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Conserved domains on  [gi|491558561|ref|WP_005416147|]
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MULTISPECIES: MBL fold metallo-hydrolase [Stenotrophomonas]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10888683)

uncharacterized member of the MBL fold metallo-hydrolase superfamily

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 1-263 2.76e-134

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: 380.30  E-value: 2.76e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561   1 MKLWSIRGNSQRLDGGAMFGNAPRALWEKWAAPDELNRIELACRALLASPlEGKTVLFETGIGAFFDPRMRERYgVQESQ 80
Cdd:cd16281    1 MQLHSIEGGYFKLDGGAMFGVVPKPLWQKWYPADEDNRITLAMRCLLIET-GGRNILIDTGIGDKQDPKFRSIY-VQHSE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  81 HVLIDSLREAGFEHEDIDVVVLSHLHFDHAGGLLAAWsEGREPELLFPNATYVVGAQHWQRAVRPHPRDRASFIPELPGL 160
Cdd:cd16281   79 HSLLKSLARLGLSPEDITDVILTHLHFDHCGGATRAD-DDGLVELLFPNATYWVQKRHWEWALNPNPRERASFLPENIEP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561 161 LQASGRLEVVEGEySKALGRSVRFSYSDGHTPGLMLAEIvghahagEDAHGGVVFCADLIPGRSWVHVPITMGYDRNAEL 240
Cdd:cd16281  158 LEESGRLKLIDGS-DAELGPGIRFHLSDGHTPGQMLPEI-------STPGGTVVFAADLIPTSAHIPLPWVMGYDRRPLL 229

                        250       260
                 ....*....|....*....|...
gi 491558561 241 LIDEKRQFLEDKLARNVRLFFTH 263
Cdd:cd16281  230 TIEEKERLLDEAVEEGGRLFFEH 252
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 1-263 2.76e-134

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: 380.30  E-value: 2.76e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561   1 MKLWSIRGNSQRLDGGAMFGNAPRALWEKWAAPDELNRIELACRALLASPlEGKTVLFETGIGAFFDPRMRERYgVQESQ 80
Cdd:cd16281    1 MQLHSIEGGYFKLDGGAMFGVVPKPLWQKWYPADEDNRITLAMRCLLIET-GGRNILIDTGIGDKQDPKFRSIY-VQHSE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  81 HVLIDSLREAGFEHEDIDVVVLSHLHFDHAGGLLAAWsEGREPELLFPNATYVVGAQHWQRAVRPHPRDRASFIPELPGL 160
Cdd:cd16281   79 HSLLKSLARLGLSPEDITDVILTHLHFDHCGGATRAD-DDGLVELLFPNATYWVQKRHWEWALNPNPRERASFLPENIEP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561 161 LQASGRLEVVEGEySKALGRSVRFSYSDGHTPGLMLAEIvghahagEDAHGGVVFCADLIPGRSWVHVPITMGYDRNAEL 240
Cdd:cd16281  158 LEESGRLKLIDGS-DAELGPGIRFHLSDGHTPGQMLPEI-------STPGGTVVFAADLIPTSAHIPLPWVMGYDRRPLL 229

                        250       260
                 ....*....|....*....|...
gi 491558561 241 LIDEKRQFLEDKLARNVRLFFTH 263
Cdd:cd16281  230 TIEEKERLLDEAVEEGGRLFFEH 252
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 30-277 1.71e-13

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: 68.18  E-value: 1.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  30 WAAPDELNRIELACRALLASPlEGKTVLFETGigafFDPRMRERygvqesqhvLIDSLREAGfehEDIDVVVLSHLHFDH 109
Cdd:COG0491    2 YVLPGGTPGAGLGVNSYLIVG-GDGAVLIDTG----LGPADAEA---------LLAALAALG---LDIKAVLLTHLHPDH 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561 110 AGGlLAAWSEGRepellfpNATYVVGAQHWQRAVRPHPRDRASFIPELPGLLqasgrleVVEGEYSKALGRSVRFSYSDG 189
Cdd:COG0491   65 VGG-LAALAEAF-------GAPVYAHAAEAEALEAPAAGALFGREPVPPDRT-------LEDGDTLELGGPGLEVIHTPG 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561 190 HTPGLMLAEIvghahagedAHGGVVFCADLIPGRSwvhVPITMGYDRNAELLIDEKRQFLEDKlarNVRLFFTHDPQVAL 269
Cdd:COG0491  130 HTPGHVSFYV---------PDEKVLFTGDALFSGG---VGRPDLPDGDLAQWLASLERLLALP---PDLVIPGHGPPTTA 194


