLN02398  230 -KIISLPDDTNIYCGH 244
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 22-158 8.62e-15

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: 69.87  E-value: 8.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  22 KTNEAAIVDPGGD---AEKIKRAVADAGISVKQILLTHGHLDHVGAAAELAEHYQVAIIGPQIEDAFwLEGLPAQSRMFG 98
Cdd:cd07743    16 GDKEALLIDSGLDedaGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAF-IENPLLEPSYLG 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2316062970  99 LEECAPLTPSRWLQ----------EGDEVTVGETTLAVFHCPGHTPGHI-------VFFdaesrlaqVGDVIFNGGV 158
Cdd:cd07743    95 GAYPPKELRNKFLMakpskvddiiEEGELELGGVGLEIIPLPGHSFGQIgiltpdgVLF--------AGDALFGEEV 163
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 38-194 1.32e-14

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: 69.10  E-value: 1.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  38 IKRAVADAGI-SVKQILLTHGHLDHVGAAAELAEHyqvaIIGPQIEdaFWLEGLPAQSRMFGLEEcAPLTPsrwLQEGDE 116
Cdd:cd07722    45 LKSVLDSEGNaTISDILLTHWHHDHVGGLPDVLDL----LRGPSPR--VYKFPRPEEDEDPDEDG-GDIHD---LQDGQV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970 117 VTVGETTLAVFHCPGHTPGHIVFFDAEsrlaqvGDVIFNG----GVGRTDFpqGNHQALIASIKnKLLPLGDDVTFiPGH 192
Cdd:cd07722   115 FKVEGATLRVIHTPGHTTDHVCFLLEE------ENALFTGdcvlGHGTAVF--EDLAAYMASLK-KLLSLGPGRIY-PGH 184


                  ..
gi 2316062970 193 GP 194
Cdd:cd07722   185 GP 186
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 7-195 5.01e-14

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: 67.61  E-value: 5.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   7 PVTAFSqNCTLLWCEKTNeaAIVDPGG--DAEKIKRAVADAGISVKQI---LLTHGHLDHVGAAA--ELAEHYqvaiIGP 79
Cdd:cd07711    17 GFRASS-TVTLIKDGGKN--ILVDTGTpwDRDLLLKALAEHGLSPEDIdyvVLTHGHPDHIGNLNlfPNATVI----VGW 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  80 QIEDAFWLeglpaqsrMFGLEECAPLTPSrwlqegDEVTvgettlaVFHCPGHTPGHI-VFFDAES--RLAQVGDVIF-- 154
Cdd:cd07711    90 DICGDSYD--------DHSLEEGDGYEID------ENVE-------VIPTPGHTPEDVsVLVETEKkgTVAVAGDLFEre 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2316062970 155 NGGVGRTDFPQGNHQ--ALIASIKnKLLPLGDDVtfIPGHGPM 195
Cdd:cd07711   149 EDLEDPILWDPLSEDpeLQEESRK-RILALADWI--IPGHGPP 188
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 111-211 4.21e-11

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 60.58  E-value: 4.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970 111 LQEGDEVTVGETTLAVFHCPGHTPGHIVFFDAES------RLAQVGDVIFNGGVGRTDFPQGNHQALIASIKNKLLPLGD 184
Cdd:PLN02962  104 VEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGpdqpqpRMAFTGDALLIRGCGRTDFQGGSSDQLYKSVHSQIFTLPK 183

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2316062970 185 DVTFIPGHG----PMSTLGHERKTNPFLRED 211
Cdd:PLN02962  184 DTLIYPAHDykgfTVSTVGEEMLYNPRLTKD 214
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 38-135 6.00e-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: 60.18  E-value: 6.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  38 IKRAVADAGISVKQI---LLTHGHLDHVGAAAELAEHYQvAIIGPQIEDAFWLEGLPAQSRMFGLEEC--APLTPSRWLQ 112
Cdd:cd16308    47 IKKNIQALGFKFKDIkilLTTQAHYDHVGAMAAIKQQTG-AKMMVDEKDAKVLADGGKSDYEMGGYGStfAPVKADKLLH 125

                          90       100
                  ....*....|....*....|...
gi 2316062970 113 EGDEVTVGETTLAVFHCPGHTPG 135
Cdd:cd16308   126 DGDTIKLGGTKLTLLHHPGHTKG 148
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 22-135 1.16e-10

