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Conserved domains on  [gi|13274146|emb|CAC33832|]
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THIN-B proetin [Janthinobacterium lividum]

Protein Classification

subclass B3 metallo-beta-lactamase( domain architecture ID 10888868)

subclass B3 metallo-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
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 41-298 4.79e-173

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: 479.48  E-value: 4.79e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  41 WNGEVTPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAAL 120
Cdd:cd16312   1 WNQPVKPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIEALGFRIEDVKLILNSHAHWDHAGGIAAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 121 QAASGATVVASASGALGLQSGTNGKDDPQFQAKPVVHVAKVEKVKVVGEGDAIKLGPLNLTAHMTPGHTPGATTWTWTSC 200
Cdd:cd16312  81 QKASGATVAASAHGAQVLQSGTNGKDDPQYQAKPVVHVAKVAKVKEVGEGDTLKVGPLRLTAHMTPGHTPGGTTWTWTSC 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 201 EGQRCLDVVYADSLNPYSSGDFTYTGKGDGPDISASFAASIAKVAALPCDIILSVHPDSTGVLDKAAKRSGEHNPFIDAN 280
Cdd:cd16312 161 EGQRCLDVVYADSLNPYSSGDFYYTGKGGYPDISASFRASIAKVAALPCDIIIAVHPGFTDVLDKAKRRSGDTNPFIDAE 240

                       250
                ....*....|....*...
gi 13274146 281 ACRAYAATADAMLTKRLA 298
Cdd:cd16312 241 ACRAYAAGAAKSLEKRLA 258
 
Name Accession Description Interval E-value
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 41-298 4.79e-173

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: 479.48  E-value: 4.79e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  41 WNGEVTPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAAL 120
Cdd:cd16312   1 WNQPVKPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIEALGFRIEDVKLILNSHAHWDHAGGIAAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 121 QAASGATVVASASGALGLQSGTNGKDDPQFQAKPVVHVAKVEKVKVVGEGDAIKLGPLNLTAHMTPGHTPGATTWTWTSC 200
Cdd:cd16312  81 QKASGATVAASAHGAQVLQSGTNGKDDPQYQAKPVVHVAKVAKVKEVGEGDTLKVGPLRLTAHMTPGHTPGGTTWTWTSC 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 201 EGQRCLDVVYADSLNPYSSGDFTYTGKGDGPDISASFAASIAKVAALPCDIILSVHPDSTGVLDKAAKRSGEHNPFIDAN 280
Cdd:cd16312 161 EGQRCLDVVYADSLNPYSSGDFYYTGKGGYPDISASFRASIAKVAALPCDIIIAVHPGFTDVLDKAKRRSGDTNPFIDAE 240

                       250
                ....*....|....*...
gi 13274146 281 ACRAYAATADAMLTKRLA 298
Cdd:cd16312 241 ACRAYAAGAAKSLEKRLA 258
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 64-256 6.34e-24

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: 97.07  E-value: 6.34e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  64 AVLVTSPQGHVLLD-GALPQSAPLIIANIAALGfriEDVKFILNSHAHWDHAGGIAALQAASGATVVASASGALGLQSGT 142
Cdd:COG0491  17 SYLIVGGDGAVLIDtGLGPADAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEAPA 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 143 NGKDDPQFQAKPvvhvakvekVKVVGEGDAIKLGPLNLTAHMTPGHTPGATTWTwtsCEGQRCL---DVVYADSlnpyss 219
Cdd:COG0491  94 AGALFGREPVPP---------DRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFY---VPDEKVLftgDALFSGG------ 155

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 13274146 220 gdftyTGKGDGPDISAS-FAASIAKVAALPCDIILSVH 256
Cdd:COG0491 156 -----VGRPDLPDGDLAqWLASLERLLALPPDLVIPGH 188
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 63-256 2.48e-22

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: 91.85  E-value: 2.48e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146     63 SAVLVTSPQGHVLLDgALPQSAPLIIANIAALGfrIEDVKFILNSHAHWDHAGGIAALQAASGATVVASASGALGLqsgt 142
Cdd:smart00849   1 NSYLVRDDGGAILID-TGPGEAEDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELL---- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146    143 ngKDDPQFQAKPVVHVAKVEKVKVVGEGDAIKLGPLNLTAHMTPGHTPGATTWTWtscegqRCLDVVYA-DSLNPYSSGD 221
Cdd:smart00849  74 --KDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL------PEGKILFTgDLLFAGGDGR 145

