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Conserved domains on  [gi|914658877|ref|WP_050649979|]
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MULTISPECIES: MBL fold metallo-hydrolase [Vibrio]

Protein Classification

COG1237 family protein( domain architecture ID 10003202)

COG1237 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
1-281 5.65e-98

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


:

Pssm-ID: 440850  Cd Length: 273  Bit Score: 288.32  E-value: 5.65e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877   1 MKITTLVDNSRLDNrtDLAVERGLSLHIETEKLKILFDMGSGDTFCQNAPLLGIDIKDVDLAVISHRHHDHCNGTADFVA 80
Cdd:COG1237    2 MKITVLVDNTAGDE--GLLAEHGLSALIETEGKRILFDTGQSDVLLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLPALLE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877  81 HNSKAKVFL-KNCEQKSYHFRAFGFKSDVGINKDLLENSNERLVFVNRTTEIAPNVFVITDISAKHEQPKGNKYLYTQSK 159
Cdd:COG1237   80 LNPKAPVYAhPDAFEKRYSKRPGGKYIGIPFSREELEKLGARLILVKEPTEIAPGVYLTGEIPRVTDFEKGDPGLYVKED 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877 160 NQRERDLFDHELLLVIKEPDGLVIFTGCAHSGVLNMVDTAVTLFPGERIKAVVGGFHLVGLPlfnsiggtKQDIRELGLT 239
Cdd:COG1237  160 GGLVPDPFLDEQALVIKTDKGLVVITGCSHAGIVNILEYAKEVTGGKRIYAVIGGFHLLGAS--------EERIEKTIEA 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 914658877 240 LSQYPIDKLYTGHCTGKKAYSLLKEVLGERLEAMPTGRRINV 281
Cdd:COG1237  232 LKELGVEKIYPGHCTGLEAIAALKERFGDRFIELGVGSVIEF 273
 
Name Accession Description Interval E-value
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
1-281 5.65e-98

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 288.32  E-value: 5.65e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877   1 MKITTLVDNSRLDNrtDLAVERGLSLHIETEKLKILFDMGSGDTFCQNAPLLGIDIKDVDLAVISHRHHDHCNGTADFVA 80
Cdd:COG1237    2 MKITVLVDNTAGDE--GLLAEHGLSALIETEGKRILFDTGQSDVLLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLPALLE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877  81 HNSKAKVFL-KNCEQKSYHFRAFGFKSDVGINKDLLENSNERLVFVNRTTEIAPNVFVITDISAKHEQPKGNKYLYTQSK 159
Cdd:COG1237   80 LNPKAPVYAhPDAFEKRYSKRPGGKYIGIPFSREELEKLGARLILVKEPTEIAPGVYLTGEIPRVTDFEKGDPGLYVKED 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877 160 NQRERDLFDHELLLVIKEPDGLVIFTGCAHSGVLNMVDTAVTLFPGERIKAVVGGFHLVGLPlfnsiggtKQDIRELGLT 239
Cdd:COG1237  160 GGLVPDPFLDEQALVIKTDKGLVVITGCSHAGIVNILEYAKEVTGGKRIYAVIGGFHLLGAS--------EERIEKTIEA 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 914658877 240 LSQYPIDKLYTGHCTGKKAYSLLKEVLGERLEAMPTGRRINV 281
Cdd:COG1237  232 LKELGVEKIYPGHCTGLEAIAALKERFGDRFIELGVGSVIEF 273
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 2-279 1.60e-93

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


Pssm-ID: 293799  Cd Length: 269  Bit Score: 277.20  E-value: 1.60e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877   2 KITTLVDNSRLDNrtDLAVERGLSLHIETEKLKILFDMGSGDTFCQNAPLLGIDIKDVDLAVISHRHHDHCNGTADFVAH 81
Cdd:cd07713    1 KITVLVDNTAGDE--GLLAEHGLSLLIETEGKKILFDTGQSGVLLHNAKKLGIDLSDIDAVVLSHGHYDHTGGLKALLEL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877  82 NSKAKVFL-KNCEQKSYHFRaFGFKSDVGINKDLLENSNERLVFVNRTTEIAPNVFVITDISAKHEQPKGNKYLYTQSKN 160
Cdd:cd07713   79 NPKAPVYAhPDAFEPRYSKR-GGGKKGIGIGREELEKAGARLVLVEEPTEIAPGVYLTGEIPRVTDFEKGNPGLFVKEDG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877 161 QRERDLFDHELLLVIKEPDGLVIFTGCAHSGVLNMVDTAVTLFPGERIKAVVGGFHLVGLPlfnsiggtKQDIRELGLTL 240
Cdd:cd07713  158 GLVPDDFEDEQALVIDTKKGLVVITGCSHAGIVNILEHAKKLTGGDKIYAVIGGFHLVGAS--------EERIEKTIAAL 229