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: 59.26  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  22 KTNEAAIVDPGGDAEK---IKRAVADAGISVKQI---LLTHGHLDHVGAAAEL-----AEHYQVAIIGPQIE-----DAF 85
Cdd:cd16288    28 TTPQGLILIDTGLESSapmIKANIRKLGFKPSDIkilLNSHAHLDHAGGLAALkkltgAKLMASAEDAALLAsggksDFH 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2316062970  86 WLEGLPAQSrmfgleecaPLTPSRWLQEGDEVTVGETTLAVFHCPGHTPG 135
Cdd:cd16288   108 YGDDSLAFP---------PVKVDRVLKDGDRVTLGGTTLTAHLTPGHTRG 148
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 32-158 1.14e-09

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: 56.40  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  32 GGDAEKIKRAVADAGISVKQI---LLTHGHLDHVG----AAAEL----AEHYqVaiigPQIEDAFWL-----EGLPAQSR 95
Cdd:cd07720    72 GPTAGKLLANLAAAGIDPEDIddvLLTHLHPDHIGglvdAGGKPvfpnAEVH-V----SEAEWDFWLddanaAKAPEGAK 146

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  96 MFgLEEC----APLTPSRWLQEGDEVTVGETTLAvfhCPGHTPGHiVFFDAES---RLAQVGDVIFNGGV 158
Cdd:cd07720   147 RF-FDAArdrlRPYAAAGRFEDGDEVLPGITAVP---APGHTPGH-TGYRIESggeRLLIWGDIVHHPAL 211
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-135 3.32e-09

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: 55.38  E-value: 3.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  49 VKQILLTHGHLDHVGAAAELaEHYQVAIIGPQIEDAFWL---EGLPAQSRMFGLEECAPLTPSRWLQEGDEVTVGETTLA 125
Cdd:cd16311    61 VKLILNSHGHIDHAGGLAEL-QRRSGALVAASPSAALDLasgEVGPDDPQYHALPKYPPVKDMRLARDGGQFNVGPVSLT 139

                          90
                  ....*....|
gi 2316062970 126 VFHCPGHTPG 135
Cdd:cd16311   140 AHATPGHTPG 149
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-135 4.53e-09

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: 54.66  E-value: 4.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  49 VKQILLTHGHLDHVGAAAEL-----AEHYQVAIIGPQIEDAfwlEGLPAQSRMFGLEECAPLTPSRWLQEGDEVTVGETT 123
Cdd:cd16315    61 VRWLLSSHEHFDHVGGLAALqratgARVAASAAAAPVLESG---KPAPDDPQAGLHEPFPPVRVDRIVEDGDTVALGSLR 137

                          90
                  ....*....|..
gi 2316062970 124 LAVFHCPGHTPG 135
Cdd:cd16315   138 LTAHATPGHTPG 149
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 ...
 35-135 7.62e-09

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: 54.28  E-value: 7.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  35 AEKIKRAVADAGIS---VKQILLTHGHLDHVGAAAELAEHY--QVAIIGPQIEDAFWLEGLPAQSRMFGLEECAPLTPSR 109
Cdd:cd16290    44 APQIEANIRALGFRledVKLILNSHAHFDHAGGIAALQRDSgaTVAASPAGAAALRSGGVDPDDPQAGAADPFPPVAKVR 123

                          90       100
                  ....*....|....*....|....*.
gi 2316062970 110 WLQEGDEVTVGETTLAVFHCPGHTPG 135
Cdd:cd16290   124 VVADGEVVKLGPLAVTAHATPGHTPG 149
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 49-135 9.62e-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: 53.70  E-value: 9.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  49 VKQILLTHGHLDHVGAAAELAEHYQVAIIGPQiEDAFWLEGLPAQSRMFGLEECAPLTPS---RWLQEGDEVTVGETTLA 125
Cdd:cd07708    61 TKLILISHAHFDHAGGSAEIKKQTGAKVMAGA-EDVSLLLSGGSSDFHYANDSSTYFPQStvdRAVHDGERVTLGGTVLT 139

                          90
                  ....*....|
gi 2316062970 126 VFHCPGHTPG 135
Cdd:cd07708   140 AHATPGHTPG 149
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 14-80 1.07e-08

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


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 52.27  E-value: 1.07e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  14 NCTLLwcEKTNEAAIVDPGGDAEKIKRAVADAGISVKQ---ILLTHGHLDHVGAAAELAEHYQVAIIGPQ 80
Cdd:cd07733    10 NCTYL--ETEDGKLLIDAGLSGRKITGRLAEIGRDPEDidaILVTHEHADHIKGLGVLARKYNVPIYATA 77
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 24-192 1.30e-08