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 13274146    222 FTYTGkgdGPDISASFAASIAKVAALPCDIILSVH 256
Cdd:smart00849 146 TLVDG---GDAAASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
63-256 1.31e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 71.25  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146    63 SAVLVTSPQGHVLLDGALPQSAPLIIAnIAALGFRIEDVKFILNSHAHWDHAGGIAALQAASGATVVASASGALglqSGT 142
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLL-LAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAR---ELL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146   143 NGKDDPQFQAK--PVVHVAKVEKVKVVGEGDAIKLGPLNLTAHMTPGHTPGAttwtwtSCEGQRCLDVVYA-DSLNPYSS 219
Cdd:pfam00753  83 DEELGLAASRLglPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGH------VVVYYGGGKVLFTgDLLFAGEI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 13274146   220 GDFTYTGKG---DGPDISASFAASIAKVAALPCDIILSVH 256
Cdd:pfam00753 157 GRLDLPLGGllvLHPSSAESSLESLLKLAKLKAAVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 91-132 1.19e-04

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 43.29  E-value: 1.19e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 13274146   91 IAALGFRIEDVKFILNSHAHWDHAGGIAALQAASGATVVASA 132
Cdd:PLN02398 112 IDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSA 153
 
Name Accession Description Interval E-value
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 41-298 4.79e-173

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: 479.48  E-value: 4.79e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  41 WNGEVTPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAAL 120
Cdd:cd16312   1 WNQPVKPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIEALGFRIEDVKLILNSHAHWDHAGGIAAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 121 QAASGATVVASASGALGLQSGTNGKDDPQFQAKPVVHVAKVEKVKVVGEGDAIKLGPLNLTAHMTPGHTPGATTWTWTSC 200
Cdd:cd16312  81 QKASGATVAASAHGAQVLQSGTNGKDDPQYQAKPVVHVAKVAKVKEVGEGDTLKVGPLRLTAHMTPGHTPGGTTWTWTSC 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 201 EGQRCLDVVYADSLNPYSSGDFTYTGKGDGPDISASFAASIAKVAALPCDIILSVHPDSTGVLDKAAKRSGEHNPFIDAN 280
Cdd:cd16312 161 EGQRCLDVVYADSLNPYSSGDFYYTGKGGYPDISASFRASIAKVAALPCDIIIAVHPGFTDVLDKAKRRSGDTNPFIDAE 240

                       250
                ....*....|....*...
gi 13274146 281 ACRAYAATADAMLTKRLA 298
Cdd:cd16312 241 ACRAYAAGAAKSLEKRLA 258
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 ...
 41-297 1.99e-143

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: 404.42  E-value: 1.99e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  41 WNGEVTPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAAL 120
Cdd:cd16290   1 WNQPQAPFRIHGNTYYVGTGGLSAVLITSPQGLILIDGALPQSAPQIEANIRALGFRLEDVKLILNSHAHFDHAGGIAAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 121 QAASGATVVASASGALGLQSGTNGKDDPQFQAKPvvHVAKVEKVKVVGEGDAIKLGPLNLTAHMTPGHTPGATTWTWTSC 200
Cdd:cd16290  81 QRDSGATVAASPAGAAALRSGGVDPDDPQAGAAD--PFPPVAKVRVVADGEVVKLGPLAVTAHATPGHTPGGTSWTWRSC 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 201 EGQRCLDVVYADSLNPYSSGDFTYTGKGdGPDISASFAASIAKVAALPCDIILSVHPDSTGVLDKAAKRSGE--HNPFID 278
Cdd:cd16290 159 EGGRCLDIVYADSLTAVSADGFRFSDDA-HPARVAAFRRSIATVAALPCDILISAHPDASGLWEKLARRAREpgPNPFID 237

                       250
                ....*....|....*....
gi 13274146 279 ANACRAYAATADAMLTKRL 297
Cdd:cd16290 238 PNACRAYAAAAEARLEARL 256
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 41-298 9.71e-107

