NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|63025212|ref|NP_981942|]
View 

metallo-beta-lactamase domain-containing protein 1 [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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; ...
 20-236 5.85e-69

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: 211.29  E-value: 5.85e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  20 SVVVLLQGYAEPEGvGDAVRADGSVTLVlpqtrgpasshrespRGSGGAeaaleeaargpILVDTGGPWAREALLGALAG 99
Cdd:cd07711   1 EVKVLVEGYARRDS-DGGFRASSTVTLI---------------KDGGKN-----------ILVDTGTPWDRDLLLKALAE 53

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212 100 QGVAPGDVTLVVGTHGHSDHIGNLGLFPGAALLVSHDFClpGGRYLPHGLGEGQPLRLGPGLEVWATPGHGGQrDVSVVV 179
Cdd:cd07711  54 HGLSPEDIDYVVLTHGHPDHIGNLNLFPNATVIVGWDIC--GDSYDDHSLEEGDGYEIDENVEVIPTPGHTPE-DVSVLV 130

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212 180 AGTALGTVVVAGDVFERDGDEDS---WQALSEDPAAQERSRKRVLVVADVVVPGHGPPFR 236
Cdd:cd07711 131 ETEKKGTVAVAGDLFEREEDLEDpilWDPLSEDPELQEESRKRILALADWIIPGHGPPFK 190
 
Name Accession Description Interval E-value
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 20-236 5.85e-69

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: 211.29  E-value: 5.85e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  20 SVVVLLQGYAEPEGvGDAVRADGSVTLVlpqtrgpasshrespRGSGGAeaaleeaargpILVDTGGPWAREALLGALAG 99
Cdd:cd07711   1 EVKVLVEGYARRDS-DGGFRASSTVTLI---------------KDGGKN-----------ILVDTGTPWDRDLLLKALAE 53

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212 100 QGVAPGDVTLVVGTHGHSDHIGNLGLFPGAALLVSHDFClpGGRYLPHGLGEGQPLRLGPGLEVWATPGHGGQrDVSVVV 179
Cdd:cd07711  54 HGLSPEDIDYVVLTHGHPDHIGNLNLFPNATVIVGWDIC--GDSYDDHSLEEGDGYEIDENVEVIPTPGHTPE-DVSVLV 130

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212 180 AGTALGTVVVAGDVFERDGDEDS---WQALSEDPAAQERSRKRVLVVADVVVPGHGPPFR 236
Cdd:cd07711 131 ETEKKGTVAVAGDLFEREEDLEDpilWDPLSEDPELQEESRKRILALADWIIPGHGPPFK 190
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 77-239 2.13e-11

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: 61.63  E-value: 2.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  77 RGPILVDTG-GPWAREALLGALAGQGVapgDVTLVVGTHGHSDHIGNLGLFP---GAALLVSHD-----------FCLPG 141
Cdd:COG0491  24 DGAVLIDTGlGPADAEALLAALAALGL---DIKAVLLTHLHPDHVGGLAALAeafGAPVYAHAAeaealeapaagALFGR 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212 142 GRYLP-HGLGEGQPLRLG-PGLEVWATPGH--GgqrDVSVVVAGtalGTVVVAGDVFERdGDEDSWQALSEDPAAQERSR 217
Cdd:COG0491 101 EPVPPdRTLEDGDTLELGgPGLEVIHTPGHtpG---HVSFYVPD---EKVLFTGDALFS-GGVGRPDLPDGDLAQWLASL 173

                       170       180
                ....*....|....*....|...
gi 63025212 218 KR-VLVVADVVVPGHGPPFRVLR 239
Cdd:COG0491 174 ERlLALPPDLVIPGHGPPTTAEA 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 80-231 1.31e-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: 58.72  E-value: 1.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212     80 ILVDTGGPWArEALLGALAGQGvaPGDVTLVVGTHGHSDHIGNLGLF---PGAALLVSHDFC---------------LPG 141
Cdd:smart00849  12 ILIDTGPGEA-EDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPELleaPGAPVYAPEGTAellkdllallgelgaEAE 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212    142 GRYLPHGLGEGQPLRLG-PGLEVWATPGH-GGqrDVSVVVAGtalGTVVVAGDVFERDGDEDSWQALSEDPAAQ--ERSR 217
Cdd:smart00849  89 PAPPDRTLKDGDELDLGgGELEVIHTPGHtPG--SIVLYLPE---GKILFTGDLLFAGGDGRTLVDGGDAAASDalESLL 163