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: 53.37  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  24 NEAAIVDPGGDAEKIKRAV----------ADAGIS---VKQILLTHGHLDHVGAAAEL--AEHY-QVAiigpQIEDAFWL 87
Cdd:cd07729    51 HPDAADDPGGLELAFPPGVteeqtleeqlARLGLDpedIDYVILSHLHFDHAGGLDLFpnATIIvQRA----ELEYATGP 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  88 EGLPAQSRMFGLEECAPLTPSRWlqegdEVTVGETTLA----VFHCPGHTPGHI-VFFDAESR---LAqvGDVIF---NG 156
Cdd:cd07729   127 DPLAAGYYEDVLALDDDLPGGRV-----RLVDGDYDLFpgvtLIPTPGHTPGHQsVLVRLPEGtvlLA--GDAAYtyeNL 199

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2316062970 157 GVGRTDFPQGNHQALIASIKnKLLPL--GDDVTFIPGH 192
Cdd:cd07729   200 EEGRPPGINYDPEAALASLE-RLKALaeREGARVIPGH 236
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 23-135 1.64e-08

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: 53.22  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  23 TNEAAIVDPGG---DAEKIKRAVADAGIS---VKQILLTHGHLDHVGAAAELAEHYQVAIIGpQIEDAFWLE-GLPAQSR 95
Cdd:cd16310    29 SNHGAILLDGGleeNAALIEQNIKALGFKlsdIKIIINTHAHYDHAGGLAQLKADTGAKLWA-SRGDRPALEaGKHIGDN 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2316062970  96 MFGLEECAPLTPSRWLQEGDEVTVGETTLAVFHCPGHTPG 135
Cdd:cd16310   108 ITQPAPFPAVKVDRILGDGEKIKLGDITLTATLTPGHTKG 147
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-135 2.97e-08

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: 52.49  E-value: 2.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  49 VKQILLTHGHLDHVGAAAELAEHYQVAIIGPQiEDAFWLEGLPAQSRMFGLEECAPLTPSRWLQEGDEVTVGETTLAVFH 128
Cdd:cd16309    61 VKYLLNTHAHFDHAGGLAELKKATGAQLVASA-ADKPLLESGYVGSGDTKNLQFPPVRVDRVIGDGDKVTLGGTTLTAHL 139


                  ....*..
gi 2316062970 129 CPGHTPG 135
Cdd:cd16309   140 TPGHSPG 146
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 22-137 3.93e-08

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: 52.13  E-value: 3.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  22 KTNEAAIVDPGG---DAEKIKRAVADAGIS---VKQILLTHGHLDHVGAAAELAEHYQVAIIGpQIEDAFWLEGLPAQSR 95
Cdd:cd16289    28 KTPDGAVLLDGGmpqAADMLLDNMRALGVApgdLKLILHSHAHADHAGPLAALKRATGARVAA-NAESAVLLARGGSDDI 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2316062970  96 MFGLEEC-APLTPSRWLQEGDEVTVGETTLAVFHCPGHTPGHI 137
Cdd:cd16289   107 HFGDGITfPPVQADRIVMDGEVVTLGGVTFTAHFTPGHTPGST 149
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 23-194 3.33e-07

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 48.74  E-value: 3.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  23 TNEAAIV-D-PGGDAEKIKRAVAD-AGISVKQILLTHGHLDHVGAAAELAEHYqVAIIGpQIEDAFWLEGLPAQSRmfgl 99
Cdd:cd16276    17 TDKGVIVvDaPPSLGENLLAAIRKvTDKPVTHVVYSHNHADHIGGASIFKDEG-ATIIA-HEATAELLKRNPDPKR---- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970 100 eecaPLtPSRWLQEGDEVTVGETTLA-VFHCPGHTPGHIVFFDAESRLAQVGDVIFNGGVGRTDFPQGNH-QALIASIKn 177
Cdd:cd16276    91 ----PV-PTVTFDDEYTLEVGGQTLElSYFGPNHGPGNIVIYLPKQKVLMAVDLINPGWVPFFNFAGSEDiPGYIEALD- 164

                         170
                  ....*....|....*..
gi 2316062970 178 KLLPLgDDVTFIPGHGP 194
Cdd:cd16276   165 ELLEY-DFDTFVGGHGN 180
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 24-135 5.34e-07

