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Conserved domains on  [gi|115497922|ref|NP_001068680|]
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metallo-beta-lactamase domain-containing protein 1 [Bos taurus]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10869770)

MBL fold metallo-hydrolase similar to uncharacterized human metallo-beta-lactamase domain-containing protein 1 (MBLAC1 )

Gene Ontology:  GO:0016787
PubMed:  17597585

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 24-238 1.58e-70

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: 215.14  E-value: 1.58e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  24 SVVVLLQGYAEPEGvGDAVRADGSVTLVlpqawgpasshrepqpyeaktaleeaaRGP---ILVDTAGPWAREALLGALA 100
Cdd:cd07711    1 EVKVLVEGYARRDS-DGGFRASSTVTLI---------------------------KDGgknILVDTGTPWDRDLLLKALA 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922 101 GQGVAPGDVTLVVGTHGHSDHIGNLGLFPGAALLVSHDFClpGGRYLPHGLGEERPLRLGPGLEVWATPGHGGQrDVSVL 180
Cdd:cd07711   53 EHGLSPEDIDYVVLTHGHPDHIGNLNLFPNATVIVGWDIC--GDSYDDHSLEEGDGYEIDENVEVIPTPGHTPE-DVSVL 129

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115497922 181 VAGTALGTVMVVGDVFERDGDEGS---WQALSEDPVAQKHSRKRILGTADVVVPGHGAPFR 238
Cdd:cd07711  130 VETEKKGTVAVAGDLFEREEDLEDpilWDPLSEDPELQEESRKRILALADWIIPGHGPPFK 190
 
Name Accession Description Interval E-value
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 24-238 1.58e-70

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: 215.14  E-value: 1.58e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  24 SVVVLLQGYAEPEGvGDAVRADGSVTLVlpqawgpasshrepqpyeaktaleeaaRGP---ILVDTAGPWAREALLGALA 100
Cdd:cd07711    1 EVKVLVEGYARRDS-DGGFRASSTVTLI---------------------------KDGgknILVDTGTPWDRDLLLKALA 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922 101 GQGVAPGDVTLVVGTHGHSDHIGNLGLFPGAALLVSHDFClpGGRYLPHGLGEERPLRLGPGLEVWATPGHGGQrDVSVL 180
Cdd:cd07711   53 EHGLSPEDIDYVVLTHGHPDHIGNLNLFPNATVIVGWDIC--GDSYDDHSLEEGDGYEIDENVEVIPTPGHTPE-DVSVL 129

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115497922 181 VAGTALGTVMVVGDVFERDGDEGS---WQALSEDPVAQKHSRKRILGTADVVVPGHGAPFR 238
Cdd:cd07711  130 VETEKKGTVAVAGDLFEREEDLEDpilWDPLSEDPELQEESRKRILALADWIIPGHGPPFK 190
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 79-241 5.79e-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: 66.25  E-value: 5.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  79 RGPILVDT-AGPWAREALLGALAGQGVapgDVTLVVGTHGHSDHIGNLGLFP---GAALLVSHD------FCLPGGRYLP 148
Cdd:COG0491   24 DGAVLIDTgLGPADAEALLAALAALGL---DIKAVLLTHLHPDHVGGLAALAeafGAPVYAHAAeaealeAPAAGALFGR 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922 149 HGLGEERPLR-------LGPGLEVWATPGH--GgqrDVSVLVAGtalGTVMVVGDVFERdGDEGSWQALSEDPVAQKHSR 219
Cdd:COG0491  101 EPVPPDRTLEdgdtlelGGPGLEVIHTPGHtpG---HVSFYVPD---EKVLFTGDALFS-GGVGRPDLPDGDLAQWLASL 173

                        170       180
                 ....*....|....*....|...
gi 115497922 220 KRILG-TADVVVPGHGAPFRVIR 241
Cdd:COG0491  174 ERLLAlPPDLVIPGHGPPTTAEA 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 82-233 2.66e-09

