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Conserved domains on  [gi|2557100986|gb|WLB36399|]
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subclass B3 metallo-beta-lactamase BJP-1 [Bradyrhizobium diazoefficiens]

Protein Classification

subclass B3 metallo-beta-lactamase( domain architecture ID 10888865)

subclass B3 metallo-beta-lactamase, similar to Bradyrhizobium diazoefficiens BJP-1 which hydrolyzes the beta-lactam ring of a wide range of beta-lactam antibiotics

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 34-285 2.27e-164

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: 456.56  E-value: 2.27e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  34 WTAPFEPFQLIDNIYYVGTDGIAVYVIKTSQGLILMDTAMPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEI 113
Cdd:cd16309     1 WNEPMEPFKLIGNIYYVGTAGLGVFLITTPEGHILIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 114 KKETGAQLVAGERDKPLLEGGYY-PGDEKNedLAFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMTVKDG- 191
Cdd:cd16309    81 KKATGAQLVASAADKPLLESGYVgSGDTKN--LQFPPVRVDRVIGDGDKVTLGGTTLTAHLTPGHSPGCTSWTTTVKDTa 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 192 KEDREVLFFCSGTVALNRLVGQPTYAGIVDDYRATFAKAKAMKIDVLLGPHPEVYGMQAKRAEMKDGAPNPFIKPGELVT 271
Cdd:cd16309   159 GPPREVLFFCSATVAGNQLVGPPTYPGIVDDYRATFAKARAMKADVFLANHPEFFGLVAKRARQSAGEPDAFVDAGELQR 238

                         250
                  ....*....|....
gi 2557100986 272 YATSLSEDFDKQLA 285
Cdd:cd16309   239 FNTKMEDDFEKALA 252
 
Name Accession Description Interval E-value
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 34-285 2.27e-164

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: 456.56  E-value: 2.27e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  34 WTAPFEPFQLIDNIYYVGTDGIAVYVIKTSQGLILMDTAMPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEI 113
Cdd:cd16309     1 WNEPMEPFKLIGNIYYVGTAGLGVFLITTPEGHILIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 114 KKETGAQLVAGERDKPLLEGGYY-PGDEKNedLAFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMTVKDG- 191
Cdd:cd16309    81 KKATGAQLVASAADKPLLESGYVgSGDTKN--LQFPPVRVDRVIGDGDKVTLGGTTLTAHLTPGHSPGCTSWTTTVKDTa 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 192 KEDREVLFFCSGTVALNRLVGQPTYAGIVDDYRATFAKAKAMKIDVLLGPHPEVYGMQAKRAEMKDGAPNPFIKPGELVT 271
Cdd:cd16309   159 GPPREVLFFCSATVAGNQLVGPPTYPGIVDDYRATFAKARAMKADVFLANHPEFFGLVAKRARQSAGEPDAFVDAGELQR 238

                         250
                  ....*....|....
gi 2557100986 272 YATSLSEDFDKQLA 285
Cdd:cd16309   239 FNTKMEDDFEKALA 252
B3_Acin_new1 NF033184
putative subclass B3 metallo-beta-lactamase; This is one of two families of putative ...
 11-284 8.77e-71

putative subclass B3 metallo-beta-lactamase; This is one of two families of putative metallo-beta-lactamases of subclass B3 that are restricted to the genus Acinetobacter, and undescribed as of January 2017.


Pssm-ID: 439394  Cd Length: 283  Bit Score: 220.37  E-value: 8.77e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  11 LTLLSTGAQAQTIKDflavamkKWTAPFEPFQLIDNIYYVGTDGIAVYVIKTSQGLILMDTAMPQSTGMIKDNIAKLGFK 90
Cdd:NF033184   12 LTSLSTSAAPLKLPD-------DWTQNTQPFQITENIYYVGTHGLAAYLLASGHQALLIDTGLPENTEQIEQNIKQLGFK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  91 VADIKLILNTHAHLDHTGGFAEIKKETGAQLVAGERDKPLLEGGYYPGDEKNEDLAFPAVKVDRAVKEGDRVTLGDTTLT 170
Cdd:NF033184   85 LSDVKIMVTSHAHWDHVGALARIKQDTGAKLIAMQQDVKALEIGKPIGENTFQTIPFTPVKVDKVIHDGEVVKLGKFKLK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 171 AHATPGHSPGCTSWEMTVKDGKEDREVLFFCSGTVALNRLVGQPTYAGIVDDYRATFAKAKAMKIDVLLGPHPEVYGMQA 250
Cdd:NF033184  165 ATLTPGHTPGCTTWSTEVKSNGKNLNVVFPCSLSVAGNVLQNNHQYPNIVADYRKSFERLKNMKADIVLTSHPEVADVLG 244

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2557100986 251 KRAEMKDGAPNPFIKPGELVTYATSLSEDFDKQL 284
Cdd:NF033184  245 NKARKDAGQTNAFIQPEKLSSIVKDAEMAFEKSL 278
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 47-264 6.19e-37

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: 130.97  E-value: 6.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  47 IYYVGT------DGIAVYVIKTSQGLILMDTAM-PQSTGMIKDNIAKLGfkvADIKLILNTHAHLDHTGGFAEIKKETGA 119
Cdd:COG0491     1 VYVLPGgtpgagLGVNSYLIVGGDGAVLIDTGLgPADAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFGA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 120 QLVAGERDKPLLEggyypGDEKNEDLAFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMtvkdgkEDREVLF 199
Cdd:COG0491    78 PVYAHAAEAEALE-----APAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV------PDEKVLF 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2557100986 200 fcSGTVALNRLVGQPTYAGI-VDDYRATFAKAKAMKIDVLLGPHPEVYGMQAKRAEMKDGA-----PNPFI 264
Cdd:COG0491   147 --TGDALFSGGVGRPDLPDGdLAQWLASLERLLALPPDLVIPGHGPPTTAEAIDYLEELLAalgerANPFL 215
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 57-242 7.17e-31

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: 113.80  E-value: 7.17e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986   57 VYVIKTSQGLILMDTAMPQSTGMIKDnIAKLGfkVADIKLILNTHAHLDHTGGFAEIKKETGAQLVAGERDKPLLEGGYY 136
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDLLAE-LKKLG--PKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  137 pgDEKNEDLAFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMtvkdgkEDREVLFF-CSGTVALNRLVGQPT 215
Cdd:smart00849  79 --LLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL------PEGKILFTgDLLFAGGDGRTLVDG 150

                          170       180
                   ....*....|....*....|....*..
gi 2557100986  216 YAGIVDDYRATFAKAKAMKIDVLLGPH 242
Cdd:smart00849 151 GDAAASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
50-242 1.77e-23

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 94.74  E-value: 1.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  50 VGTDGIAVYVIKTSQGLILMDTAMPQSTGMIKDnIAKLGFKVADIKLILNTHAHLDHTGGFAEIKKETGAQLVAGERDKP 129
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLLL-LAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 130 LLEGGY---YPGDEKNEDLAFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMtvkdgkEDREVLF------- 199
Cdd:pfam00753  80 ELLDEElglAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYY------GGGKVLFtgdllfa 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2557100986 200 FCSGTVALNRLVGQPTYAGIVDDYRATFAKAKAMKIDVLLGPH 242
Cdd:pfam00753 154 GEIGRLDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 97-184 6.24e-08

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 52.92  E-value: 6.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  97 ILNTHAHLDHTGGFAEIKKETGAQLVAGERDKPLLEGgyypgdeknedlafpavkVDRAVKEGDRVTLGDTTLTAHATPG 176
Cdd:PLN02398  125 ILNTHHHYDHTGGNLELKARYGAKVIGSAVDKDRIPG------------------IDIVLKDGDKWMFAGHEVLVMETPG 186


                  ....*...
gi 2557100986 177 HSPGCTSW 184
Cdd:PLN02398  187 HTRGHISF 194
 
Name Accession Description Interval E-value
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 34-285 2.27e-164

