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Conserved domains on  [gi|190695778|gb|ACE89863|]
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putative beta-lactamase family protein [Rhizobium etli CIAT 652]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869928)

MBL fold metallo-hydrolase may have substrate towards phosphotriesters, esters, and/or lactones; similar to Pseudomonas pseudoalcaligenes phosphotriesterase opch2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 52-303 8.97e-91

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: 271.34  E-value: 8.97e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778  52 FKLGSYRFTVVRDGIniSEKPYETYGTNQDPETVRALLtANFLPADKLLNGYAPVLIDTGSDLILVDTGFGAAGRARGlG 131
Cdd:cd07720    1 FKVGDFEVTALSDGT--LPLPLDLLLGGAAPEAEAALL-AAFLPPDPVETSVNAFLVRTGGRLILVDTGAGGLFGPTA-G 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 132 KLAEGLKVAGYSPEDVTLVALTHLHGDHIGGLM-EDGAPAFRNARYVIGAAEYDFWSNTAREGTPAEA---GHKAVLANV 207
Cdd:cd07720   77 KLLANLAAAGIDPEDIDDVLLTHLHPDHIGGLVdAGGKPVFPNAEVHVSEAEWDFWLDDANAAKAPEGakrFFDAARDRL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 208 APLAEKATFiKDGAAVAPGVTAMLAAGHSPGHMVFHAESEGKRMVLTGDTANHYILSLLRPDWEVRFDMDKAQAAATRRK 287
Cdd:cd07720  157 RPYAAAGRF-EDGDEVLPGITAVPAPGHTPGHTGYRIESGGERLLIWGDIVHHPALQFAHPDWTIAFDVDPEQAAATRRR 235

                        250
                 ....*....|....*.
gi 190695778 288 VFDMIATDKIAFLGYH 303
Cdd:cd07720  236 LLDRAAAEGLLVAGAH 251
 
Name Accession Description Interval E-value
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 52-303 8.97e-91

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: 271.34  E-value: 8.97e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778  52 FKLGSYRFTVVRDGIniSEKPYETYGTNQDPETVRALLtANFLPADKLLNGYAPVLIDTGSDLILVDTGFGAAGRARGlG 131
Cdd:cd07720    1 FKVGDFEVTALSDGT--LPLPLDLLLGGAAPEAEAALL-AAFLPPDPVETSVNAFLVRTGGRLILVDTGAGGLFGPTA-G 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 132 KLAEGLKVAGYSPEDVTLVALTHLHGDHIGGLM-EDGAPAFRNARYVIGAAEYDFWSNTAREGTPAEA---GHKAVLANV 207
Cdd:cd07720   77 KLLANLAAAGIDPEDIDDVLLTHLHPDHIGGLVdAGGKPVFPNAEVHVSEAEWDFWLDDANAAKAPEGakrFFDAARDRL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 208 APLAEKATFiKDGAAVAPGVTAMLAAGHSPGHMVFHAESEGKRMVLTGDTANHYILSLLRPDWEVRFDMDKAQAAATRRK 287
Cdd:cd07720  157 RPYAAAGRF-EDGDEVLPGITAVPAPGHTPGHTGYRIESGGERLLIWGDIVHHPALQFAHPDWTIAFDVDPEQAAATRRR 235

                        250
                 ....*....|....*.
gi 190695778 288 VFDMIATDKIAFLGYH 303
Cdd:cd07720  236 LLDRAAAEGLLVAGAH 251
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 95-291 1.23e-23

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: 96.68  E-value: 1.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778  95 PADKLLNGYAPVLIDTGSDLILVDTGFGAAGRARglgkLAEGLKVAGyspEDVTLVALTHLHGDHIGGLMEDGApAFrNA 174
Cdd:COG0491    7 GTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEA----LLAALAALG---LDIKAVLLTHLHPDHVGGLAALAE-AF-GA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 175 RYVIGAAEYDFWSNTAREGTPAEAGHKAvlanvaplaekATFIKDGAAV---APGVTAMLAAGHSPGHMVFHAESEgkRM 251
Cdd:COG0491   78 PVYAHAAEAEALEAPAAGALFGREPVPP-----------DRTLEDGDTLelgGPGLEVIHTPGHTPGHVSFYVPDE--KV 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 190695778 252 VLTGDTAnhYILSLLRPDwevRFDMDKAQAAATRRKVFDM 291
Cdd:COG0491  145 LFTGDAL--FSGGVGRPD---LPDGDLAQWLASLERLLAL 179
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 106-295 4.92e-19

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: 82.99  E-value: 4.92e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778   106 VLIDTGSDLILVDTGFGAAGRArgLGKLAEglkvagYSPEDVTLVALTHLHGDHIGGLmeDGAPAFRNARYVIGAAEYDF 185
Cdd:smart00849   3 YLVRDDGGAILIDTGPGEAEDL--LAELKK------LGPKKIDAIILTHGHPDHIGGL--PELLEAPGAPVYAPEGTAEL 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778   186 WSNTAREGTPAEAghkavlanVAPLAEKATFIKDGAAV---APGVTAMLAAGHSPGHMVFHAESEgkRMVLTGDTANHYI 262
Cdd:smart00849  73 LKDLLALLGELGA--------EAEPAPPDRTLKDGDELdlgGGELEVIHTPGHTPGSIVLYLPEG--KILFTGDLLFAGG 142

                          170       180       190
                   ....*....|....*....|....*....|...
gi 190695778   263 LSLLRPDWevrFDMDKAQAAATRRKVFDMIATD 295
Cdd:smart00849 143 DGRTLVDG---GDAAASDALESLLKLLKLLPKL 172
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
106-300 1.56e-17

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 79.33  E-value: 1.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778  106 VLIDTGSDLILVDTGFGAAGrarglgKLAEGLKVAGYSPEDVTLVALTHLHGDHIGGLMEdGAPAFRNARYVIGAAEYDF 185
Cdd:pfam00753   9 YLIEGGGGAVLIDTGGSAEA------ALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGE-LAEATDVPVIVVAEEAREL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778  186 WsntAREGTPAEAGHKAVLANVAPLAEKATFIKDGAAVAPGVTAMLAAGHSPGHMVFHAESEGKRMVLTGDT---ANHYI 262
Cdd:pfam00753  82 L---DEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLlfaGEIGR 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 190695778  263 LSLLRPDWEVRFDMDKAQAaatrRKVFDMIATDKIAFL 300
Cdd:pfam00753 159 LDLPLGGLLVLHPSSAESS----LESLLKLAKLKAAVI 192
PRK00055 PRK00055
ribonuclease Z; Reviewed
 106-165 7.03e-05