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 48.70  E-value: 5.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  24 NEAAIVDPGGD------AEKIKRAVADAGIS-VKQILLTHGHLDHVGAAAELAEHYQVA--IIGPQIEDAFWLEGLPAQS 94
Cdd:COG2333    21 GKTILIDTGPRpsfdagERVVLPYLRALGIRrLDLLVLTHPDADHIGGLAAVLEAFPVGrvLVSGPPDTSETYERLLEAL 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2316062970  95 RMFGleecaplTPSRWLQEGDEVTVGETTLAVFHCPGHTPG 135
Cdd:COG2333   101 KEKG-------IPVRPCRAGDTWQLGGVRFEVLWPPEDLLE 134
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-135 5.46e-06

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: 45.65  E-value: 5.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  49 VKQILLTHGHLDHVGAAAELAEHYQVAIIGPQIEDAFWLEGLPAQS--RMFGLEECAPLTPSRWLQEGDEVTVGETTLAV 126
Cdd:cd16314    61 VRYIVSSHEHFDHAGGIARLQRATGAPVVAREPAATTLERGRSDRSdpQFLVVEKFPPVASVQRIGDGEVLRVGPLALTA 140


                  ....*....
gi 2316062970 127 FHCPGHTPG 135
Cdd:cd16314   141 HATPGHTPG 149
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 24-128 1.51e-05

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 43.66  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  24 NEAAIVDPGGDAEKIKRAVAD----AGIS-VKQILLTHGHLDHVGAAAELAEHYQVA-IIGPQIEDAFWLEglpaqsRMF 97
Cdd:cd07731    19 GKTILIDTGPRDSFGEDVVVPylkaRGIKkLDYLILTHPDADHIGGLDAVLKNFPVKeVYMPGVTHTTKTY------EDL 92

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2316062970  98 GLEECAPLTPSRWLQEGDEVTVGETTLAVFH 128
Cdd:cd07731    93 LDAIKEKGIPVTPCKAGDRWQLGGVSFEVLS 123
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 49-154 1.55e-05

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


Pssm-ID: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 43.72  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  49 VKQILLTHghLDHVGAAAELAEHYQVAIigpqiedafWLEGLPAQSRMFGlEECAPLtpsrwlqEGDEVTVGETTLAVFH 128
Cdd:cd07727    48 IRYIFLTH--RDDVADHAKWAERFGAKR---------IIHEDDVNAVTRP-DEVIVL-------WGGDPWELDPDLTLIP 108

                          90       100
                  ....*....|....*....|....*.
gi 2316062970 129 CPGHTPGHIVFFDAESRLAQVGDVIF 154
Cdd:cd07727   109 VPGHTRGSVVLLYKEKGVLFTGDHLA 134
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 49-79 2.37e-05

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 43.93  E-value: 2.37e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2316062970  49 VKQILLTHGHLDHVGAAAELAEHYQVAIIGP 79
Cdd:cd07714    56 IKGIFITHGHEDHIGALPYLLPELNVPIYAT 86
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 13-72 1.26e-04

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 41.80  E-value: 1.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  13 QNCTLLWCEKTNeaAIVDPGGDAEKIKRAVADAGISVKQILLTHGHLDHVGAAAELAEHY 72
Cdd:COG1235    35 RSSILVEADGTR--LLIDAGPDLREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRY 92
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 49-135 3.25e-04

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


Pssm-ID: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 40.62  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  49 VKQILLTHGHLDHVGAAAELAEHYQVAIIGPQIEDAFWLEGLPAQS--RMFGLEECAPLTPSRWLQEGDEVTVGETTLAV 126
Cdd:cd16313    61 VKYILSSHDHWDHAGGIAALQKLTGAQVLASPATVAVLRSGSMGKDdpQFGGLTPMPPVASVRAVRDGEVVKLGPLAVTA 140


                  ....*....
gi 2316062970 127 FHCPGHTPG 135
Cdd:cd16313   141 HATPGHTTG 149
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 28-140 4.49e-04

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. 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: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 40.18  E-value: 4.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  28 IVDPGGDAEKIKRAVAD-----AGISVKQILLTHGHLDHVGAA---AELAEHYQVAIIGPQ-IEDAFWLEGL---PAQSR 95
Cdd:cd07710    31 IIDTLESAEAAKAALELfrkhtGDKPVKAIIYTHSHPDHFGGAggfVEEEDSGKVPIIAPEgFMEEAVSENVlagNAMSR 110