                          170
                   ....*....|....
gi 63025212    218 KRVLVVADVVVPGH 231
Cdd:smart00849 164 KLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
80-201 3.92e-08

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 52.37  E-value: 3.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212    80 ILVDTGGPWAREALLgALAGQGVAPGDVTLVVGTHGHSDHIGNLGLFPGA----ALLVSHDFCLPGGRYL-----PHGLG 150
Cdd:pfam00753  18 VLIDTGGSAEAALLL-LLAALGLGPKDIDAVILTHGHFDHIGGLGELAEAtdvpVIVVAEEARELLDEELglaasRLGLP 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63025212   151 EGQPLRLGPGLEVW-------------ATPGHGGQRDVSVVVAGtaLGTVVVAGDVFERDGDED 201
Cdd:pfam00753  97 GPPVVPLPPDVVLEegdgilggglgllVTHGPGHGPGHVVVYYG--GGKVLFTGDLLFAGEIGR 158
 
Name Accession Description Interval E-value
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 20-236 5.85e-69

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: 211.29  E-value: 5.85e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  20 SVVVLLQGYAEPEGvGDAVRADGSVTLVlpqtrgpasshrespRGSGGAeaaleeaargpILVDTGGPWAREALLGALAG 99
Cdd:cd07711   1 EVKVLVEGYARRDS-DGGFRASSTVTLI---------------KDGGKN-----------ILVDTGTPWDRDLLLKALAE 53

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212 100 QGVAPGDVTLVVGTHGHSDHIGNLGLFPGAALLVSHDFClpGGRYLPHGLGEGQPLRLGPGLEVWATPGHGGQrDVSVVV 179
Cdd:cd07711  54 HGLSPEDIDYVVLTHGHPDHIGNLNLFPNATVIVGWDIC--GDSYDDHSLEEGDGYEIDENVEVIPTPGHTPE-DVSVLV 130

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212 180 AGTALGTVVVAGDVFERDGDEDS---WQALSEDPAAQERSRKRVLVVADVVVPGHGPPFR 236
Cdd:cd07711 131 ETEKKGTVAVAGDLFEREEDLEDpilWDPLSEDPELQEESRKRILALADWIIPGHGPPFK 190
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 78-219 3.02e-16

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: 75.71  E-value: 3.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  78 GPILVDTGGPWA------------------REALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLFPGAALLVS----- 134
Cdd:cd07729  42 GTILVDTGFHPDaaddpgglelafppgvteEQTLEEQLARLGLDPEDIDYVILSHLHFDHAGGLDLFPNATIIVQraele 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212 135 ------------------HDFCLPGGRYLPHGlGEGQplrLGPGLEVWATPGH--GGQrdvSVVVAgTALGTVVVAGDV- 193
Cdd:cd07729 122 yatgpdplaagyyedvlaLDDDLPGGRVRLVD-GDYD---LFPGVTLIPTPGHtpGHQ---SVLVR-LPEGTVLLAGDAa 193

                       170       180
                ....*....|....*....|....*..
gi 63025212 194 -FERDGDEDSWQALSEDPAAQERSRKR 219
Cdd:cd07729 194 yTYENLEEGRPPGINYDPEAALASLER 220
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 77-169 2.90e-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: 69.56  E-value: 2.90e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  77 RGPILVDTGGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLF---PGAALLVSHD--FCLPGGRYLP----- 146
Cdd:cd07721  20 DGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALkeaPGAPVYAHEReaPYLEGEKPYPppvrl 99

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 63025212 147 ------------------HGLGEGQPLRLGPGLEVWATPGH 169
Cdd:cd07721 100 gllgllspllpvkpvpvdRTLEDGDTLDLAGGLRVIHTPGH 140
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 77-239 2.13e-11