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: 456.56  E-value: 2.27e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  34 WTAPFEPFQLIDNIYYVGTDGIAVYVIKTSQGLILMDTAMPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEI 113
Cdd:cd16309     1 WNEPMEPFKLIGNIYYVGTAGLGVFLITTPEGHILIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 114 KKETGAQLVAGERDKPLLEGGYY-PGDEKNedLAFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMTVKDG- 191
Cdd:cd16309    81 KKATGAQLVASAADKPLLESGYVgSGDTKN--LQFPPVRVDRVIGDGDKVTLGGTTLTAHLTPGHSPGCTSWTTTVKDTa 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 192 KEDREVLFFCSGTVALNRLVGQPTYAGIVDDYRATFAKAKAMKIDVLLGPHPEVYGMQAKRAEMKDGAPNPFIKPGELVT 271
Cdd:cd16309   159 GPPREVLFFCSATVAGNQLVGPPTYPGIVDDYRATFAKARAMKADVFLANHPEFFGLVAKRARQSAGEPDAFVDAGELQR 238

                         250
                  ....*....|....
gi 2557100986 272 YATSLSEDFDKQLA 285
Cdd:cd16309   239 FNTKMEDDFEKALA 252
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 34-278 3.61e-149

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: 417.72  E-value: 3.61e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  34 WTAPFEPFQLIDNIYYVGTDGIAVYVIKTSQGLILMDTAMPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEI 113
Cdd:cd07708     1 WPNPFPPFQIAGNTYYVGTDDLAAYLIVTPQGNILIDGDMEQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 114 KKETGAQLVAGERDKPLLEGGY--YPGDEKNEDLAFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMTVKDG 191
Cdd:cd07708    81 KKQTGAKVMAGAEDVSLLLSGGssDFHYANDSSTYFPQSTVDRAVHDGERVTLGGTVLTAHATPGHTPGCTTWTMTLKDH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 192 KEDREVLFFCSGTVAL-NRLVGQPTYAGIVDDYRATFAKAKAMKIDVLLGPHPEVYGMQAKRAEMKDGAPNPFIKPGELV 270
Cdd:cd07708   161 GKQYQVVFADSLTVNPgYRLVDNPTYPKIVEDYRHSFAVVEAMRCDILLGPHPGVFDMKNKYVLLSKGQNNPFVDPGGCK 240


                  ....*...
gi 2557100986 271 TYATSLSE 278
Cdd:cd07708   241 AYAEAKAN 248
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 34-285 9.51e-139

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: 391.68  E-value: 9.51e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  34 WTAPFEPFQLIDNIYYVGTDGIAVYVIKTSQGLILMDTAMPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEI 113
Cdd:cd16288     1 WNAPFEPFRIAGNVYYVGTSGLASYLITTPQGLILIDTGLESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 114 KKETGAQLVAGERDKPLLEGG----YYPGDEKnedLAFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMTVK 189
Cdd:cd16288    81 KKLTGAKLMASAEDAALLASGgksdFHYGDDS---LAFPPVKVDRVLKDGDRVTLGGTTLTAHLTPGHTRGCTTWTMTVK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 190 DGKEDREVLFFCSGTVAL-NRLVGQPTYAGIVDDYRATFAKAKAMKIDVLLGPHPEVYGMQAKRAEMKDGAPNPFIKPGE 268
Cdd:cd16288   158 DDGKVYQVVFADSLTVNPgYKLVGNPTYPGIAEDYRHSFATLRALQCDIFLASHAEYFDLKEKRARLAAGQPNAFIDPEG 237

                         250
                  ....*....|....*..
gi 2557100986 269 LVTYATSLSEDFDKQLA 285
Cdd:cd16288   238 YRNFIEKAKADFEKQLA 254
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 34-285 1.77e-105

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


Pssm-ID: 293868  Cd Length: 252  Bit Score: 307.45  E-value: 1.77e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  34 WTAPFEPFQLIDNIYYVGTDGIAVYVIKTSQGLILMDTAMPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEI 113
Cdd:cd16310     1 WTAPTEPFRIVDNIYYVGTKGIGSYLITSNHGAILLDGGLEENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 114 KKETGAQLVAGERDKPLLEGGYYPGDEKNEDLAFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMTVKDGKE 193
Cdd:cd16310    81 KADTGAKLWASRGDRPALEAGKHIGDNITQPAPFPAVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTWSTTVKENGR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 194 DREVLFFCSGTVALNRLVGQPTYAGIVDDYRATFAKAKAMKIDVLLGPHPEVYGMQAKRAEMKDGAPNPFIKPGELVTYA 273
Cdd:cd16310   161 PLRVVFPCSLSVAGNVLVGNKTYPTIVEDYRASFARLRAMKADIVLTSHPEVADLLARKAKQDAGQANAFVDPGELARIV 240

                         250
                  ....*....|..
gi 2557100986 274 TSLSEDFDKQLA 285
Cdd:cd16310   241 DQSEAAFNKELA 252
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 34-285 1.45e-76

Fluoribacter gormanii FEZ-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 FEZ-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: 293865  Cd Length: 255  Bit Score: 233.88  E-value: 1.45e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  34 WTAPFEPFQLIDNIYYVGTDGIAVYVIKTSQGLILMDTAMPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEI 113
Cdd:cd16307     1 WTTPFPPFRIAGNLYYVGSRDLASYLITTPRGNILINSNLESSVPQIKASIEKLGFKFSDTKILLISHAHFDHAAGSALI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 114 KKETGAQLVAGERDKPLLEGG----YYPGDEKneDLAFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMTVK 189
Cdd:cd16307    81 KRETHAKYMVMDGDVDVVESGgksdFFYGNDP--STYFPPAHVDKVLHDGEQVELGGTVLTAHLTAGHTKGCTTWTMKVK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 190 DGKEDREVLFFCSGTV-ALNRLVGQPTYAGIVDDYRATFAKAKAMKIDVLLGPHPEVYGMQAKRAEMKDGAPNPFIKPGE 268
Cdd:cd16307   159 DHGKTYDVVIVGSPNVnPGAKLVNNITYPGIAEDYAHTFAVLRSLPCDIFLGAHGGYFDLKNKYVRLQKGGANPFIDPEG 238

                         250
                  ....*....|....*..
gi 2557100986 269 LVTYATSLSEDFDKQLA 285
Cdd:cd16307   239 YKAYVAEKEQAFRTELE 255
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 ...
 34-286 7.78e-74

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: 226.85  E-value: 7.78e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  34 WTAPFEPFQLIDNIYYVGTDGIAVYVIKTSQGLILMDTAMPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEI 113
Cdd:cd16290     1 WNQPQAPFRIHGNTYYVGTGGLSAVLITSPQGLILIDGALPQSAPQIEANIRALGFRLEDVKLILNSHAHFDHAGGIAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 114 KKETGAQLVAGERDKPLLE-GGYYPGDEKNEDL-AFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMTVKDG 191
Cdd:cd16290    81 QRDSGATVAASPAGAAALRsGGVDPDDPQAGAAdPFPPVAKVRVVADGEVVKLGPLAVTAHATPGHTPGGTSWTWRSCEG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 192 KEDREVLFFCS-GTVALNRL-VGQPTYAGIVDDYRATFAKAKAMKIDVLLGPHPEVYGMQAKRAEM-KDGAPNPFIKPGE 268
Cdd:cd16290   161 GRCLDIVYADSlTAVSADGFrFSDDAHPARVAAFRRSIATVAALPCDILISAHPDASGLWEKLARRaREPGPNPFIDPNA 240

                         250
                  ....*....|....*...
gi 2557100986 269 LVTYAtslsEDFDKQLAK 286
Cdd:cd16290   241 CRAYA----AAAEARLEA 254
B3_Acin_new1 NF033184
putative subclass B3 metallo-beta-lactamase; This is one of two families of putative ...
 11-284 8.77e-71

putative subclass B3 metallo-beta-lactamase; This is one of two families of putative metallo-beta-lactamases of subclass B3 that are restricted to the genus Acinetobacter, and undescribed as of January 2017.