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 43.63  E-value: 7.03e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190695778 106 VLIDTGSDLILVDTGfgaagrarglgklaEG----LKVAGYSPEDVTLVALTHLHGDHIGGLME 165
Cdd:PRK00055  23 ILLRLGGELFLFDCG--------------EGtqrqLLKTGIKPRKIDKIFITHLHGDHIFGLPG 72
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 106-164 3.72e-03

ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of endonuclease or exonuclease activity, and differs in different species. Member of this family are ribonuclease Z, a tRNA 3-prime endonuclease that processes tRNAs to prepare for addition of CCA. In species where all tRNA sequences already have the CCA tail, such as E. coli, the need for such an enzyme is unclear. Protein similar to the E. coli enzyme, matched by TIGRFAMs model TIGR02649, are designated ribonuclease BN. [Transcription, RNA processing]


Pssm-ID: 274246 [Multi-domain]  Cd Length: 299  Bit Score: 38.35  E-value: 3.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190695778  106 VLIDTGSDLILVDTGfgaagrarglgklaEG----LKVAGYSPEDVTLVALTHLHGDHIGGLM 164
Cdd:TIGR02651  21 IALKLNGELWLFDCG--------------EGtqrqMLRSGISPMKIDRIFITHLHGDHILGLP 69
 
Name Accession Description Interval E-value
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 52-303 8.97e-91

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: 271.34  E-value: 8.97e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778  52 FKLGSYRFTVVRDGIniSEKPYETYGTNQDPETVRALLtANFLPADKLLNGYAPVLIDTGSDLILVDTGFGAAGRARGlG 131
Cdd:cd07720    1 FKVGDFEVTALSDGT--LPLPLDLLLGGAAPEAEAALL-AAFLPPDPVETSVNAFLVRTGGRLILVDTGAGGLFGPTA-G 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 132 KLAEGLKVAGYSPEDVTLVALTHLHGDHIGGLM-EDGAPAFRNARYVIGAAEYDFWSNTAREGTPAEA---GHKAVLANV 207
Cdd:cd07720   77 KLLANLAAAGIDPEDIDDVLLTHLHPDHIGGLVdAGGKPVFPNAEVHVSEAEWDFWLDDANAAKAPEGakrFFDAARDRL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 208 APLAEKATFiKDGAAVAPGVTAMLAAGHSPGHMVFHAESEGKRMVLTGDTANHYILSLLRPDWEVRFDMDKAQAAATRRK 287
Cdd:cd07720  157 RPYAAAGRF-EDGDEVLPGITAVPAPGHTPGHTGYRIESGGERLLIWGDIVHHPALQFAHPDWTIAFDVDPEQAAATRRR 235

                        250
                 ....*....|....*.
gi 190695778 288 VFDMIATDKIAFLGYH 303
Cdd:cd07720  236 LLDRAAAEGLLVAGAH 251
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 107-303 1.71e-51

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 169.63  E-value: 1.71e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 107 LIDTGSDLILVDTGFGAaGRARGLGKLA--------EGLKVAGYSPEDVTLVALTHLHGDHIGGL--MEDG--APAFRNA 174
Cdd:cd16277   17 LVRTPGRTILVDTGIGN-DKPRPGPPAFhnlntpylERLAAAGVRPEDVDYVLCTHLHVDHVGWNtrLVDGrwVPTFPNA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 175 RYVIGAAEYDFWSNTAREGTPaeagHKAVLA-NVAPLAE--KATFIKDGAAVAPGVTAMLAAGHSPGHMVFHAESEGKRM 251
Cdd:cd16277   96 RYLFSRAEYDHWSSPDAGGPP----NRGVFEdSVLPVIEagLADLVDDDHEILDGIRLEPTPGHTPGHVSVELESGGERA 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 190695778 252 VLTGDTANHYIlSLLRPDWEVRFDMDKAQAAATRRKVFDMIATDKIAFLGYH 303
Cdd:cd16277  172 LFTGDVMHHPI-QVARPDWSSVFDEDPAQAAATRRRLLERAADTDTLLFPAH 222
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 106-288 5.90e-37

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: 132.34  E-value: 5.90e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 106 VLIDTGSDLILVDTGFGAAGRARGLGK-------------LAEGLKVAGYSPEDVTLVALTHLHGDHIGGLmedgaPAFR 172
Cdd:cd07729   35 YLIEHPEGTILVDTGFHPDAADDPGGLelafppgvteeqtLEEQLARLGLDPEDIDYVILSHLHFDHAGGL-----DLFP 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 173 NARYVIGAAEYDFWsnTAREGTPAEAGHKAVLANVAPLAEKATFIKDGAAVAPGVTAMLAAGHSPGHMVFHAESEGKRMV 252
Cdd:cd07729  110 NATIIVQRAELEYA--TGPDPLAAGYYEDVLALDDDLPGGRVRLVDGDYDLFPGVTLIPTPGHTPGHQSVLVRLPEGTVL 187

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 190695778 253 LTGDTANHYilSLLRPDWEVRFDMDKAQAAATRRKV 288
Cdd:cd07729  188 LAGDAAYTY--ENLEEGRPPGINYDPEAALASLERL 221
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 95-291 1.23e-23