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 914658877 241 SQYPIDKLYTGHCTGKKAYSLLKEVLGERLEAMPTGRRI 279
Cdd:cd07713  230 KELGVEKIYPGHCTGFKAIAALKEALGDKFIPLGVGTVI 268
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 25-88 3.73e-06

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: 46.39  E-value: 3.73e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914658877    25 SLHIETEKLKILFDMGSGDTFCQNAPLLGIDIKDVDLAVISHRHHDHCnGTADFVAHNSKAKVF 88
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDLLAELKKLGPKKIDAIILTHGHPDHI-GGLPELLEAPGAPVY 64
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
28-252 1.31e-04

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 41.97  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877   28 IETEKLKILFD--MGSGDTFCQNAPLLGIDIKDVDLAVISHRHHDHCNGTADFVAHNSKAKVflknCEQKSYHFrafgfk 105
Cdd:pfam00753  11 IEGGGGAVLIDtgGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVI----VVAEEARE------ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877  106 sdvgINKDLLENSNERLVFVNRTTEIAPNVFVITDISAKHEQPKGNKYLYTQSknqrerdlfDHELLLVIKEPDGLVIFT 185
Cdd:pfam00753  81 ----LLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPG---------HGPGHVVVYYGGGKVLFT 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914658877  186 GCahsgvlnmvdtavTLFPGERIKavvggFHLVGLPLFNSIGGTKQDIRELGLTLSQYPIDKLYTGH 252
Cdd:pfam00753 148 GD-------------LLFAGEIGR-----LDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
 
Name Accession Description Interval E-value
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
1-281 5.65e-98

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 288.32  E-value: 5.65e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877   1 MKITTLVDNSRLDNrtDLAVERGLSLHIETEKLKILFDMGSGDTFCQNAPLLGIDIKDVDLAVISHRHHDHCNGTADFVA 80
Cdd:COG1237    2 MKITVLVDNTAGDE--GLLAEHGLSALIETEGKRILFDTGQSDVLLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLPALLE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877  81 HNSKAKVFL-KNCEQKSYHFRAFGFKSDVGINKDLLENSNERLVFVNRTTEIAPNVFVITDISAKHEQPKGNKYLYTQSK 159
Cdd:COG1237   80 LNPKAPVYAhPDAFEKRYSKRPGGKYIGIPFSREELEKLGARLILVKEPTEIAPGVYLTGEIPRVTDFEKGDPGLYVKED 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877 160 NQRERDLFDHELLLVIKEPDGLVIFTGCAHSGVLNMVDTAVTLFPGERIKAVVGGFHLVGLPlfnsiggtKQDIRELGLT 239
Cdd:COG1237  160 GGLVPDPFLDEQALVIKTDKGLVVITGCSHAGIVNILEYAKEVTGGKRIYAVIGGFHLLGAS--------EERIEKTIEA 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 914658877 240 LSQYPIDKLYTGHCTGKKAYSLLKEVLGERLEAMPTGRRINV 281
Cdd:COG1237  232 LKELGVEKIYPGHCTGLEAIAALKERFGDRFIELGVGSVIEF 273
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 2-279 1.60e-93

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


Pssm-ID: 293799  Cd Length: 269  Bit Score: 277.20  E-value: 1.60e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877   2 KITTLVDNSRLDNrtDLAVERGLSLHIETEKLKILFDMGSGDTFCQNAPLLGIDIKDVDLAVISHRHHDHCNGTADFVAH 81
Cdd:cd07713    1 KITVLVDNTAGDE--GLLAEHGLSLLIETEGKKILFDTGQSGVLLHNAKKLGIDLSDIDAVVLSHGHYDHTGGLKALLEL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877  82 NSKAKVFL-KNCEQKSYHFRaFGFKSDVGINKDLLENSNERLVFVNRTTEIAPNVFVITDISAKHEQPKGNKYLYTQSKN 160
Cdd:cd07713   79 NPKAPVYAhPDAFEPRYSKR-GGGKKGIGIGREELEKAGARLVLVEEPTEIAPGVYLTGEIPRVTDFEKGNPGLFVKEDG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877 161 QRERDLFDHELLLVIKEPDGLVIFTGCAHSGVLNMVDTAVTLFPGERIKAVVGGFHLVGLPlfnsiggtKQDIRELGLTL 240
Cdd:cd07713  158 GLVPDDFEDEQALVIDTKKGLVVITGCSHAGIVNILEHAKKLTGGDKIYAVIGGFHLVGAS--------EERIEKTIAAL 229