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: 311.41  E-value: 9.71e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  41 WNGEVTPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAAL 120
Cdd:cd16313   1 WNAPQEPFQIYGNTYYVGTGGISAVLITSPQGHILIDGGFPKSPEQIAASIRQLGFKLEDVKYILSSHDHWDHAGGIAAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 121 QAASGATVVASASGALGLQSGTNGKDDPQFQAKPVVHVAKVEKVKVVGEgdAIKLGPLNLTAHMTPGHTPGATTWTWTSC 200
Cdd:cd16313  81 QKLTGAQVLASPATVAVLRSGSMGKDDPQFGGLTPMPPVASVRAVRDGE--VVKLGPLAVTAHATPGHTTGGTSWTWQSC 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 201 EGQRCLDVVYADSLNPYSSGDFTYTGKgdgPDISASFAASIAKVAALPCDIILSVHPDSTGVLDKAAKRSGEHNP-FIDA 279
Cdd:cd16313 159 EQGRCANMVFADSLTAVSADGYRFSAH---PAVLADVEQSIAAVEKLACDILVSAHPEFSDMWTRVKRGAAEGNAaFIDG 235

                       250
                ....*....|....*....
gi 13274146 280 NACRAYAATADAMLTKRLA 298
Cdd:cd16313 236 GGCRAYAAKAREKLNKRLA 254
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 41-298 2.98e-105

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: 308.07  E-value: 2.98e-105
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  41 WNGEVTPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAAL 120
Cdd:cd16311   1 WNADQAPFRIFGNTYYVGVKGLSSVLVTSPQGHVLVDGGLPESAPKIIANIEALGFRIEDVKLILNSHGHIDHAGGLAEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 121 QAASGATVVASASGALGLQSGTNGKDDPQFQAKPVVHVAKVEKVKVVGEgdAIKLGPLNLTAHMTPGHTPGATTWTWTSC 200
Cdd:cd16311  81 QRRSGALVAASPSAALDLASGEVGPDDPQYHALPKYPPVKDMRLARDGG--QFNVGPVSLTAHATPGHTPGGLSWTWQSC 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 201 EGQRCLDVVYADSLNPYSSGDFTYTGKGDGPDISASFAASIAKVAALPCDIILSVHPDSTGVLDK-AAKRSGEHNPFIDA 279
Cdd:cd16311 159 DGPRCLNMVYADSQNAVSRPGFKFSASSEYPNAVADLRRSFETLEKLPCDVLISAHPEASQLWERlEASDRSARPALVDR 238

                       250
                ....*....|....*....
gi 13274146 280 NACRAYAATADAMLTKRLA 298
Cdd:cd16311 239 EACRRYASRAREALEKRIA 257
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 41-300 1.40e-98

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: 291.02  E-value: 1.40e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  41 WNGEVTPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAAL 120
Cdd:cd16314   1 WDDPAPPRRIYGNTWYVGTCGISALLVTSDAGHILIDGGTDKAAPLIEANIRALGFRPEDVRYIVSSHEHFDHAGGIARL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 121 QAASGATVVASASGALGLQSGTNGKDDPQFQAkpVVHVAKVEKVKVVGEGDAIKLGPLNLTAHMTPGHTPGATTWTWTSC 200
Cdd:cd16314  81 QRATGAPVVAREPAATTLERGRSDRSDPQFLV--VEKFPPVASVQRIGDGEVLRVGPLALTAHATPGHTPGGTSWTWRSC 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 201 EGQRCLDVVYADSLNPYSSGDFTYTgkgDGPDISASFAASIAKVAALPCDIILSVHPDSTGVLDKAAKRSGEhnPFIDAN 280
Cdd:cd16314 159 EGAVCRDMVYADSVTAISDDIYRYS---DHPGMVAAFRNTLDTVAALPCDILVTPHPSASGLWERLGPAAGI--PLADTG 233

                       250       260
                ....*....|....*....|
gi 13274146 281 ACRAYAATADAMLTKRLAKE 300
Cdd:cd16314 234 ACRAYAQTGRARLDARLADE 253
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 41-297 2.90e-96

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: 284.63  E-value: 2.90e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  41 WNGEVTPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAAL 120
Cdd:cd16315   1 WDKPAPPARIFGNTYYVGTCGISAILITGDDGHVLIDSGTEEAAPLVLANIRKLGFDPKDVRWLLSSHEHFDHVGGLAAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 121 QAASGATVVASASGALGLQSGTNGKDDPQFQAKPvvHVAKVEKVKVVGEGDAIKLGPLNLTAHMTPGHTPGATTWTWTSC 200
Cdd:cd16315  81 QRATGARVAASAAAAPVLESGKPAPDDPQAGLHE--PFPPVRVDRIVEDGDTVALGSLRLTAHATPGHTPGALSWTWRSC 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 201 EGQRCLDVVYADSLNPYSSGDFTYTgkgDGPDISASFAASIAKVAALPCDIILSVHPDSTGVLDKAAKRSgehnPFIDAN 280
Cdd:cd16315 159 EGADCRTIVYADSLSPVSADGYRFS---DHPDYVAAYRAGLAKVAALPCDILLTPHPSASDMFERLSGGA----PLADPD 231

                       250
                ....*....|....*..
gi 13274146 281 ACRAYAATADAMLTKRL 297
Cdd:cd16315 232 ACAAYAAGAEKRLDERL 248
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 41-289 1.22e-83

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: 252.47  E-value: 1.22e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  41 WNGEVTPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAAL 120
Cdd:cd07708   1 WPNPFPPFQIAGNTYYVGTDDLAAYLIVTPQGNILIDGDMEQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAEI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 121 QAASGATVVASASGALGLQSGtnGKDDPQFQAKPVVHVAKVEKVKVVGEGDAIKLGPLNLTAHMTPGHTPGATTWTWTSC 200
Cdd:cd07708  81 KKQTGAKVMAGAEDVSLLLSG--GSSDFHYANDSSTYFPQSTVDRAVHDGERVTLGGTVLTAHATPGHTPGCTTWTMTLK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 201 EGQRCLDVVYADSLNpySSGDFTYTGKGDGPDISASFAASIAKVAALPCDIILSVHPDSTGVLDKAAKRS-GEHNPFIDA 279
Cdd:cd07708 159 DHGKQYQVVFADSLT--VNPGYRLVDNPTYPKIVEDYRHSFAVVEAMRCDILLGPHPGVFDMKNKYVLLSkGQNNPFVDP 236

                       250
                ....*....|
gi 13274146 280 NACRAYAATA 289
Cdd:cd07708 237 GGCKAYAEAK 246
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 41-298 6.68e-80

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: 243.38  E-value: 6.68e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  41 WNGEVTPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAAL 120
Cdd:cd16288   1 WNAPFEPFRIAGNVYYVGTSGLASYLITTPQGLILIDTGLESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 121 QAASGATVVASASGALGLQSGtnGKDDPQFqAKPVVHVAKVEKVKVVGEGDAIKLGPLNLTAHMTPGHTPGATTWTWTSC 200
Cdd:cd16288  81 KKLTGAKLMASAEDAALLASG--GKSDFHY-GDDSLAFPPVKVDRVLKDGDRVTLGGTTLTAHLTPGHTRGCTTWTMTVK 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 201 EGQRCLDVVYADSLNpySSGDFTYTGKGDGPDISASFAASIAKVAALPCDIILSVHPDSTGVLDKAAK-RSGEHNPFIDA 279
Cdd:cd16288 158 DDGKVYQVVFADSLT--VNPGYKLVGNPTYPGIAEDYRHSFATLRALQCDIFLASHAEYFDLKEKRARlAAGQPNAFIDP 235

                       250
                ....*....|....*....
gi 13274146 280 NACRAYAATADAMLTKRLA 298
Cdd:cd16288 236 EGYRNFIEKAKADFEKQLA 254
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 41-298 1.91e-70

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: 218.89  E-value: 1.91e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  41 WNGEVTPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAAL 120
Cdd:cd16309   1 WNEPMEPFKLIGNIYYVGTAGLGVFLITTPEGHILIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAEL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 121 QAASGATVVASASGALGLQSGTNGKDDPQFQAKPvvhvaKVEKVKVVGEGDAIKLGPLNLTAHMTPGHTPGATTWTWTSC 200
Cdd:cd16309  81 KKATGAQLVASAADKPLLESGYVGSGDTKNLQFP-----PVRVDRVIGDGDKVTLGGTTLTAHLTPGHSPGCTSWTTTVK 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 201 EGQR--------CLDVVYADSLnpysSGDFTYtgkgdgPDISASFAASIAKVAALPCDIILSVHPDSTGVLDKAAKRS-G 271
Cdd:cd16309 156 DTAGpprevlffCSATVAGNQL----VGPPTY------PGIVDDYRATFAKARAMKADVFLANHPEFFGLVAKRARQSaG 225

                       250       260
                ....*....|....*....|....*..
gi 13274146 272 EHNPFIDANACRAYAATADAMLTKRLA 298
Cdd:cd16309 226 EPDAFVDAGELQRFNTKMEDDFEKALA 252
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 41-298 9.62e-65

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: 204.61  E-value: 9.62e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  41 WNGEVTPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAAL 120
Cdd:cd16310   1 WTAPTEPFRIVDNIYYVGTKGIGSYLITSNHGAILLDGGLEENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 121 QAASGATVVASASGALGLQSGTNgKDDPQFQAKPvvhVAKVEKVKVVGEGDAIKLGPLNLTAHMTPGHTPGATTWTWTSC 200
Cdd:cd16310  81 KADTGAKLWASRGDRPALEAGKH-IGDNITQPAP---FPAVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTWSTTVK 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 201 EGQRCLDVVYADSLnpySSGDFTYTGKGDGPDISASFAASIAKVAALPCDIILSVHPDSTGVLDKAAKR-SGEHNPFIDA 279
Cdd:cd16310 157 ENGRPLRVVFPCSL---SVAGNVLVGNKTYPTIVEDYRASFARLRAMKADIVLTSHPEVADLLARKAKQdAGQANAFVDP 233

                       250
                ....*....|....*....
gi 13274146 280 NACRAYAATADAMLTKRLA 298
Cdd:cd16310 234 GELARIVDQSEAAFNKELA 252
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 41-291 1.29e-58

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: 188.10  E-value: 1.29e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  41 WNGEVTPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAAL 120
Cdd:cd16289   1 WLQPMAPLQIADHTWYIGTESLTALLVKTPDGAVLLDGGMPQAADMLLDNMRALGVAPGDLKLILHSHAHADHAGPLAAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 121 QAASGATVVASASGALGLQSGtnGKDDPQFQAKPVVHVAKVEKVKVVGEgdAIKLGPLNLTAHMTPGHTPGATTWTWTSC 200
Cdd:cd16289  81 KRATGARVAANAESAVLLARG--GSDDIHFGDGITFPPVQADRIVMDGE--VVTLGGVTFTAHFTPGHTPGSTSWTWTDT 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 201 EGQRCLDVVYADSLnpySSGDFTYTGKGDGPDISASFAASIAKVAALPCDIILSVHPDSTGvLDKAAKRSGEHNPFidan 280
Cdd:cd16289 157 RDGKPVRIAYADSL---SAPGYQLLGNPRYPRIVEDYRRTFATVRALPCDVLLTPHPGASG-WDYAAGAAPHAKPM---- 228

                       250
                ....*....|.
gi 13274146 281 ACRAYAATADA 291
Cdd:cd16289 229 TCKAYADAAEQ 239
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 41-298 7.94e-54

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: 176.48  E-value: 7.94e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  41 WNGEVTPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAAL 120
Cdd:cd16307   1 WTTPFPPFRIAGNLYYVGSRDLASYLITTPRGNILINSNLESSVPQIKASIEKLGFKFSDTKILLISHAHFDHAAGSALI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 121 QAASGATVVASASGALGLQSGtnGKDDPQFQAKPVVHVAKVEKVKVVGEGDAIKLGPLNLTAHMTPGHTPGATTWTWTSC 200
Cdd:cd16307  81 KRETHAKYMVMDGDVDVVESG--GKSDFFYGNDPSTYFPPAHVDKVLHDGEQVELGGTVLTAHLTAGHTKGCTTWTMKVK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 201 EGQRCLDVVYADSLNPYSSGDFTYTGKgdGPDISASFAASIAKVAALPCDIILSVHPDSTGVLDKAAKRSGEH-NPFIDA 279
Cdd:cd16307 159 DHGKTYDVVIVGSPNVNPGAKLVNNIT--YPGIAEDYAHTFAVLRSLPCDIFLGAHGGYFDLKNKYVRLQKGGaNPFIDP 236

                       250
                ....*....|....*....
gi 13274146 280 NACRAYAATADAMLTKRLA 298
Cdd:cd16307 237 EGYKAYVAEKEQAFRTELE 255
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 41-298 3.72e-43

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: 148.50  E-value: 3.72e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  41 WNGEVTPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDgAL--PQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIA 118
Cdd:cd16280   1 KKGYVEPFQVFDNLYYVGNKWVSAWAIDTGDGLILID-ALnnNEAADLIVDGLEKLGLDPADIKYILITHGHGDHYGGAA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 119 ALQAASGATVVASASGALGLQSGTNGKDDPQFQAKPVVHVAKVekvkvvgEGDAIKLGPLNLTAHMTPGHTPGATTWTWT 198
Cdd:cd16280  80 YLKDLYGAKVVMSEADWDMMEEPPEEGDNPRWGPPPERDIVIK-------DGDTLTLGDTTITVYLTPGHTPGTLSLIFP 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 199 SCEGQRcldvvyadslnPYSSGDFTYTGKGDGPDISA--SFAASIAKVAAL----PCDIILSVHPDSTGVLDKAAK---- 268
Cdd:cd16280 153 VKDGGK-----------THRAGLWGGTGLNTGPNLERreQYIASLERFKKIaeeaGVDVFLSNHPFQDGSLEKREAlrnr 221

                       250       260       270
                ....*....|....*....|....*....|
gi 13274146 269 RSGEHNPFIDANACRAYAATADAMLTKRLA 298
Cdd:cd16280 222 KPGEPNPFVDGQAWVDFYDEVLALCARVLA 251
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 41-278 2.94e-42

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: 146.46  E-value: 2.94e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  41 WNGEVTPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAAL 120
Cdd:cd16308   1 WSQPYAPFRIAGNLYYVGTYDLACYLIVTPKGNILINTGLAESVPLIKKNIQALGFKFKDIKILLTTQAHYDHVGAMAAI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 121 QAASGATVVASASGALGLQSGtnGKDDPQFqAKPVVHVAKVEKVKVVGEGDAIKLGPLNLTAHMTPGHTPGATTWTWTSC 200
Cdd:cd16308  81 KQQTGAKMMVDEKDAKVLADG--GKSDYEM-GGYGSTFAPVKADKLLHDGDTIKLGGTKLTLLHHPGHTKGSCSFLFDVK 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 201 EGQRCLDVVYAD--SLNPyssgDFTYTGKGDGPDISASFAASIAKVAALPCDIILSVHPDSTGvLDKAAKRSGEHNP--F 276
Cdd:cd16308 158 DEKRTYRVLIANmpTILP----DTKLSGMPGYPGIAKDYAYTFEAMKALSFDIWLASHASQFD-LHQKHKPGAPYNPaaF 232


                ..
gi 13274146 277 ID 278
Cdd:cd16308 233 AD 234
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 64-256 6.34e-24

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: 97.07  E-value: 6.34e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  64 AVLVTSPQGHVLLD-GALPQSAPLIIANIAALGfriEDVKFILNSHAHWDHAGGIAALQAASGATVVASASGALGLQSGT 142
Cdd:COG0491  17 SYLIVGGDGAVLIDtGLGPADAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEAPA 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 143 NGKDDPQFQAKPvvhvakvekVKVVGEGDAIKLGPLNLTAHMTPGHTPGATTWTwtsCEGQRCL---DVVYADSlnpyss 219
Cdd:COG0491  94 AGALFGREPVPP---------DRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFY---VPDEKVLftgDALFSGG------ 155

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 13274146 220 gdftyTGKGDGPDISAS-FAASIAKVAALPCDIILSVH 256
Cdd:COG0491 156 -----VGRPDLPDGDLAqWLASLERLLALPPDLVIPGH 188
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 63-256 2.48e-22

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: 91.85  E-value: 2.48e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146     63 SAVLVTSPQGHVLLDgALPQSAPLIIANIAALGfrIEDVKFILNSHAHWDHAGGIAALQAASGATVVASASGALGLqsgt 142
Cdd:smart00849   1 NSYLVRDDGGAILID-TGPGEAEDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELL---- 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146    143 ngKDDPQFQAKPVVHVAKVEKVKVVGEGDAIKLGPLNLTAHMTPGHTPGATTWTWtscegqRCLDVVYA-DSLNPYSSGD 221
Cdd:smart00849  74 --KDLLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL------PEGKILFTgDLLFAGGDGR 145

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 13274146    222 FTYTGkgdGPDISASFAASIAKVAALPCDIILSVH 256
Cdd:smart00849 146 TLVDG---GDAAASDALESLLKLLKLLPKLVVPGH 177
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 58-256 9.76e-21

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: 88.05  E-value: 9.76e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  58 GTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAALQAASGATVVASASGALG 137
Cdd:cd07721   7 LLPPVNAYLIEDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYAHEREAPY 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 138 LQSGTNGKDDPQFQAKPVVHV----AKVEKVKVVGEGDAIKLGPlNLTAHMTPGHTPGattwtwtSCegqrCL-----DV 208
Cdd:cd07721  87 LEGEKPYPPPVRLGLLGLLSPllpvKPVPVDRTLEDGDTLDLAG-GLRVIHTPGHTPG-------HI----SLyleedGV 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13274146 209 VYAdslnpyssGDFTYTGKGDGPDISASF-------AASIAKVAALPCDIILSVH 256
Cdd:cd07721 155 LIA--------GDALVTVGGELVPPPPPFtwdmeeaLESLRKLAELDPEVLAPGH 201
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 44-213 1.10e-16

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: 76.56  E-value: 1.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  44 EVTPFNVFG-NTWYVGTAGLSAVLVtspqghvllD-GALPQSAplIIANIAALGfriEDVKFILNSHAHWDHAGGIAALQ 121
Cdd:cd06262   1 KRLPVGPLQtNCYLVSDEEGEAILI---------DpGAGALEK--ILEAIEELG---LKIKAILLTHGHFDHIGGLAELK 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 122 AASGATVVASASGALGLQSGtngkdDPQFQAKPVVHVAKVEKVKVVGEGDAIKLGPLNLTAHMTPGHTPGATTWTwtsCE 201
Cdd:cd06262  67 EAPGAPVYIHEADAELLEDP-----ELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFY---IE 138

                       170
                ....*....|....*
gi 13274146 202 GQRCL---DVVYADS 213
Cdd:cd06262 139 EEGVLftgDTLFAGS 153
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
63-256 1.31e-14

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 71.25  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146    63 SAVLVTSPQGHVLLDGALPQSAPLIIAnIAALGFRIEDVKFILNSHAHWDHAGGIAALQAASGATVVASASGALglqSGT 142
Cdd:pfam00753   7 NSYLIEGGGGAVLIDTGGSAEAALLLL-LAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAR---ELL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146   143 NGKDDPQFQAK--PVVHVAKVEKVKVVGEGDAIKLGPLNLTAHMTPGHTPGAttwtwtSCEGQRCLDVVYA-DSLNPYSS 219
Cdd:pfam00753  83 DEELGLAASRLglPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGH------VVVYYGGGKVLFTgDLLFAGEI 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 13274146   220 GDFTYTGKG---DGPDISASFAASIAKVAALPCDIILSVH 256
Cdd:pfam00753 157 GRLDLPLGGllvLHPSSAESSLESLLKLAKLKAAVIVPGH 196
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 63-191 7.15e-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: 66.85  E-value: 7.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  63 SAVLVTSPQGHVLLDGALPQSAP------------------LIIANIAALGFRIEDVKFILNSHAHWDHAGGIAALQaas 124
Cdd:cd07729  33 YAYLIEHPEGTILVDTGFHPDAAddpgglelafppgvteeqTLEEQLARLGLDPEDIDYVILSHLHFDHAGGLDLFP--- 109

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13274146 125 GATVV------ASASGALGLQSGTNGKDDPQFQAKPVVHVAKVekvkvvgEGDAiKLGPlNLTAHMTPGHTPG 191
Cdd:cd07729 110 NATIIvqraelEYATGPDPLAAGYYEDVLALDDDLPGGRVRLV-------DGDY-DLFP-GVTLIPTPGHTPG 173
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 87-191 1.40e-11

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: 61.71  E-value: 1.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  87 IIANIAALGFRIedvKFILNSHAHWDHAGGIAALQAASG-ATVVASASGALglqsgtNGKDDPqfqakpvvhvakvekvk 165
Cdd:cd07723  33 VLAALEKNGLTL---TAILTTHHHWDHTGGNAELKALFPdAPVYGPAEDRI------PGLDHP----------------- 86

                        90       100
                ....*....|....*....|....*.
gi 13274146 166 vVGEGDAIKLGPLNLTAHMTPGHTPG 191
Cdd:cd07723  87 -VKDGDEIKLGGLEVKVLHTPGHTLG 111
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 83-198 6.75e-11

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: 60.11  E-value: 6.75e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  83 SAPLIIANIAALGFRIedvKFILNSHAHWDHAGGIAALQAASGATVVASAsgalglqsgtngKDDPQFQAKPVVhvakve 162
Cdd:cd07724  34 SVDRYLDLAAELGLKI---TYVLETHVHADHVSGARELAERTGAPIVIGE------------GAPASFFDRLLK------ 92

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 13274146 163 kvkvvgEGDAIKLGPLNLTAHMTPGHTPGATTWTWT 198
Cdd:cd07724  93 ------DGDVLELGNLTLEVLHTPGHTPESVSYLVG 122
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 44-277 2.12e-10