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: 55.25  E-value: 2.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922    82 ILVDTAGPWArEALLGALAGQGvaPGDVTLVVGTHGHSDHIGNLGLF---PGAALLVSHDFC--LPGGRYLPHGLGEERP 156
Cdd:smart00849  12 ILIDTGPGEA-EDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPELleaPGAPVYAPEGTAelLKDLLALLGELGAEAE 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922   157 LRL--------------GPGLEVWATPGHGGQrDVSVLVAGtalGTVMVVGDVFERDGDEGSWQALSEDPVAQ--KHSRK 220
Cdd:smart00849  89 PAPpdrtlkdgdeldlgGGELEVIHTPGHTPG-SIVLYLPE---GKILFTGDLLFAGGDGRTLVDGGDAAASDalESLLK 164

                          170
                   ....*....|...
gi 115497922   221 RILGTADVVVPGH 233
Cdd:smart00849 165 LLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
82-233 3.85e-08

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 51.99  E-value: 3.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922   82 ILVDTaGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLFPGA----ALLVSHDFCLPGGRYL-----PHGLG 152
Cdd:pfam00753  18 VLIDT-GGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEAtdvpVIVVAEEARELLDEELglaasRLGLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  153 EERPLRLGPGLEVW-------------ATPGHGGQRDVSVLVAGtaLGTVMVVGDVFERD--GDEGSWQALSEDPVAQKH 217
Cdd:pfam00753  97 GPPVVPLPPDVVLEegdgilggglgllVTHGPGHGPGHVVVYYG--GGKVLFTGDLLFAGeiGRLDLPLGGLLVLHPSSA 174

                         170       180
                  ....*....|....*....|..
gi 115497922  218 S------RKRILGTADVVVPGH 233
Cdd:pfam00753 175 EssleslLKLAKLKAAVIVPGH 196
 
Name Accession Description Interval E-value
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 24-238 1.58e-70

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: 215.14  E-value: 1.58e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  24 SVVVLLQGYAEPEGvGDAVRADGSVTLVlpqawgpasshrepqpyeaktaleeaaRGP---ILVDTAGPWAREALLGALA 100
Cdd:cd07711    1 EVKVLVEGYARRDS-DGGFRASSTVTLI---------------------------KDGgknILVDTGTPWDRDLLLKALA 52

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922 101 GQGVAPGDVTLVVGTHGHSDHIGNLGLFPGAALLVSHDFClpGGRYLPHGLGEERPLRLGPGLEVWATPGHGGQrDVSVL 180
Cdd:cd07711   53 EHGLSPEDIDYVVLTHGHPDHIGNLNLFPNATVIVGWDIC--GDSYDDHSLEEGDGYEIDENVEVIPTPGHTPE-DVSVL 129

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115497922 181 VAGTALGTVMVVGDVFERDGDEGS---WQALSEDPVAQKHSRKRILGTADVVVPGHGAPFR 238
Cdd:cd07711  130 VETEKKGTVAVAGDLFEREEDLEDpilWDPLSEDPELQEESRKRILALADWIIPGHGPPFK 190
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 76-233 4.26e-17

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: 78.03  E-value: 4.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  76 EAARGPILVDT---------------AGPWAR---EALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLFPGAALLVS- 136
Cdd:cd07729   38 EHPEGTILVDTgfhpdaaddpgglelAFPPGVteeQTLEEQLARLGLDPEDIDYVILSHLHFDHAGGLDLFPNATIIVQr 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922 137 ----------------------HDFCLPGGRYLPHglgeERPLRLGPGLEVWATPGH--GGQrdvSVLVAgTALGTVMVV 192
Cdd:cd07729  118 aeleyatgpdplaagyyedvlaLDDDLPGGRVRLV----DGDYDLFPGVTLIPTPGHtpGHQ---SVLVR-LPEGTVLLA 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 115497922 193 GDV--FERDGDEGSWQALSEDPVAQKHSRKRIL----GTADVVVPGH 233
Cdd:cd07729  190 GDAayTYENLEEGRPPGINYDPEAALASLERLKalaeREGARVIPGH 236
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 76-234 1.33e-14