Pssm-ID: 439394  Cd Length: 283  Bit Score: 220.37  E-value: 8.77e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  11 LTLLSTGAQAQTIKDflavamkKWTAPFEPFQLIDNIYYVGTDGIAVYVIKTSQGLILMDTAMPQSTGMIKDNIAKLGFK 90
Cdd:NF033184   12 LTSLSTSAAPLKLPD-------DWTQNTQPFQITENIYYVGTHGLAAYLLASGHQALLIDTGLPENTEQIEQNIKQLGFK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  91 VADIKLILNTHAHLDHTGGFAEIKKETGAQLVAGERDKPLLEGGYYPGDEKNEDLAFPAVKVDRAVKEGDRVTLGDTTLT 170
Cdd:NF033184   85 LSDVKIMVTSHAHWDHVGALARIKQDTGAKLIAMQQDVKALEIGKPIGENTFQTIPFTPVKVDKVIHDGEVVKLGKFKLK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 171 AHATPGHSPGCTSWEMTVKDGKEDREVLFFCSGTVALNRLVGQPTYAGIVDDYRATFAKAKAMKIDVLLGPHPEVYGMQA 250
Cdd:NF033184  165 ATLTPGHTPGCTTWSTEVKSNGKNLNVVFPCSLSVAGNVLQNNHQYPNIVADYRKSFERLKNMKADIVLTSHPEVADVLG 244

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2557100986 251 KRAEMKDGAPNPFIKPGELVTYATSLSEDFDKQL 284
Cdd:NF033184  245 NKARKDAGQTNAFIQPEKLSSIVKDAEMAFEKSL 278
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 34-284 7.01e-69

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: 214.14  E-value: 7.01e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  34 WTAPFEPFQLIDNIYYVGTDGIAVYVIKTSQGLILMDTAMPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEI 113
Cdd:cd16315     1 WDKPAPPARIFGNTYYVGTCGISAILITGDDGHVLIDSGTEEAAPLVLANIRKLGFDPKDVRWLLSSHEHFDHVGGLAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 114 KKETGAQLVAGERDKPLLEGGY-YPGDEKNEDL-AFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMTVKDG 191
Cdd:cd16315    81 QRATGARVAASAAAAPVLESGKpAPDDPQAGLHePFPPVRVDRIVEDGDTVALGSLRLTAHATPGHTPGALSWTWRSCEG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 192 KEDREVLFFCS-GTVALN--RLVGQPTYagiVDDYRATFAKAKAMKIDVLLGPHPEVYGMqakRAEMKDGApnPFIKPGE 268
Cdd:cd16315   161 ADCRTIVYADSlSPVSADgyRFSDHPDY---VAAYRAGLAKVAALPCDILLTPHPSASDM---FERLSGGA--PLADPDA 232

                         250
                  ....*....|....*.
gi 2557100986 269 LVTYATSLSEDFDKQL 284
Cdd:cd16315   233 CAAYAAGAEKRLDERL 248
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 34-294 8.99e-65

Elizabethkingia meningoseptica GOB-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 GOB-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: 293866 [Multi-domain]  Cd Length: 254  Bit Score: 203.86  E-value: 8.99e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  34 WTAPFEPFQLIDNIYYVGTDGIAVYVIKTSQGLILMDTAMPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEI 113
Cdd:cd16308     1 WSQPYAPFRIAGNLYYVGTYDLACYLIVTPKGNILINTGLAESVPLIKKNIQALGFKFKDIKILLTTQAHYDHVGAMAAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 114 KKETGAQLVAGERDKPLLEGG----YYPGdekNEDLAFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMTVK 189
Cdd:cd16308    81 KQQTGAKMMVDEKDAKVLADGgksdYEMG---GYGSTFAPVKADKLLHDGDTIKLGGTKLTLLHHPGHTKGSCSFLFDVK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 190 DGKEDREVLFFCSGTVALNR-LVGQPTYAGIVDDYRATFAKAKAMKIDVLLGPHPEVYGMQAKRaemKDGAPnpfIKPGE 268
Cdd:cd16308   158 DEKRTYRVLIANMPTILPDTkLSGMPGYPGIAKDYAYTFEAMKALSFDIWLASHASQFDLHQKH---KPGAP---YNPAA 231

                         250       260
                  ....*....|....*....|....*.
gi 2557100986 269 LVTYAtslseDFDKQLAKQTAALEKK 294
Cdd:cd16308   232 FADRA-----GYDKALAGLEKSYDKK 252
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 34-247 3.75e-64

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: 201.58  E-value: 3.75e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  34 WTAPFEPFQLIDNIYYVGTDGIAVYVIKTSQGLILMDTAMPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEI 113
Cdd:cd16289     1 WLQPMAPLQIADHTWYIGTESLTALLVKTPDGAVLLDGGMPQAADMLLDNMRALGVAPGDLKLILHSHAHADHAGPLAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 114 KKETGAQLVAGERDKPLLEGGYYPGDEKNEDLAFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMT-VKDGK 192
Cdd:cd16289    81 KRATGARVAANAESAVLLARGGSDDIHFGDGITFPPVQADRIVMDGEVVTLGGVTFTAHFTPGHTPGSTSWTWTdTRDGK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2557100986 193 EDReVLFFCSGTVALNRLVGQPTYAGIVDDYRATFAKAKAMKIDVLLGPHPEVYG 247
Cdd:cd16289   161 PVR-IAYADSLSAPGYQLLGNPRYPRIVEDYRRTFATVRALPCDVLLTPHPGASG 214
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 34-285 7.69e-63

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: 198.58  E-value: 7.69e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  34 WTAPFEPFQLIDNIYYVGTDGIAVYVIKTSQGLILMDTA-MPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAE 112
Cdd:cd16280     1 KKGYVEPFQVFDNLYYVGNKWVSAWAIDTGDGLILIDALnNNEAADLIVDGLEKLGLDPADIKYILITHGHGDHYGGAAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 113 IKKETGAQLVAGERDKPLLEGgyyPGDEKNEDLAFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMTVKD-G 191
Cdd:cd16280    81 LKDLYGAKVVMSEADWDMMEE---PPEEGDNPRWGPPPERDIVIKDGDTLTLGDTTITVYLTPGHTPGTLSLIFPVKDgG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 192 KEDREVLFfcsGTVALNRLVGQPtyagIVDDYRATFAK----AKAMKIDVLLGPHPEVYGMQAKRAEM---KDGAPNPFI 264
Cdd:cd16280   158 KTHRAGLW---GGTGLNTGPNLE----RREQYIASLERfkkiAEEAGVDVFLSNHPFQDGSLEKREALrnrKPGEPNPFV 230

                         250       260
                  ....*....|....*....|.
gi 2557100986 265 KPGELVTYATSLSEDFDKQLA 285
Cdd:cd16280   231 DGQAWVDFYDEVLALCARVLA 251
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 34-285 1.18e-56

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


Pssm-ID: 293870 [Multi-domain]  Cd Length: 258  Bit Score: 183.26  E-value: 1.18e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  34 WTAPFEPFQLIDNIYYVGTDGIAVYVIKTSQGLILMDTAMPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEI 113
Cdd:cd16312     1 WNQPVKPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIEALGFRIEDVKLILNSHAHWDHAGGIAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 114 KKETGAQLVAGERDKPLLEGGyYPGDEKNEDLAFPAVKVDRA-----VKEGDRVTLGDTTLTAHATPGHSPGCTSWEMTV 188
Cdd:cd16312    81 QKASGATVAASAHGAQVLQSG-TNGKDDPQYQAKPVVHVAKVakvkeVGEGDTLKVGPLRLTAHMTPGHTPGGTTWTWTS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 189 KDGKEDREVLFFCSGTVALN---RLVGQPTYAGIVDDYRATFAKAKAMKIDVLLGPHPEVYGMQAKrAEMKDGAPNPFIK 265
Cdd:cd16312   160 CEGQRCLDVVYADSLNPYSSgdfYYTGKGGYPDISASFRASIAKVAALPCDIIIAVHPGFTDVLDK-AKRRSGDTNPFID 238

                         250       260
                  ....*....|....*....|
gi 2557100986 266 PGELVTYATSLSEDFDKQLA 285
Cdd:cd16312   239 AEACRAYAAGAAKSLEKRLA 258
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 34-285 8.41e-56