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: 61.63  E-value: 2.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  77 RGPILVDTG-GPWAREALLGALAGQGVapgDVTLVVGTHGHSDHIGNLGLFP---GAALLVSHD-----------FCLPG 141
Cdd:COG0491  24 DGAVLIDTGlGPADAEALLAALAALGL---DIKAVLLTHLHPDHVGGLAALAeafGAPVYAHAAeaealeapaagALFGR 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212 142 GRYLP-HGLGEGQPLRLG-PGLEVWATPGH--GgqrDVSVVVAGtalGTVVVAGDVFERdGDEDSWQALSEDPAAQERSR 217
Cdd:COG0491 101 EPVPPdRTLEDGDTLELGgPGLEVIHTPGHtpG---HVSFYVPD---EKVLFTGDALFS-GGVGRPDLPDGDLAQWLASL 173

                       170       180
                ....*....|....*....|...
gi 63025212 218 KR-VLVVADVVVPGHGPPFRVLR 239
Cdd:COG0491 174 ERlLALPPDLVIPGHGPPTTAEA 196
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 80-231 1.31e-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: 58.72  E-value: 1.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212     80 ILVDTGGPWArEALLGALAGQGvaPGDVTLVVGTHGHSDHIGNLGLF---PGAALLVSHDFC---------------LPG 141
Cdd:smart00849  12 ILIDTGPGEA-EDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPELleaPGAPVYAPEGTAellkdllallgelgaEAE 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212    142 GRYLPHGLGEGQPLRLG-PGLEVWATPGH-GGqrDVSVVVAGtalGTVVVAGDVFERDGDEDSWQALSEDPAAQ--ERSR 217
Cdd:smart00849  89 PAPPDRTLKDGDELDLGgGELEVIHTPGHtPG--SIVLYLPE---GKILFTGDLLFAGGDGRTLVDGGDAAASDalESLL 163

                          170
                   ....*....|....
gi 63025212    218 KRVLVVADVVVPGH 231
Cdd:smart00849 164 KLLKLLPKLVVPGH 177
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 80-134 1.67e-09

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: 56.79  E-value: 1.67e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63025212  80 ILVDTG-----GPWArEALLGALAGQGVAPGDVTLVVGTHGHSDHIGNL------GLFPGAALLVS 134
Cdd:cd07720  61 ILVDTGagglfGPTA-GKLLANLAAAGIDPEDIDDVLLTHLHPDHIGGLvdaggkPVFPNAEVHVS 125
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 80-219 3.14e-09

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 55.61  E-value: 3.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  80 ILVDTG--------GPWA----REALLGALAGQGVAPGDVTLVVGTHGHSDHIG-NLGL--------FPGAALLVSH--- 135
Cdd:cd16277  25 ILVDTGigndkprpGPPAfhnlNTPYLERLAAAGVRPEDVDYVLCTHLHVDHVGwNTRLvdgrwvptFPNARYLFSRaey 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212 136 DFCLPGGRYLPHGLG-----------EGQPL------RLGPGLEVWATPGHG-GQrdVSVVVaGTALGTVVVAGDVF--- 194
Cdd:cd16277 105 DHWSSPDAGGPPNRGvfedsvlpvieAGLADlvdddhEILDGIRLEPTPGHTpGH--VSVEL-ESGGERALFTGDVMhhp 181

                       170       180       190
                ....*....|....*....|....*....|
gi 63025212 195 ----ERDgdedsW-QALSEDPAAQERSRKR 219
Cdd:cd16277 182 iqvaRPD-----WsSVFDEDPAQAAATRRR 206
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 80-241 1.56e-08

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: 53.07  E-value: 1.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  80 ILVDTG--GPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLF--PGAALLVSHDFclpggrylpHGLGEGQPL 155
Cdd:cd07725  27 TLIDTGlaTEEDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLqeKSGATVYILDV---------TPVKDGDKI 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212 156 RLGP-GLEVWATPGHG-GQrdVSVVVAGtalGTVVVAGD-VFERDGDEDSWQALSED---PAAQERSRKRVLVVADVVVP 229
Cdd:cd07725  98 DLGGlRLKVIETPGHTpGH--IVLYDED---RRELFVGDaVLPKITPNVSLWAVRVEdplGAYLESLDKLEKLDVDLAYP 172

                       170
                ....*....|..
gi 63025212 230 GHGPPFRVLREA 241
Cdd:cd07725 173 GHGGPIKDPKAR 184
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
80-201 3.92e-08