                 ....*...
gi 491558561 270 AQLGRDDK 277
Cdd:COG0491  195 EAIDYLEE 202
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
52-263 1.10e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 59.69  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561   52 EGKTVLFETGIGAFFDprmrerygvqesqhvLIDSLREAGFEHEDIDVVVLSHLHFDHAGGLLAAWSEGREPELLFPNAT 131
Cdd:pfam00753  14 GGGAVLIDTGGSAEAA---------------LLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  132 YVVGAQHWQRAVRPHPRDRASFIPELPGLLQASGRLEVVEgeyskalGRSVRFSYSDGHTPGLMLAEIVGhahagedahG 211
Cdd:pfam00753  79 RELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGG-------GLGLLVTHGPGHGPGHVVVYYGG---------G 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 491558561  212 GVVFCADLIPGRSWVHVPITMG--YDRNAELLIDEKRQFLEDKLARNVRLFFTH 263
Cdd:pfam00753 143 KVLFTGDLLFAGEIGRLDLPLGglLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 52-252 8.52e-10

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: 56.79  E-value: 8.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561    52 EGKTVLFETGIGaffdprmrerygvqeSQHVLIDSLREAGfeHEDIDVVVLSHLHFDHAGGLlaawsegrePELL-FPNA 130
Cdd:smart00849   8 DGGAILIDTGPG---------------EAEDLLAELKKLG--PKKIDAIILTHGHPDHIGGL---------PELLeAPGA 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561   131 TYVVGAQHWQRAVRPHPRdrasFIPELPGLLQASGRLEVVEGEYSKALGRSVRFSYSDGHTPGLMLAEIVGhahagedah 210
Cdd:smart00849  62 PVYAPEGTAELLKDLLAL----LGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPE--------- 128

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 491558561   211 GGVVFCADLIPGRSWVHVPITMGYDRNAELLIDEKRQFLEDK 252
Cdd:smart00849 129 GKILFTGDLLFAGGDGRTLVDGGDAAASDALESLLKLLKLLP 170
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 1-263 2.76e-134

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: 380.30  E-value: 2.76e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561   1 MKLWSIRGNSQRLDGGAMFGNAPRALWEKWAAPDELNRIELACRALLASPlEGKTVLFETGIGAFFDPRMRERYgVQESQ 80
Cdd:cd16281    1 MQLHSIEGGYFKLDGGAMFGVVPKPLWQKWYPADEDNRITLAMRCLLIET-GGRNILIDTGIGDKQDPKFRSIY-VQHSE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  81 HVLIDSLREAGFEHEDIDVVVLSHLHFDHAGGLLAAWsEGREPELLFPNATYVVGAQHWQRAVRPHPRDRASFIPELPGL 160
Cdd:cd16281   79 HSLLKSLARLGLSPEDITDVILTHLHFDHCGGATRAD-DDGLVELLFPNATYWVQKRHWEWALNPNPRERASFLPENIEP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561 161 LQASGRLEVVEGEySKALGRSVRFSYSDGHTPGLMLAEIvghahagEDAHGGVVFCADLIPGRSWVHVPITMGYDRNAEL 240
Cdd:cd16281  158 LEESGRLKLIDGS-DAELGPGIRFHLSDGHTPGQMLPEI-------STPGGTVVFAADLIPTSAHIPLPWVMGYDRRPLL 229

                        250       260
                 ....*....|....*....|...
gi 491558561 241 LIDEKRQFLEDKLARNVRLFFTH 263
Cdd:cd16281  230 TIEEKERLLDEAVEEGGRLFFEH 252
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 1-263 1.60e-37

