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Conserved domains on  [gi|1207571770|ref|WP_087956320|]
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MULTISPECIES: MBL fold metallo-hydrolase [Bacillus]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10888708)

MBL fold metallo-hydrolase similar to outer membrane protein RomA from Bacillus and Enterobacter

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 60-236 2.75e-103

Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. 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: 293841  Cd Length: 181  Bit Score: 300.35  E-value: 2.75e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770  60 WIGHSTFLIQTNGLNILTDPVWATKLKLVP-----RLTEPGLSIQELPKIDIVLISHGHYDHLDFSTLRQLNDDVLYLVP 134
Cdd:cd16283     1 WIGHATFLIQIEGLNILTDPVFSERASPVSfggpkRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPPYLVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770 135 IGLKKLFTRKKFTHVEEYNWWENTTVSDVSIHFVPAQHWTRRSLFDMNTSHWGGWIInnETTKETIYFCGDSGYFQGFKE 214
Cdd:cd16283    81 LGLKKWFLKKGITNVVELDWWQSTEIGGVRITFVPAQHWSRRTLFDTNESLWGGWVI--EGEGFRIYFAGDTGYFPGFRE 158

                         170       180
                  ....*....|....*....|...
gi 1207571770 215 IGKRFS-IDIALMPIGAYEPEWF 236
Cdd:cd16283   159 IGRRFGpIDLALLPIGAYEPRWF 181
 
Name Accession Description Interval E-value
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 60-236 2.75e-103

Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. 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: 293841  Cd Length: 181  Bit Score: 300.35  E-value: 2.75e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770  60 WIGHSTFLIQTNGLNILTDPVWATKLKLVP-----RLTEPGLSIQELPKIDIVLISHGHYDHLDFSTLRQLNDDVLYLVP 134
Cdd:cd16283     1 WIGHATFLIQIEGLNILTDPVFSERASPVSfggpkRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPPYLVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770 135 IGLKKLFTRKKFTHVEEYNWWENTTVSDVSIHFVPAQHWTRRSLFDMNTSHWGGWIInnETTKETIYFCGDSGYFQGFKE 214
Cdd:cd16283    81 LGLKKWFLKKGITNVVELDWWQSTEIGGVRITFVPAQHWSRRTLFDTNESLWGGWVI--EGEGFRIYFAGDTGYFPGFRE 158

                         170       180
                  ....*....|....*....|...
gi 1207571770 215 IGKRFS-IDIALMPIGAYEPEWF 236
Cdd:cd16283   159 IGRRFGpIDLALLPIGAYEPRWF 181
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 57-281 9.29e-86

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 257.15  E-value: 9.29e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770  57 TVTWIGHSTFLIQTNGLNILTDPVWATKLKLVPrltEPGLSIQELPKIDIVLISHGHYDHLDFSTLRQL-NDDVLYLVPI 135
Cdd:COG2220     5 KITWLGHATFLIETGGKRILIDPVFSGRASPVN---PLPLDPEDLPKIDAVLVTHDHYDHLDDATLRALkRTGATVVAPL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770 136 GLKKLFTRKKFTHVEEYNWWENTTVSDVSIHFVPAQHWTRRslFDMNTSHWGGWIInnETTKETIYFCGDSGYFQGFKEI 215
Cdd:COG2220    82 GVAAWLRAWGFPRVTELDWGESVELGGLTVTAVPARHSSGR--PDRNGGLWVGFVI--ETDGKTIYHAGDTGYFPEMKEI 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207571770 216 GKRFSIDIALMPIGAYEpewfmkiSHVSPEEAVQAYLDLNATHFIPMHYGAFALADETPREAVTRL 281
Cdd:COG2220   158 GERFPIDVALLPIGAYP-------FTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDEDPLERFAAA 216
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 74-264 1.93e-42

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: 145.53  E-value: 1.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770  74 NILTDPVWATkLKLVPRLTEPGLSIQElpKIDIVLISHGHYDHL-DFSTLRQLNDDVLYL---VPIGLKKLF-----TRK 144
Cdd:pfam12706   2 RILIDPGPDL-RQQALPALQPGRLRDD--PIDAVLLTHDHYDHLaGLLDLREGRPRPLYAplgVLAHLRRNFpylflLEH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770 145 KFTHVEEYNWWENTTV--SDVSIHFVPAQHWTRRsLFDMNTSHWGGWIInnETTKETIYFCGDSGYFQGfkEIGKRFS-I 221
Cdd:pfam12706  79 YGVRVHEIDWGESFTVgdGGLTVTATPARHGSPR-GLDPNPGDTLGFRI--EGPGKRVYYAGDTGYFPD--EIGERLGgA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1207571770 222 DIALMPIGAYEPEWFMKISHVSPEEAVQAYLDLNATHFIPMHY 264
Cdd:pfam12706 154 DLLLLDGGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 58-276 5.63e-27