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 52.37  E-value: 3.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212    80 ILVDTGGPWAREALLgALAGQGVAPGDVTLVVGTHGHSDHIGNLGLFPGA----ALLVSHDFCLPGGRYL-----PHGLG 150
Cdd:pfam00753  18 VLIDTGGSAEAALLL-LLAALGLGPKDIDAVILTHGHFDHIGGLGELAEAtdvpVIVVAEEARELLDEELglaasRLGLP 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 63025212   151 EGQPLRLGPGLEVW-------------ATPGHGGQRDVSVVVAGtaLGTVVVAGDVFERDGDED 201
Cdd:pfam00753  97 GPPVVPLPPDVVLEegdgilggglgllVTHGPGHGPGHVVVYYG--GGKVLFTGDLLFAGEIGR 158
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 80-193 4.33e-08

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: 51.90  E-value: 4.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  80 ILVDTGGPwAREALLGALAGQGVapgDVTLVVGTHGHSDHIGNLGLF---PGAALLVSHD-----------FCLPGGRYL 145
Cdd:cd06262  23 ILIDPGAG-ALEKILEAIEELGL---KIKAILLTHGHFDHIGGLAELkeaPGAPVYIHEAdaelledpelnLAFFGGGPL 98

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 63025212 146 P-----HGLGEGQPLRLGP-GLEVWATPGH--GGqrdVSVVVAGtalGTVVVAGDV 193
Cdd:cd06262  99 PppepdILLEDGDTIELGGlELEVIHTPGHtpGS---VCFYIEE---EGVLFTGDT 148
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 80-169 7.19e-08

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: 50.92  E-value: 7.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  80 ILVDTGGPwarEALLGALAGQGVapgDVTLVVGTHGHSDHI-GNLGL---FPGAALLVSHDFCLPGgryLPHGLGEGQPL 155
Cdd:cd07723  23 AVVDPGEA---EPVLAALEKNGL---TLTAILTTHHHWDHTgGNAELkalFPDAPVYGPAEDRIPG---LDHPVKDGDEI 93

                        90
                ....*....|....*
gi 63025212 156 RLGPG-LEVWATPGH 169
Cdd:cd07723  94 KLGGLeVKVLHTPGH 108
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 80-123 2.99e-07

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: 49.44  E-value: 2.99e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 63025212  80 ILVDTGGPW--AREALLGALAGQGVapGDVTLVVGTHGHSDHIGNL 123
Cdd:cd07731  22 ILIDTGPRDsfGEDVVVPYLKARGI--KKLDYLILTHPDADHIGGL 65
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 78-169 1.93e-06

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: 47.49  E-value: 1.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  78 GPILVDTGGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGL----FPGAALLVsH------------------ 135
Cdd:cd07726  26 RPALIDTGPSSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLlaeaLPNAKVYV-Hprgarhlidpsklwasar 104

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 63025212 136 -----DFCLPGGRYLP------HGLGEGQPLRLGP-GLEVWATPGH 169
Cdd:cd07726 105 avygdEADRLGGEILPvpeervIVLEDGETLDLGGrTLEVIDTPGH 150
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 77-138 2.28e-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: 47.65  E-value: 2.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  77 RGPILVDTG--------GPWAREALLG-------------ALAGQGVAPGDVTLVVGTHGHSDHIGNLGLFPGAALLVSH 135
Cdd:cd07730  33 GGKILFDLGyrkdfeeyTPRVPERLYRtpvpleveedvaeQLAAGGIDPEDIDAVILSHLHWDHIGGLSDFPNARLIVGP 112


                ...
gi 63025212 136 DFC 138
Cdd:cd07730 113 GAK 115
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 78-123 1.07e-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: 45.58  E-value: 1.07e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 63025212  78 GPILVDTGGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNL 123
Cdd:cd16289  32 GAVLLDGGMPQAADMLLDNMRALGVAPGDLKLILHSHAHADHAGPL 77
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 80-123 1.66e-05