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: 96.68  E-value: 1.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778  95 PADKLLNGYAPVLIDTGSDLILVDTGFGAAGRARglgkLAEGLKVAGyspEDVTLVALTHLHGDHIGGLMEDGApAFrNA 174
Cdd:COG0491    7 GTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEA----LLAALAALG---LDIKAVLLTHLHPDHVGGLAALAE-AF-GA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 175 RYVIGAAEYDFWSNTAREGTPAEAGHKAvlanvaplaekATFIKDGAAV---APGVTAMLAAGHSPGHMVFHAESEgkRM 251
Cdd:COG0491   78 PVYAHAAEAEALEAPAAGALFGREPVPP-----------DRTLEDGDTLelgGPGLEVIHTPGHTPGHVSFYVPDE--KV 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 190695778 252 VLTGDTAnhYILSLLRPDwevRFDMDKAQAAATRRKVFDM 291
Cdd:COG0491  145 LFTGDAL--FSGGVGRPD---LPDGDLAQWLASLERLLAL 179
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 105-288 5.67e-21

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: 88.82  E-value: 5.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 105 PVLIDTGSDLILVDTGFGAAGRarglgKLAEGLKVAGYSPEDVTLVALTHLHGDHIGGLmedgaPAFR---NARYVIGAA 181
Cdd:cd07721   13 AYLIEDDDGLTLIDTGLPGSAK-----RILKALRELGLSPKDIRRILLTHGHIDHIGSL-----AALKeapGAPVYAHER 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 182 EYDFWSNTAREGTPAEAGHKAVLANVAPLAEKAT--FIKDGAAV--APGVTAMLAAGHSPGHMVFHAESEgkRMVLTGDT 257
Cdd:cd07721   83 EAPYLEGEKPYPPPVRLGLLGLLSPLLPVKPVPVdrTLEDGDTLdlAGGLRVIHTPGHTPGHISLYLEED--GVLIAGDA 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 190695778 258 ANHYILSLLRPDWevRFDMDKAQAAATRRKV 288
Cdd:cd07721  161 LVTVGGELVPPPP--PFTWDMEEALESLRKL 189
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 107-270 1.14e-20

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


Pssm-ID: 293839  Cd Length: 252  Bit Score: 89.48  E-value: 1.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 107 LIDTGSDLILVDTGFGAA--------GRARGLGKLAEGLKVAGYSPEDVTLVALTHLHGDHIGGLM---EDG--APAFRN 173
Cdd:cd16281   47 LIETGGRNILIDTGIGDKqdpkfrsiYVQHSEHSLLKSLARLGLSPEDITDVILTHLHFDHCGGATradDDGlvELLFPN 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 174 ARYVIGAAEYDfwsnTAREGTPAEAGHkAVLANVAPLAE--KATFIKDGAAV-APGVTAMLAAGHSPGHMVFHAESEGKR 250
Cdd:cd16281  127 ATYWVQKRHWE----WALNPNPRERAS-FLPENIEPLEEsgRLKLIDGSDAElGPGIRFHLSDGHTPGQMLPEISTPGGT 201

                        170       180
                 ....*....|....*....|...
gi 190695778 251 MVLTGD---TANHyilslLRPDW 270
Cdd:cd16281  202 VVFAADlipTSAH-----IPLPW 219
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 101-257 2.62e-19

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: 83.87  E-value: 2.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 101 NGYapVLIDTGSDLILVDTGFGAagrarglgkLAEGLKVAGYSPEDVTLVALTHLHGDHIGGLmedgaPAFR---NARYV 177
Cdd:cd06262   11 NCY--LVSDEEGEAILIDPGAGA---------LEKILEAIEELGLKIKAILLTHGHFDHIGGL-----AELKeapGAPVY 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 178 IGAAEYDFWSNtaregtpAEAGHKAVLANVAPLAEKATFIKDGAAVAPG---VTAMLAAGHSPGHMVFHAESEGkrMVLT 254
Cdd:cd06262   75 IHEADAELLED-------PELNLAFFGGGPLPPPEPDILLEDGDTIELGgleLEVIHTPGHTPGSVCFYIEEEG--VLFT 145


                 ...
gi 190695778 255 GDT 257
Cdd:cd06262  146 GDT 148
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 106-295 4.92e-19

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: 82.99  E-value: 4.92e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778   106 VLIDTGSDLILVDTGFGAAGRArgLGKLAEglkvagYSPEDVTLVALTHLHGDHIGGLmeDGAPAFRNARYVIGAAEYDF 185
Cdd:smart00849   3 YLVRDDGGAILIDTGPGEAEDL--LAELKK------LGPKKIDAIILTHGHPDHIGGL--PELLEAPGAPVYAPEGTAEL 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778   186 WSNTAREGTPAEAghkavlanVAPLAEKATFIKDGAAV---APGVTAMLAAGHSPGHMVFHAESEgkRMVLTGDTANHYI 262
Cdd:smart00849  73 LKDLLALLGELGA--------EAEPAPPDRTLKDGDELdlgGGELEVIHTPGHTPGSIVLYLPEG--KILFTGDLLFAGG 142

                          170       180       190
                   ....*....|....*....|....*....|...
gi 190695778   263 LSLLRPDWevrFDMDKAQAAATRRKVFDMIATD 295
Cdd:smart00849 143 DGRTLVDG---GDAAASDALESLLKLLKLLPKL 172
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
106-300 1.56e-17

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 79.33  E-value: 1.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778  106 VLIDTGSDLILVDTGFGAAGrarglgKLAEGLKVAGYSPEDVTLVALTHLHGDHIGGLMEdGAPAFRNARYVIGAAEYDF 185
Cdd:pfam00753   9 YLIEGGGGAVLIDTGGSAEA------ALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGE-LAEATDVPVIVVAEEAREL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778  186 WsntAREGTPAEAGHKAVLANVAPLAEKATFIKDGAAVAPGVTAMLAAGHSPGHMVFHAESEGKRMVLTGDT---ANHYI 262
Cdd:pfam00753  82 L---DEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLlfaGEIGR 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 190695778  263 LSLLRPDWEVRFDMDKAQAaatrRKVFDMIATDKIAFL 300
Cdd:pfam00753 159 LDLPLGGLLVLHPSSAESS----LESLLKLAKLKAAVI 192
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 105-256 4.84e-16

Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus subtilis YtnP inhibits the signaling pathway required for the streptomycin production and development of aerial mycelium in Streptomyces griseus. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293814  Cd Length: 249  Bit Score: 76.53  E-value: 4.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 105 PVLIDTGSDLILVDTGFG------AAGRARGL---GKLAEGLKVAGYSPEDVTLVALTHLHGDHIGGL--MEDGA--PAF 171
Cdd:cd07728   45 PILIQYQGKNYLIDAGIGngklteKQKRNFGVteeSSIEESLAELGLTPEDIDYVLMTHLHFDHASGLtkVKGEQlvSVF 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 172 RNARYVIGAAEydfWS-----NTAREGTPAEAGHKAVLANVAPLAEKATfikdgaaVAPGVTAMLAAGHSPGHMVFHAES 246
Cdd:cd07728  125 PNATIYVSEIE---WEemrnpNIRSKNTYWKENWEPIEDQVKTFSDEIE-------IVPGITMIHTGGHSDGHSIIEIEQ 194

                        170
                 ....*....|
gi 190695778 247 EGKRMVLTGD 256
Cdd:cd07728  195 GGETAIHMAD 204
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 133-297 2.66e-14

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: 71.53  E-value: 2.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 133 LAEGLKVAGYSPEDVTLVALTHLHGDHIGGLmedgaPAFRNARYVIGAAEYDFwsntAREGTPAEAGHKAVLAN--VAPL 210
Cdd:cd07730   70 VAEQLAAGGIDPEDIDAVILSHLHWDHIGGL-----SDFPNARLIVGPGAKEA----LRPPGYPSGFLPELLPSdfEGRL 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 211 AEKATFIKDGAAVAPGVTAML-----------AAGHSPGHM-VFHAESEGKRMVLTGDTAnHYILSLLRPD-----WEVR 273
Cdd:cd07730  141 VRWEEDDFLWVPLGPFPRALDlfgdgslylvdLPGHAPGHLgLLARTTSGTWVFLAGDAC-HHRIGLLRPSpllplPDLD 219

                        170       180
                 ....*....|....*....|....
gi 190695778 274 FDMDKAQAAATRRKVFDMIATDKI 297
Cdd:cd07730  220 DGADREAARETLARLRELDAAPDV 243
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 106-291 1.40e-13

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: 68.38  E-value: 1.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 106 VLIDTGSDLILVDTGfGAAGRARGLGKLAEglkvAGYSPEDVTLVALTHLHGDHIGGLmedgaPAFRNAR----YVIGAA 181
Cdd:cd07711   25 TLIKDGGKNILVDTG-TPWDRDLLLKALAE----HGLSPEDIDYVVLTHGHPDHIGNL-----NLFPNATvivgWDICGD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 182 EYDFWSntaregtpaeaghkavlanvaplaekaTFIKDGAAVAPGVTAMLAAGHSPGHM-VFHAESEGKRMVLTGD---T 257
Cdd:cd07711   95 SYDDHS---------------------------LEEGDGYEIDENVEVIPTPGHTPEDVsVLVETEKKGTVAVAGDlfeR 147

                        170       180       190
                 ....*....|....*....|....*....|....
gi 190695778 258 ANhyilSLLRPDWEVRFDMDKAQAAATRRKVFDM 291
Cdd:cd07711  148 EE----DLEDPILWDPLSEDPELQEESRKRILAL 177
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 104-266 8.72e-13

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: 65.75  E-value: 8.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 104 APVLIDTGSDLILVDTGFGAAGRarglgklaegLKVAGYSPEDVTLVALTHLHGDHIGGLMEdgAPAFRNAR------YV 177
Cdd:cd16272   18 SSYLLETGGTRILLDCGEGTVYR----------LLKAGVDPDKLDAIFLSHFHLDHIGGLPT--LLFARRYGgrkkplTI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 178 IGAAEY-DFWSNTAREGTPAEAGHKAVlaNVAPLAEKATFIKDGAAVapgVTAMLAaGHSPGHMVFHAESEGKRMVLTGD 256
Cdd:cd16272   86 YGPKGIkEFLEKLLNFPVEILPLGFPL--EIEELEEGGEVLELGDLK---VEAFPV-KHSVESLGYRIEAEGKSIVYSGD 159

                        170
                 ....*....|
gi 190695778 257 TANHYILSLL 266
Cdd:cd16272  160 TGPCENLVEL 169
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 106-184 1.30e-12

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


Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 66.49  E-value: 1.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 106 VLIDTGSDLILVDTGFG----AAGRARGLGKLAEGLKVA--------------GYSPEDVTLVALTHLHGDHIGGLMEdg 167
Cdd:cd07742   22 LLVETDDGLVLVDTGFGladvADPKRRLGGPFRRLLRPRldedetavrqiealGFDPSDVRHIVLTHLDLDHAGGLAD-- 99

                         90
                 ....*....|....*..
gi 190695778 168 apaFRNARYVIGAAEYD 184
Cdd:cd07742  100 ---FPHATVHVHAAELD 113
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 107-250 3.62e-12

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 65.30  E-value: 3.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 107 LIDTGSDLILVDTGFGAagRARGLgkLAEGLKVAGYSPEDVTLVALTHLHGDHIGglmedGAPAFR---NARYVIGAAEY 183
Cdd:cd16280   26 AIDTGDGLILIDALNNN--EAADL--IVDGLEKLGLDPADIKYILITHGHGDHYG-----GAAYLKdlyGAKVVMSEADW 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 190695778 184 DFWSNTAREGTPAEAGhkavlanvaPLAEKATFIKDGAAVAPG---VTAMLAAGHSPG--HMVFHAESEGKR 250
Cdd:cd16280   97 DMMEEPPEEGDNPRWG---------PPPERDIVIKDGDTLTLGdttITVYLTPGHTPGtlSLIFPVKDGGKT 159
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 102-306 2.61e-11

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: 61.55  E-value: 2.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 102 GYAPV-LIDTGSDLILVDTGFgAAGRARGLgkLAEGLKVAGYSPEDVTLVALTHLHGDHIGglmedGAPAFRnaryviga 180
Cdd:cd07725   13 GHVNVyLLRDGDETTLIDTGL-ATEEDAEA--LWEGLKELGLKPSDIDRVLLTHHHPDHIG-----LAGKLQ-------- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 181 aeydfwsntaregtpAEAGHKAVLANVAPLAEKATFIKDGAavapGVTAMLAAGHSPGHMVFHaeSEGKRMVLTGDTanh 260
Cdd:cd07725   77 ---------------EKSGATVYILDVTPVKDGDKIDLGGL----RLKVIETPGHTPGHIVLY--DEDRRELFVGDA--- 132