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: 133.15  E-value: 1.60e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561   1 MKLWSIRGNSQRLDGGAMFGNAPRALWEKWAAPDELNRIELACRALLASpLEGKTVLFETGIGaffDPRMRER----YGV 76
Cdd:cd07728    1 IKLTWLDGGVTHLDGGAMFGVVPKPLWSKKYPANEKNQIELRTDPILIQ-YQGKNYLIDAGIG---NGKLTEKqkrnFGV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  77 QESQHVlIDSLREAGFEHEDIDVVVLSHLHFDHAGGLLAAWSEGREPelLFPNATYVVGAQHWQRAVRPHPRDRASFIPE 156
Cdd:cd07728   77 TEESSI-EESLAELGLTPEDIDYVLMTHLHFDHASGLTKVKGEQLVS--VFPNATIYVSEIEWEEMRNPNIRSKNTYWKE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561 157 LPGLLQA-----SGRLEVVEGeyskalgrsVRFSYSDGHTPGLMLAEIvghAHAGEDAhggvVFCADLIPGRS-----WV 226
Cdd:cd07728  154 NWEPIEDqvktfSDEIEIVPG---------ITMIHTGGHSDGHSIIEI---EQGGETA----IHMADLMPTHAhqnplWV 217

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 491558561 227 hvpitMGYDRNAELLIDEKRQFLEDKLARNVRLFFTH 263
Cdd:cd07728  218 -----LAYDDYPMTSIEAKEKWLKEGIKNNYWFTFYH 249
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 53-265 1.51e-25

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: 101.52  E-value: 1.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  53 GKTVLFETGIGA-----FFDPRMRERYGVQESQHvLIDSLREAGFEHEDIDVVVLSHLHFDHAGGLlaawsegrepeLLF 127
Cdd:cd07729   41 EGTILVDTGFHPdaaddPGGLELAFPPGVTEEQT-LEEQLARLGLDPEDIDYVILSHLHFDHAGGL-----------DLF 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561 128 PNATYVVGAQHWQRAVRPHPRDRASFIPEL-PGLLQASGRLEVVEGEYskALGRSVRFSYSDGHTPGLMLAEIvghahag 206
Cdd:cd07729  109 PNATIIVQRAELEYATGPDPLAAGYYEDVLaLDDDLPGGRVRLVDGDY--DLFPGVTLIPTPGHTPGHQSVLV------- 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491558561 207 EDAHGGVVFCADLIPGR-SWVH-VPITMGYDRNAELL-IDEKRQFLEdklARNVRLFFTHDP 265
Cdd:cd07729  180 RLPEGTVLLAGDAAYTYeNLEEgRPPGINYDPEAALAsLERLKALAE---REGARVIPGHDP 238
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 52-263 1.06e-21

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 90.66  E-value: 1.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  52 EGKTVLFETGIGAFFDPRMRERYgvQESQHVLIDSLREAGFEHEDIDVVVLSHLHFDHAGGLLaAWSEGR-EPelLFPNA 130
Cdd:cd16277   21 PGRTILVDTGIGNDKPRPGPPAF--HNLNTPYLERLAAAGVRPEDVDYVLCTHLHVDHVGWNT-RLVDGRwVP--TFPNA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561 131 TYVVGAQ---HWQRAVRPHPRDRASFI-PELPglLQASGRLEVVEGEYSkaLGRSVRFSYSDGHTPGLMLAEIVghaHAG 206
Cdd:cd16277   96 RYLFSRAeydHWSSPDAGGPPNRGVFEdSVLP--VIEAGLADLVDDDHE--ILDGIRLEPTPGHTPGHVSVELE---SGG 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491558561 207 EDAhggvVFCADLIpgrswvHVPI-------TMGYDRNAELLIDEKRQFLEDKLARNVRLFFTH 263
Cdd:cd16277  169 ERA----LFTGDVM------HHPIqvarpdwSSVFDEDPAQAAATRRRLLERAADTDTLLFPAH 222
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 53-251 1.28e-19