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: 70.33  E-value: 1.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  76 EAARGPILVDTAGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLF---PGAALLVSHD--FCLPGGRYLP-- 148
Cdd:cd07721   17 EDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALkeaPGAPVYAHEReaPYLEGEKPYPpp 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922 149 ---------------------HGLGEERPLRLGPGLEVWATPGH-GGQrdVSVLVAGTAlgtVMVVGDVFERDGDE--GS 204
Cdd:cd07721   97 vrlgllgllspllpvkpvpvdRTLEDGDTLDLAGGLRVIHTPGHtPGH--ISLYLEEDG---VLIAGDALVTVGGElvPP 171

                        170       180       190
                 ....*....|....*....|....*....|.
gi 115497922 205 WQALSEDPVAQKHSRKRILGT-ADVVVPGHG 234
Cdd:cd07721  172 PPPFTWDMEEALESLRKLAELdPEVLAPGHG 202
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 79-241 5.79e-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: 66.25  E-value: 5.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  79 RGPILVDT-AGPWAREALLGALAGQGVapgDVTLVVGTHGHSDHIGNLGLFP---GAALLVSHD------FCLPGGRYLP 148
Cdd:COG0491   24 DGAVLIDTgLGPADAEALLAALAALGL---DIKAVLLTHLHPDHVGGLAALAeafGAPVYAHAAeaealeAPAAGALFGR 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922 149 HGLGEERPLR-------LGPGLEVWATPGH--GgqrDVSVLVAGtalGTVMVVGDVFERdGDEGSWQALSEDPVAQKHSR 219
Cdd:COG0491  101 EPVPPDRTLEdgdtlelGGPGLEVIHTPGHtpG---HVSFYVPD---EKVLFTGDALFS-GGVGRPDLPDGDLAQWLASL 173

                        170       180
                 ....*....|....*....|...
gi 115497922 220 KRILG-TADVVVPGHGAPFRVIR 241
Cdd:COG0491  174 ERLLAlPPDLVIPGHGPPTTAEA 196
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 82-233 3.23e-10

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: 58.07  E-value: 3.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  82 ILVDTAGPwAREALLGALAGQGVapgDVTLVVGTHGHSDHIGNLGLF---PGAALLVSHD--FCL--PGGRYLPHGLGEE 154
Cdd:cd06262   23 ILIDPGAG-ALEKILEAIEELGL---KIKAILLTHGHFDHIGGLAELkeaPGAPVYIHEAdaELLedPELNLAFFGGGPL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922 155 RP------------LRLGP-GLEVWATPGH--GGqrdVSVLVAGtalGTVMVVGDV-FErdGDEGSWQALSEDPVAQKHS 218
Cdd:cd06262   99 PPpepdilledgdtIELGGlELEVIHTPGHtpGS---VCFYIEE---EGVLFTGDTlFA--GSIGRTDLPGGDPEQLIES 170

                        170
                 ....*....|....*...
gi 115497922 219 RKRILGTAD---VVVPGH 233
Cdd:cd06262  171 IKKLLLLLPddtVVYPGH 188
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 82-233 2.66e-09

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: 55.25  E-value: 2.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922    82 ILVDTAGPWArEALLGALAGQGvaPGDVTLVVGTHGHSDHIGNLGLF---PGAALLVSHDFC--LPGGRYLPHGLGEERP 156
Cdd:smart00849  12 ILIDTGPGEA-EDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPELleaPGAPVYAPEGTAelLKDLLALLGELGAEAE 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922   157 LRL--------------GPGLEVWATPGHGGQrDVSVLVAGtalGTVMVVGDVFERDGDEGSWQALSEDPVAQ--KHSRK 220
Cdd:smart00849  89 PAPpdrtlkdgdeldlgGGELEVIHTPGHTPG-SIVLYLPE---GKILFTGDLLFAGGDGRTLVDGGDAAASDalESLLK 164