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  96 ----MFG--LEECAP------------------LTPSRWLQE-GDEVTVGETTLAVFHCPGHTPGHIVFF 140
Cdd:cd07710   111 raayQFGalLPKGEKgqvgaglgpglstgtvgfIPPTITITEtGETLTIDGVELEFQHAPGEAPDEMMVW 180
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 7-156 5.04e-04

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


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 39.79  E-value: 5.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970   7 PVTAFSQNCTLLWCEKtnEAAIVDPG---GDAEKIKRAVADAGISVKQILLTHGHLDHVGAAAELAEHYQ---------- 73
Cdd:cd07739    10 EISSFPVTSTLIYGET--EAVLVDAQftrADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAFPdakvvatpav 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  74 VAIIGPQIED--AFWLEGLPAQsrmfgleecAPLTPS-RWLQEGDEVTV-GETTLAVFHCPGHTPGHIVFFDAESRLAQV 149
Cdd:cd07739    88 VAHIKAQLEPklAFWGPLLGGN---------APARLVvPEPLDGDTLTLeGHPLEIVGVGGGDTDDTTYLWIPSLKTVVA 158


                  ....*..
gi 2316062970 150 GDVIFNG 156
Cdd:cd07739   159 GDVVYNG 165
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 28-79 5.16e-04

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 39.79  E-value: 5.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2316062970  28 IVDP---GGDAEKIKraVADAGISVkqILLTHGHLDHVGAAAELAEHYQVAIIGP 79
Cdd:PRK00685   21 LIDPfitGNPLADLK--PEDVKVDY--ILLTHGHGDHLGDTVEIAKRTGATVIAN 71
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
49-151 7.61e-04

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


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 39.66  E-value: 7.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  49 VKQILLTHGHLDHVGAAAELAEHYQVAIIGPQIEDAFwleglpAQSRM--FGLEECAPLTPsrwLQEGDEVTVGETTLAV 126
Cdd:COG0595    64 IKGIVLTHGHEDHIGALPYLLKELNVPVYGTPLTLAL------LEAKLkeHGLLKKVKLHV---VKPGDRIKFGPFKVEF 134

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2316062970 127 FH----CPG------HTP-GHIVF-----FDA---------ESRLAQVGD 151
Cdd:COG0595   135 FRvthsIPDslglaiRTPaGTIVHtgdfkFDQtpvdgeptdLARLAELGE 184
HAGH_C pfam16123
Hydroxyacylglutathione hydrolase C-terminus; This domain is found at the C-terminus of ...
 196-214 8.79e-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: 37.03  E-value: 8.79e-04
                          10        20
                  ....*....|....*....|
gi 2316062970 196 STLGHERKTNPFLR-EDAAI 214
Cdd:pfam16123  40 STLGDEKATNPFLRvDDPAV 59
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-135 2.17e-03

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: 38.20  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  49 VKQILLTHGHLDHVGAAAELAE--HYQVAIIGPqieDAFWLEGLPAQSRMFGLEECAPLTPS---RWLQEGDEVTVGETT 123
Cdd:cd16307    61 TKILLISHAHFDHAAGSALIKRetHAKYMVMDG---DVDVVESGGKSDFFYGNDPSTYFPPAhvdKVLHDGEQVELGGTV 137

                          90
                  ....*....|..
gi 2316062970 124 LAVFHCPGHTPG 135
Cdd:cd16307   138 LTAHLTAGHTKG 149
Lactamase_B_5 pfam14597
Metallo-beta-lactamase superfamily; This is a small family of putative metal-dependent ...
 52-153 9.79e-03

Metallo-beta-lactamase superfamily; This is a small family of putative metal-dependent hydrolases.


Pssm-ID: 373150  Cd Length: 199  Bit Score: 35.98  E-value: 9.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316062970  52 ILLTHGhlDHVGAAAELAEHYQVAIIGPQIEdafwleglpaqsrmfglEECAPLTPSRWLQEGDEVTVGettLAVFHCPG 131
Cdd:pfam14597  59 IVLTNS--DHIRAAKEIAHQTYAKIAGPAGE-----------------KETFPIACDRWLSDGDELVPG---LQVLELQG 116

                          90       100
                  ....*....|....*....|...
gi 2316062970 132 -HTPGHIVFFDAESRLAqVGDVI 153
Cdd:pfam14597 117 sKTPGELALLLEETTLI-TGDLV 138
 
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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