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: 85.68  E-value: 1.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  53 GKTVLFETGIGAFFDPRMreryGVqesqhvLIDSLREAGFEHEDIDVVVLSHLHFDHAGGLLAAwsegrEPELLFPNATY 132
Cdd:cd07720   58 GRLILVDTGAGGLFGPTA----GK------LLANLAAAGIDPEDIDDVLLTHLHPDHIGGLVDA-----GGKPVFPNAEV 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561 133 VVGAQ---HWQRAvrphprDRASFIPEL--PGLLQASGRLEVVEGEYSKALGRSV----RFSYSDGHTPGLMLAEIvgha 203
Cdd:cd07720  123 HVSEAewdFWLDD------ANAAKAPEGakRFFDAARDRLRPYAAAGRFEDGDEVlpgiTAVPAPGHTPGHTGYRI---- 192

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491558561 204 hagEDAHGGVVFCADLipgrswVHVP--------ITMGYDRNAELLIDEKRQFLED 251
Cdd:cd07720  193 ---ESGGERLLIWGDI------VHHPalqfahpdWTIAFDVDPEQAAATRRRLLDR 239
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 52-156 1.31e-13

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: 68.83  E-value: 1.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  52 EGKTVLFETGIGAFFD---PRMRER-------YGVQESqhvLIDSLREAGFEHEDIDVVVLSHLHFDHAGGLlaawsegr 121
Cdd:cd07730   32 TGGKILFDLGYRKDFEeytPRVPERlyrtpvpLEVEED---VAEQLAAGGIDPEDIDAVILSHLHWDHIGGL-------- 100

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 491558561 122 epeLLFPNATYVVGAQHWQ--RAVRPHPRDRASFIPE 156
Cdd:cd07730  101 ---SDFPNARLIVGPGAKEalRPPGYPSGFLPELLPS 134
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 30-277 1.71e-13

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: 68.18  E-value: 1.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  30 WAAPDELNRIELACRALLASPlEGKTVLFETGigafFDPRMRERygvqesqhvLIDSLREAGfehEDIDVVVLSHLHFDH 109
Cdd:COG0491    2 YVLPGGTPGAGLGVNSYLIVG-GDGAVLIDTG----LGPADAEA---------LLAALAALG---LDIKAVLLTHLHPDH 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561 110 AGGlLAAWSEGRepellfpNATYVVGAQHWQRAVRPHPRDRASFIPELPGLLqasgrleVVEGEYSKALGRSVRFSYSDG 189
Cdd:COG0491   65 VGG-LAALAEAF-------GAPVYAHAAEAEALEAPAAGALFGREPVPPDRT-------LEDGDTLELGGPGLEVIHTPG 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561 190 HTPGLMLAEIvghahagedAHGGVVFCADLIPGRSwvhVPITMGYDRNAELLIDEKRQFLEDKlarNVRLFFTHDPQVAL 269
Cdd:COG0491  130 HTPGHVSFYV---------PDEKVLFTGDALFSGG---VGRPDLPDGDLAQWLASLERLLALP---PDLVIPGHGPPTTA 194


                 ....*...
gi 491558561 270 AQLGRDDK 277
Cdd:COG0491  195 EAIDYLEE 202
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 52-147 9.40e-11

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: 59.91  E-value: 9.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  52 EGKTVLFETGigaffDPRMRERygvqesqhvLIDSLREAGFEHEDIDVVVLSHLHFDHAGGLlaawsegrepeLLFPNAT 131
Cdd:cd07711   30 GGKNILVDTG-----TPWDRDL---------LLKALAEHGLSPEDIDYVVLTHGHPDHIGNL-----------NLFPNAT 84