                          170
                   ....*....|...
gi 115497922   221 RILGTADVVVPGH 233
Cdd:smart00849 165 LLKLLPKLVVPGH 177
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 82-243 7.91e-09

uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1429 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 53.84  E-value: 7.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  82 ILVDT--AGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLF--PGAALLVSHDFclpggRYLPHG----LGE 153
Cdd:cd07725   27 TLIDTglATEEDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLqeKSGATVYILDV-----TPVKDGdkidLGG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922 154 ERplrlgpgLEVWATPGHG-GQrdVSVLVAGtalGTVMVVGD-VFERDGDEGSWQALS-EDPVAQ--KHSRKRILGTADV 228
Cdd:cd07725  102 LR-------LKVIETPGHTpGH--IVLYDED---RRELFVGDaVLPKITPNVSLWAVRvEDPLGAylESLDKLEKLDVDL 169

                        170
                 ....*....|....*
gi 115497922 229 VVPGHGAPFRVIREA 243
Cdd:cd07725  170 AYPGHGGPIKDPKAR 184
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 82-136 2.66e-08

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: 53.32  E-value: 2.66e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 115497922  82 ILVDT-----AGPWArEALLGALAGQGVAPGDVTLVVGTHGHSDHIGNL------GLFPGAALLVS 136
Cdd:cd07720   61 ILVDTgagglFGPTA-GKLLANLAAAGIDPEDIDDVLLTHLHPDHIGGLvdaggkPVFPNAEVHVS 125
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
82-233 3.85e-08

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 51.99  E-value: 3.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922   82 ILVDTaGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLFPGA----ALLVSHDFCLPGGRYL-----PHGLG 152
Cdd:pfam00753  18 VLIDT-GGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEAtdvpVIVVAEEARELLDEELglaasRLGLP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  153 EERPLRLGPGLEVW-------------ATPGHGGQRDVSVLVAGtaLGTVMVVGDVFERD--GDEGSWQALSEDPVAQKH 217
Cdd:pfam00753  97 GPPVVPLPPDVVLEegdgilggglgllVTHGPGHGPGHVVVYYG--GGKVLFTGDLLFAGeiGRLDLPLGGLLVLHPSSA 174

                         170       180
                  ....*....|....*....|..
gi 115497922  218 S------RKRILGTADVVVPGH 233
Cdd:pfam00753 175 EssleslLKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 82-233 1.17e-07

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 50.98  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  82 ILVDTA--------GPWA----REALLGALAGQGVAPGDVTLVVGTHGHSDHIG-NLGL--------FPGAALLVSH--- 137
Cdd:cd16277   25 ILVDTGigndkprpGPPAfhnlNTPYLERLAAAGVRPEDVDYVLCTHLHVDHVGwNTRLvdgrwvptFPNARYLFSRaey 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922 138 DFCLPGGRYLP---------------HGLGE--ERPLRLGPGLEVWATPGHG-GQrdVSVLVaGTALGTVMVVGDVF--- 196
Cdd:cd16277  105 DHWSSPDAGGPpnrgvfedsvlpvieAGLADlvDDDHEILDGIRLEPTPGHTpGH--VSVEL-ESGGERALFTGDVMhhp 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 115497922 197 ----ERDgdegsW-QALSEDPVAQKHSRKRIL----GTADVVVPGH 233
Cdd:cd16277  182 iqvaRPD-----WsSVFDEDPAQAAATRRRLLeraaDTDTLLFPAH 222
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 91-174 2.56e-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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 47.26  E-value: 2.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  91 AREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLFPGAALLVSHDFC--LPGGRYLPHGLGEERPLRLGPGLEVWAT 168
Cdd:cd07730   66 VEEDVAEQLAAGGIDPEDIDAVILSHLHWDHIGGLSDFPNARLIVGPGAKeaLRPPGYPSGFLPELLPSDFEGRLVRWEE 145