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


Pssm-ID: 293871 [Multi-domain]  Cd Length: 254  Bit Score: 180.83  E-value: 8.41e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  34 WTAPFEPFQLIDNIYYVGTDGIAVYVIKTSQGLILMDTAMPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEI 113
Cdd:cd16313     1 WNAPQEPFQIYGNTYYVGTGGISAVLITSPQGHILIDGGFPKSPEQIAASIRQLGFKLEDVKYILSSHDHWDHAGGIAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 114 KKETGAQLVAGERDKPLLEGGYYPGDEKN--EDLAFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMTVKDG 191
Cdd:cd16313    81 QKLTGAQVLASPATVAVLRSGSMGKDDPQfgGLTPMPPVASVRAVRDGEVVKLGPLAVTAHATPGHTTGGTSWTWQSCEQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 192 KEDREVLFFCSGT-VALN--RLVGQPTyagIVDDYRATFAKAKAMKIDVLLGPHPEVYGMQAKRAEMKDGAPNPFIKPGE 268
Cdd:cd16313   161 GRCANMVFADSLTaVSADgyRFSAHPA---VLADVEQSIAAVEKLACDILVSAHPEFSDMWTRVKRGAAEGNAAFIDGGG 237

                         250
                  ....*....|....*..
gi 2557100986 269 LVTYATSLSEDFDKQLA 285
Cdd:cd16313   238 CRAYAAKAREKLNKRLA 254
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 34-285 1.89e-51

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: 169.78  E-value: 1.89e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  34 WTAPFEPFQLIDNIYYVGTDGIAVYVIKTSQGLILMDTAMPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEI 113
Cdd:cd16311     1 WNADQAPFRIFGNTYYVGVKGLSSVLVTSPQGHVLVDGGLPESAPKIIANIEALGFRIEDVKLILNSHGHIDHAGGLAEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 114 KKETGAQLVA---GERDkpLLEGGYYPGDEKNEDL-AFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMTVK 189
Cdd:cd16311    81 QRRSGALVAAspsAALD--LASGEVGPDDPQYHALpKYPPVKDMRLARDGGQFNVGPVSLTAHATPGHTPGGLSWTWQSC 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 190 DGKEDREVLFFCSGTvALNR----LVGQPTYAGIVDDYRATFAKAKAMKIDVLLGPHPEVYGMQAKRAEMKDGAPNPFIK 265
Cdd:cd16311   159 DGPRCLNMVYADSQN-AVSRpgfkFSASSEYPNAVADLRRSFETLEKLPCDVLISAHPEASQLWERLEASDRSARPALVD 237

                         250       260
                  ....*....|....*....|
gi 2557100986 266 PGELVTYATSLSEDFDKQLA 285
Cdd:cd16311   238 REACRRYASRAREALEKRIA 257
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 34-289 5.16e-44

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: 150.43  E-value: 5.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  34 WTAPFEPFQLIDNIYYVGTDGIAVYVIKTSQGLILMDTAMPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEI 113
Cdd:cd16314     1 WDDPAPPRRIYGNTWYVGTCGISALLVTSDAGHILIDGGTDKAAPLIEANIRALGFRPEDVRYIVSSHEHFDHAGGIARL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 114 KKETGAQLVAGERDKPLLEGGyYPG--DEKNEDLA-FPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMTVKD 190
Cdd:cd16314    81 QRATGAPVVAREPAATTLERG-RSDrsDPQFLVVEkFPPVASVQRIGDGEVLRVGPLALTAHATPGHTPGGTSWTWRSCE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 191 GKEDREVLFFCSGTVALNRLVGQPTYAGIVDDYRATFAKAKAMKIDVLLGPHPEVYGMQAKRAemKDGAPnPFIKPGELV 270
Cdd:cd16314   160 GAVCRDMVYADSVTAISDDIYRYSDHPGMVAAFRNTLDTVAALPCDILVTPHPSASGLWERLG--PAAGI-PLADTGACR 236

                         250
                  ....*....|....*....
gi 2557100986 271 TYATSLSEDFDKQLAKQTA 289
Cdd:cd16314   237 AYAQTGRARLDARLADEAA 255
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 47-264 6.19e-37

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: 130.97  E-value: 6.19e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  47 IYYVGT------DGIAVYVIKTSQGLILMDTAM-PQSTGMIKDNIAKLGfkvADIKLILNTHAHLDHTGGFAEIKKETGA 119
Cdd:COG0491     1 VYVLPGgtpgagLGVNSYLIVGGDGAVLIDTGLgPADAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFGA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 120 QLVAGERDKPLLEggyypGDEKNEDLAFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMtvkdgkEDREVLF 199
Cdd:COG0491    78 PVYAHAAEAEALE-----APAAGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV------PDEKVLF 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2557100986 200 fcSGTVALNRLVGQPTYAGI-VDDYRATFAKAKAMKIDVLLGPHPEVYGMQAKRAEMKDGA-----PNPFI 264
Cdd:COG0491   147 --TGDALFSGGVGRPDLPDGdLAQWLASLERLLALPPDLVIPGHGPPTTAEAIDYLEELLAalgerANPFL 215
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 46-183 6.53e-36

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: 127.72  E-value: 6.53e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  46 NIYYV-GTDGIAVYVIKTSQGLILMDTAMPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEIKKETGAQLVAG 124
Cdd:cd07721     1 GVYQLpLLPPVNAYLIEDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYAH 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2557100986 125 ERDKPLLEGGY-YPGDEKNEDLAF-------PAVKVDRAVKEGDRVTLGDtTLTAHATPGHSPGCTS 183
Cdd:cd07721    81 EREAPYLEGEKpYPPPVRLGLLGLlspllpvKPVPVDRTLEDGDTLDLAG-GLRVIHTPGHTPGHIS 146
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 57-242 7.17e-31

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: 113.80  E-value: 7.17e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986   57 VYVIKTSQGLILMDTAMPQSTGMIKDnIAKLGfkVADIKLILNTHAHLDHTGGFAEIKKETGAQLVAGERDKPLLEGGYY 136
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDLLAE-LKKLG--PKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  137 pgDEKNEDLAFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMtvkdgkEDREVLFF-CSGTVALNRLVGQPT 215
Cdd:smart00849  79 --LLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL------PEGKILFTgDLLFAGGDGRTLVDG 150

                          170       180
                   ....*....|....*....|....*..
gi 2557100986  216 YAGIVDDYRATFAKAKAMKIDVLLGPH 242
Cdd:smart00849 151 GDAAASDALESLLKLLKLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 57-199 1.28e-25

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: 100.44  E-value: 1.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  57 VYVIKTSQG-LILMDTAMPqSTGMIKDNIAKLGFKvadIKLILNTHAHLDHTGGFAEIKKETGAQLVAGERDKPLLEGGY 135
Cdd:cd06262    12 CYLVSDEEGeAILIDPGAG-ALEKILEAIEELGLK---IKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAELLEDPE 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2557100986 136 YPGDEkNEDLAFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMtvkdgkEDREVLF 199
Cdd:cd06262    88 LNLAF-FGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYI------EEEGVLF 144
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
50-242 1.77e-23

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 94.74  E-value: 1.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  50 VGTDGIAVYVIKTSQGLILMDTAMPQSTGMIKDnIAKLGFKVADIKLILNTHAHLDHTGGFAEIKKETGAQLVAGERDKP 129
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLLL-LAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 130 LLEGGY---YPGDEKNEDLAFPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMtvkdgkEDREVLF------- 199
Cdd:pfam00753  80 ELLDEElglAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYY------GGGKVLFtgdllfa 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2557100986 200 FCSGTVALNRLVGQPTYAGIVDDYRATFAKAKAMKIDVLLGPH 242
Cdd:pfam00753 154 GEIGRLDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 43-242 3.11e-20

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: 86.39  E-value: 3.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  43 LIDnIYYVGTDG-IAVYVIKTSQGLILMDTAMPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEI-KKETGAQ 120
Cdd:cd07726     4 LID-LGFLGFPGrIASYLLDGEGRPALIDTGPSSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLaEALPNAK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 121 LVAGERDKP-------LLEGG---YypGDEkNEDLAFPAVKVD----RAVKEGDRVTLGDTTLTAHATPGHSPGctswEM 186
Cdd:cd07726    83 VYVHPRGARhlidpskLWASAravY--GDE-ADRLGGEILPVPeervIVLEDGETLDLGGRTLEVIDTPGHAPH----HL 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2557100986 187 TVKDGKEDreVLFfcSGTVALNRLVGQPTYAGI--------VDDYRATFAKAKAMKIDVLLGPH 242
Cdd:cd07726   156 SFLDEESD--GLF--TGDAAGVRYPELDVVGPPstpppdfdPEAWLESLDRLLSLKPERIYLTH 215
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 55-180 1.94e-19

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: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 84.12  E-value: 1.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  55 IAVYVIKtSQGLILMDTAMPQSTG-MIKDNIAKLGFKvadIKLILNTHAHLDHTGGFAEIKKETGAQLVAGERDKPLLE- 132
Cdd:cd07743    10 IGVYVFG-DKEALLIDSGLDEDAGrKIRKILEELGWK---LKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAFIEn 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2557100986 133 ---------GGYYPGDEKNEDLAFPAVKVDRAVKEGDrVTLGDTTLTAHATPGHSPG 180
Cdd:cd07743    86 pllepsylgGAYPPKELRNKFLMAKPSKVDDIIEEGE-LELGGVGLEIIPLPGHSFG 141
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 84-184 2.07e-19

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: 83.22  E-value: 2.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  84 IAKLGFKvadIKLILNTHAHLDHTGGFAEIKKETGAQLVAGERDkplleggyypgdeknedlafPAVKVDRAVKEGDRVT 163
Cdd:cd07724    42 AAELGLK---ITYVLETHVHADHVSGARELAERTGAPIVIGEGA--------------------PASFFDRLLKDGDVLE 98

                          90       100
                  ....*....|....*....|.
gi 2557100986 164 LGDTTLTAHATPGHSPGCTSW 184
Cdd:cd07724    99 LGNLTLEVLHTPGHTPESVSY 119
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 84-180 9.21e-19

uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized Thermus thermophilus TTHA1623 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. This family includes homologs present in a wide range of bacteria and archaea and some eukaryota. Members of the MBL-fold metallo-hydrolase superfamily exhibit a variety of active site metallo-chemistry, TTHA1623 exhibiting a uniquely shaped putative substrate-binding pocket with a glyoxalase II-type metal-coordination mode.


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 82.40  E-value: 9.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  84 IAKLGFKVADIKLILNTHAHLDHTGGFAEIKKETGAQLVAGERDKPLLEGgyYPGDEKNEDL-AFPAVKVDRAVKEGDRV 162
Cdd:cd16322    37 LARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDLPLYEA--ADLGAKAFGLgIEPLPPPDRLLEDGQTL 114

                          90
                  ....*....|....*...
gi 2557100986 163 TLGDTTLTAHATPGHSPG 180
Cdd:cd16322   115 TLGGLEFKVLHTPGHSPG 132
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 57-245 4.26e-18

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: 80.04  E-value: 4.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  57 VYVIKTSQGLILMDTAM--PQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEIKKETGAQLVAGErdkpllegg 134
Cdd:cd07725    17 VYLLRDGDETTLIDTGLatEEDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGATVYILD--------- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 135 yypgdeknedlafpavkvDRAVKEGDRVTLGDTTLTAHATPGHSPGctswEMTVKDgkEDREVLFfcSGTVALNRL---V 211
Cdd:cd07725    88 ------------------VTPVKDGDKIDLGGLRLKVIETPGHTPG----HIVLYD--EDRRELF--VGDAVLPKItpnV 141

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2557100986 212 G--QPTYAGIVDDYRATFAKAKAMKIDVLLGPHPEV 245
Cdd:cd07725   142 SlwAVRVEDPLGAYLESLDKLEKLDVDLAYPGHGGP 177
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 84-180 9.47e-17

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: 75.96  E-value: 9.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  84 IAKLGFKvadIKLILNTHAHLDHTGGFAEIKKETG-AQLVAGERDKPlleggyyPGdeknedlafpavkVDRAVKEGDRV 162
Cdd:cd07723    37 LEKNGLT---LTAILTTHHHWDHTGGNAELKALFPdAPVYGPAEDRI-------PG-------------LDHPVKDGDEI 93

                          90
                  ....*....|....*...
gi 2557100986 163 TLGDTTLTAHATPGHSPG 180
Cdd:cd07723    94 KLGGLEVKVLHTPGHTLG 111
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 55-183 5.35e-15

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: 72.63  E-value: 5.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  55 IAVYVIKTSQGLILMDTAMPQSTG------------------MIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEIKke 116
Cdd:cd07729    32 VYAYLIEHPEGTILVDTGFHPDAAddpgglelafppgvteeqTLEEQLARLGLDPEDIDYVILSHLHFDHAGGLDLFP-- 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2557100986 117 tGAQLVAGERDkplLEGGYYPgDEKNEDLAFPAVKVDRAVKEGDRVTL-GDTTL----TAHATPGHSPGCTS 183
Cdd:cd07729   110 -NATIIVQRAE---LEYATGP-DPLAAGYYEDVLALDDDLPGGRVRLVdGDYDLfpgvTLIPTPGHTPGHQS 176
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 80-180 7.24e-15

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


Pssm-ID: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 71.43  E-value: 7.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  80 IKDNIAKLGFKVadiKLILNTHAHLDHTGGFAEIKKETGAQLVA-GERDKPLLEGGyypgDEKNEDLAFP---AVKVDRA 155
Cdd:cd07737    36 ILQAIEDLGLTL---KKILLTHGHLDHVGGAAELAEHYGVPIIGpHKEDKFLLENL----PEQSQMFGFPpaeAFTPDRW 108

                          90       100
                  ....*....|....*....|....*
gi 2557100986 156 VKEGDRVTLGDTTLTAHATPGHSPG 180
Cdd:cd07737   109 LEEGDTVTVGNLTLEVLHCPGHTPG 133
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 92-239 2.50e-14

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 69.83  E-value: 2.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  92 ADIKLILNTHAHLDHTGGFAEIKKETGAQLVAgerdkplleggYYPGDEKNEDLAFPAvkvDRAVKEGDRVTLGDTTLTA 171
Cdd:cd16278    52 GRVSAILVTHTHRDHSPGAARLAERTGAPVRA-----------FGPHRAGGQDTDFAP---DRPLADGEVIEGGGLRLTV 117

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2557100986 172 HATPGHSPG--CTSWemtvkdgkEDREVLFfcSGTVALNR---LVGQPtyAGIVDDYRATFAKAKAMKIDVLL 239
Cdd:cd16278   118 LHTPGHTSDhlCFAL--------EDEGALF--TGDHVMGWsttVIAPP--DGDLGDYLASLERLLALDDRLLL 178
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 67-242 1.38e-12

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: 64.96  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  67 ILMDTAMPQSTgmIKDNIAKLGFKVAdikLILNTHAHLDHTGG---FAEIkketgaqlVAGERDKPLLEGGYypGDEKNE 143
Cdd:cd07712    21 LLIDTGLGIGD--LKEYVRTLTDLPL---LVVATHGHFDHIGGlheFEEV--------YVHPADAEILAAPD--NFETLT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 144 DLA----FPAVKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTS-WEmtvkdgkEDREVLF----FCSGTVALNRlvgqp 214
Cdd:cd07712    86 WDAatysVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIAlLD-------RANRLLFsgdvVYDGPLIMDL----- 153

                         170       180       190
                  ....*....|....*....|....*....|
gi 2557100986 215 tYAGIVDDYRATFAKAKAMK--IDVLLGPH 242
Cdd:cd07712   154 -PHSDLDDYLASLEKLSKLPdeFDKVLPGH 182
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 59-238 1.06e-11

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: 62.97  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  59 VIKTSQGLILMDTAM-PQSTGMIKDNIAKLGFKvaDIKLILNTHAHLDHTGG---FAEIK------KETGAQLVAGERDK 128
Cdd:cd16282    19 FIVGDDGVVVIDTGAsPRLARALLAAIRKVTDK--PVRYVVNTHYHGDHTLGnaaFADAGapiiahENTREELAARGEAY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 129 PLLEGGYYPGDEKNEDLAFPavkvDRAVKEGDRVTLGDTTLTAHAT-PGHSPGctswEMTVKDGKEDreVLFfcSGTVAL 207
Cdd:cd16282    97 LELMRRLGGDAMAGTELVLP----DRTFDDGLTLDLGGRTVELIHLgPAHTPG----DLVVWLPEEG--VLF--AGDLVF 164

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2557100986 208 NRLVGqPTYAGIVDDYRATFAKAKAMKIDVL 238
Cdd:cd16282   165 NGRIP-FLPDGSLAGWIAALDRLLALDATVV 194
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 55-192 1.61e-11

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: 62.95  E-value: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  55 IAVYVIKTSQGLILMDT----AMPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEIKKET---GAQLVAGERD 127
Cdd:cd07720    49 VNAFLVRTGGRLILVDTgaggLFGPTAGKLLANLAAAGIDPEDIDDVLLTHLHPDHIGGLVDAGGKPvfpNAEVHVSEAE 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2557100986 128 kplLEggyYPGDEKNEDLAFPAVKVD--------RAVKEGDRVTLGDTTL---TAHATPGHSPGCTSWEMTVKDGK 192
Cdd:cd07720   129 ---WD---FWLDDANAAKAPEGAKRFfdaardrlRPYAAAGRFEDGDEVLpgiTAVPAPGHTPGHTGYRIESGGER 198
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 42-181 3.05e-11

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


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 62.12  E-value: 3.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  42 QLIDNIYYVGT---------------DGIA--VYVIKTSQGlILMDTAMPQSTGMIKDNIAKLgFKVADIK-LILNtHAH 103
Cdd:cd07709     2 EIADDIYWVGVndwdlrlfegeyptpRGTSynSYLIKDEKT-ALIDTVKEPFFDEFLENLEEV-IDPRKIDyIVVN-HQE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 104 LDHTGGFAEIKKET-GAQLVAGERDKPLLEGgYYPGDEKNedlafpavkvDRAVKEGDRVTLGDTTLTAHATPG-HSPGC 181
Cdd:cd07709    79 PDHSGSLPELLELApNAKIVCSKKAARFLKH-FYPGIDER----------FVVVKDGDTLDLGKHTLKFIPAPMlHWPDT 147
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 84-183 6.37e-11

Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; Bacillus amyloliquefaciens BaeB may play a role in the synthesis of the antibiotic polyketide bacillaene. 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: 293833 [Multi-domain]  Cd Length: 174  Bit Score: 59.86  E-value: 6.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  84 IAKLGFKVADIKLILNTHAHLDHTGGFAEIKKETGAQLVAGERDKPlleggYYpgDEKNEDLafpavkvdRAVKEGDRVT 163
Cdd:cd16275    38 LAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEID-----YY--GFRCPNL--------IPLEDGDTIK 102

                          90       100
                  ....*....|....*....|
gi 2557100986 164 LGDTTLTAHATPGHSPGCTS 183
Cdd:cd16275   103 IGDTEITCLLTPGHTPGSMC 122
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 56-183 1.70e-09

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: 56.05  E-value: 1.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  56 AVYVIKTSQGLILMDTAMPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTG------------GFAEIKKEtgaqlva 123
Cdd:cd07711    23 TVTLIKDGGKNILVDTGTPWDRDLLLKALAEHGLSPEDIDYVVLTHGHPDHIGnlnlfpnatvivGWDICGDS------- 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 124 gERDKPLLEGGYYPGDEKNEDLafpavkvdravkegdrvtlgdttltahATPGHSPGCTS 183
Cdd:cd07711    96 -YDDHSLEEGDGYEIDENVEVI---------------------------PTPGHTPEDVS 127
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 58-178 5.35e-08

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: 51.77  E-value: 5.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  58 YVIKTSQGLILMDTA--MPQSTGMIKDNIAKLGfkVADIKLILNTHAHLDHTGGFAEIKKetgaqlvagerdkpLLEGGY 135
Cdd:cd07722    21 YLVGTGKRRILIDTGegRPSYIPLLKSVLDSEG--NATISDILLTHWHHDHVGGLPDVLD--------------LLRGPS 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2557100986 136 -----YPGDEKNEDLAFPAVKVDRaVKEGDRVTLGDTTLTAHATPGHS 178
Cdd:cd07722    85 prvykFPRPEEDEDPDEDGGDIHD-LQDGQVFKVEGATLRVIHTPGHT 131
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 97-184 6.24e-08

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 52.92  E-value: 6.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  97 ILNTHAHLDHTGGFAEIKKETGAQLVAGERDKPLLEGgyypgdeknedlafpavkVDRAVKEGDRVTLGDTTLTAHATPG 176
Cdd:PLN02398  125 ILNTHHHYDHTGGNLELKARYGAKVIGSAVDKDRIPG------------------IDIVLKDGDKWMFAGHEVLVMETPG 186


                  ....*...
gi 2557100986 177 HSPGCTSW 184
Cdd:PLN02398  187 HTRGHISF 194
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
43-125 1.36e-07

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 51.81  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  43 LIDNI----YYVGTDGIAVYvIKTSQGLILMDTAmpQSTGMIKdNIAKLGFKVADIKLILNTHAHLDHTGGFAEI-KKET 117
Cdd:COG1237     7 LVDNTagdeGLLAEHGLSAL-IETEGKRILFDTG--QSDVLLK-NAEKLGIDLSDIDAVVLSHGHYDHTGGLPALlELNP 82


                  ....*...
gi 2557100986 118 GAQLVAGE 125
Cdd:COG1237    83 KAPVYAHP 90
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 43-164 1.80e-07

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: 51.08  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  43 LIDNiyYVGTD------GIAVYvIKTSQGLILMDTAmpqSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEIKKE 116
Cdd:cd07713     5 LVDN--TAGDEgllaehGLSLL-IETEGKKILFDTG---QSGVLLHNAKKLGIDLSDIDAVVLSHGHYDHTGGLKALLEL 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2557100986 117 T-GAQLVAGE-------RDKPLLEGGYYPGDEKNEDLAFPAVKVDRAVKEGDRVTL 164
Cdd:cd07713    79 NpKAPVYAHPdafeprySKRGGGKKGIGIGREELEKAGARLVLVEEPTEIAPGVYL 134
NorV COG0426
Flavorubredoxin [Energy production and conversion];
40-180 7.76e-07

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 49.83  E-value: 7.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  40 PFQLIDNIYYVGTD---------------GIAV--YVIKTSQGlILMDTAMPQSTGMIKDNIAKLgFKVADIK-LILNtH 101
Cdd:COG0426     2 AVEIAHGVYWVGVLdwdrrlfegeyptprGTTYnsYLIVDEKT-ALIDTVGESFFEEFLENLSKV-IDPKKIDyIIVN-H 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 102 AHLDHTGGFAEI-KKETGAQLVAGERDKPLLEGgYYPGDEKNedlaFpavkvdRAVKEGDRVTLGDTTLTAHATPG-HSP 179
Cdd:COG0426    79 QEPDHSGSLPELlELAPNAKIVCSKKAARFLPH-FYGIPDFR----F------IVVKEGDTLDLGGHTLQFIPAPMlHWP 147


                  .
gi 2557100986 180 G 180
Cdd:COG0426   148 D 148
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 46-247 1.21e-06

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 47.96  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  46 NIYYVgTDGI--AVYVIkTSQGLILMDTamPQSTGmikDNIAKLGFKVAD--IKLILNTHAHLDHTGGfAEIKKETGAQL 121
Cdd:cd16276     1 GVYWV-TDGGyqSMFLV-TDKGVIVVDA--PPSLG---ENLLAAIRKVTDkpVTHVVYSHNHADHIGG-ASIFKDEGATI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 122 VAGERDKPLLEGgyypgdEKNEDLAFPAVKVDRAvkegDRVTLGDTTLTAHAT-PGHSPGCTSWEMtvkdgKEDReVLFF 200
Cdd:cd16276    73 IAHEATAELLKR------NPDPKRPVPTVTFDDE----YTLEVGGQTLELSYFgPNHGPGNIVIYL-----PKQK-VLMA 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2557100986 201 CSgtvalnrLV--GQPTYAGI-----VDDYRATFAKAKAMKIDVLLGPHPEVYG 247
Cdd:cd16276   137 VD-------LInpGWVPFFNFagsedIPGYIEALDELLEYDFDTFVGGHGNRLG 183
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
 92-191 1.84e-06

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 48.22  E-value: 1.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  92 ADIKLILNTHAHLDHTGGFAEIKKE-TGAQLVAGERDKplLEGGYYPgdeknedlafpavkvdraVKEGDRVTLG-DTTL 169
Cdd:PLN02469   45 AKIKLVLTTHHHWDHAGGNEKIKKLvPGIKVYGGSLDN--VKGCTHP------------------VENGDKLSLGkDVNI 104

                          90       100
                  ....*....|....*....|..
gi 2557100986 170 TAHATPGHSPGCTSWEMTVKDG 191
Cdd:PLN02469  105 LALHTPCHTKGHISYYVTGKEG 126
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 60-183 6.78e-06

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 45.71  E-value: 6.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  60 IKTSQGLILMD---TAMPqstgmikdNIAKLGFKVADIKLILNTHAHLDHTGGFAEIKKEtgAQLVAGeRDKPLLEGGYY 136
Cdd:cd07740    21 VASEAGRFLIDcgaSSLI--------ALKRAGIDPNAIDAIFITHLHGDHFGGLPFFLLD--AQFVAK-RTRPLTIAGPP 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2557100986 137 PGDEKNE---DLAFPAV-KVDRA-------VKEGDRVTLGDTTLTAHATPgHSPGCTS 183
Cdd:cd07740    90 GLRERLRramEALFPGSsKVPRRfdlevieLEPGEPTTLGGVTVTAFPVV-HPSGALP 146
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 47-199 9.98e-06

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 45.59  E-value: 9.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  47 IYYVgTDGIAVYVIKTSQGLILMDT------------AMPQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGG----- 109
Cdd:cd16277     6 ITRI-VELIHSWLVRTPGRTILVDTgigndkprpgppAFHNLNTPYLERLAAAGVRPEDVDYVLCTHLHVDHVGWntrlv 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 110 -------FAEikketgAQLVAGERDKPLLEGGYYPGDEKN---EDLAFPAVKVDRA--VKEGDRVTlgdTTLTAHATPGH 177
Cdd:cd16277    85 dgrwvptFPN------ARYLFSRAEYDHWSSPDAGGPPNRgvfEDSVLPVIEAGLAdlVDDDHEIL---DGIRLEPTPGH 155

                         170       180
                  ....*....|....*....|..
gi 2557100986 178 SPGCTSWEmtVKDGkeDREVLF 199
Cdd:cd16277   156 TPGHVSVE--LESG--GERALF 173
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 80-180 1.56e-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. Some members of this subgroup are annotated as GumP protein.


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 45.34  E-value: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  80 IKDNIAKLGFKVADIKLILNTHAHLDHTGGfaeIKKETGAQLVAGERDKPLL-EGGYYPGDEKN---EDlaFPAVKVDRA 155
Cdd:cd07730    70 VAEQLAAGGIDPEDIDAVILSHLHWDHIGG---LSDFPNARLIVGPGAKEALrPPGYPSGFLPEllpSD--FEGRLVRWE 144

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2557100986 156 VKEGDRVTL----------GDTTLTAHATPGHSPG 180
Cdd:cd07730   145 EDDFLWVPLgpfpraldlfGDGSLYLVDLPGHAPG 179
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 80-117 1.71e-05

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


Pssm-ID: 293814  Cd Length: 249  Bit Score: 45.33  E-value: 1.71e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2557100986  80 IKDNIAKLGFKVADIKLILNTHAHLDHTGGFAEIKKET 117
Cdd:cd07728    82 IEESLAELGLTPEDIDYVLMTHLHFDHASGLTKVKGEQ 119
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 58-108 2.71e-05

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 45.18  E-value: 2.71e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2557100986  58 YVIKTSQGLILMDTAMPQstGMIKDNIAKLGFKVADIKLILNTHAHLDHTG 108
Cdd:COG1236    17 YLLETGGTRILIDCGLFQ--GGKERNWPPFPFRPSDVDAVVLTHAHLDHSG 65
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 46-182 4.09e-05

uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YmaE and Nostoc all1228 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. 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: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 43.34  E-value: 4.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  46 NIYYVGTD-----GIAVYVIKTSQGLILMDTamPQSTGMIKDNIAKLGfkvaDIKLILNTHAhlDHTGGFAEIKKETGAQ 120
Cdd:cd07727     1 GVYYCGFHseksfGAASYLILRPEGNILVDS--PRYSPPLAKRIEALG----GIRYIFLTHR--DDVADHAKWAERFGAK 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2557100986 121 LVAGERDKpllegGYYPGDEKNEDLafpavkvdravKEGDRVTLGDTtLTAHATPGHSPGCT 182
Cdd:cd07727    73 RIIHEDDV-----NAVTRPDEVIVL-----------WGGDPWELDPD-LTLIPVPGHTRGSV 117
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 58-207 5.51e-05

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 43.73  E-value: 5.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  58 YVIKTSQGLILMDTampqSTGmIKDNIAKLGFKVADIKLILNTHAHLDHTGG---FAEIKKETGAQLVAGERDKPLLEGG 134
Cdd:COG1235    38 ILVEADGTRLLIDA----GPD-LREQLLRLGLDPSKIDAILLTHEHADHIAGlddLRPRYGPNPIPVYATPGTLEALERR 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2557100986 135 Y-YPGDEKNEDLAFpavkvdRAVKEGDRVTLGDTTLTAHATPGHSPGCTSWEMTVKDGKedrevLFFCSGTVAL 207
Cdd:COG1235   113 FpYLFAPYPGKLEF------HEIEPGEPFEIGGLTVTPFPVPHDAGDPVGYRIEDGGKK-----LAYATDTGYI 175
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 58-181 5.90e-05

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


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 43.02  E-value: 5.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  58 YVIKTSQGLILMDT---AMPQstgmikdnIAKLGFKVADIKLILNTHAHLDHTGGFAEI-------KKETGAQLVAGERD 127
Cdd:cd16272    20 YLLETGGTRILLDCgegTVYR--------LLKAGVDPDKLDAIFLSHFHLDHIGGLPTLlfarrygGRKKPLTIYGPKGI 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2557100986 128 KPLLEgGYYPGDEKNEDLAFPaVKVDRAVKEGDRVTLGDTTLTAHATPgHSPGC 181
Cdd:cd16272    92 KEFLE-KLLNFPVEILPLGFP-LEIEELEEGGEVLELGDLKVEAFPVK-HSVES 142
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 60-111 5.98e-05

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


Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 43.38  E-value: 5.98e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2557100986  60 IKTSQGLILMDT-------AMPQSTgMIKD-----------------NIAKLGFKVADIKLILNTHAHLDHTGGFA 111
Cdd:cd07742    24 VETDDGLVLVDTgfgladvADPKRR-LGGPfrrllrprldedetavrQIEALGFDPSDVRHIVLTHLDLDHAGGLA 98
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 67-184 6.04e-05

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 43.63  E-value: 6.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  67 ILMDTAMPQSTGMIKDNIAK-----------LGFKvadIKLILNTHAHLDHTGGFAEIK-KETGAQLVAGERDKPllegg 134
Cdd:PLN02962   27 LLADVSHPDKPALLIDPVDKtvdrdlslvkeLGLK---LIYAMNTHVHADHVTGTGLLKtKLPGVKSIISKASGS----- 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2557100986 135 yypgdeknedlafpavKVDRAVKEGDRVTLGDTTLTAHATPGHSPGCTSW 184
Cdd:PLN02962   99 ----------------KADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTY 132
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 48-247 6.81e-05

metallo-beta-lactamases; subclasses B1 and B2 and related proteins; 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. B1 MBls include 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. B2 MBLs have a narrow substrate profile that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis. B2 MBLs include Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I.


Pssm-ID: 293793 [Multi-domain]  Cd Length: 219  Bit Score: 43.30  E-value: 6.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  48 YYVGTDGIavyVIKTSQGLILMDTAM-PQSTGMIKDNIAK-LGFKVADIkliLNTHAHLDHTGGfAEIKKETGAQLVAGE 125
Cdd:cd07707    17 GSVPSNGL---VYNGSKGLVLVDSTWtPKTTKELIKEIEKvSQKPVTEV---INTHFHTDRAGG-NAYLKERGAKTVSTA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986 126 RDKPLLEggyypgDEKNEDLAFPAVKVDRAVKEG----DRVTLGDTTL------TAHATPGHSPgctswemtvkdgkeDR 195
Cdd:cd07707    90 LTRDLAK------SEWAEIVAFTRKGLPEYPDLGyelpDGVLDGDFNLqfgkveAFYPGPAHTP--------------DN 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2557100986 196 EVLFFCSGTVALNRLVGQPTYAGIVDD-----YRATFAKAKAM--KIDVLLGPHPEVYG 247
Cdd:cd07707   150 IVVYFPQENVLYGGCIIKETDLGNVADadvkeWPTSIERLKKRyrNIKAVIPGHGEVGG 208
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 93-178 1.06e-04

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 42.30  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  93 DIKLILNTHAHLDHTGGFAEIKKETGAQLVAGERDKPLLEGGyYPGDEKNEDLAFPAVKVDravkEGDRVTLGDTTLTAH 172
Cdd:pfam12706  28 PIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLRRN-FPYLFLLEHYGVRVHEID----WGESFTVGDGGLTVT 102


                  ....*.
gi 2557100986 173 ATPGHS 178
Cdd:pfam12706 103 ATPARH 108
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 41-109 3.19e-04

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. 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: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 41.33  E-value: 3.19e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2557100986  41 FQLIDNIYYVGTDGIA-VYVIKTSQGLILMDTAMPQSTG-MIKDNIAKlgfKVAD--IKLILNTHAHLDHTGG 109
Cdd:cd07710     3 FEVTDGVYQVRGYDLSnMTFIEGDTGLIIIDTLESAEAAkAALELFRK---HTGDkpVKAIIYTHSHPDHFGG 72
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 59-170 4.23e-04

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 40.20  E-value: 4.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  59 VIKTSQGLILMDTAMPQSTGM--IKDNIAKLGfkVADIKLILNTHAHLDHTGGFAEIKKE-TGAQLVAGERDKPLLEGGY 135
Cdd:cd07731    14 LIQTPGKTILIDTGPRDSFGEdvVVPYLKARG--IKKLDYLILTHPDADHIGGLDAVLKNfPVKEVYMPGVTHTTKTYED 91

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2557100986 136 YPGDEKNEDLAFpavkvdRAVKEGDRVTLGDTTLT 170
Cdd:cd07731    92 LLDAIKEKGIPV------TPCKAGDRWQLGGVSFE 120
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 59-170 4.33e-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: 41.00  E-value: 4.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  59 VIKTSQG-LILMDTAMPQSTGMIKDNIA----KLGfkVADIKLILNTHAHLDHTGGFAEIKKE-TGAQLVAGERDKPLLE 132
Cdd:COG2333    15 LIRTPDGkTILIDTGPRPSFDAGERVVLpylrALG--IRRLDLLVLTHPDADHIGGLAAVLEAfPVGRVLVSGPPDTSET 92

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2557100986 133 GGYYPGDEKNEDLAFpavkvdRAVKEGDRVTLGDTTLT 170
Cdd:COG2333    93 YERLLEALKEKGIPV------RPCRAGDTWQLGGVRFE 124
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 58-108 5.20e-04

Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General function prediction only];


Pssm-ID: 441388 [Multi-domain]  Cd Length: 460  Bit Score: 41.27  E-value: 5.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2557100986  58 YVIKTSQGLILMDTAMPQSTGMI-KDNIAKLGFKVADIKLILNTHAHLDHTG 108
Cdd:COG1782    17 HLLETGESRILLDCGLFQGGREErERNNDAFPFDPEELDAVVLTHAHLDHSG 68
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 58-108 6.38e-04

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


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 40.13  E-value: 6.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2557100986  58 YVIKTSQGLILMDTAMPQSTGMIKD-NIAKLGFKVADIKLILNTHAHLDHTG 108
Cdd:cd16295    15 YLLETGGKRILLDCGLFQGGKELEElNNEPFPFDPKEIDAVILTHAHLDHSG 66
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 66-109 8.02e-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: 8.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2557100986  66 LILMDTAM-------------PQSTGMIKDNIAKLGFKVADIKLILNTHAHLDHTGG 109
Cdd:cd16281    54 NILIDTGIgdkqdpkfrsiyvQHSEHSLLKSLARLGLSPEDITDVILTHLHFDHCGG 110
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 59-116 1.19e-03

Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Bacillus cereus Beta-lactamase 2, also called BcII. MBLs (class B of the Ambler beta-lactamase classification) 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. BcII is a chromosome-encoded B1 MBL. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293862 [Multi-domain]  Cd Length: 212  Bit Score: 39.19  E-value: 1.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2557100986  59 VIKTSQGLILMDTA-----MPQSTGMIKDNIAKlgfkvaDIKLILNTHAHLDHTGGFAEIKKE 116
Cdd:cd16304    30 IVETSKGVVLIDTPwddeqTEELLDWIKKKLKK------PVTLAIVTHAHDDRIGGIKALQKR 86
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 90-123 1.48e-03

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 39.02  E-value: 1.48e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2557100986  90 KVADIK--LILNTHAHLDHTGGFAEIKKETGAQLVA 123
Cdd:PRK00685   35 KPEDVKvdYILLTHGHGDHLGDTVEIAKRTGATVIA 70
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
 83-113 1.60e-03

Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.


Pssm-ID: 293805 [Multi-domain]  Cd Length: 193  Bit Score: 38.65  E-value: 1.60e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2557100986  83 NIAKLGFKVADIKLILNTHAHLDHTGGFAEI 113
Cdd:cd07719    41 RLAQAGLPLGDLDAVFLTHLHSDHVADLPAL 71
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 91-180 2.48e-03

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 38.36  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  91 VADIKLILNTHAHLDHTG--GFAEIKKeTGAQLVAGERDKPLLEGgyypgdeknedLAFPAVkvdRAVKEGDRVTLGDtt 168
Cdd:COG2220    46 LPKIDAVLVTHDHYDHLDdaTLRALKR-TGATVVAPLGVAAWLRA-----------WGFPRV---TELDWGESVELGG-- 108

                          90
                  ....*....|...
gi 2557100986 169 LTAHATPG-HSPG 180
Cdd:COG2220   109 LTVTAVPArHSSG 121
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
83-184 5.68e-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: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  83 NIAKLGFKVADIKLILNTHAHLDHTGGFAEIkketgaqLVA---GERDKPL-LeggYYP-GDEK---------NEDLAFP 148
Cdd:COG1234    42 QLLRAGLDPRDIDAIFITHLHGDHIAGLPGL-------LSTrslAGREKPLtI---YGPpGTKEfleallkasGTDLDFP 111

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2557100986 149 aVKVdRAVKEGDRVTLGDTTLTAHATPgHSPGCTSW 184
Cdd:COG1234   112 -LEF-HEIEPGEVFEIGGFTVTAFPLD-HPVPAYGY 144
SPM-1-like_MBL-B1-B2-like cd16286
Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; ...
 98-179 6.77e-03

Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; MBL-fold metallo-hydrolase domain; SPM-1 was first identified in a Pseudomonas aeruginosa strain from a paediatric leukaemia patient and is a major clinical problem. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs are most closely related to each other. SPM-1 appears to be a hybrid B1/B2 MBL.


Pssm-ID: 293844 [Multi-domain]  Cd Length: 236  Bit Score: 37.13  E-value: 6.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2557100986  98 LNTHAHLDHTGGfAEIKKETGAQLVA-----------GERDKPLLEGGYYPGDEKNEDLAFPAVKVDRA--VKEGDRVTL 164
Cdd:cd16286    70 INTHFHLDGTGG-NEALKKRGIPTWGsdltkqlllerGKADRIKAAEFLKNEDLKRRIESSPPVPPDNVfdLKEGKVFSF 148

                          90
                  ....*....|....*.
gi 2557100986 165 GDTTLTAH-ATPGHSP 179
Cdd:cd16286   149 GNELVEVSfPGPAHAP 164
 
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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