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 105.66  E-value: 5.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770  58 VTWIGHSTFLIQTNGLNILTDPvWATKLKLVPrltepgLSIQELpKIDIVLISHGHYDHL-DFSTLRQlNDDVLYLVPIG 136
Cdd:PRK00685    3 ITWLGHSAFLIETGGKKILIDP-FITGNPLAD------LKPEDV-KVDYILLTHGHGDHLgDTVEIAK-RTGATVIANAE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770 137 LKKLFTRKKFTHVEEYNWWENTTVSDVSIHFVPAQHWTrrSLFDMNTSHWG----GWIInnETTKETIYFCGDSGYFQGF 212
Cdd:PRK00685   74 LANYLSEKGVEKTHPMNIGGTVEFDGGKVKLTPALHSS--SFIDEDGITYLgnptGFVI--TFEGKTIYHAGDTGLFSDM 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207571770 213 KEIGKRFSIDIALMPIGayepEWF-MkishvSPEEAVQAYLDLNATHFIPMHYGAFALADETPRE 276
Cdd:PRK00685  150 KLIGELHKPDVALLPIG----DNFtM-----GPEDAALAVELIKPKIVIPMHYNTFPLIEQDPEK 205
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 64-244 2.16e-07

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: 50.24  E-value: 2.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770   64 STFLIQTNGLNILTDPVWATKLKLVPRLTEPGLSiqelpKIDIVLISHGHYDHldFSTLRqlnddvlylvpiGLKKLFTR 143
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPK-----KIDAIILTHGHPDH--IGGLP------------ELLEAPGA 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770  144 KKFTHVEEYNWWENTTVSDVSIHFVPAQHWTRRSL----------FDMNTSHWGGWIINN---ETTKETIYFCGDSGYFQ 210
Cdd:smart00849  62 PVYAPEGTAELLKDLLALLGELGAEAEPAPPDRTLkdgdeldlggGELEVIHTPGHTPGSivlYLPEGKILFTGDLLFAG 141

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1207571770  211 GFKEIGKRFSIDIALMPIGAYEPEWFMKISHVSP 244
Cdd:smart00849 142 GDGRTLVDGGDAAASDALESLLKLLKLLPKLVVP 175
 
Name Accession Description Interval E-value
RomA-like_MBL-fold cd16283
Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; ...
 60-236 2.75e-103

Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain; Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. 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: 293841  Cd Length: 181  Bit Score: 300.35  E-value: 2.75e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770  60 WIGHSTFLIQTNGLNILTDPVWATKLKLVP-----RLTEPGLSIQELPKIDIVLISHGHYDHLDFSTLRQLNDDVLYLVP 134
Cdd:cd16283     1 WIGHATFLIQIEGLNILTDPVFSERASPVSfggpkRLTPPGLPLEELPPIDAVLISHNHYDHLDLPTVKRLGGRPPYLVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770 135 IGLKKLFTRKKFTHVEEYNWWENTTVSDVSIHFVPAQHWTRRSLFDMNTSHWGGWIInnETTKETIYFCGDSGYFQGFKE 214
Cdd:cd16283    81 LGLKKWFLKKGITNVVELDWWQSTEIGGVRITFVPAQHWSRRTLFDTNESLWGGWVI--EGEGFRIYFAGDTGYFPGFRE 158

                         170       180
                  ....*....|....*....|...
gi 1207571770 215 IGKRFS-IDIALMPIGAYEPEWF 236
Cdd:cd16283   159 IGRRFGpIDLALLPIGAYEPRWF 181
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 57-281 9.29e-86

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 257.15  E-value: 9.29e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770  57 TVTWIGHSTFLIQTNGLNILTDPVWATKLKLVPrltEPGLSIQELPKIDIVLISHGHYDHLDFSTLRQL-NDDVLYLVPI 135
Cdd:COG2220     5 KITWLGHATFLIETGGKRILIDPVFSGRASPVN---PLPLDPEDLPKIDAVLVTHDHYDHLDDATLRALkRTGATVVAPL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770 136 GLKKLFTRKKFTHVEEYNWWENTTVSDVSIHFVPAQHWTRRslFDMNTSHWGGWIInnETTKETIYFCGDSGYFQGFKEI 215
Cdd:COG2220    82 GVAAWLRAWGFPRVTELDWGESVELGGLTVTAVPARHSSGR--PDRNGGLWVGFVI--ETDGKTIYHAGDTGYFPEMKEI 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207571770 216 GKRFSIDIALMPIGAYEpewfmkiSHVSPEEAVQAYLDLNATHFIPMHYGAFALADETPREAVTRL 281
Cdd:COG2220   158 GERFPIDVALLPIGAYP-------FTMGPEEAAEAARDLKPKVVIPIHYGTFPLLDEDPLERFAAA 216
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 74-264 1.93e-42