                 ....*.
gi 115497922 169 PGHGGQ 174
Cdd:cd07730  146 DDFLWV 151
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 82-125 8.35e-06

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: 45.20  E-value: 8.35e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 115497922  82 ILVDTAGPW--AREALLGALAGQGVapGDVTLVVGTHGHSDHIGNL 125
Cdd:cd07731   22 ILIDTGPRDsfGEDVVVPYLKARGI--KKLDYLILTHPDADHIGGL 65
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 82-171 1.22e-05

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 44.37  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  82 ILVDTAGPwarEALLGALAGQGVapgDVTLVVGTHGHSDHI-GNLGL---FPGAALLVSHDFCLPGgryLPHGLGEERPL 157
Cdd:cd07723   23 AVVDPGEA---EPVLAALEKNGL---TLTAILTTHHHWDHTgGNAELkalFPDAPVYGPAEDRIPG---LDHPVKDGDEI 93

                         90
                 ....*....|....*
gi 115497922 158 RLGPG-LEVWATPGH 171
Cdd:cd07723   94 KLGGLeVKVLHTPGH 108
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 74-125 5.66e-05

Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of L1- and Pom-1-like MBLs belongs to the B3 subclass. Subclass B3 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. These B3 enzymes have a modified Zn2/DCH site (Asp-His-His).


Pssm-ID: 293847  Cd Length: 239  Bit Score: 43.27  E-value: 5.66e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 115497922  74 LEEAARGPILVDTAGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNL 125
Cdd:cd16289   26 LVKTPDGAVLLDGGMPQAADMLLDNMRALGVAPGDLKLILHSHAHADHAGPL 77
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 80-137 7.17e-05

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


Pssm-ID: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 42.96  E-value: 7.17e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 115497922  80 GPILVDTAgpWAREA---LLGALAGQGVAPGDVTLVVGTHGHSDHIGnlglfpGAALLVSH 137
Cdd:cd16280   32 GLILIDAL--NNNEAadlIVDGLEKLGLDPADIKYILITHGHGDHYG------GAAYLKDL 84
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 93-236 8.82e-05

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 42.09  E-value: 8.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  93 EALLGALAGqgvapGDVTLVVGTHGHSDHIGNLGLF----------PGAALLVSHDFCLPGGRYLPHGLGEERPlrlGPG 162
Cdd:cd16278   43 DALLAALGG-----GRVSAILVTHTHRDHSPGAARLaertgapvraFGPHRAGGQDTDFAPDRPLADGEVIEGG---GLR 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922 163 LEVWATPGHGG------QRDVSVLVAG-TALG--TVMVVgdvfERDGDEGSWQAlsedpvaqkhSRKRILGTADVVV-PG 232
Cdd:cd16278  115 LTVLHTPGHTSdhlcfaLEDEGALFTGdHVMGwsTTVIA----PPDGDLGDYLA----------SLERLLALDDRLLlPG 180


                 ....
gi 115497922 233 HGAP 236
Cdd:cd16278  181 HGPP 184
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 76-135 1.24e-04

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: 42.09  E-value: 1.24e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 115497922  76 EAARGPILVDTAGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGL----FPGAALLV 135
Cdd:cd07726   22 DGEGRPALIDTGPSSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLlaeaLPNAKVYV 85
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 76-165 2.34e-04

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: 41.45  E-value: 2.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  76 EAARGPILVDTaGPwaREALL---GALagqGVAPGDVTLVVGTHGHSDHIGNL----GLFPGAALLVSHDFCLP-----G 143
Cdd:cd07713   26 ETEGKKILFDT-GQ--SGVLLhnaKKL---GIDLSDIDAVVLSHGHYDHTGGLkallELNPKAPVYAHPDAFEPryskrG 99