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 190695778 261 yILSLLRPD---WEVRFDMDKAQAAATRRKVFDMiaTDKIAFLGYHMPF 306
Cdd:cd07725  133 -VLPKITPNvslWAVRVEDPLGAYLESLDKLEKL--DVDLAYPGHGGPI 178
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 106-258 1.23e-10

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: 59.84  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 106 VLIDTGSDLILVDTGFGAAGRarglgkLAEglkvAGYSPEDVTLVALTHLHGDHIGGLmedgaPAFRNARY--------- 176
Cdd:cd07719   21 TLVVVGGRVYLVDAGSGVVRR------LAQ----AGLPLGDLDAVFLTHLHSDHVADL-----PALLLTAWlagrktplp 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 177 VIG-----------AAEYDFWSNTAREGTPAEAGHKAVLANVAPLAEKATFIKDGAAVapgVTAMLAAgHSPghmVFHA- 244
Cdd:cd07719   86 VYGppgtralvdglLAAYALDIDYRARIGDEGRPDPGALVEVHEIAAGGVVYEDDGVK---VTAFLVD-HGP---VPPAl 158

                        170
                 ....*....|....*...
gi 190695778 245 ----ESEGKRMVLTGDTA 258
Cdd:cd07719  159 ayrfDTPGRSVVFSGDTG 176
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 107-258 5.37e-10

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: 58.27  E-value: 5.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 107 LIDTGSDLILVDTGFGAAgrargLGKLAEGLKVAGYSPEDVTLVALTHLHGDHIGG---LMED--GAPAF---RNARYVI 178
Cdd:cd07726   20 LLDGEGRPALIDTGPSSS-----VPRLLAALEALGIAPEDVDYIILTHIHLDHAGGaglLAEAlpNAKVYvhpRGARHLI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 179 -------------GAAEYDFWSNTarEGTPAEaghkavlaNVAPLAEKATFIKDGAavapGVTAMLAAGHSPGHMVFHAE 245
Cdd:cd07726   95 dpsklwasaravyGDEADRLGGEI--LPVPEE--------RVIVLEDGETLDLGGR----TLEVIDTPGHAPHHLSFLDE 160

                        170
                 ....*....|...
gi 190695778 246 SEGkrMVLTGDTA 258
Cdd:cd07726  161 ESD--GLFTGDAA 171
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 107-256 1.31e-09

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 57.19  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 107 LIDTGSDLILVDTGFGAAgRARGLgkLAEglkVAGYSPEDVTLVALTHLHGDHIGG---LMEDGAP--AFRNARYVIGAA 181
Cdd:cd16282   19 FIVGDDGVVVIDTGASPR-LARAL--LAA---IRKVTDKPVRYVVNTHYHGDHTLGnaaFADAGAPiiAHENTREELAAR 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190695778 182 EYDFWSNTAREGTPAEAGHKAVLANVaPLAEKATfIKDGaavapGVTAML---AAGHSPGHMVFHAESEGkrMVLTGD 256
Cdd:cd16282   93 GEAYLELMRRLGGDAMAGTELVLPDR-TFDDGLT-LDLG-----GRTVELihlGPAHTPGDLVVWLPEEG--VLFAGD 161
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 ...
 102-250 1.91e-08

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: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 102 GYAPVLIDTGSDLILVDtgfgaAGRARGLGKLAEGLKVAGYSPEDVTLVALTHLHGDHIGGLME----DGAPAfrnARYV 177
Cdd:cd16290   21 GLSAVLITSPQGLILID-----GALPQSAPQIEANIRALGFRLEDVKLILNSHAHFDHAGGIAAlqrdSGATV---AASP 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190695778 178 IGAAeydfwsnTAREGTPAEAGHKA-VLANVAPLAEKATfIKDGAAVAPG---VTAMLAAGHSPGHMVFHAES-EGKR 250
Cdd:cd16290   93 AGAA-------ALRSGGVDPDDPQAgAADPFPPVAKVRV-VADGEVVKLGplaVTAHATPGHTPGGTSWTWRScEGGR 162
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
106-164 3.58e-08

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 53.66  E-value: 3.58e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 190695778 106 VLIDTGSDLILVDTGFGAAGRarglgklaegLKVAGYSPEDVTLVALTHLHGDHIGGLM 164
Cdd:COG1234   22 YLLEAGGERLLIDCGEGTQRQ----------LLRAGLDPRDIDAIFITHLHGDHIAGLP 70
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 102-238 5.36e-08

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: 52.93  E-value: 5.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 102 GYAPVLIDTGSDLILVDTGFGAagrarGLGKLAEGLKVAGYSPEDVTLVALTHLHGDHIGGLMEdgAPAFRNARYVIGAA 181
Cdd:cd07708   21 DLAAYLIVTPQGNILIDGDMEQ-----NAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAE--IKKQTGAKVMAGAE 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 182 EYDfwsnTAREGTPAEAGHKAVLANVAPLAEKATFIKDGAAVAPG---VTAMLAAGHSPG 238
Cdd:cd07708   94 DVS----LLLSGGSSDFHYANDSSTYFPQSTVDRAVHDGERVTLGgtvLTAHATPGHTPG 149
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 101-257 1.22e-07

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: 50.99  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 101 NGYapvLIDTGSDLILVDTGFGAAGRARGLGKLAEGLKVAgyspeDVTLVALTHLHGDHIGGLmedgaPAFRNaryVIGA 180
Cdd:cd07722   19 NTY---LVGTGKRRILIDTGEGRPSYIPLLKSVLDSEGNA-----TISDILLTHWHHDHVGGL-----PDVLD---LLRG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 181 AEYDFWSNTAREGTPAEaghkavlanvAPLAEKATFIKDGAAVA-PGVT--AMLAAGHSPGHMVFHAESEgkRMVLTGDT 257
Cdd:cd07722   83 PSPRVYKFPRPEEDEDP----------DEDGGDIHDLQDGQVFKvEGATlrVIHTPGHTTDHVCFLLEEE--NALFTGDC 150
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 103-257 3.76e-07