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: 145.53  E-value: 1.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770  74 NILTDPVWATkLKLVPRLTEPGLSIQElpKIDIVLISHGHYDHL-DFSTLRQLNDDVLYL---VPIGLKKLF-----TRK 144
Cdd:pfam12706   2 RILIDPGPDL-RQQALPALQPGRLRDD--PIDAVLLTHDHYDHLaGLLDLREGRPRPLYAplgVLAHLRRNFpylflLEH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770 145 KFTHVEEYNWWENTTV--SDVSIHFVPAQHWTRRsLFDMNTSHWGGWIInnETTKETIYFCGDSGYFQGfkEIGKRFS-I 221
Cdd:pfam12706  79 YGVRVHEIDWGESFTVgdGGLTVTATPARHGSPR-GLDPNPGDTLGFRI--EGPGKRVYYAGDTGYFPD--EIGERLGgA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1207571770 222 DIALMPIGAYEPEWFMKISHVSPEEAVQAYLDLNATHFIPMHY 264
Cdd:pfam12706 154 DLLLLDGGAWRDDEMIHMGHMTPEEAVEAAADLGARRKVLIHI 196
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 58-276 5.63e-27

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 105.66  E-value: 5.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770  58 VTWIGHSTFLIQTNGLNILTDPvWATKLKLVPrltepgLSIQELpKIDIVLISHGHYDHL-DFSTLRQlNDDVLYLVPIG 136
Cdd:PRK00685    3 ITWLGHSAFLIETGGKKILIDP-FITGNPLAD------LKPEDV-KVDYILLTHGHGDHLgDTVEIAK-RTGATVIANAE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770 137 LKKLFTRKKFTHVEEYNWWENTTVSDVSIHFVPAQHWTrrSLFDMNTSHWG----GWIInnETTKETIYFCGDSGYFQGF 212
Cdd:PRK00685   74 LANYLSEKGVEKTHPMNIGGTVEFDGGKVKLTPALHSS--SFIDEDGITYLgnptGFVI--TFEGKTIYHAGDTGLFSDM 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207571770 213 KEIGKRFSIDIALMPIGayepEWF-MkishvSPEEAVQAYLDLNATHFIPMHYGAFALADETPRE 276
Cdd:PRK00685  150 KLIGELHKPDVALLPIG----DNFtM-----GPEDAALAVELIKPKIVIPMHYNTFPLIEQDPEK 205
Lactamase_B_3 pfam13483
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 57-263 3.80e-21

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


Pssm-ID: 433247 [Multi-domain]  Cd Length: 160  Bit Score: 88.03  E-value: 3.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770  57 TVTWIGHSTFLIQTNGLNILTDPVWATKLKLVPRLTepglsiqelpkIDIVLISHGHYDHLDFSTLRQlnddvlylvpig 136
Cdd:pfam13483   1 EITWLGHSSFLIEGGGARILTDPFRATVGYRPPPVT-----------ADLVLISHGHDDHGHPETLPG------------ 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770 137 lkklftrkKFTHVEEynwWENTTVSDVSIHFVPAQHWtrrslfdmntSHWGGWIINN-----ETTKETIYFCGDSGY--- 208
Cdd:pfam13483  58 --------NPHVLDG---GGSYTVGGLEIRGVPTDHD----------RVGGRRRGGNsiflfEQDGLTIYHLGHLGHpls 116

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207571770 209 FQGFKEIGkrfSIDIALMPIGAyePEWfmkishVSPEEAVQAYLDLNATHFIPMH 263
Cdd:pfam13483 117 DEQLAELG---RVDVLLIPVGG--PLT------YGAEEALELAKRLRPRVVIPMH 160
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 64-244 2.16e-07

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: 50.24  E-value: 2.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770   64 STFLIQTNGLNILTDPVWATKLKLVPRLTEPGLSiqelpKIDIVLISHGHYDHldFSTLRqlnddvlylvpiGLKKLFTR 143
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAELKKLGPK-----KIDAIILTHGHPDH--IGGLP------------ELLEAPGA 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770  144 KKFTHVEEYNWWENTTVSDVSIHFVPAQHWTRRSL----------FDMNTSHWGGWIINN---ETTKETIYFCGDSGYFQ 210
Cdd:smart00849  62 PVYAPEGTAELLKDLLALLGELGAEAEPAPPDRTLkdgdeldlggGELEVIHTPGHTPGSivlYLPEGKILFTGDLLFAG 141