                         90       100
                 ....*....|....*....|..
gi 115497922 144 GRYLPHGLGEERPLRLGPGLEV 165
Cdd:cd07713  100 GGKKGIGIGREELEKAGARLVL 121
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 76-128 2.86e-04

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


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 40.32  E-value: 2.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 115497922  76 EAARGPILVDtAGPWAREaLLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLF 128
Cdd:cd07733   15 ETEDGKLLID-AGLSGRK-ITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVL 65
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 82-125 5.04e-04

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 40.61  E-value: 5.04e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 115497922  82 ILVDTAGPW----AREALLGALAGQGVapGDVTLVVGTHGHSDHIGNL 125
Cdd:COG2333   24 ILIDTGPRPsfdaGERVVLPYLRALGI--RRLDLLVLTHPDADHIGGL 69
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 82-137 6.04e-04

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 40.17  E-value: 6.04e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115497922  82 ILVDTA-------------GPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLG----------LFPGAALLVSH 137
Cdd:cd16281   55 ILIDTGigdkqdpkfrsiyVQHSEHSLLKSLARLGLSPEDITDVILTHLHFDHCGGATradddglvelLFPNATYWVQK 133
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
76-154 1.11e-03

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 39.48  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  76 EAARGPILVDTAGPwarEALL---GALagqGVAPGDVTLVVGTHGHSDHIGNLGLF----PGAALLVSHDFCLPggRYLP 148
Cdd:COG1237   28 ETEGKRILFDTGQS---DVLLknaEKL---GIDLSDIDAVVLSHGHYDHTGGLPALlelnPKAPVYAHPDAFEK--RYSK 99


                 ....*.
gi 115497922 149 HGLGEE 154
Cdd:COG1237  100 RPGGKY 105
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 80-136 1.27e-03

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: 39.25  E-value: 1.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  80 GPILVDTAGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLF---PGAALLVS 136
Cdd:cd16315   32 GHVLIDSGTEEAAPLVLANIRKLGFDPKDVRWLLSSHEHFDHVGGLAALqraTGARVAAS 91
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 79-193 1.90e-03

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: 38.68  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  79 RGPILVDTAGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLF---PGAALLV---SHDFCLPGGRYLPHGLG 152
Cdd:cd07708   31 QGNILIDGDMEQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAEIkkqTGAKVMAgaeDVSLLLSGGSSDFHYAN 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 115497922 153 EERP----------------LRLGP-GLEVWATPGH--------------GGQRDVSVLVAGTALGTVMVVG 193
Cdd:cd07708  111 DSSTyfpqstvdravhdgerVTLGGtVLTAHATPGHtpgcttwtmtlkdhGKQYQVVFADSLTVNPGYRLVD 182
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 79-236 2.60e-03

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 37.93  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  79 RGPILVDTAGPWAR-EALLGALAGqgVAPGDVTLVVGTHGHSDHIGNLGLFPGA-ALLVSHDFCLpggRYLPHGLGEERP 156
Cdd:cd16282   24 DGVVVIDTGASPRLaRALLAAIRK--VTDKPVRYVVNTHYHGDHTLGNAAFADAgAPIIAHENTR---EELAARGEAYLE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922 157 LRLGPGLEVWATPG--------------HGGQRDVSVLVAGTA--LGTVMV---------VGDVFE-------RDGDEGS 204
Cdd:cd16282   99 LMRRLGGDAMAGTElvlpdrtfddgltlDLGGRTVELIHLGPAhtPGDLVVwlpeegvlfAGDLVFngripflPDGSLAG 178

                        170       180       190
                 ....*....|....*....|....*....|...
gi 115497922 205 WQALSEdpvaqkhsrkRILGT-ADVVVPGHGAP 236
Cdd:cd16282  179 WIAALD----------RLLALdATVVVPGHGPV 201
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 111-233 3.16e-03

uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 37.61  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922 111 LVVGTHGHSDHIGNLGLFP-------GAALLVSHD----FCLPGGRYLPHGLGEERPLR------LGP-GLEVWATPGH- 171
Cdd:cd07712   45 LVVATHGHFDHIGGLHEFEevyvhpaDAEILAAPDnfetLTWDAATYSVPPAGPTLPLRdgdvidLGDrQLEVIHTPGHt 124