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 914658877 241 SQYPIDKLYTGHCTGKKAYSLLKEVLGERLEAMPTGRRI 279
Cdd:cd07713  230 KELGVEKIYPGHCTGFKAIAALKEALGDKFIPLGVGTVI 268
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 28-80 3.06e-08

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


Pssm-ID: 293802 [Multi-domain]  Cd Length: 175  Bit Score: 52.06  E-value: 3.06e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 914658877  28 IETEKLKILFDMGSGdTFcqnAPLLG-IDIKDVDLAVISHRHHDHCngtADFVA 80
Cdd:cd07716   23 LEADGFRILLDCGSG-VL---SRLQRyIDPEDLDAVVLSHLHPDHC---ADLGV 69
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 28-138 1.02e-06

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: 48.75  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877  28 IETEKLKILFDMGSGDTFCQNAPL---------------------LGIDIKDVDLAVISHRHHDHCNGTADFvahnSKAK 86
Cdd:cd07729   37 IEHPEGTILVDTGFHPDAADDPGGlelafppgvteeqtleeqlarLGLDPEDIDYVILSHLHFDHAGGLDLF----PNAT 112

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 914658877  87 VFLknceQK-------SYHFRAFGFKSDVGINKDLLENSneRLVFVNRTTEIAPNVFVI 138
Cdd:cd07729  113 IIV----QRaeleyatGPDPLAAGYYEDVLALDDDLPGG--RVRLVDGDYDLFPGVTLI 165
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 23-72 2.94e-06

Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; Includes the archaeal cleavage and polyadenylation specificity factors (CPSFs) such as Methanothermobacter thermautotrophicus MTH1203, and Pyrococcus horikoshii PH1404. In addition to the MBL-fold metallo-hydrolase nuclease and the beta-CASP domains, members of this subgroup contain two contiguous KH domains. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 46.68  E-value: 2.94e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 914658877  23 GLSLHIETEKLKILFD----MGSGDTFCQNAPLLGIDIKDVDLAVISHRHHDHC 72
Cdd:cd16295   12 GSCYLLETGGKRILLDcglfQGGKELEELNNEPFPFDPKEIDAVILTHAHLDHS 65
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
25-74 2.98e-06

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 47.50  E-value: 2.98e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 914658877  25 SLHIETEKLKILFDMGSGdtfCQNAPL-LGIDIKDVDLAVISHRHHDHCNG 74
Cdd:COG1234   21 SYLLEAGGERLLIDCGEG---TQRQLLrAGLDPRDIDAIFITHLHGDHIAG 68
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 13-229 3.18e-06

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


Pssm-ID: 293839  Cd Length: 252  Bit Score: 47.10  E-value: 3.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877  13 DNRTDLAVeRglSLHIETEKLKILFDMGSGDT--------FCQNAPL--------LGIDIKDVDLAVISHRHHDHCNGTa 76
Cdd:cd16281   36 DNRITLAM-R--CLLIETGGRNILIDTGIGDKqdpkfrsiYVQHSEHsllkslarLGLSPEDITDVILTHLHFDHCGGA- 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877  77 dfvahnskakvfLKNCEQKSyhfrafgfksdvginkdllensnERLVFVNRTteiapnvFVitdISAKHeqpkgnkYLYT 156
Cdd:cd16281  112 ------------TRADDDGL-----------------------VELLFPNAT-------YW---VQKRH-------WEWA 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914658877 157 QSKNQRERDLFDHELLLVIKEpdglviftgcahSGVLNMVDTA-VTLFPGERIKAVVGgfHLVG--LPLFNSIGGT 229
Cdd:cd16281  140 LNPNPRERASFLPENIEPLEE------------SGRLKLIDGSdAELGPGIRFHLSDG--HTPGqmLPEISTPGGT 201
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 25-88 3.73e-06

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: 46.39  E-value: 3.73e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914658877    25 SLHIETEKLKILFDMGSGDTFCQNAPLLGIDIKDVDLAVISHRHHDHCnGTADFVAHNSKAKVF 88
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDLLAELKKLGPKKIDAIILTHGHPDHI-GGLPELLEAPGAPVY 64
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 25-78 8.23e-06

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 46.04  E-value: 8.23e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 914658877  25 SLHIETEKLKILFDMGSGdtFCQNAPLLGIDIKDVDLAVISHRHHDHCNGTADF 78
Cdd:COG1235   37 SILVEADGTRLLIDAGPD--LREQLLRLGLDPSKIDAILLTHEHADHIAGLDDL 88
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 28-74 1.72e-05

Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as tRNase Z or 3' tRNase) catalyzes the endonucleolytic removal of the 3' extension of the majority of tRNA precursors. Two forms of RNase Z exist in eukaryotes, one long (ELAC2) and one short form (ELAC1), the former may have resulted from a duplication of the shorter enzyme. Only the short form exists in bacteria. It includes the C-terminus of human ELAC2 and Escherichia coli zinc phosphodiesterase (ZiPD, also known as ecoZ, tRNase Z, or RNase BN) is a 3' tRNA-processing endonuclease, encoded by the elaC gene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 44.18  E-value: 1.72e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 914658877  28 IETEKLKILFDMGSGdTFCQnapLL--GIDIKDVDLAVISHRHHDHCNG 74
Cdd:cd16272   22 LETGGTRILLDCGEG-TVYR---LLkaGVDPDKLDAIFLSHFHLDHIGG 66
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 23-72 2.63e-05

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 45.18  E-value: 2.63e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 914658877  23 GLSLHIETEKLKILFDMG-SGDTFCQNAPLLGIDIKDVDLAVISHRHHDHC 72
Cdd:COG1236   14 GSCYLLETGGTRILIDCGlFQGGKERNWPPFPFRPSDVDAVVLTHAHLDHS 64
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 23-74 2.76e-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: 2.76e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 914658877  23 GLSLHIETEKLKILFDMGSGDTFCQNA---PLLGIDIKDVDLAVISHRHHDHCNG 74
Cdd:cd07731   10 GDAILIQTPGKTILIDTGPRDSFGEDVvvpYLKARGIKKLDYLILTHPDADHIGG 64
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 28-88 5.85e-05

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: 43.31  E-value: 5.85e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 914658877  28 IETEKLKILFDMGSGDTFCQNAPLL-------GIDIKDVDLAVISHRHHDHCNGTADfvahNSKAKVF 88
Cdd:cd07720   54 VRTGGRLILVDTGAGGLFGPTAGKLlanlaaaGIDPEDIDDVLLTHLHPDHIGGLVD----AGGKPVF 117
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 25-88 7.01e-05

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 42.98  E-value: 7.01e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 914658877  25 SLHIETEKLKILFD-MGSGDTFCQNAPLLGI-DIKDVDLAVISHRHHDHCNGTADFVAHNSKAKVF 88
Cdd:COG2220   13 TFLIETGGKRILIDpVFSGRASPVNPLPLDPeDLPKIDAVLVTHDHYDHLDDATLRALKRTGATVV 78
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
28-252 1.31e-04

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 41.97  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877   28 IETEKLKILFD--MGSGDTFCQNAPLLGIDIKDVDLAVISHRHHDHCNGTADFVAHNSKAKVflknCEQKSYHFrafgfk 105
Cdd:pfam00753  11 IEGGGGAVLIDtgGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVI----VVAEEARE------ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877  106 sdvgINKDLLENSNERLVFVNRTTEIAPNVFVITDISAKHEQPKGNKYLYTQSknqrerdlfDHELLLVIKEPDGLVIFT 185
Cdd:pfam00753  81 ----LLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPG---------HGPGHVVVYYGGGKVLFT 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 914658877  186 GCahsgvlnmvdtavTLFPGERIKavvggFHLVGLPLFNSIGGTKQDIRELGLTLSQYPIDKLYTGH 252
Cdd:pfam00753 148 GD-------------LLFAGEIGR-----LDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 25-79 3.56e-04

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


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 40.58  E-value: 3.56e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 914658877  25 SLHIETEKLKILFDMGSGDTfcQNAPLLGIDIKDVDLAVISHRHHDHCNGTADFV 79
Cdd:cd07719   20 STLVVVGGRVYLVDAGSGVV--RRLAQAGLPLGDLDAVFLTHLHSDHVADLPALL 72
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 28-88 5.89e-04

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: 39.90  E-value: 5.89e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914658877  28 IETEKLKILFDMG---SGDTFCQNAPLLGIDIKDVDLAVISHRHHDHCNGTADFVAHnSKAKVF 88
Cdd:cd07721   16 IEDDDGLTLIDTGlpgSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEA-PGAPVY 78
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 18-81 6.72e-04

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 40.23  E-value: 6.72e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 914658877  18 LAVERGLSLHIETEKLK-ILFDMGSGDTFCQN----APLL-GIDIKDVDLAVISHRHHDHCNGTADFVAH 81
Cdd:COG2333    6 LDVGQGDAILIRTPDGKtILIDTGPRPSFDAGervvLPYLrALGIRRLDLLVLTHPDADHIGGLAAVLEA 75
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
 25-74 1.57e-03

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


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 38.61  E-value: 1.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 914658877  25 SLHIETEKLKILFDmgSGDTFCQNAplLGIDIKDVDLAVISHRHHDHCNG 74
Cdd:cd16279   37 SILIETGGKNILID--TGPDFRQQA--LRAGIRKLDAVLLTHAHADHIHG 82
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 22-74 2.54e-03

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


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 37.63  E-value: 2.54e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 914658877  22 RGLSLHIETEKLKILFDMG-SGDTFCQNAPLLGIDIKDVDLAVISHRHHDHCNG 74
Cdd:cd07733    8 KGNCTYLETEDGKLLIDAGlSGRKITGRLAEIGRDPEDIDAILVTHEHADHIKG 61
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 ...
 22-87 3.46e-03

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: 38.10  E-value: 3.46e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914658877  22 RGLS-LHIETEKLKILFDmgsgDTFCQNAPL-------LGIDIKDVDLAVISHRHHDHCNGTADfVAHNSKAKV 87
Cdd:cd16290   20 GGLSaVLITSPQGLILID----GALPQSAPQieaniraLGFRLEDVKLILNSHAHFDHAGGIAA-LQRDSGATV 88
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 43-101 4.19e-03

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: 37.13  E-value: 4.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 914658877  43 DTFCQNAPLLGIDIKDVdlaVISHRHHDHCNGtADFVAHNSKAKVFLKNCEQKSYHFRA 101
Cdd:cd16275   35 EKILAKLNELGLTLTGI---LLTHSHFDHVNL-VEPLLAKYDAPVYMSKEEIDYYGFRC 89
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 28-88 5.39e-03

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: 37.09  E-value: 5.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914658877  28 IETEKLKILFDMGSGDTF-CQNAPL--LGIDIKDVDLAVISHRHHDHCNGTADFVAHNSKAKVF 88
Cdd:cd07726   21 LDGEGRPALIDTGPSSSVpRLLAALeaLGIAPEDVDYIILTHIHLDHAGGAGLLAEALPNAKVY 84
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 28-88 5.42e-03

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: 37.18  E-value: 5.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 914658877  28 IETEKLKILFDMGSGdtfcQNAPLL-------GIDIKDVDLAVISHRHHDHCNGTADFvahnSKAKVF 88
Cdd:cd07711   27 IKDGGKNILVDTGTP----WDRDLLlkalaehGLSPEDIDYVVLTHGHPDHIGNLNLF----PNATVI 86
CPSF3-like_MBL-fold cd16292
cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; ...
 21-89 5.42e-03

cleavage and polyadenylation specificity factor (CPSF) subunit 3 and related proteins; MBL-fold metallo-hydrolase domain; CPSF3 (also known as cleavage and polyadenylation specificity factor 73 kDa subunit/CPSF-73) functions as a 3' endonuclease in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and in 3' end processing of metazoan histone pre-mRNAs. This subgroup also contains the yeast homolog of CPSF-73, Ysh1/Brr5 which has roles in mRNA and snoRNA synthesis. In addition to this MBL-fold metallo-hydrolase domain, members of this subgroup contain a beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain, and a RMMBL domain (RNA-metabolizing metallo-beta-lactamase). 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: 293850  Cd Length: 194  Bit Score: 37.18  E-value: 5.42e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 914658877  21 ERGLSLHI-ETEKLKILFDMG--SGDTFCQNAPLL-GIDIKDVDLAVISHRHHDHCNGTADFVAH-NSKAKVFL 89
Cdd:cd16292   11 EVGRSCVIlEFKGKTIMLDCGihPGYSGLASLPFFdEIDLSEIDLLLITHFHLDHCGALPYFLQKtNFKGRVFM 84
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 34-78 6.64e-03

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


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 37.25  E-value: 6.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 914658877  34 KILFDMGSGDTFCQNAPLL------------------------GIDIKDVDLAVISHRHHDHCNGTADF 78
Cdd:cd07730   35 KILFDLGYRKDFEEYTPRVperlyrtpvpleveedvaeqlaagGIDPEDIDAVILSHLHWDHIGGLSDF 103
 
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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