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1207571770  211 GFKEIGKRFSIDIALMPIGAYEPEWFMKISHVSP 244
Cdd:smart00849 142 GDGRTLVDGGDAAASDALESLLKLLKLLPKLVVP 175
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
58-147 3.91e-07

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 49.67  E-value: 3.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770  58 VTWIGHSTFLIQTNGLNILTDPVWATKLKLVPRLTEPGLsiqELPKIDIVLISHGHYDHL-DFSTLRQLNDDVLYLVPIG 136
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGL---GPKDIDAVILTHGHFDHIgGLGELAEATDVPVIVVAEE 77

                          90
                  ....*....|.
gi 1207571770 137 LKKLFTRKKFT 147
Cdd:pfam00753  78 ARELLDEELGL 88
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
62-272 1.11e-06

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 49.04  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770  62 GHSTFLIQTNGLNILTDPVWATklklVPRLTEPGLSIQelpKIDIVLISHGHYDH-LDFSTLRQL-----NDDVLYLV-P 134
Cdd:COG1234    18 ATSSYLLEAGGERLLIDCGEGT----QRQLLRAGLDPR---DIDAIFITHLHGDHiAGLPGLLSTrslagREKPLTIYgP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770 135 IGLKKLFTRkkftHVEEYNWWEN-------------TTVSDVSIHFVPAQHwTRRSLfdmntshwgGWIInnETTKETIY 201
Cdd:COG1234    91 PGTKEFLEA----LLKASGTDLDfplefheiepgevFEIGGFTVTAFPLDH-PVPAY---------GYRF--EEPGRSLV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770 202 FCGDSGYFQGFKEIGKrfsiDIALMPIGAY----EPEWFMKISHVSPEEAVQAYLDLNA-----THFIPMHYGAFALADE 272
Cdd:COG1234   155 YSGDTRPCEALVELAK----GADLLIHEATfldeEAELAKETGHSTAKEAAELAAEAGVkrlvlTHFSPRYDDPEELLAE 230
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 64-116 5.13e-06

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: 46.42  E-value: 5.13e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1207571770  64 STFLIQTNGLNILTDP--VWATKLkLVPRLTEPGLSiqeLPKIDIVLISHGHYDH 116
Cdd:cd07711    23 TVTLIKDGGKNILVDTgtPWDRDL-LLKALAEHGLS---PEDIDYVVLTHGHPDH 73
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 66-168 6.07e-05

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: 43.76  E-value: 6.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770  66 FLIQTNGLNILTD----PVW---ATKLKLVPRltepglsiqelpKIDIVLISHGHYDHLD-FSTLRQLNDDV-LYLVPIG 136
Cdd:cd07713    23 LLIETEGKKILFDtgqsGVLlhnAKKLGIDLS------------DIDAVVLSHGHYDHTGgLKALLELNPKApVYAHPDA 90

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1207571770 137 LKKLFTRKKFTHVEEYNWWENTTVSDVSIHFV 168
Cdd:cd07713    91 FEPRYSKRGGGKKGIGIGREELEKAGARLVLV 122
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 67-116 1.23e-04

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 42.12  E-value: 1.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1207571770  67 LIQTNGLNILTD--PVWAT-KLKLVPRLTEPGLSiqelpKIDIVLISHGHYDH 116
Cdd:cd07731    14 LIQTPGKTILIDtgPRDSFgEDVVVPYLKARGIK-----KLDYLILTHPDADH 61
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 66-263 1.83e-04

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 42.19  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770  66 FLIQTNGLNILTDpvwATklklvprltePGLSIQEL------PKIDIVLISHGHYDH---LDF----------------S 120
Cdd:COG1235    38 ILVEADGTRLLID---AG----------PDLREQLLrlgldpSKIDAILLTHEHADHiagLDDlrprygpnpipvyatpG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770 121 TLRQLNDDVLYLVPIGLKKLftrkKFTHVEEYnwwENTTVSDVSIHFVPAQHWTRRSLfdmntshwgGWIInnETTKETI 200
Cdd:COG1235   105 TLEALERRFPYLFAPYPGKL----EFHEIEPG---EPFEIGGLTVTPFPVPHDAGDPV---------GYRI--EDGGKKL 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207571770 201 YFCGDSGYFqgFKEIGKRFS-IDIALmpIGA--YEPEWfmkiSHVSPEEAVQAYLDLNATHFIPMH 263
Cdd:COG1235   167 AYATDTGYI--PEEVLELLRgADLLI--LDAtyDDPEP----GHLSNEEALELLARLGPKRLVLTH 224
COG2248 COG2248
Predicted hydrolase, metallo-beta-lactamase superfamily [General function prediction only];
64-118 2.96e-04