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: 44.85  E-value: 1.66e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 63025212  80 ILVDTGGPW----AREALLGALAGQGVapGDVTLVVGTHGHSDHIGNL 123
Cdd:COG2333  24 ILIDTGPRPsfdaGERVVLPYLRALGI--RRLDLLVLTHPDADHIGGL 69
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 78-186 1.97e-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: 44.88  E-value: 1.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  78 GPILVDTGgpWAREA---LLGALAGQGVAPGDVTLVVGTHGHSDHIGnlglfpGAALLVS------------------HD 136
Cdd:cd16280  32 GLILIDAL--NNNEAadlIVDGLEKLGLDPADIKYILITHGHGDHYG------GAAYLKDlygakvvmseadwdmmeePP 103

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63025212 137 FCLPGGRYLPHG-----LGEGQPLRLG-PGLEVWATPGH-------------GGQRDVSVVVAGTALGT 186
Cdd:cd16280 104 EEGDNPRWGPPPerdivIKDGDTLTLGdTTITVYLTPGHtpgtlslifpvkdGGKTHRAGLWGGTGLNT 172
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 80-135 3.33e-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: 293839  Cd Length: 252  Bit Score: 44.02  E-value: 3.33e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 63025212  80 ILVDTG-------------GPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLG----------LFPGAALLVSH 135
Cdd:cd16281  55 ILIDTGigdkqdpkfrsiyVQHSEHSLLKSLARLGLSPEDITDVILTHLHFDHCGGATradddglvelLFPNATYWVQK 133
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 64-169 4.91e-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: 43.69  E-value: 4.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  64 GSGGAEAALEEAARGPILVDTGGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLF---PGAALLV---SHDF 137
Cdd:cd07708  18 GTDDLAAYLIVTPQGNILIDGDMEQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAEIkkqTGAKVMAgaeDVSL 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 63025212 138 CLPGGRYLPH----------------GLGEGQPLRLGP-GLEVWATPGH 169
Cdd:cd07708  98 LLSGGSSDFHyandsstyfpqstvdrAVHDGERVTLGGtVLTAHATPGH 146
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
80-156 7.58e-05

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 42.95  E-value: 7.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  80 ILVDTGGPwarEALL---GALagqGVAPGDVTLVVGTHGHSDHIGNLGLF----PGAALLVSHDFCLPGGRYLPHGLGEG 152
Cdd:COG1237  34 ILFDTGQS---DVLLknaEKL---GIDLSDIDAVVLSHGHYDHTGGLPALlelnPKAPVYAHPDAFEKRYSKRPGGKYIG 107


                ....
gi 63025212 153 QPLR 156
Cdd:COG1237 108 IPFS 111
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 80-169 1.02e-04

uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold metallo hydrolase domain; Includes functionally uncharacterized human lactamase beta 2. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 42.14  E-value: 1.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  80 ILVDTG--GPWAREALLGALAGQGVAPgdVTLVVGTHGHSDHIGNL----GLFPGAAL------LVSHDFCLPGGRYLPH 147
Cdd:cd07722  30 ILIDTGegRPSYIPLLKSVLDSEGNAT--ISDILLTHWHHDHVGGLpdvlDLLRGPSPrvykfpRPEEDEDPDEDGGDIH 107

                        90       100
                ....*....|....*....|....
gi 63025212 148 GLGEGQPLRLgPG--LEVWATPGH 169
Cdd:cd07722 108 DLQDGQVFKV-EGatLRVIHTPGH 130
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 80-163 1.02e-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: 42.61  E-value: 1.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  80 ILVDTGgpwAREALL---GALagqGVAPGDVTLVVGTHGHSDHIGNL----GLFPGAALLVSHDFCLP-----GGRYLPH 147
Cdd:cd07713  32 ILFDTG---QSGVLLhnaKKL---GIDLSDIDAVVLSHGHYDHTGGLkallELNPKAPVYAHPDAFEPryskrGGGKKGI 105

                        90
                ....*....|....*.
gi 63025212 148 GLGEGQPLRLGPGLEV 163
Cdd:cd07713 106 GIGREELEKAGARLVL 121
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 91-169 1.09e-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: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 42.09  E-value: 1.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  91 EALLGALAGqgvapGDVTLVVGTHGHSDHIGNLGLF----------PGAALLVSHDFCLPGGRYLPHglgeGQPLRL-GP 159
Cdd:cd16278  43 DALLAALGG-----GRVSAILVTHTHRDHSPGAARLaertgapvraFGPHRAGGQDTDFAPDRPLAD----GEVIEGgGL 113