                         90
                 ....*....|....*.
gi 491558561 132 YVVGAQHWQRAVRPHP 147
Cdd:cd07711   85 VIVGWDICGDSYDDHS 100
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
52-263 1.10e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 59.69  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561   52 EGKTVLFETGIGAFFDprmrerygvqesqhvLIDSLREAGFEHEDIDVVVLSHLHFDHAGGLLAAWSEGREPELLFPNAT 131
Cdd:pfam00753  14 GGGAVLIDTGGSAEAA---------------LLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  132 YVVGAQHWQRAVRPHPRDRASFIPELPGLLQASGRLEVVEgeyskalGRSVRFSYSDGHTPGLMLAEIVGhahagedahG 211
Cdd:pfam00753  79 RELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGG-------GLGLLVTHGPGHGPGHVVVYYGG---------G 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 491558561  212 GVVFCADLIPGRSWVHVPITMG--YDRNAELLIDEKRQFLEDKLARNVRLFFTH 263
Cdd:pfam00753 143 KVLFTGDLLFAGEIGRLDLPLGglLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 52-218 3.74e-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: 58.66  E-value: 3.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  52 EGKTVLFETGIGAFFDPrmrerygvqesqhvLIDSLREAGFEHEDIDVVVLSHLHFDHAGGllaAWsegrepELL--FPN 129
Cdd:cd07726   24 EGRPALIDTGPSSSVPR--------------LLAALEALGIAPEDVDYIILTHIHLDHAGG---AG------LLAeaLPN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561 130 ATYVV---GAQH-------WQRAVR------------PHPrdrasfIPElpgllqasGRLEVVEGEYSKALG-RSVRFSY 186
Cdd:cd07726   81 AKVYVhprGARHlidpsklWASARAvygdeadrlggeILP------VPE--------ERVIVLEDGETLDLGgRTLEVID 146

                        170       180       190
                 ....*....|....*....|....*....|..
gi 491558561 187 SDGHTPglmlaeivgHAHAGEDAHGGVVFCAD 218
Cdd:cd07726  147 TPGHAP---------HHLSFLDEESDGLFTGD 169
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 52-252 8.52e-10

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: 56.79  E-value: 8.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561    52 EGKTVLFETGIGaffdprmrerygvqeSQHVLIDSLREAGfeHEDIDVVVLSHLHFDHAGGLlaawsegrePELL-FPNA 130
Cdd:smart00849   8 DGGAILIDTGPG---------------EAEDLLAELKKLG--PKKIDAIILTHGHPDHIGGL---------PELLeAPGA 61

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561   131 TYVVGAQHWQRAVRPHPRdrasFIPELPGLLQASGRLEVVEGEYSKALGRSVRFSYSDGHTPGLMLAEIVGhahagedah 210
Cdd:smart00849  62 PVYAPEGTAELLKDLLAL----LGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLPE--------- 128

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 491558561   211 GGVVFCADLIPGRSWVHVPITMGYDRNAELLIDEKRQFLEDK 252
Cdd:smart00849 129 GKILFTGDLLFAGGDGRTLVDGGDAAASDALESLLKLLKLLP 170
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 82-263 1.33e-09

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: 56.53  E-value: 1.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  82 VLID-------SLREAGFEH-EDIDVVVLSHLHFDHAGGlLAAWSEGrepellfPNATYVVGAQHWQRAVRPHPRDRASF 153
Cdd:cd06262   23 ILIDpgagaleKILEAIEELgLKIKAILLTHGHFDHIGG-LAELKEA-------PGAPVYIHEADAELLEDPELNLAFFG 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561 154 IPELPGLLQAsgrLEVVEGEYSKALGRSVRFSYSDGHTPG---LMLAEivghahagedahGGVVFCADLIPGRSwvhVPI 230
Cdd:cd06262   95 GGPLPPPEPD---ILLEDGDTIELGGLELEVIHTPGHTPGsvcFYIEE------------EGVLFTGDTLFAGS---IGR 156

                        170       180       190
                 ....*....|....*....|....*....|...
gi 491558561 231 TMGYDRNAELLIDEKRQFLEdKLARNVRLFFTH 263
Cdd:cd06262  157 TDLPGGDPEQLIESIKKLLL-LLPDDTVVYPGH 188
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
52-115 6.14e-07

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 49.88  E-value: 6.14e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491558561  52 EGKTVLFETGigaffdprmrerygvqeSQHVLIDSLREAGFEHEDIDVVVLSHLHFDHAGGLLA 115
Cdd:COG1237   30 EGKRILFDTG-----------------QSDVLLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLPA 76
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 45-115 8.11e-07

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 49.09  E-value: 8.11e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491558561  45 ALLASPLEGKTVLFETGIGAFFDPrmrerygvqeSQHVLIDSLREAGFEHedIDVVVLSHLHFDHAGGLLA 115
Cdd:COG2333   13 AILIRTPDGKTILIDTGPRPSFDA----------GERVVLPYLRALGIRR--LDLLVLTHPDADHIGGLAA 71
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 80-125 8.82e-07

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: 48.28  E-value: 8.82e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491558561  80 QHVLID-------SLREAGFEHEDIDVVVLSHLHFDHAGGL----LAAWSEGREPEL 125
Cdd:cd07719   28 RVYLVDagsgvvrRLAQAGLPLGDLDAVFLTHLHSDHVADLpallLTAWLAGRKTPL 84
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 77-112 1.26e-06

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 48.74  E-value: 1.26e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 491558561  77 QESQHVLIDSLREAGFEHEDIDVVVLSHLHFDHAGG 112
Cdd:cd16280   42 NEAADLIVDGLEKLGLDPADIKYILITHGHGDHYGG 77
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 52-115 1.42e-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: 48.77  E-value: 1.42e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491558561  52 EGKTVLFETGIGAffdprmrerygvqesqhVLIDSLREAGFEHEDIDVVVLSHLHFDHAGGLLA 115
Cdd:cd07713   28 EGKKILFDTGQSG-----------------VLLHNAKKLGIDLSDIDAVVLSHGHYDHTGGLKA 74
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 87-218 2.57e-06

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


Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 47.62  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  87 LREAGFEHEDIDVVVLSHLHFDHAGGLLAawsegrepellFPNATYVVGAQHWQRAVRPHPRDRASFIPelpgLLQASGR 166
Cdd:cd07742   71 IEALGFDPSDVRHIVLTHLDLDHAGGLAD-----------FPHATVHVHAAELDAATSPRTRYERRRYR----PQQLAHG 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561 167 LEVVEGEYSKA--LG-RSVRfsYSDGHTPGLMLAEIVGH--AHAG---EDAHGGVVFCAD 218
Cdd:cd07742  136 PWWVTYAAGGErwFGfEAVR--PLDGLPPEILLVPLPGHtrGHCGvavRTGDRWLLHAGD 193
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 ...
 81-193 3.21e-06

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: 47.34  E-value: 3.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  81 HVLID------------SLREAGFEHEDIDVVVLSHLHFDHAGGL--LAAWSEGrepellfPNATYVVGAQHWQRAVRPH 146
Cdd:cd16290   33 LILIDgalpqsapqieaNIRALGFRLEDVKLILNSHAHFDHAGGIaaLQRDSGA-------TVAASPAGAAALRSGGVDP 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 491558561 147 PRDRASFIPELPgllqASGRLEVV-EGEYSKALGRSVRFSYSDGHTPG 193
Cdd:cd16290  106 DDPQAGAADPFP----PVAKVRVVaDGEVVKLGPLAVTAHATPGHTPG 149
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
78-125 3.51e-06

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 47.11  E-value: 3.51e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491558561  78 ESQHVLID-------SLREAGFEHEDIDVVVLSHLHFDHAGGL----LAAWSEGREPEL 125
Cdd:COG1234   27 GGERLLIDcgegtqrQLLRAGLDPRDIDAIFITHLHGDHIAGLpgllSTRSLAGREKPL 85
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 77-193 1.33e-05

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: 45.61  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  77 QESQHVLiDSLREAGFEHEDIDVVVLSHLHFDHAGGLLAAWSEgrepellfPNATYVVGAQHWQRAVRPHPRDRASFIPE 156
Cdd:cd07708   42 QNAPMIK-ANIKKLGFKFSDTKLILISHAHFDHAGGSAEIKKQ--------TGAKVMAGAEDVSLLLSGGSSDFHYANDS 112

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 491558561 157 LPGLLQASGRLEVVEGEYSKALGRSVRFSYSDGHTPG 193
Cdd:cd07708  113 STYFPQSTVDRAVHDGERVTLGGTVLTAHATPGHTPG 149
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 78-193 2.70e-05