Predicted hydrolase, metallo-beta-lactamase superfamily [General function prediction only];


Pssm-ID: 441849  Cd Length: 300  Bit Score: 41.85  E-value: 2.96e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207571770  64 STFlIQTNGLNILTDPVWAtklkLVP-------------RLTEPGLSIQELP-KIDIVLISHGHYDHLD 118
Cdd:COG2248    17 ATF-VETKDVRILIDPGVS----LAPrryglpphpreleRLEELREEIQEYAkKADIIIITHYHYDHHD 80
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 66-116 3.53e-04

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


Pssm-ID: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 41.02  E-value: 3.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207571770  66 FLIQTNGLNILTDP-----VWATKLKLVPRltepglsiqelpKIDIVLISHGHYDH 116
Cdd:cd07741    23 IWIELNGKNIHIDPgpgalVRMCRPKLDPT------------KLDAIILSHRHLDH 66
RNaseZ_short-form-like_MBL-fold cd07716
uncharacterized bacterial subgroup of Ribonuclease Z, short form; MBL-fold metallo-hydrolase ...
 64-123 1.51e-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: 38.96  E-value: 1.51e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207571770  64 STFLIQTNGLNILTDPVWATklklVPRLtepgLSIQELPKIDIVLISHGHYDH-LDFSTLR 123
Cdd:cd07716    19 SGYLLEADGFRILLDCGSGV----LSRL----QRYIDPEDLDAVVLSHLHPDHcADLGVLQ 71
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 36-116 1.56e-03

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: 39.45  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770  36 FLVEQSPVKQSKFLQNNFEKTTVTWiGHSTFLIQTNGLNILTD----PVWATKL-KLVPRLTEPGLSiqelPK-IDIVLI 109
Cdd:cd07720    23 LLGGAAPEAEAALLAAFLPPDPVET-SVNAFLVRTGGRLILVDtgagGLFGPTAgKLLANLAAAGID----PEdIDDVLL 97


                  ....*..
gi 1207571770 110 SHGHYDH 116
Cdd:cd07720    98 THLHPDH 104
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 62-217 1.59e-03

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: 38.78  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770  62 GHSTFLIQTNGLNILTDPVWATklklVPRLTEPGLSIQelpKIDIVLISHGHYDH-LDFSTL-----RQLNDDVLYL-VP 134
Cdd:cd16272    16 NTSSYLLETGGTRILLDCGEGT----VYRLLKAGVDPD---KLDAIFLSHFHLDHiGGLPTLlfarrYGGRKKPLTIyGP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207571770 135 IGLKKLFTRkkfthVEEYNWWENTTVSDVSIHFVPAQHWTRR------SLFDMNtsHWG---GWIINNETTkeTIYFCGD 205
Cdd:cd16272    89 KGIKEFLEK-----LLNFPVEILPLGFPLEIEELEEGGEVLElgdlkvEAFPVK--HSVeslGYRIEAEGK--SIVYSGD 159

                         170
                  ....*....|..
gi 1207571770 206 SGYFQGFKEIGK 217
Cdd:cd16272   160 TGPCENLVELAK 171
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
66-116 1.73e-03

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 39.48  E-value: 1.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1207571770  66 FLIQTNGLNILTD----PVW---ATKLKLvprltepglsiqELPKIDIVLISHGHYDH 116
Cdd:COG1237    25 ALIETEGKRILFDtgqsDVLlknAEKLGI------------DLSDIDAVVLSHGHYDH 70
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 56-116 2.10e-03

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: 38.90  E-value: 2.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207571770  56 TTVTWIGHSTFLIQTNGLNILTDPVWATKL--KLVPRLTEPGLsiqelpKIDIVLISHGHYDH 116
Cdd:COG0491     8 TPGAGLGVNSYLIVGGDGAVLIDTGLGPADaeALLAALAALGL------DIKAVLLTHLHPDH 64
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 61-116 7.31e-03

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 37.86  E-value: 7.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1207571770  61 IGHSTFLIQTNGLNILTDPVWATKLKLVPRLTEPglsiQELPKIDIVLISHGHYDH 116
Cdd:COG1236    12 VTGSCYLLETGGTRILIDCGLFQGGKERNWPPFP----FRPSDVDAVVLTHAHLDH 63
 
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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