                        90
                ....*....|
gi 63025212 160 GLEVWATPGH 169
Cdd:cd16278 114 RLTVLHTPGH 123
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 78-169 1.15e-04

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: 42.34  E-value: 1.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  78 GPILVDTGGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLF---PGAALLVSHDF--CLPGGRYLP----HG 148
Cdd:cd16315  32 GHVLIDSGTEEAAPLVLANIRKLGFDPKDVRWLLSSHEHFDHVGGLAALqraTGARVAASAAAapVLESGKPAPddpqAG 111

                        90       100       110
                ....*....|....*....|....*....|....*
gi 63025212 149 -------------LGEGQPLRLGP-GLEVWATPGH 169
Cdd:cd16315 112 lhepfppvrvdriVEDGDTVALGSlRLTAHATPGH 146
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 77-126 4.52e-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: 39.55  E-value: 4.52e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 63025212  77 RGPILVDTGGPwAREaLLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLF 126
Cdd:cd07733  18 DGKLLIDAGLS-GRK-ITGRLAEIGRDPEDIDAILVTHEHADHIKGLGVL 65
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 78-134 5.23e-04

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


Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 40.30  E-value: 5.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  78 GPILVDTG--------------GPWAR---------EALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLFPGAALLVS 134
Cdd:cd07742  29 GLVLVDTGfgladvadpkrrlgGPFRRllrprldedETAVRQIEALGFDPSDVRHIVLTHLDLDHAGGLADFPHATVHVH 108
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 78-169 2.23e-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: 38.62  E-value: 2.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  78 GPILVDTGGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLF---PGAALLVSH--DFCLPGGRYLP------ 146
Cdd:cd16309  32 GHILIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAELkkaTGAQLVASAadKPLLESGYVGSgdtknl 111

                        90       100       110
                ....*....|....*....|....*....|..
gi 63025212 147 --------HGLGEGQPLRLGP-GLEVWATPGH 169
Cdd:cd16309 112 qfppvrvdRVIGDGDKVTLGGtTLTAHLTPGH 143
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 77-136 2.39e-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: 38.32  E-value: 2.39e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 63025212  77 RGPILVDTGGPWAR-EALLGALAGqgVAPGDVTLVVGTHGHSDHIGNLGLFPGA-ALLVSHD 136
Cdd:cd16282  24 DGVVVIDTGASPRLaRALLAAIRK--VTDKPVRYVVNTHYHGDHTLGNAAFADAgAPIIAHE 83
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 77-169 2.51e-03

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: 38.46  E-value: 2.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  77 RGPILVDTGGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLF---PGAALLVS------------HDFCL-- 139
Cdd:cd16288  31 QGLILIDTGLESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAALkklTGAKLMASaedaallasggkSDFHYgd 110

                        90       100       110
                ....*....|....*....|....*....|....*
gi 63025212 140 PGGRYLP----HGLGEGQPLRLGPG-LEVWATPGH 169
Cdd:cd16288 111 DSLAFPPvkvdRVLKDGDRVTLGGTtLTAHLTPGH 145
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 80-207 2.77e-03

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 38.34  E-value: 2.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  80 ILVDTGgPWAREALLGAlagqGVAPGDVTLVVGTHGHSDHIGNLGLF----------------PGAALL--VSHDFCLPG 141
Cdd:COG1235  47 LLIDAG-PDLREQLLRL----GLDPSKIDAILLTHEHADHIAGLDDLrprygpnpipvyatpgTLEALErrFPYLFAPYP 121

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 63025212 142 GRYLPHGLGEGQPLRLGpGLEVWATPGHGGQRDVSVVVAGTALGTVVVAGDVfeRDGDEDSWQALS 207
Cdd:COG1235 122 GKLEFHEIEPGEPFEIG-GLTVTPFPVPHDAGDPVGYRIEDGGKKLAYATDT--GYIPEEVLELLR 184
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 109-169 3.01e-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: 3.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212 109 LVVGTHGHSDHIGNLGLFP-------GAALLVSHD------------FCLPGGRYLPhgLGEGQPLRLGP-GLEVWATPG 168
Cdd:cd07712  45 LVVATHGHFDHIGGLHEFEevyvhpaDAEILAAPDnfetltwdaatySVPPAGPTLP--LRDGDVIDLGDrQLEVIHTPG 122