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: 49.38  E-value: 3.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 103 YAPVLIDTGSD-LILVDTGFGAagrarglgKLAEGLKVAGYSPedvTLVALTHLHGDHIGGLMEDGApAFRNARyVIGAA 181
Cdd:cd07723   10 YIYLIVDEATGeAAVVDPGEAE--------PVLAALEKNGLTL---TAILTTHHHWDHTGGNAELKA-LFPDAP-VYGPA 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 190695778 182 EYDFwsntaregtpaeaghkavlanvaPLAEKatFIKDGAAVAPG---VTAMLAAGHSPGHMVFHAESEGkrMVLTGDT 257
Cdd:cd07723   77 EDRI-----------------------PGLDH--PVKDGDEIKLGgleVKVLHTPGHTLGHICYYVPDEP--ALFTGDT 128
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 102-238 1.89e-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: 48.35  E-value: 1.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 102 GYAPVLIDTGSDLILVDTGFGAAGrarglGKLAEGLKVAGYSPEDVTLVALTHLHGDHIGGLME----DGAPAFRNARYV 177
Cdd:cd16314   21 GISALLVTSDAGHILIDGGTDKAA-----PLIEANIRALGFRPEDVRYIVSSHEHFDHAGGIARlqraTGAPVVAREPAA 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190695778 178 IgaaeydfwsnTAREGTPAEAGHK-AVLANVAPLAEKATfIKDGAAVAPG---VTAMLAAGHSPG 238
Cdd:cd16314   96 T----------TLERGRSDRSDPQfLVVEKFPPVASVQR-IGDGEVLRVGplaLTAHATPGHTPG 149
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 106-163 4.04e-06

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: 46.10  E-value: 4.04e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 190695778 106 VLIDTGSDLILVDTGFGAAgrarglgKLAEGLKVAGYSPEDVTLVALTHLHGDHIGGL 163
Cdd:cd07733   12 TYLETEDGKLLIDAGLSGR-------KITGRLAEIGRDPEDIDAILVTHEHADHIKGL 62
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 102-241 4.46e-06

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: 47.16  E-value: 4.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 102 GYAPVLIDTGSDLILVDTGFgaagrARGLGKLAEGLKVAGYSPEDVTLVALTHLHGDHIGGLMEdgAPAFRNARYVIGAA 181
Cdd:cd16313   21 GISAVLITSPQGHILIDGGF-----PKSPEQIAASIRQLGFKLEDVKYILSSHDHWDHAGGIAA--LQKLTGAQVLASPA 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 190695778 182 EYDfwsnTAREGTPAEAGHK-AVLANVAPLAEKATfIKDGAAVAPGVTAMlAAGHSPGHMV 241
Cdd:cd16313   94 TVA----VLRSGSMGKDDPQfGGLTPMPPVASVRA-VRDGEVVKLGPLAV-TAHATPGHTT 148
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 106-163 4.78e-06

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: 47.23  E-value: 4.78e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 190695778 106 VLIDTGSDLILVDTGFGaagrarglGKLAEGLKVAGYSPEDVTLVALTHLHGDHIGGL 163
Cdd:cd07713   23 LLIETEGKKILFDTGQS--------GVLLHNAKKLGIDLSDIDAVVLSHGHYDHTGGL 72
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
106-165 9.53e-06

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 46.41  E-value: 9.53e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 106 VLIDTGSDLILVDTGFGAAgrarglgkLAEGLKVAGYSPEDVTLVALTHLHGDHIGGLME 165
Cdd:COG1237   25 ALIETEGKRILFDTGQSDV--------LLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLPA 76
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 115-256 1.32e-05

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: 45.42  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 115 ILVDTGFGAAGRARGLGklAEGLKVAGyspedvtlVALTHLHGDHIGGLmedgAPAFR--NARYVIGAAEYDFWSNtare 192
Cdd:cd16322   25 VLVDPGDESEKLLARFG--TTGLTLLY--------ILLTHAHFDHVGGV----ADLRRhpGAPVYLHPDDLPLYEA---- 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190695778 193 gtpAEAGHKAVLANVAPLAEKATFIKDGAAVAPGVT---AMLAAGHSPGHMVFHAESEGkrMVLTGD 256
Cdd:cd16322   87 ---ADLGAKAFGLGIEPLPPPDRLLEDGQTLTLGGLefkVLHTPGHSPGHVCFYVEEEG--LLFSGD 148
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 115-257 1.46e-05

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: 44.93  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 115 ILVDTGFGaagrargLGKLAEGLKVAGYSPedVTLVAlTHLHGDHIGGLMEdgapaFrnARYVIGAAEYDFwsntAREGT 194
Cdd:cd07712   21 LLIDTGLG-------IGDLKEYVRTLTDLP--LLVVA-THGHFDHIGGLHE-----F--EEVYVHPADAEI----LAAPD 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190695778 195 PAEAGHKAVLANVAPLAEKATFIKDGAAVAPG---VTAMLAAGHSPGHMVFHaeSEGKRMVLTGDT 257
Cdd:cd07712   80 NFETLTWDAATYSVPPAGPTLPLRDGDVIDLGdrqLEVIHTPGHTPGSIALL--DRANRLLFSGDV 143
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 102-238 1.60e-05

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


Pssm-ID: 293873 [Multi-domain]  Cd Length: 248  Bit Score: 45.42  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 102 GYAPVLIDTGSDLILVDtgfgaAGRARGLGKLAEGLKVAGYSPEDVTLVALTHLHGDHIGGLME----DGAP--AFRNAR 175
Cdd:cd16315   21 GISAILITGDDGHVLID-----SGTEEAAPLVLANIRKLGFDPKDVRWLLSSHEHFDHVGGLAAlqraTGARvaASAAAA 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190695778 176 YVIgaaeydfwsntaREGTPAEAGHKAVLANVAPLAEKATFIKDGAAVAPG---VTAMLAAGHSPG 238
Cdd:cd16315   96 PVL------------ESGKPAPDDPQAGLHEPFPPVRVDRIVEDGDTVALGslrLTAHATPGHTPG 149
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 136-163 2.66e-05