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


Pssm-ID: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 44.59  E-value: 2.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  78 ESQHVLIDSLREAGFEHEDIDVVVLSHLHFDHAGGLLAAWSEGrepellfpNATYVV---GAQHWQRAV--RPHPRDRAS 152
Cdd:cd16312   42 QSAPLIIANIEALGFRIEDVKLILNSHAHWDHAGGIAALQKAS--------GATVAAsahGAQVLQSGTngKDDPQYQAK 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 491558561 153 FIPELPGLLQASgrlEVVEGEYSKALGRSVRFSYSDGHTPG 193
Cdd:cd16312  114 PVVHVAKVAKVK---EVGEGDTLKVGPLRLTAHMTPGHTPG 151
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 81-115 3.29e-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: 44.26  E-value: 3.29e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 491558561  81 HVLIDS------------LREAGFEHEDIDVVVLSHLHFDHAGGLLA 115
Cdd:cd16315   33 HVLIDSgteeaaplvlanIRKLGFDPKDVRWLLSSHEHFDHVGGLAA 79
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 51-115 3.89e-05

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 43.28  E-value: 3.89e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491558561  51 LEGKTVLFETGigaffdprmrERYGVQESqhVLIDSLREAGFEHedIDVVVLSHLHFDHAGGLLA 115
Cdd:cd07731   17 TPGKTILIDTG----------PRDSFGED--VVVPYLKARGIKK--LDYLILTHPDADHIGGLDA 67
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 81-193 7.68e-05

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: 43.31  E-value: 7.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  81 HVLID------------SLREAGFEHEDIDVVVLSHLHFDHAGGLLAAWSegrepellFPNATYVVGAQHWQ--RAVRPH 146
Cdd:cd16313   33 HILIDggfpkspeqiaaSIRQLGFKLEDVKYILSSHDHWDHAGGIAALQK--------LTGAQVLASPATVAvlRSGSMG 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491558561 147 PRDrasfiPELPGLLQ----ASGRlEVVEGEYSKALGRSVRFSYSDGHTPG 193
Cdd:cd16313  105 KDD-----PQFGGLTPmppvASVR-AVRDGEVVKLGPLAVTAHATPGHTTG 149
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 78-125 9.78e-05

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


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 42.25  E-value: 9.78e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491558561  78 ESQHVLID-------SLREAGFEHEDIDVVVLSHLHFDHAGGL----LAAWSEGREPEL 125
Cdd:cd16272   25 GGTRILLDcgegtvyRLLKAGVDPDKLDAIFLSHFHLDHIGGLptllFARRYGGRKKPL 83
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 52-113 1.05e-04

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 42.21  E-value: 1.05e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491558561  52 EGKTVLFETGIgaffdPRMRERygvqesqhvLIDSLREAGFEHEDIDVVVLSHLHFDHAGGL 113
Cdd:cd07721   19 DDGLTLIDTGL-----PGSAKR---------ILKALRELGLSPKDIRRILLTHGHIDHIGSL 66
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 81-113 1.70e-04

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: 42.19  E-value: 1.70e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 491558561  81 HVLID------------SLREAGFEHEDIDVVVLSHLHFDHAGGL 113
Cdd:cd16314   33 HILIDggtdkaaplieaNIRALGFRPEDVRYIVSSHEHFDHAGGI 77
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 75-113 3.02e-04

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


Pssm-ID: 293869  Cd Length: 257  Bit Score: 41.51  E-value: 3.02e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 491558561  75 GVQESQHVLIDSLREAGFEHEDIDVVVLSHLHFDHAGGL 113
Cdd:cd16311   39 GLPESAPKIIANIEALGFRIEDVKLILNSHGHIDHAGGL 77
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 75-118 5.75e-04

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: 40.77  E-value: 5.75e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 491558561  75 GVQESQHVLIDSLREAGFEHEDIDVVVLSHLHFDHAGGL--LAAWS 118
Cdd:cd16288   39 GLESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLaaLKKLT 84
NorV COG0426
Flavorubredoxin [Energy production and conversion];
53-184 6.69e-04

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 40.97  E-value: 6.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  53 GKTVLFETGIGAFFDPrmrerygvqesqhvLIDSLREAgFEHEDIDVVVLSHLHFDHAGGLlaawsegrePELL--FPNA 130
Cdd:COG0426   42 EKTALIDTVGESFFEE--------------FLENLSKV-IDPKKIDYIIVNHQEPDHSGSL---------PELLelAPNA 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491558561 131 TyVVGAQHWQRavrphprdrasFIPELPGllQASGRLEVVEGEYSKALG-RSVRF 184
Cdd:COG0426   98 K-IVCSKKAAR-----------FLPHFYG--IPDFRFIVVKEGDTLDLGgHTLQF 138
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 79-113 1.19e-03

Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of Mbl1b-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293868  Cd Length: 252  Bit Score: 39.74  E-value: 1.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 491558561  79 SQHVLIDSLREA------------GFEHEDIDVVVLSHLHFDHAGGL 113
Cdd:cd16310   31 HGAILLDGGLEEnaalieqnikalGFKLSDIKIIINTHAHYDHAGGL 77
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 60-113 1.54e-03

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: 39.39  E-value: 1.54e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491558561  60 TGIGAFFdprmrerygVQESQ-HVLID------------SLREAGFEHEDIDVVVLSHLHFDHAGGL 113
Cdd:cd16309   20 AGLGVFL---------ITTPEgHILIDgampqstplikdNIKKLGFDVKDVKYLLNTHAHFDHAGGL 77
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 88-113 4.29e-03

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


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 37.44  E-value: 4.29e-03
                         10        20
                 ....*....|....*....|....*.
gi 491558561  88 REAGFEHEDIDVVVLSHLHFDHAGGL 113
Cdd:cd16295   43 EPFPFDPKEIDAVILTHAHLDHSGRL 68
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 78-114 5.27e-03

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 37.57  E-value: 5.27e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 491558561  78 ESQHVLID---SLRE----AGFEHEDIDVVVLSHLHFDHAGGLL 114
Cdd:COG1235   43 DGTRLLIDagpDLREqllrLGLDPSKIDAILLTHEHADHIAGLD 86
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 78-113 5.55e-03

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 37.24  E-value: 5.55e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 491558561  78 ESQHVLID-------SLREAGFEHEDIDVVVLSHLHFDHAGGL 113
Cdd:cd07740   24 EAGRFLIDcgassliALKRAGIDPNAIDAIFITHLHGDHFGGL 66
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 94-114 6.31e-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: 36.90  E-value: 6.31e-03
                          10        20
                  ....*....|....*....|.
gi 491558561   94 HEDIDVVVLSHLHFDHAGGLL 114
Cdd:pfam12706  26 DDPIDAVLLTHDHYDHLAGLL 46
RNaseZ_ELAC1_ELAC2-C-term-like_MBL-fold cd07718
Ribonuclease Z ELAC1, C-terminus of ELAC2, and related proteins; MBL-fold metallo-hydrolase ...
 70-135 8.38e-03

Ribonuclease Z ELAC1, C-terminus of ELAC2, 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. 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 eukaryotic subgroup includes short forms (ELAC1) and the C-terminus of long forms including human ELAC2. 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: 293804 [Multi-domain]  Cd Length: 204  Bit Score: 36.76  E-value: 8.38e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491558561  70 MRERYGVQESQHVLIDslreagfehedIDVVVLSHLHFDHAGGL---LAAWSEGREPEllfPNATYVVG 135
Cdd:cd07718   42 LRRHYGPEEADEVLRN-----------LKCIFISHLHADHHLGLirlLAERKKLFKPP---SPPLYVVA 96
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 53-144 8.83e-03

catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold metallo-hydrolase domain; FDPs catalyze the reduction of oxygen and/or nitric oxide to water or nitrous oxide respectively. In addition to this N-terminal catalytic domain they contain a C-terminal flavin mononucleotide-binding flavodoxin-like domain. Although some FDPs are able to reduce NO or O2 with similar catalytic efficiencies others are selective for either NO or O2, such as Escherichia coli flavorubredoxin which is selective toward NO and G. intestinalis FDP which is selective toward O2. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. Some members of this subgroup are single domain.


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 36.70  E-value: 8.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491558561  53 GKTVLFETGIGAFFDprmrerygvqesqhVLIDSLREAgFEHEDIDVVVLSHLHFDHAGGLlaawsegrePELL--FPNA 130
Cdd:cd07709   40 EKTALIDTVKEPFFD--------------EFLENLEEV-IDPRKIDYIVVNHQEPDHSGSL---------PELLelAPNA 95

                         90
                 ....*....|....
gi 491558561 131 TyVVGAQHWQRAVR 144
Cdd:cd07709   96 K-IVCSKKAARFLK 108
 
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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