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 115497922 172 -GG----QRDVSVLVAGTALGTVMVVGDVFERDGDE--GSWQALSEDPvaqkhsrkrilGTADVVVPGH 233
Cdd:cd07712  125 pGSiallDRANRLLFSGDVVYDGPLIMDLPHSDLDDylASLEKLSKLP-----------DEFDKVLPGH 182
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 76-136 4.11e-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: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 37.60  E-value: 4.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  76 EAARGPILVDTA--------------GPWAR---------EALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLFPGAA 132
Cdd:cd07742   25 ETDDGLVLVDTGfgladvadpkrrlgGPFRRllrprldedETAVRQIEALGFDPSDVRHIVLTHLDLDHAGGLADFPHAT 104


                 ....
gi 115497922 133 LLVS 136
Cdd:cd07742  105 VHVH 108
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 80-136 6.45e-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: 37.08  E-value: 6.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  80 GPILVDTAGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLF---PGAALLVS 136
Cdd:cd16309   32 GHILIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAELkkaTGAQLVAS 91
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 80-138 6.73e-03

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 36.79  E-value: 6.73e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  80 GPILVDtAGPWAREALLGALagQGVAPGDVTLVVGTHGHSDHIGNLGLFPGA-ALLVSHD 138
Cdd:cd16276   20 GVIVVD-APPSLGENLLAAI--RKVTDKPVTHVVYSHNHADHIGGASIFKDEgATIIAHE 76
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 80-125 8.01e-03

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: 36.89  E-value: 8.01e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 115497922  80 GPILVDTAGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNL 125
Cdd:cd16311   32 GHVLVDGGLPESAPKIIANIEALGFRIEDVKLILNSHGHIDHAGGL 77
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 ...
 80-125 8.38e-03

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


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 36.94  E-value: 8.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 115497922  80 GPILVDTAGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNL 125
Cdd:cd16290   32 GLILIDGALPQSAPQIEANIRALGFRLEDVKLILNSHAHFDHAGGI 77
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 82-170 8.39e-03

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 36.80  E-value: 8.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  82 ILVDtAGPWAREALLGAlagqGVAPGDVTLVVGTHGHSDHIgnlglfpgaallvshdfclpggrylpHGLGEERPLRLGP 161
Cdd:COG1235   47 LLID-AGPDLREQLLRL----GLDPSKIDAILLTHEHADHI--------------------------AGLDDLRPRYGPN 95


                 ....*....
gi 115497922 162 GLEVWATPG 170
Cdd:COG1235   96 PIPVYATPG 104
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 82-236 8.78e-03

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


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 36.49  E-value: 8.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922  82 ILVDTagPWAR---EALLGALAGQGVAPgdVTLVVGTHGHSDHIGNLGLF----------PGAALLVSHDfclpGGRYLP 148
Cdd:cd16285   38 VLIDT--PWTEaqtATLLDWIEKKLGKP--VTAAISTHSHDDRTGGIKALnargiptyatALTNELAKKE----GKPVPT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 115497922 149 HGLGEERPLRLGPgLEVWaTPGHGGQRD-VSVLVAGTALgtvmVVGDVFERDGDEGSWQALSE-DPVAQKHSRKRIL--- 223
Cdd:cd16285  110 HSLKGALTLGFGP-LEVF-YPGPGHTPDnIVVWLPKSKI----LFGGCLVKSASATSLGNVGDaDVEAWPKSIENLKaky 183

                        170
                 ....*....|...
gi 115497922 224 GTADVVVPGHGAP 236
Cdd:cd16285  184 PEARMVVPGHGAP 196
 
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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