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 44.17  E-value: 2.66e-05
                         10        20
                 ....*....|....*....|....*...
gi 190695778 136 GLKVAGYSPEDVTLVALTHLHGDHIGGL 163
Cdd:cd07740   39 ALKRAGIDPNAIDAIFITHLHGDHFGGL 66
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 107-257 3.29e-05

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 44.02  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 107 LIDTGSDLILVDTGFGAAGRARGLGKLAEGlkvagyspEDVTLVALTHLHGDHigglmEDGAPAFRnaryvigaaeydfw 186
Cdd:cd16278   22 LLGAPDGVVVIDPGPDDPAHLDALLAALGG--------GRVSAILVTHTHRDH-----SPGAARLA-------------- 74

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190695778 187 sntAREGTPAEAGHKAVLANVAPLAEKATFIKDGAAVAPG---VTAMLAAGHSPGHMVFHAESEGkrMVLTGDT 257
Cdd:cd16278   75 ---ERTGAPVRAFGPHRAGGQDTDFAPDRPLADGEVIEGGglrLTVLHTPGHTSDHLCFALEDEG--ALFTGDH 143
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 102-238 3.97e-05

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


Pssm-ID: 293867 [Multi-domain]  Cd Length: 252  Bit Score: 44.40  E-value: 3.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 102 GYAPVLIDTGSDLILVDTGFGAAGrarglGKLAEGLKVAGYSPEDVTLVALTHLHGDHIGGLMEdgAPAFRNARYVIGAA 181
Cdd:cd16309   21 GLGVFLITTPEGHILIDGAMPQST-----PLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAE--LKKATGAQLVASAA 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 182 eyDFWsntAREGTPAEAGHKAVLANVAPLAEKAtfIKDGAAVAPG---VTAMLAAGHSPG 238
Cdd:cd16309   94 --DKP---LLESGYVGSGDTKNLQFPPVRVDRV--IGDGDKVTLGgttLTAHLTPGHSPG 146
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 106-175 5.05e-05

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 44.12  E-value: 5.05e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 106 VLIDTGSDLILVDTGFGAagRARGLGklaeglkvAGYSPEDVTLVALTHLHGDHIGGLMeDGAPAFRNAR 175
Cdd:COG1235   38 ILVEADGTRLLIDAGPDL--REQLLR--------LGLDPSKIDAILLTHEHADHIAGLD-DLRPRYGPNP 96
PRK00055 PRK00055
ribonuclease Z; Reviewed
 106-165 7.03e-05

ribonuclease Z; Reviewed


Pssm-ID: 234602 [Multi-domain]  Cd Length: 270  Bit Score: 43.63  E-value: 7.03e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190695778 106 VLIDTGSDLILVDTGfgaagrarglgklaEG----LKVAGYSPEDVTLVALTHLHGDHIGGLME 165
Cdd:PRK00055  23 ILLRLGGELFLFDCG--------------EGtqrqLLKTGIKPRKIDKIFITHLHGDHIFGLPG 72
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 102-238 7.22e-05

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: 43.46  E-value: 7.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 102 GYAPVLIDTGSDLILVDTGFGAAGrarglGKLAEGLKVAGYSPEDVTLVALTHLHGDHIGGLMEdgAPAFRNARYVIGAA 181
Cdd:cd16288   21 GLASYLITTPQGLILIDTGLESSA-----PMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAA--LKKLTGAKLMASAE 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 182 EYDFwsnTAREGTPAEAGHKAVLANVAPLAEKAtfIKDGAAVAPG---VTAMLAAGHSPG 238
Cdd:cd16288   94 DAAL---LASGGKSDFHYGDDSLAFPPVKVDRV--LKDGDRVTLGgttLTAHLTPGHTRG 148
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 146-257 1.04e-04

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: 42.39  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 146 DVTLVALTHLHGDHIGGlmedgAPAFR---NARYVIGAAeydfwsntaregtpaeaghkavlanvAPLAEKATFIKDGAA 222
Cdd:cd07724   48 KITYVLETHVHADHVSG-----ARELAertGAPIVIGEG--------------------------APASFFDRLLKDGDV 96

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 190695778 223 VAPG---VTAMLAAGHSPGHMVFHAESEGkrMVLTGDT 257
Cdd:cd07724   97 LELGnltLEVLHTPGHTPESVSYLVGDPD--AVFTGDT 132
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 115-257 1.22e-04

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


Pssm-ID: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 42.15  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 115 ILVDTGfgaaGRARGLGKLAEGLKVAgyspedVTLVALTHLHGDHIGGLME----DGAPafrnaryVIGAAEYD-FWSNT 189
Cdd:cd07737   25 AVIDPG----GDADKILQAIEDLGLT------LKKILLTHGHLDHVGGAAElaehYGVP-------IIGPHKEDkFLLEN 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 190695778 190 AREgtPAEAGHKAVLANVAPlaekATFIKDGAAVAPGVTAMLAA---GHSPGHMVFHAESEgkRMVLTGDT 257
Cdd:cd07737   88 LPE--QSQMFGFPPAEAFTP----DRWLEEGDTVTVGNLTLEVLhcpGHTPGHVVFFNRES--KLAIVGDV 150
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 106-256 2.22e-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: 42.15  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 106 VLIDTGSD-LILVDTGfGAAGRARGLGKLAEGLKVAGYspEDVTLVALTHLHGDHIGGLmedgAPAFRNARyvIGAaeyd 184
Cdd:COG2333   14 ILIRTPDGkTILIDTG-PRPSFDAGERVVLPYLRALGI--RRLDLLVLTHPDADHIGGL----AAVLEAFP--VGR---- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 185 FWSNTAREGTPAeagHKAVLANVAPLAEKATFIKDGAAVA-PGVTA-MLAAGHSPGH--------MVFHAESEGKRMVLT 254
Cdd:COG2333   81 VLVSGPPDTSET---YERLLEALKEKGIPVRPCRAGDTWQlGGVRFeVLWPPEDLLEgsdennnsLVLRLTYGGFSFLLT 157