                .
gi 63025212 169 H 169
Cdd:cd07712 123 H 123
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 80-192 4.22e-03

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 37.59  E-value: 4.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  80 ILVDtggPW--AREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLFP----GAALLVSHDfclpGGRYLP------- 146
Cdd:COG2220  23 ILID---PVfsGRASPVNPLPLDPEDLPKIDAVLVTHDHYDHLDDATLRAlkrtGATVVAPLG----VAAWLRawgfprv 95

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 63025212 147 HGLGEGQPLRLGpGLEVWATPG-HGGQRD-------VSVVVAGTAlGTVVVAGD 192
Cdd:COG2220  96 TELDWGESVELG-GLTVTAVPArHSSGRPdrngglwVGFVIETDG-KTIYHAGD 147
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
80-151 4.58e-03

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 37.48  E-value: 4.58e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 63025212  80 ILVDTGgpwarEALLGALAGQGVAPGDVTLVVGTHGHSDHIgnLGLFPgaaLLVSHDFclpGGR------YLPHGLGE 151
Cdd:COG1234  31 LLIDCG-----EGTQRQLLRAGLDPRDIDAIFITHLHGDHI--AGLPG---LLSTRSL---AGRekpltiYGPPGTKE 95
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 78-123 5.05e-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: 37.66  E-value: 5.05e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 63025212  78 GPILVDTGGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNL 123
Cdd:cd16311  32 GHVLVDGGLPESAPKIIANIEALGFRIEDVKLILNSHGHIDHAGGL 77
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 78-169 6.03e-03

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: 37.18  E-value: 6.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  78 GPILVDTGGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLF------------PGAALLV------SHDFCL 139
Cdd:cd16314  32 GHILIDGGTDKAAPLIEANIRALGFRPEDVRYIVSSHEHFDHAGGIARLqratgapvvarePAATTLErgrsdrSDPQFL 111

                        90       100       110
                ....*....|....*....|....*....|....*
gi 63025212 140 PGGRYLPHG----LGEGQPLRLGP-GLEVWATPGH 169
Cdd:cd16314 112 VVEKFPPVAsvqrIGDGEVLRVGPlALTAHATPGH 146
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 91-169 6.63e-03

ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; MBL-fold metallo-hydrolase domain; Persulfide dioxygenase (PDO, also known as sulfur dioxygenase, SDO, EC 1.13.11.18) is a non-heme iron-dependent oxygenase which catalyzes the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria. Mutations in ethe1 (the human PDO gene) are responsible for a rare autosomal recessive metabolic disorder called ethylmalonic encephalopathy. Arabidopsis thaliana ETHE1 is essential for embryo and endosperm development. Bacterial ETHE1-type PDOs are also called Type 1 PDOs. Type II PDOs (also called PDOAs), are mainly proteobacterial. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293810 [Multi-domain]  Cd Length: 177  Bit Score: 36.61  E-value: 6.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  91 EALLGALAGQGVapgDVTLVVGTHGHSDHI---GNLGLFPGAALLVSHDfclPGGRYLPHGLGEGQPLRLG-PGLEVWAT 166
Cdd:cd07724  36 DRYLDLAAELGL---KITYVLETHVHADHVsgaRELAERTGAPIVIGEG---APASFFDRLLKDGDVLELGnLTLEVLHT 109


                ...
gi 63025212 167 PGH 169
Cdd:cd07724 110 PGH 112
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 ...
 78-169 9.19e-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: 36.56  E-value: 9.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 63025212  78 GPILVDTGGPWAREALLGALAGQGVAPGDVTLVVGTHGHSDHIGNLGLF------------PGAALL----VSHDFclPG 141
Cdd:cd16290  32 GLILIDGALPQSAPQIEANIRALGFRLEDVKLILNSHAHFDHAGGIAALqrdsgatvaaspAGAAALrsggVDPDD--PQ 109

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 63025212 142 GRYLPH--------GLGEGQPLRLGP-GLEVWATPGH 169
Cdd:cd16290 110 AGAADPfppvakvrVVADGEVVKLGPlAVTAHATPGH 146
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH