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Conserved domains on  [gi|1238338877|gb|ASV80088|]
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GOB family subclass B3 metallo-beta-lactamase [Elizabethkingia anophelis]

Protein Classification

GOB family subclass B3 metallo-beta-lactamase( domain architecture ID 10888864)

beta lactamase hydrolyzes the beta-lactam ring of beta-lactam antibiotics such as penicillin, cephalosporin and carbapenem, resulting in antibiotic resistance

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
31-284 8.23e-171

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: 472.72  E-value: 8.23e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  31 WNQTYEPFRIAGNLYYVGTYDLASYLIVTDKGNILINTGTAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDL 110
Cdd:cd16308     1 WSQPYAPFRIAGNLYYVGTYDLACYLIVTPKGNILINTGLAESVPLIKKNIQALGFKFKDIKILLTTQAHYDHVGAMAAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 111 KTETGAKFYADKADADVLRTGGNSDYEMGKYGVTFKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETKDEK 190
Cdd:cd16308    81 KQQTGAKMMVDEKDAKVLADGGKSDYEMGGYGSTFAPVKADKLLHDGDTIKLGGTKLTLLHHPGHTKGSCSFLFDVKDEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 191 RKYRVLIANMPSIIVDKKFSEVTAYLNIQSDYAYTFKAMKNLDFDLWVASHASQFDLHEKRKEGDPYNPQLFMDKQSYFQ 270
Cdd:cd16308   161 RTYRVLIANMPTILPDTKLSGMPGYPGIAKDYAYTFEAMKALSFDIWLASHASQFDLHQKHKPGAPYNPAAFADRAGYDK 240
                         250
                  ....*....|....
gi 1238338877 271 NLNDLEKSYLDKIK 284
Cdd:cd16308   241 ALAGLEKSYDKKIK 254
 
Name Accession Description Interval E-value
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
31-284 8.23e-171

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: 472.72  E-value: 8.23e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  31 WNQTYEPFRIAGNLYYVGTYDLASYLIVTDKGNILINTGTAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDL 110
Cdd:cd16308     1 WSQPYAPFRIAGNLYYVGTYDLACYLIVTPKGNILINTGLAESVPLIKKNIQALGFKFKDIKILLTTQAHYDHVGAMAAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 111 KTETGAKFYADKADADVLRTGGNSDYEMGKYGVTFKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETKDEK 190
Cdd:cd16308    81 KQQTGAKMMVDEKDAKVLADGGKSDYEMGGYGSTFAPVKADKLLHDGDTIKLGGTKLTLLHHPGHTKGSCSFLFDVKDEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 191 RKYRVLIANMPSIIVDKKFSEVTAYLNIQSDYAYTFKAMKNLDFDLWVASHASQFDLHEKRKEGDPYNPQLFMDKQSYFQ 270
Cdd:cd16308   161 RTYRVLIANMPTILPDTKLSGMPGYPGIAKDYAYTFEAMKALSFDIWLASHASQFDLHQKHKPGAPYNPAAFADRAGYDK 240
                         250
                  ....*....|....
gi 1238338877 271 NLNDLEKSYLDKIK 284
Cdd:cd16308   241 ALAGLEKSYDKKIK 254
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
54-241 7.98e-32

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: 116.11  E-value: 7.98e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877   54 SYLIVTDKGNILINTGTAESLPIIKAnIQKLGfnYKDIKILLLTQAHYDHTGALQDLKTETGAKFYADKADADVLRtggN 133
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDLLAE-LKKLG--PKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLK---D 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  134 SDYEMGKYGVTFKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFEtkdekrKYRVLIAN--MPSIIVDKKFSE 211
Cdd:smart00849  76 LLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLP------EGKILFTGdlLFAGGDGRTLVD 149
                          170       180       190
                   ....*....|....*....|....*....|
gi 1238338877  212 VTAYLNiqSDYAYTFKAMKNLDFDLWVASH 241
Cdd:smart00849 150 GGDAAA--SDALESLLKLLKLLPKLVVPGH 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
54-255 5.47e-31

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: 115.17  E-value: 5.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  54 SYLIVTDKGNILINTG-TAESLPIIKANIQKLGfnyKDIKILLLTQAHYDHTGALQDLKTETGAKFYADKADADVLRTGG 132
Cdd:COG0491    17 SYLIVGGDGAVLIDTGlGPADAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEAPA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 133 NSDYemgkygVTFKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETKdekrkyRVLIAN---MPSIIVDKKF 209
Cdd:COG0491    94 AGAL------FGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDE------KVLFTGdalFSGGVGRPDL 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1238338877 210 SEVTAylniqSDYAYTFKAMKNLDFDLWVASHASQFDLHEKRKEGD 255
Cdd:COG0491   162 PDGDL-----AQWLASLERLLALPPDLVIPGHGPPTTAEAIDYLEE 202
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
54-241 4.86e-20

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 85.50  E-value: 4.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  54 SYLIVTDKGNILINTGTAESLPIIkANIQKLGFNYKDIKILLLTQAHYDHTGALQDLKTETGAKFYADKADADVLRTGGN 133
Cdd:pfam00753   8 SYLIEGGGGAVLIDTGGSAEAALL-LLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEEL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 134 SDYEMGKYGVTFKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETKDEkrkyRVLIA-----NMPSIIVDKK 208
Cdd:pfam00753  87 GLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGG----KVLFTgdllfAGEIGRLDLP 162
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1238338877 209 -FSEVTAYLNIQSDYAYTFKAMKNLDFDLWVASH 241
Cdd:pfam00753 163 lGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
66-184 1.16e-08

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 55.23  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  66 INTGT------AESLPIIKAnIQKLGFNYKDIkilLLTQAHYDHTGALQDLKTETGAKFYADKADADvlRTGGnsdyemg 139
Cdd:PLN02398   95 EDTGTvgvvdpSEAVPVIDA-LSRKNRNLTYI---LNTHHHYDHTGGNLELKARYGAKVIGSAVDKD--RIPG------- 161
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1238338877 140 kygvtfkpvtPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIF 184
Cdd:PLN02398  162 ----------IDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYF 196
 
Name Accession Description Interval E-value
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
31-284 8.23e-171

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: 472.72  E-value: 8.23e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  31 WNQTYEPFRIAGNLYYVGTYDLASYLIVTDKGNILINTGTAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDL 110
Cdd:cd16308     1 WSQPYAPFRIAGNLYYVGTYDLACYLIVTPKGNILINTGLAESVPLIKKNIQALGFKFKDIKILLTTQAHYDHVGAMAAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 111 KTETGAKFYADKADADVLRTGGNSDYEMGKYGVTFKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETKDEK 190
Cdd:cd16308    81 KQQTGAKMMVDEKDAKVLADGGKSDYEMGGYGSTFAPVKADKLLHDGDTIKLGGTKLTLLHHPGHTKGSCSFLFDVKDEK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 191 RKYRVLIANMPSIIVDKKFSEVTAYLNIQSDYAYTFKAMKNLDFDLWVASHASQFDLHEKRKEGDPYNPQLFMDKQSYFQ 270
Cdd:cd16308   161 RTYRVLIANMPTILPDTKLSGMPGYPGIAKDYAYTFEAMKALSFDIWLASHASQFDLHQKHKPGAPYNPAAFADRAGYDK 240
                         250
                  ....*....|....
gi 1238338877 271 NLNDLEKSYLDKIK 284
Cdd:cd16308   241 ALAGLEKSYDKKIK 254
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
31-284 4.23e-106

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: 308.87  E-value: 4.23e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  31 WNQTYEPFRIAGNLYYVGTYDLASYLIVTDKGNILINTGTAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDL 110
Cdd:cd16288     1 WNAPFEPFRIAGNVYYVGTSGLASYLITTPQGLILIDTGLESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 111 KTETGAKFYADKADADVLRTGGNSDYEMGKYGVTFKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETKDEK 190
Cdd:cd16288    81 KKLTGAKLMASAEDAALLASGGKSDFHYGDDSLAFPPVKVDRVLKDGDRVTLGGTTLTAHLTPGHTRGCTTWTMTVKDDG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 191 RKYRVLIANMPSIIVDKKFSEVTAYLNIQSDYAYTFKAMKNLDFDLWVASHASQFDLHEKRKEGDPYNPQLFMDKQSYFQ 270
Cdd:cd16288   161 KVYQVVFADSLTVNPGYKLVGNPTYPGIAEDYRHSFATLRALQCDIFLASHAEYFDLKEKRARLAAGQPNAFIDPEGYRN 240
                         250
                  ....*....|....
gi 1238338877 271 NLNDLEKSYLDKIK 284
Cdd:cd16288   241 FIEKAKADFEKQLA 254
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
31-284 7.81e-72

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: 221.55  E-value: 7.81e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  31 WNQTYEPFRIAGNLYYVGTYDLASYLIVTDKGNILINTGTAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDL 110
Cdd:cd16307     1 WTTPFPPFRIAGNLYYVGSRDLASYLITTPRGNILINSNLESSVPQIKASIEKLGFKFSDTKILLISHAHFDHAAGSALI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 111 KTETGAKFYADKADADVLRTGGNSDYEMGKYGVT-FKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETKDE 189
Cdd:cd16307    81 KRETHAKYMVMDGDVDVVESGGKSDFFYGNDPSTyFPPAHVDKVLHDGEQVELGGTVLTAHLTAGHTKGCTTWTMKVKDH 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 190 KRKYRVLIANMPSIIVDKKFSEVTAYLNIQSDYAYTFKAMKNLDFDLWVASHASQFDLHEKRKEGDPYNPQLFMDKQSYF 269
Cdd:cd16307   161 GKTYDVVIVGSPNVNPGAKLVNNITYPGIAEDYAHTFAVLRSLPCDIFLGAHGGYFDLKNKYVRLQKGGANPFIDPEGYK 240
                         250
                  ....*....|....*
gi 1238338877 270 QNLNDLEKSYLDKIK 284
Cdd:cd16307   241 AYVAEKEQAFRTELE 255
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
31-264 2.94e-69

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: 214.72  E-value: 2.94e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  31 WNQTYEPFRIAGNLYYVGTYDLASYLIVTDKGNILINTGTAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDL 110
Cdd:cd07708     1 WPNPFPPFQIAGNTYYVGTDDLAAYLIVTPQGNILIDGDMEQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAEI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 111 KTETGAKFYADKADADVLRTGGNSDYEMGK-YGVTFKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETKDE 189
Cdd:cd07708    81 KKQTGAKVMAGAEDVSLLLSGGSSDFHYANdSSTYFPQSTVDRAVHDGERVTLGGTVLTAHATPGHTPGCTTWTMTLKDH 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238338877 190 KRKYRVLIANMPSIIVDKKFSEVTAYLNIQSDYAYTFKAMKNLDFDLWVASHASQFDLHEKRKEGDPYNPQLFMD 264
Cdd:cd07708   161 GKQYQVVFADSLTVNPGYRLVDNPTYPKIVEDYRHSFAVVEAMRCDILLGPHPGVFDMKNKYVLLSKGQNNPFVD 235
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
31-280 8.86e-66

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: 206.18  E-value: 8.86e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  31 WNQTYEPFRIAGNLYYVGTYDLASYLIVTDKGNILINTGTAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDL 110
Cdd:cd16309     1 WNEPMEPFKLIGNIYYVGTAGLGVFLITTPEGHILIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 111 KTETGAKFYADKADADVLRtGGNSDYEMGKYgVTFKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETKDEK 190
Cdd:cd16309    81 KKATGAQLVASAADKPLLE-SGYVGSGDTKN-LQFPPVRVDRVIGDGDKVTLGGTTLTAHLTPGHSPGCTSWTTTVKDTA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 191 RKYRVLIANMPSIIVDKKFSEVTAYLNIQSDYAYTFKAMKNLDFDLWVASHASQFDLHEKRKEGDPYNPQLFMDKQSYFQ 270
Cdd:cd16309   159 GPPREVLFFCSATVAGNQLVGPPTYPGIVDDYRATFAKARAMKADVFLANHPEFFGLVAKRARQSAGEPDAFVDAGELQR 238
                         250
                  ....*....|
gi 1238338877 271 NLNDLEKSYL 280
Cdd:cd16309   239 FNTKMEDDFE 248
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
31-266 8.50e-64

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: 201.14  E-value: 8.50e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  31 WNQTYEPFRIAGNLYYVGTYDLASYLIVTDKGNILINTGTAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDL 110
Cdd:cd16310     1 WTAPTEPFRIVDNIYYVGTKGIGSYLITSNHGAILLDGGLEENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 111 KTETGAKFYADKADADVLRTGGNSDyEMGKYGVTFKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETKDEK 190
Cdd:cd16310    81 KADTGAKLWASRGDRPALEAGKHIG-DNITQPAPFPAVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTWSTTVKENG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 191 RKYRVL----IANMPSIIVDKKfsevtAYLNIQSDYAYTFKAMKNLDFDLWVASHASQFDLHEKRKEGDPYNPQLFMDKQ 266
Cdd:cd16310   160 RPLRVVfpcsLSVAGNVLVGNK-----TYPTIVEDYRASFARLRAMKADIVLTSHPEVADLLARKAKQDAGQANAFVDPG 234
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
31-284 9.97e-52

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: 170.07  E-value: 9.97e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  31 WNQTYEPFRIAGNLYYVGTYDLASYLIVTDKGNILINTG-TAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQD 109
Cdd:cd16280     1 KKGYVEPFQVFDNLYYVGNKWVSAWAIDTGDGLILIDALnNNEAADLIVDGLEKLGLDPADIKYILITHGHGDHYGGAAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 110 LKTETGAKFYADKADADVLRTggnsDYEMGKYGVTFKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETKDE 189
Cdd:cd16280    81 LKDLYGAKVVMSEADWDMMEE----PPEEGDNPRWGPPPERDIVIKDGDTLTLGDTTITVYLTPGHTPGTLSLIFPVKDG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 190 KRKYRVLI---ANMPSIivdKKFSEVTAYlnIQSdyAYTFKAMKNL-DFDLWVASHASQFDLHEKRKE-----GDPYNPq 260
Cdd:cd16280   157 GKTHRAGLwggTGLNTG---PNLERREQY--IAS--LERFKKIAEEaGVDVFLSNHPFQDGSLEKREAlrnrkPGEPNP- 228
                         250       260
                  ....*....|....*....|....
gi 1238338877 261 lFMDKQSYFQNLNDLEKSYLDKIK 284
Cdd:cd16280   229 -FVDGQAWVDFYDEVLALCARVLA 251
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 ...
31-266 2.55e-48

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: 161.36  E-value: 2.55e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  31 WNQTYEPFRIAGNLYYVGTYDLASYLIVTDKGNILINTGTAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDL 110
Cdd:cd16290     1 WNQPQAPFRIHGNTYYVGTGGLSAVLITSPQGLILIDGALPQSAPQIEANIRALGFRLEDVKLILNSHAHFDHAGGIAAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 111 KTETGAKFYADKADADVLRTGGNS--DYEMGkYGVTFKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETKD 188
Cdd:cd16290    81 QRDSGATVAASPAGAAALRSGGVDpdDPQAG-AADPFPPVAKVRVVADGEVVKLGPLAVTAHATPGHTPGGTSWTWRSCE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 189 EKRKYRVLIANMPSIIVDK--KFSEvTAYLNIQSDYAYTFKAMKNLDFDLWVASHASQFDLHEK---RKEGDPYNPqlFM 263
Cdd:cd16290   160 GGRCLDIVYADSLTAVSADgfRFSD-DAHPARVAAFRRSIATVAALPCDILISAHPDASGLWEKlarRAREPGPNP--FI 236

                  ...
gi 1238338877 264 DKQ 266
Cdd:cd16290   237 DPN 239
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
31-260 1.37e-46

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: 156.74  E-value: 1.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  31 WNQTYEPFRIAGNLYYVGTYDLASYLIVTDKGNILINTGTAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDL 110
Cdd:cd16315     1 WDKPAPPARIFGNTYYVGTCGISAILITGDDGHVLIDSGTEEAAPLVLANIRKLGFDPKDVRWLLSSHEHFDHVGGLAAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 111 KTETGAKFYADKADADVLRTGGNSDyEMGKYGV--TFKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETKD 188
Cdd:cd16315    81 QRATGARVAASAAAAPVLESGKPAP-DDPQAGLhePFPPVRVDRIVEDGDTVALGSLRLTAHATPGHTPGALSWTWRSCE 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238338877 189 EKRKYRVLIANMPSIIV--DKKFSEVTAYLniqSDYAYTFKAMKNLDFDLWVASHASQFDLHEKRKEGDP-YNPQ 260
Cdd:cd16315   160 GADCRTIVYADSLSPVSadGYRFSDHPDYV---AAYRAGLAKVAALPCDILLTPHPSASDMFERLSGGAPlADPD 231
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
31-264 2.81e-41

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: 143.08  E-value: 2.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  31 WNQTYEPFRIAGNLYYVGTYDLASYLIVTDKGNILINTGTAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDL 110
Cdd:cd16313     1 WNAPQEPFQIYGNTYYVGTGGISAVLITSPQGHILIDGGFPKSPEQIAASIRQLGFKLEDVKYILSSHDHWDHAGGIAAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 111 KTETGAKFYADKADADVLRTG--GNSDYEMGkyGVT-FKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETK 187
Cdd:cd16313    81 QKLTGAQVLASPATVAVLRSGsmGKDDPQFG--GLTpMPPVASVRAVRDGEVVKLGPLAVTAHATPGHTTGGTSWTWQSC 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238338877 188 DEKRKYRVLIANMPSIIVDKKFSeVTAYLNIQSDYAYTFKAMKNLDFDLWVASHASQFDLHEKRKEGDPYNPQLFMD 264
Cdd:cd16313   159 EQGRCANMVFADSLTAVSADGYR-FSAHPAVLADVEQSIAAVEKLACDILVSAHPEFSDMWTRVKRGAAEGNAAFID 234
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
31-267 1.78e-37

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: 133.57  E-value: 1.78e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  31 WNQTYEPFRIAGNLYYVGTYDLASYLIVTDKGNILINTGTAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDL 110
Cdd:cd16311     1 WNADQAPFRIFGNTYYVGVKGLSSVLVTSPQGHVLVDGGLPESAPKIIANIEALGFRIEDVKLILNSHGHIDHAGGLAEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 111 KTETGAKFYADKADADVLRTG--GNSDyemGKYGVT--FKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFET 186
Cdd:cd16311    81 QRRSGALVAASPSAALDLASGevGPDD---PQYHALpkYPPVKDMRLARDGGQFNVGPVSLTAHATPGHTPGGLSWTWQS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 187 KDEKRKYRVLIANMPSIIV--DKKFSEVTAYLNIQSDYAYTFKAMKNLDFDLWVASHASQFDLHEKRKEGDPYNPQLFMD 264
Cdd:cd16311   158 CDGPRCLNMVYADSQNAVSrpGFKFSASSEYPNAVADLRRSFETLEKLPCDVLISAHPEASQLWERLEASDRSARPALVD 237

                  ...
gi 1238338877 265 KQS 267
Cdd:cd16311   238 REA 240
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
31-242 1.44e-35

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: 128.01  E-value: 1.44e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  31 WNQTYEPFRIAGNLYYVGTYDLASYLIVTDKGNILINTGTAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDL 110
Cdd:cd16289     1 WLQPMAPLQIADHTWYIGTESLTALLVKTPDGAVLLDGGMPQAADMLLDNMRALGVAPGDLKLILHSHAHADHAGPLAAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 111 KTETGAKFYADKADADVLRTGGNSDYEMGKyGVTFKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIF-ETKDE 189
Cdd:cd16289    81 KRATGARVAANAESAVLLARGGSDDIHFGD-GITFPPVQADRIVMDGEVVTLGGVTFTAHFTPGHTPGSTSWTWtDTRDG 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1238338877 190 KrkyRVLIANMPSIIVDK-KFSEVTAYLNIQSDYAYTFKAMKNLDFDLWVASHA 242
Cdd:cd16289   160 K---PVRIAYADSLSAPGyQLLGNPRYPRIVEDYRRTFATVRALPCDVLLTPHP 210
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
31-250 1.23e-34

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: 125.77  E-value: 1.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  31 WNQTYEPFRIAGNLYYVGTYDLASYLIVTDKGNILINTGTAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDL 110
Cdd:cd16314     1 WDDPAPPRRIYGNTWYVGTCGISALLVTSDAGHILIDGGTDKAAPLIEANIRALGFRPEDVRYIVSSHEHFDHAGGIARL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 111 KTETGAKFYADKADADVLRTgGNSDYEMGKYGV--TFKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETKD 188
Cdd:cd16314    81 QRATGAPVVAREPAATTLER-GRSDRSDPQFLVveKFPPVASVQRIGDGEVLRVGPLALTAHATPGHTPGGTSWTWRSCE 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238338877 189 EKRKYRVLIANMPSIIVDK--KFSEVTAYLniqSDYAYTFKAMKNLDFDLWVASHASQFDLHEK 250
Cdd:cd16314   160 GAVCRDMVYADSVTAISDDiyRYSDHPGMV---AAFRNTLDTVAALPCDILVTPHPSASGLWER 220
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
31-264 2.92e-33

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: 122.40  E-value: 2.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  31 WNQTYEPFRIAGNLYYVGTYDLASYLIVTDKGNILINTGTAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDL 110
Cdd:cd16312     1 WNQPVKPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIEALGFRIEDVKLILNSHAHWDHAGGIAAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 111 KTETGAKFYADKADADVLRTG--GNSDYEMGKYGVTFKP-VTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETK 187
Cdd:cd16312    81 QKASGATVAASAHGAQVLQSGtnGKDDPQYQAKPVVHVAkVAKVKEVGEGDTLKVGPLRLTAHMTPGHTPGGTTWTWTSC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 188 DEKRKYRVLIAN--MPSIIVDKKFSEVTAYLNIQSDYAYTFKAMKNLDFDLWVASHASQFDLHEK--RKEGDpYNPqlFM 263
Cdd:cd16312   161 EGQRCLDVVYADslNPYSSGDFYYTGKGGYPDISASFRASIAKVAALPCDIIIAVHPGFTDVLDKakRRSGD-TNP--FI 237

                  .
gi 1238338877 264 D 264
Cdd:cd16312   238 D 238
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
55-198 4.01e-32

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: 117.71  E-value: 4.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  55 YLIVTDKGNILINTGTAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDLKTETGAKFYADKADADVLRTG--- 131
Cdd:cd07721    14 YLIEDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEREAPYLEGEkpy 93
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1238338877 132 --GNSDYEMGKYGVTF--KPVTPDKTLKDQDKITLGNTiLTLLHHPGHTKGSCSFIFEtkdekrKYRVLIA 198
Cdd:cd07721    94 ppPVRLGLLGLLSPLLpvKPVPVDRTLEDGDTLDLAGG-LRVIHTPGHTPGHISLYLE------EDGVLIA 157
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
54-241 7.98e-32

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: 116.11  E-value: 7.98e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877   54 SYLIVTDKGNILINTGTAESLPIIKAnIQKLGfnYKDIKILLLTQAHYDHTGALQDLKTETGAKFYADKADADVLRtggN 133
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDLLAE-LKKLG--PKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLK---D 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  134 SDYEMGKYGVTFKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFEtkdekrKYRVLIAN--MPSIIVDKKFSE 211
Cdd:smart00849  76 LLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYLP------EGKILFTGdlLFAGGDGRTLVD 149
                          170       180       190
                   ....*....|....*....|....*....|
gi 1238338877  212 VTAYLNiqSDYAYTFKAMKNLDFDLWVASH 241
Cdd:smart00849 150 GGDAAA--SDALESLLKLLKLLPKLVVPGH 177
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
54-255 5.47e-31

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: 115.17  E-value: 5.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  54 SYLIVTDKGNILINTG-TAESLPIIKANIQKLGfnyKDIKILLLTQAHYDHTGALQDLKTETGAKFYADKADADVLRTGG 132
Cdd:COG0491    17 SYLIVGGDGAVLIDTGlGPADAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEAPA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 133 NSDYemgkygVTFKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETKdekrkyRVLIAN---MPSIIVDKKF 209
Cdd:COG0491    94 AGAL------FGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDE------KVLFTGdalFSGGVGRPDL 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1238338877 210 SEVTAylniqSDYAYTFKAMKNLDFDLWVASHASQFDLHEKRKEGD 255
Cdd:COG0491   162 PDGDL-----AQWLASLERLLALPPDLVIPGHGPPTTAEAIDYLEE 202
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
47-188 1.02e-29

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: 110.84  E-value: 1.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  47 VGTYDLASYLIVTDKG-NILINTGtAESLPIIKANIQKLGfnyKDIKILLLTQAHYDHTGALQDLKTETGAKFYADKADA 125
Cdd:cd06262     5 VGPLQTNCYLVSDEEGeAILIDPG-AGALEKILEAIEELG---LKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADA 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238338877 126 DVLRTGGNSDYEMGkyGVTFKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETKD 188
Cdd:cd06262    81 ELLEDPELNLAFFG--GGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEG 141
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
54-241 4.86e-20

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 85.50  E-value: 4.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  54 SYLIVTDKGNILINTGTAESLPIIkANIQKLGFNYKDIKILLLTQAHYDHTGALQDLKTETGAKFYADKADADVLRTGGN 133
Cdd:pfam00753   8 SYLIEGGGGAVLIDTGGSAEAALL-LLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEEL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 134 SDYEMGKYGVTFKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETKDEkrkyRVLIA-----NMPSIIVDKK 208
Cdd:pfam00753  87 GLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGG----KVLFTgdllfAGEIGRLDLP 162
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1238338877 209 -FSEVTAYLNIQSDYAYTFKAMKNLDFDLWVASH 241
Cdd:pfam00753 163 lGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
47-188 4.73e-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: 83.17  E-value: 4.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  47 VGTYDLASYLIVTDKGN--ILINTGTAESLpiIKANIQKLGFnykDIKILLLTQAHYDHTGALQDLKTETGAKFYADKAD 124
Cdd:cd16322     6 LGPLQENTYLVADEGGGeaVLVDPGDESEK--LLARFGTTGL---TLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDD 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238338877 125 ADVLRtGGNSDYEMGKYGVTFKPvTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETKD 188
Cdd:cd16322    81 LPLYE-AADLGAKAFGLGIEPLP-PPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEG 142
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
43-188 1.07e-18

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: 82.16  E-value: 1.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  43 NLYYVGTYDL------ASYLIVTDKGNILINTGTAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDL-KTETG 115
Cdd:cd07726     1 GIYLIDLGFLgfpgriASYLLDGEGRPALIDTGPSSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLaEALPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 116 AKFYA-----------DKADADVLRTGGNsdyEMGKYGVTFKPVTPDK--TLKDQDKITLGNTILTLLHHPGHTKGSCSF 182
Cdd:cd07726    81 AKVYVhprgarhlidpSKLWASARAVYGD---EADRLGGEILPVPEERviVLEDGETLDLGGRTLEVIDTPGHAPHHLSF 157

                  ....*.
gi 1238338877 183 IFETKD 188
Cdd:cd07726   158 LDEESD 163
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
54-188 2.83e-14

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: 69.03  E-value: 2.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  54 SYLIVTDKGN--ILINTGTAEslPIIKAnIQKLGFNYKDIkilLLTQAHYDHTGALQDLKTETG-AKFYADKADadvlrt 130
Cdd:cd07723    11 IYLIVDEATGeaAVVDPGEAE--PVLAA-LEKNGLTLTAI---LTTHHHWDHTGGNAELKALFPdAPVYGPAED------ 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1238338877 131 ggnsdyemgkygvtfKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETKD 188
Cdd:cd07723    79 ---------------RIPGLDHPVKDGDEIKLGGLEVKVLHTPGHTLGHICYYVPDEP 121
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
56-198 1.54e-13

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 67.98  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  56 LIVTDKGNILINTGTAESL-PIIKANIQKLGFnyKDIKILLLTQAHYDHTGALQDLKtETGAKFYADKADADVLRTGGNS 134
Cdd:cd16282    19 FIVGDDGVVVIDTGASPRLaRALLAAIRKVTD--KPVRYVVNTHYHGDHTLGNAAFA-DAGAPIIAHENTREELAARGEA 95
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 135 DYEMGKYGV-----TFKPVTPDKTLKDQDKITLGNTILTLLHH-PGHTKGScSFIFetkDEKRKyrVLIA 198
Cdd:cd16282    96 YLELMRRLGgdamaGTELVLPDRTFDDGLTLDLGGRTVELIHLgPAHTPGD-LVVW---LPEEG--VLFA 159
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
54-193 2.49e-13

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: 66.88  E-value: 2.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  54 SYLIVTDKGNILINTGT-AESLPIIKANIQKLGFnykdikILLLTQAHYDHTGALQDLktetgAKFYADKADADVLRTGG 132
Cdd:cd07712    11 IYLLRGRDRALLIDTGLgIGDLKEYVRTLTDLPL------LVVATHGHFDHIGGLHEF-----EEVYVHPADAEILAAPD 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238338877 133 NSD---YEMGKYGVtfKPVTPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIfetkDEKRKY 193
Cdd:cd07712    80 NFEtltWDAATYSV--PPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGSIALL----DRANRL 137
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
31-188 3.50e-13

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: 67.62  E-value: 3.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  31 WNQTYEPFRIAGNLYYVGTYDLA--SYLIVTDKGNILINTGTAESLPI------------------IKANIQKLGFNYKD 90
Cdd:cd07729     9 TVTVDKSSLFYYGRGPGEPIDLPvyAYLIEHPEGTILVDTGFHPDAADdpgglelafppgvteeqtLEEQLARLGLDPED 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  91 IKILLLTQAHYDHTGALQDLKtetGAKFYADKADADVLRTGGNSDYEMGKYGVTFKPVTPDKTLK--DQDKITLGNtiLT 168
Cdd:cd07729    89 IDYVILSHLHFDHAGGLDLFP---NATIIVQRAELEYATGPDPLAAGYYEDVLALDDDLPGGRVRlvDGDYDLFPG--VT 163
                         170       180
                  ....*....|....*....|
gi 1238338877 169 LLHHPGHTKGSCSFIFETKD 188
Cdd:cd07729   164 LIPTPGHTPGHQSVLVRLPE 183
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
77-182 9.57e-13

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: 64.87  E-value: 9.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  77 IKANIQKLGFNYKDIKILLLTQAHYDHTGALQDLKTETGAKFYADKADADVlrtggnsdyemgkYGVTFKPVTPdktLKD 156
Cdd:cd16275    34 IEKILAKLNELGLTLTGILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDY-------------YGFRCPNLIP---LED 97
                          90       100
                  ....*....|....*....|....*.
gi 1238338877 157 QDKITLGNTILTLLHHPGHTKGSCSF 182
Cdd:cd16275    98 GDTIKIGDTEITCLLTPGHTPGSMCY 123
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
55-190 2.65e-12

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: 65.26  E-value: 2.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  55 YLIVTDKGNILINTGTAESLPI----IKANIQKLGFNYKDIKILLLTQAHYDHT-GALQDLKTET--GAKFYADKADADV 127
Cdd:cd07720    52 FLVRTGGRLILVDTGAGGLFGPtagkLLANLAAAGIDPEDIDDVLLTHLHPDHIgGLVDAGGKPVfpNAEVHVSEAEWDF 131
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 128 LRTGGNSDYEMGKYGVTFKP----VTPdktLKDQDKITLGNTIL---TLLHHPGHTKGSCSFIFETKDEK 190
Cdd:cd07720   132 WLDDANAAKAPEGAKRFFDAardrLRP---YAAAGRFEDGDEVLpgiTAVPAPGHTPGHTGYRIESGGER 198
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
54-191 5.42e-12

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: 63.09  E-value: 5.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  54 SYLIVTDKGNILINTG--TAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDLKTETGAKFYADkadadvlrtg 131
Cdd:cd07725    17 VYLLRDGDETTLIDTGlaTEEDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGATVYIL---------- 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 132 gnsdyemgkygvtfkpvtPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFEtkDEKR 191
Cdd:cd07725    87 ------------------DVTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDE--DRRE 126
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
77-183 4.04e-10

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: 57.95  E-value: 4.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  77 IKANIQKLGFNykdIKILLLTQAHYDHTGALQDLKTETGAKFYA-DKADADVLrtggNSDYEMGK-YGVTF-KPVTPDKT 153
Cdd:cd07737    36 ILQAIEDLGLT---LKKILLTHGHLDHVGGAAELAEHYGVPIIGpHKEDKFLL----ENLPEQSQmFGFPPaEAFTPDRW 108
                          90       100       110
                  ....*....|....*....|....*....|
gi 1238338877 154 LKDQDKITLGNTILTLLHHPGHTKGSCSFI 183
Cdd:cd07737   109 LEEGDTVTVGNLTLEVLHCPGHTPGHVVFF 138
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
48-188 4.81e-10

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: 57.41  E-value: 4.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  48 GTYdlaSYLIVtDKGnilinTGTA-------ESLPIIKANIQKLGFnykDIKILLLTQAHYDH-TGAlQDLKTETGAKFY 119
Cdd:cd07724    11 GTL---SYLVG-DPE-----TGEAavidpvrDSVDRYLDLAAELGL---KITYVLETHVHADHvSGA-RELAERTGAPIV 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238338877 120 AdkadadvlrtGGNSDYEMgkygvtfkpvtPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIFETKD 188
Cdd:cd07724    78 I----------GEGAPASF-----------FDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPD 125
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
60-241 5.48e-10

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: 57.54  E-value: 5.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  60 DKGNILINTGTAESLP-IIKANIQKLGFNykdIKILLLTQAHYDHTGALQDLKTETGAKFYADKADADVLR--------T 130
Cdd:cd07743    17 DKEALLIDSGLDEDAGrKIRKILEELGWK---LKAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAFIEnpllepsyL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 131 GGNS--DYEMGKYgVTFKPVTPDKTLKDqDKITLGNTILTLLHHPGHTKGSCSFIFETK---------DEK--RKYRVLi 197
Cdd:cd07743    94 GGAYppKELRNKF-LMAKPSKVDDIIEE-GELELGGVGLEIIPLPGHSFGQIGILTPDGvlfagdalfGEEvlEKYGIP- 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1238338877 198 anmpsIIVDkkfseVTAYLNiqsdyayTFKAMKNLDFDLWVASH 241
Cdd:cd07743   171 -----FLYD-----VEEQLE-------TLEKLEELDADYYVPGH 197
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
54-185 7.06e-10

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: 57.16  E-value: 7.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  54 SYLIVTDKGNILINTGtaESLPIIKANIQKL--GFNYKDIKILLLTQAHYDHTG---ALQDLKTETGAKFYADKADADvl 128
Cdd:cd07722    20 TYLVGTGKRRILIDTG--EGRPSYIPLLKSVldSEGNATISDILLTHWHHDHVGglpDVLDLLRGPSPRVYKFPRPEE-- 95
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1238338877 129 rtggnsDYEMGKYGVTFKPvtpdktLKDQDKITLGNTILTLLHHPGHTKGSCSFIFE 185
Cdd:cd07722    96 ------DEDPDEDGGDIHD------LQDGQVFKVEGATLRVIHTPGHTTDHVCFLLE 140
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
43-243 5.05e-09

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 54.90  E-value: 5.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  43 NLYYV--GTYDlaSYLIVTDKGNILI----NTGTAeslpIIKAnIQKLGFnyKDIKILLLTQAHYDHTGALQDLKTEtGA 116
Cdd:cd16276     1 GVYWVtdGGYQ--SMFLVTDKGVIVVdappSLGEN----LLAA-IRKVTD--KPVTHVVYSHNHADHIGGASIFKDE-GA 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 117 KFYADKADADVLRTGGNSdyemgkygvtfKPVTPDKTLKDQDKITLGNTILTLLHH-PGHTKGScSFIFEtkdekRKYRV 195
Cdd:cd16276    71 TIIAHEATAELLKRNPDP-----------KRPVPTVTFDDEYTLEVGGQTLELSYFgPNHGPGN-IVIYL-----PKQKV 133
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1238338877 196 LIAnmPSIIVDKK--FSEVTAYLNIQsDYAYTFKAMKNLDFDLWVASHAS 243
Cdd:cd16276   134 LMA--VDLINPGWvpFFNFAGSEDIP-GYIEALDELLEYDFDTFVGGHGN 180
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
95-185 7.30e-09

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 54.42  E-value: 7.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  95 LLTQAHYDHTGALQDLKTETGAkfyadkadadvlRTGGNSDYEMGKYGVTFKpvtPDKTLKDQDKITLGNTILTLLHHPG 174
Cdd:cd16278    58 LVTHTHRDHSPGAARLAERTGA------------PVRAFGPHRAGGQDTDFA---PDRPLADGEVIEGGGLRLTVLHTPG 122
                          90
                  ....*....|.
gi 1238338877 175 HTKGSCSFIFE 185
Cdd:cd16278   123 HTSDHLCFALE 133
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
66-184 1.16e-08

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 55.23  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  66 INTGT------AESLPIIKAnIQKLGFNYKDIkilLLTQAHYDHTGALQDLKTETGAKFYADKADADvlRTGGnsdyemg 139
Cdd:PLN02398   95 EDTGTvgvvdpSEAVPVIDA-LSRKNRNLTYI---LNTHHHYDHTGGNLELKARYGAKVIGSAVDKD--RIPG------- 161
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1238338877 140 kygvtfkpvtPDKTLKDQDKITLGNTILTLLHHPGHTKGSCSFIF 184
Cdd:PLN02398  162 ----------IDIVLKDGDKWMFAGHEVLVMETPGHTRGHISFYF 196
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
54-120 3.21e-08

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 53.35  E-value: 3.21e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1238338877  54 SYLIVTDKGNILINTGTAEslpIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQD-LKTETGAKFYA 120
Cdd:COG1237    24 SALIETEGKRILFDTGQSD---VLLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLPAlLELNPKAPVYA 88
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
53-190 5.84e-08

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 52.59  E-value: 5.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  53 ASYLIVTDKGNILINTGTAeslpiIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDLKTETGAK---FYADKADADVLR 129
Cdd:COG1235    36 SSILVEADGTRLLIDAGPD-----LREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYGPNpipVYATPGTLEALE 110
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238338877 130 TGGNSDYEMGKYGVTFKPVTPDKTlkdqdkITLGN---TILTLLHHPGHTkgsCSFIFETKDEK 190
Cdd:COG1235   111 RRFPYLFAPYPGKLEFHEIEPGEP------FEIGGltvTPFPVPHDAGDP---VGYRIEDGGKK 165
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
56-198 1.23e-07

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: 50.66  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  56 LIVTDKGNILINTGTAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDLKtetGAKFYADkadadvlrtggnSD 135
Cdd:cd07711    26 LIKDGGKNILVDTGTPWDRDLLLKALAEHGLSPEDIDYVVLTHGHPDHIGNLNLFP---NATVIVG------------WD 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1238338877 136 YEMGKYGvtfkpvtpDKTLKDQDKITLGNTIlTLLHHPGHTKGSCSFIFETKDEKrkyRVLIA 198
Cdd:cd07711    91 ICGDSYD--------DHSLEEGDGYEIDENV-EVIPTPGHTPEDVSVLVETEKKG---TVAVA 141
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
54-120 1.40e-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: 51.47  E-value: 1.40e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1238338877  54 SYLIVTDKGNILINTGTAeslPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQD-LKTETGAKFYA 120
Cdd:cd07713    22 SLLIETEGKKILFDTGQS---GVLLHNAKKLGIDLSDIDAVVLSHGHYDHTGGLKAlLELNPKAPVYA 86
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
43-196 2.12e-07

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: 49.89  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  43 NLYYVGT-----YDLASYLIVTDKGNILINTGTAesLPIIKANIQKLGfnykDIKILLLTqaHYDHTGALQDLKTETGAK 117
Cdd:cd07727     1 GVYYCGFhseksFGAASYLILRPEGNILVDSPRY--SPPLAKRIEALG----GIRYIFLT--HRDDVADHAKWAERFGAK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877 118 FYADKADAD-------VLRTGGNSDYEMGkygvtfkpvtPDktlkdqdkitlgntiLTLLHHPGHTKGSCSFIFetkdek 190
Cdd:cd07727    73 RIIHEDDVNavtrpdeVIVLWGGDPWELD----------PD---------------LTLIPVPGHTRGSVVLLY------ 121

                  ....*.
gi 1238338877 191 RKYRVL 196
Cdd:cd07727   122 KEKGVL 127
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
44-190 3.11e-07

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 49.92  E-value: 3.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  44 LYYVGTydlASYLIVTDKGNILIN---TGTAESLPIIKANIQKLGfnykDIKILLLTQAHYDHTG--ALQDLKtETGAKF 118
Cdd:COG2220     6 ITWLGH---ATFLIETGGKRILIDpvfSGRASPVNPLPLDPEDLP----KIDAVLVTHDHYDHLDdaTLRALK-RTGATV 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1238338877 119 YADKADADVLRTGGnsdyemgkygvtFKPVTPdktLKDQDKITLGNTILTLL---HHPGHTKGS----CSFIFETKDEK 190
Cdd:COG2220    78 VAPLGVAAWLRAWG------------FPRVTE---LDWGESVELGGLTVTAVparHSSGRPDRNgglwVGFVIETDGKT 141
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
63-175 1.06e-06

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: 48.07  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  63 NILINTGT---AESLPIIkaniQKLGFNYKDIKILLLTQAHYDHTGALQDLKTETGAKFYADKADADVLRTGGNSDYEMG 139
Cdd:pfam12706   2 RILIDPGPdlrQQALPAL----QPGRLRDDPIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLRRNFPYLFLLE 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1238338877 140 KYGVTFKPVTPDKTlkdqdkITLGNTILTLLHHPGH 175
Cdd:pfam12706  78 HYGVRVHEIDWGES------FTVGDGGLTVTATPAR 107
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
46-177 3.09e-06

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: 46.89  E-value: 3.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  46 YVGTYDLASYLIV-TDKGNILINTG-----TAESLPIIKANIQKlgfnykDIKILLLTQAHYDHTGALQDLKTEtGAKFY 119
Cdd:cd16304    19 FNGTPVPSNGLIVeTSKGVVLIDTPwddeqTEELLDWIKKKLKK------PVTLAIVTHAHDDRIGGIKALQKR-GIPVY 91
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1238338877 120 ADKADADVLRTGGnsdyemgkYGVtfkpvtPDKTLKDQDKITLGNT-ILTLLHHPGHTK 177
Cdd:cd16304    92 STKLTAQLAKKQG--------YPS------PDGILKDDTTLKFGNTkIETFYPGEGHTA 136
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
40-174 7.04e-06

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: 46.33  E-value: 7.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  40 IAGNLYYVGTYDLA-----------------SYLIVTDKgNILINTGTAESLPIIKANIQKLgFNYKDIKILLLTQAHYD 102
Cdd:cd07709     3 IADDIYWVGVNDWDlrlfegeyptprgtsynSYLIKDEK-TALIDTVKEPFFDEFLENLEEV-IDPRKIDYIVVNHQEPD 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1238338877 103 HTGALQDLKTET-GAKFYADKADADVLRTGGNSDYEmgkygvTFKPVtpdktlKDQDKITLGNTILTL-----LHHPG 174
Cdd:cd07709    81 HSGSLPELLELApNAKIVCSKKAARFLKHFYPGIDE------RFVVV------KDGDTLDLGKHTLKFipapmLHWPD 146
metallo-hydrolase-like_MBL-fold cd16279
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; ...
53-185 4.28e-05

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo; 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 named as octanoyltransferase (also known as lipoate-protein ligase B).


Pssm-ID: 293837 [Multi-domain]  Cd Length: 193  Bit Score: 43.23  E-value: 4.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  53 ASYLIVTDKGNILINTGtaeslP-----IIKANIQKLGFnykdikiLLLTQAHYDHTGALQDL-----KTETGAKFYADK 122
Cdd:cd16279    36 SSILIETGGKNILIDTG-----PdfrqqALRAGIRKLDA-------VLLTHAHADHIHGLDDLrpfnrLQQRPIPVYASE 103
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1238338877 123 ADADVLRTGGNSDYEMGKYGvtFKPVTPDKTLKDQDKITLGN---TILTLLHHPGHTKGscsFIFE 185
Cdd:cd16279   104 ETLDDLKRRFPYFFAATGGG--GVPKLDLHIIEPDEPFTIGGleiTPLPVLHGKLPSLG---FRFG 164
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
54-171 7.13e-05

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 42.51  E-value: 7.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  54 SYLIVTDKGNILINTGTAESL--PIIKANIQKLGfnYKDIKILLLTQAHYDHTGALQDLKTE-TGAKFYADKADADvLRT 130
Cdd:cd07731    12 AILIQTPGKTILIDTGPRDSFgeDVVVPYLKARG--IKKLDYLILTHPDADHIGGLDAVLKNfPVKEVYMPGVTHT-TKT 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1238338877 131 GGNSDYEMGKYGVTFKPVTPDktlkdqDKITLGNTILTLLH 171
Cdd:cd07731    89 YEDLLDAIKEKGIPVTPCKAG------DRWQLGGVSFEVLS 123
PRK02113 PRK02113
MBL fold metallo-hydrolase;
53-130 7.38e-05

MBL fold metallo-hydrolase;


Pssm-ID: 179371 [Multi-domain]  Cd Length: 252  Bit Score: 43.23  E-value: 7.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  53 ASYLIVTDKGNILINTGtaeslPIIKANIQKLGFnyKDIKILLLTQAHYDHTGALQDLKTETGAK---FYADKADADVLR 129
Cdd:PRK02113   36 TSALVETEGARILIDCG-----PDFREQMLRLPF--GKIDAVLITHEHYDHVGGLDDLRPFCRFGevpIYAEQYVAERLR 108

                  .
gi 1238338877 130 T 130
Cdd:PRK02113  109 S 109
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
53-107 8.25e-05

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: 42.45  E-value: 8.25e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1238338877  53 ASYLIVTDKGNILINTG---TAESLPiiKANIQKLGFNYKDIKILLLTQAHYDHTGAL 107
Cdd:cd16295    13 SCYLLETGGKRILLDCGlfqGGKELE--ELNNEPFPFDPKEIDAVILTHAHLDHSGRL 68
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
26-105 1.80e-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: 42.10  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  26 NMPKE-WNQTYEP---FRIagnlyyvgtyDLAS--YLIVTDKGNILINTGT-------------AESLPIIKANIQKLGF 86
Cdd:cd16281    21 VVPKPlWQKWYPAdedNRI----------TLAMrcLLIETGGRNILIDTGIgdkqdpkfrsiyvQHSEHSLLKSLARLGL 90
                          90
                  ....*....|....*....
gi 1238338877  87 NYKDIKILLLTQAHYDHTG 105
Cdd:cd16281    91 SPEDITDVILTHLHFDHCG 109
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
56-193 2.61e-04

Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; MBL-fold metallo-hydrolase domain; CPSF3 (cleavage and polyadenylation specificity factor subunit 3; also known as cleavage and polyadenylation specificity factor 73 kDa subunit, CPSF-73) and CPSF2 (also known as cleavage and polyadenylation specificity factor 100 kDa subunit /CPSF-100) are components of the CPSF complex, which plays a role in 3' end processing of pre-mRNAs during cleavage/polyadenylation, and during processing of metazoan histone pre-mRNAs. CPSF3 functions as a 3' endonuclease. Int11 (also known as cleavage and polyadenylation-specific factor (CPSF) 3-like protein, and protein related to CPSF subunits of 68 kDa (RC-68)), and Int9, also known as protein related to CPSF subunits of 74 kDa (RC-74) are subunits of Integrator, a metazoan-specific multifunctional protein complex composed of 14 subunits. Integrator has been implicated in a variety of Pol II transcription events including 3' end processing of snRNA, transcription initiation, promoter-proximal pausing, termination of protein-coding transcripts, and in HVS pre-miRNA 3' end processing. 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: 293820 [Multi-domain]  Cd Length: 193  Bit Score: 41.16  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  56 LIVTDKGNILINTGTAESLPIIKANIQKLGFNYKDIKILLLTQAHYDHTGALQDLKTETGAK--FYADKADADVLRTgGN 133
Cdd:cd07734    15 LVEFKGRTVLLDCGMNPGKEDPEACLPQFELLPPEIDAILISHFHLDHCGALPYLFRGFIFRgpIYATHPTVALGRL-LL 93
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1238338877 134 SDY-----EMGKYGVTFKPVTPDKTLKDQDKITLGNTI-----LTLL-HHPGHTKGSCSFIFETKDEKRKY 193
Cdd:cd07734    94 EDYvksaeRIGQDQSLYTPEDIEEALKHIVPLGYGQSIdlfpaLSLTaYNAGHVLGAAMWEIQIYGEKLVY 164
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
54-107 4.15e-04

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 41.33  E-value: 4.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1238338877  54 SYLIVTDKGNILINTGTAESLPiiKANIQKLGFNYKDIKILLLTQAHYDHTGAL 107
Cdd:COG1236    16 CYLLETGGTRILIDCGLFQGGK--ERNWPPFPFRPSDVDAVVLTHAHLDHSGAL 67
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
38-125 5.05e-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: 40.56  E-value: 5.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  38 FRIAGNLYYVGTYDLA-SYLIVTDKGNILINTG-TAESLPIIKANIQKLgFNYKDIKILLLTQAHYDHTGalqdlktetG 115
Cdd:cd07710     3 FEVTDGVYQVRGYDLSnMTFIEGDTGLIIIDTLeSAEAAKAALELFRKH-TGDKPVKAIIYTHSHPDHFG---------G 72
                          90
                  ....*....|
gi 1238338877 116 AKFYADKADA 125
Cdd:cd07710    73 AGGFVEEEDS 82
arylsulfatase_AtsA-like_MBL-fold cd07719
Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold ...
53-188 5.86e-04

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: 40.19  E-value: 5.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  53 ASYLIVTDKGNILINTGTAESLpiikaNIQKLGFNYKDIKILLLTQAHYDHTGALQDL---------------------K 111
Cdd:cd07719    19 PSTLVVVGGRVYLVDAGSGVVR-----RLAQAGLPLGDLDAVFLTHLHSDHVADLPALlltawlagrktplpvygppgtR 93
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238338877 112 TETGAKFYADKADADVLRTGGNSDYEMGKYGVTFKPVTPDKTLKDQDKITLgNTILTllHHpGHTKGSCSFIFETKD 188
Cdd:cd07719    94 ALVDGLLAAYALDIDYRARIGDEGRPDPGALVEVHEIAAGGVVYEDDGVKV-TAFLV--DH-GPVPPALAYRFDTPG 166
NorV COG0426
Flavorubredoxin [Energy production and conversion];
37-175 1.76e-03

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 39.43  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  37 PFRIAGNLYYVG-------------------TYDlaSYLIVTDKgNILINTGTAESLPIIKANIQKLgFNYKDIKILLLT 97
Cdd:COG0426     2 AVEIAHGVYWVGvldwdrrlfegeyptprgtTYN--SYLIVDEK-TALIDTVGESFFEEFLENLSKV-IDPKKIDYIIVN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  98 qaHY--DHTGALQD-LKTETGAKFYADKADADVLRtggnsDYeMGKYGVTFKPVtpdktlKDQDKITLGNTILTL----- 169
Cdd:COG0426    78 --HQepDHSGSLPElLELAPNAKIVCSKKAARFLP-----HF-YGIPDFRFIVV------KEGDTLDLGGHTLQFipapm 143

                  ....*.
gi 1238338877 170 LHHPGH 175
Cdd:COG0426   144 LHWPDT 149
PLN02469 PLN02469
hydroxyacylglutathione hydrolase
91-189 3.42e-03

hydroxyacylglutathione hydrolase


Pssm-ID: 178088 [Multi-domain]  Cd Length: 258  Bit Score: 38.20  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238338877  91 IKILLLTQAHYDHTGALQDLK-TETGAKFYadkadadvlrtGGNSDyemGKYGVTFKpvtpdktLKDQDKITLGNTILTL 169
Cdd:PLN02469   47 IKLVLTTHHHWDHAGGNEKIKkLVPGIKVY-----------GGSLD---NVKGCTHP-------VENGDKLSLGKDVNIL 105
                          90       100
                  ....*....|....*....|.
gi 1238338877 170 -LHHPGHTKGSCSFIFETKDE 189
Cdd:PLN02469  106 aLHTPCHTKGHISYYVTGKEG 126
 
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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