                 ..
gi 190695778 255 GD 256
Cdd:COG2333  158 GD 159
RNaseZ_ZiPD-like_MBL-fold cd07717
Ribonuclease Z, E. coli 3' tRNA-processing endonuclease ZiPD and related proteins; MBL-fold ...
 106-164 5.09e-04

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


Pssm-ID: 293803 [Multi-domain]  Cd Length: 247  Bit Score: 40.90  E-value: 5.09e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190695778 106 VLIDTGSDLILVDTGfgaagrarglgklaEG----LKVAGYSPEDVTLVALTHLHGDHIGGLM 164
Cdd:cd07717   20 IALRLEGELWLFDCG--------------EGtqrqLLRAGLSPSKIDRIFITHLHGDHILGLP 68
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 115-164 1.72e-03

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 38.83  E-value: 1.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 190695778  115 ILVDTGFGAAGRARGLGKLAEGLKvagyspEDVTLVALTHLHGDHIGGLM 164
Cdd:pfam12706   3 ILIDPGPDLRQQALPALQPGRLRD------DPIDAVLLTHDHYDHLAGLL 46
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 107-256 2.25e-03

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 39.40  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 107 LIDTGSDLILVDTGFGAAGRARGLGKLaeglkvaGYSPEDVTLVALTHLHGDHIGGLMEDGAPAFRNAryVIGAAE---- 182
Cdd:COG1236   18 LLETGGTRILIDCGLFQGGKERNWPPF-------PFRPSDVDAVVLTHAHLDHSGALPLLVKEGFRGP--IYATPAtadl 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 183 -----YDFWSNTAREG------TPAEAghKAVLANVAPLAEKATFikdgaaVAPGVTAMLA-AGHSPGHMVFHAESEGKR 250
Cdd:COG1236   89 arillGDSAKIQEEEAeaeplyTEEDA--ERALELFQTVDYGEPF------EIGGVRVTFHpAGHILGSAQVELEVGGKR 160


                 ....*.
gi 190695778 251 MVLTGD 256
Cdd:COG1236  161 IVFSGD 166
RNase_Z TIGR02651
ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of ...
 106-164 3.72e-03

ribonuclease Z; Processing of the 3-prime end of tRNA precursors may be the result of endonuclease or exonuclease activity, and differs in different species. Member of this family are ribonuclease Z, a tRNA 3-prime endonuclease that processes tRNAs to prepare for addition of CCA. In species where all tRNA sequences already have the CCA tail, such as E. coli, the need for such an enzyme is unclear. Protein similar to the E. coli enzyme, matched by TIGRFAMs model TIGR02649, are designated ribonuclease BN. [Transcription, RNA processing]


Pssm-ID: 274246 [Multi-domain]  Cd Length: 299  Bit Score: 38.35  E-value: 3.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190695778  106 VLIDTGSDLILVDTGfgaagrarglgklaEG----LKVAGYSPEDVTLVALTHLHGDHIGGLM 164
Cdd:TIGR02651  21 IALKLNGELWLFDCG--------------EGtqrqMLRSGISPMKIDRIFITHLHGDHILGLP 69
TaR3-like_MBL-fold cd07715
MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold ...
 106-163 5.94e-03

MBL-fold metallo-hydrolase domain of Myxococcus xanthus TaR3 and related proteins; MBL-fold metallo-hydrolase domain; Myxococcus xanthus Tar3 may function as an ammonium regulator/effector protein involved in biosynthesis of the antibiotic TA. Some are members of this subgroup are annotated as ribonucleases. 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: 293801 [Multi-domain]  Cd Length: 212  Bit Score: 37.48  E-value: 5.94e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 106 VLIDTGSDLILVDTGFGAagraRGLGK--LAEGlkvagySPEDVTLVaLTHLHGDHIGGL 163
Cdd:cd07715   26 VEVRAGGELLILDAGTGI----RELGNelMKEG------PPGEAHLL-LSHTHWDHIQGF 74
DdPDE5-like_MBL-fold cd07738
Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase ...
 137-165 7.38e-03

Dictyostelium discoideum phosphodiesterase 5 and related proteins; MBL-fold metallo hydrolase domain; Includes Dictyostelium discoideum cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase A (also known as cyclic GMP-binding protein A, phosphodiesterase 5, phosphodiesterase D, and PDE5) and cAMP/cGMP-dependent 3',5'-cAMP/cGMP phosphodiesterase B (also known as cyclic GMP-binding protein B, phosphodiesterase 6, phosphodiesterase E, and PDE6. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293824  Cd Length: 189  Bit Score: 36.89  E-value: 7.38e-03
                         10        20
                 ....*....|....*....|....*....
gi 190695778 137 LKVAGYSPEDVTLVALTHLHGDHIGGLME 165
Cdd:cd07738   39 LRQNGISPRLVDHVILTHCHADHDAGTFQ 67
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 101-174 8.53e-03

metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. Includes chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1.


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 36.88  E-value: 8.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190695778 101 NGyapVLIDTGSDLILVDTGFGAAGRARGLGKLAEGLKVagyspeDVTLVALTHLHGDHIGG---LMEDGAPAFRNA 174
Cdd:cd16285   27 NG---LIVIDGKGLVLIDTPWTEAQTATLLDWIEKKLGK------PVTAAISTHSHDDRTGGikaLNARGIPTYATA 94
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 102-258 9.65e-03

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: 36.27  E-value: 9.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 102 GYapvLIDTGSDLILVDTGFGAAGRargLGKLAEglkvagysPEDVTLVALTHLHGDHIGGLmedgaPAFRNARYVigaa 181
Cdd:cd07716   20 GY---LLEADGFRILLDCGSGVLSR---LQRYID--------PEDLDAVVLSHLHPDHCADL-----GVLQYARRY---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190695778 182 eydfwsntAREGTPAE-------AGHKAVLANVAPLAE--KATFIKDGAAVAPG---VTAMLAAGHSPGHMVfHAESEGK 249
Cdd:cd07716   77 --------HPRGARKPplplygpAGPAERLAALYGLEDvfDFHPIEPGEPLEIGpftITFFRTVHPVPCYAM-RIEDGGK 147


                 ....*....
gi 190695778 250 RMVLTGDTA 258
Cdd:cd07716  148 VLVYTGDTG 156
 
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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