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: 59.28  E-value: 2.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  44 EVTPFNVfgNTWyvgtaglsavLVTSPQGH--VLLDGALPQSAplIIANIAALGFRIedvKFILNSHAHWDHAGGIAALQ 121
Cdd:cd16322   5 TLGPLQE--NTY----------LVADEGGGeaVLVDPGDESEK--LLARFGTTGLTL---LYILLTHAHFDHVGGVADLR 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 122 AASGATVVASASGALGLQSGTNGKDDPQFQAKPVVHVAKVEKvkvvgEGDAIKLGPLNLTAHMTPGHTPGATTWTwtsCE 201
Cdd:cd16322  68 RHPGAPVYLHPDDLPLYEAADLGAKAFGLGIEPLPPPDRLLE-----DGQTLTLGGLEFKVLHTPGHSPGHVCFY---VE 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 202 GQRCL---DVVYADSLNPYssgDFTYtgkGDGpdisASFAASIAKVAALPCDI-ILSVHPDSTGVldKAAKRsgeHNPFI 277
Cdd:cd16322 140 EEGLLfsgDLLFQGSIGRT---DLPG---GDP----KAMAASLRRLLTLPDETrVFPGHGPPTTL--GEERR---TNPFL 204
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 61-131 4.64e-10

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: 59.17  E-value: 4.64e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13274146  61 GLSAvLVTSPQGHVLLD-GalpQSaPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAA-LQAASGATVVAS 131
Cdd:cd07713  20 GLSL-LIETEGKKILFDtG---QS-GVLLHNAKKLGIDLSDIDAVVLSHGHYDHTGGLKAlLELNPKAPVYAH 87
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
61-130 1.19e-09

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 57.97  E-value: 1.19e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13274146  61 GLSAvLVTSPQGHVLLD-GalpqSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAA-LQAASGATVVA 130
Cdd:COG1237  22 GLSA-LIETEGKRILFDtG----QSDVLLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLPAlLELNPKAPVYA 88
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 56-190 1.45e-09

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: 57.12  E-value: 1.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  56 YVGTAGLSAV-LVTSPQGHVLLDGALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAAL-QAASGATVV---- 129
Cdd:cd07726   9 FLGFPGRIASyLLDGEGRPALIDTGPSSSVPRLLAALEALGIAPEDVDYIILTHIHLDHAGGAGLLaEALPNAKVYvhpr 88

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13274146 130 ------------ASASGALGLQSGT-NGKDDPQFQAKpvvhvakvekVKVVGEGDAIKLGPLNLTAHMTPGHTP 190
Cdd:cd07726  89 garhlidpsklwASARAVYGDEADRlGGEILPVPEER----------VIVLEDGETLDLGGRTLEVIDTPGHAP 152
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 66-256 2.41e-09

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


Pssm-ID: 293811 [Multi-domain]  Cd Length: 184  Bit Score: 55.77  E-value: 2.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  66 LVTSPQGHVLLDGAL--PQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAALQAASGATVVASASGALglqsgtn 143
Cdd:cd07725  19 LLRDGDETTLIDTGLatEEDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGATVYILDVTPV------- 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 144 gkddpqfqakpvvhvakvekvkvvGEGDAIKLGPLNLTAHMTPGHTPGATTWtwtSCEGQR---CLDVVYAD-SLNPySS 219
Cdd:cd07725  92 ------------------------KDGDKIDLGGLRLKVIETPGHTPGHIVL---YDEDRRelfVGDAVLPKiTPNV-SL 143

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 13274146 220 GDFTYtgkgdgPDISASFAASIAKVAALPCDIILSVH 256
Cdd:cd07725 144 WAVRV------EDPLGAYLESLDKLEKLDVDLAYPGH 174
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 87-193 3.33e-08

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: 52.54  E-value: 3.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  87 IIANIAALGFRIEDvkfILNSHAHWDHAGGIAALQAASGATVVASASGAlglqsgtngkDDPQFQAKpvvhvakveKVKV 166
Cdd:cd16275  37 ILAKLNELGLTLTG---ILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEI----------DYYGFRCP---------NLIP 94

                        90       100
                ....*....|....*....|....*..
gi 13274146 167 VGEGDAIKLGPLNLTAHMTPGHTPGAT 193
Cdd:cd16275  95 LEDGDTIKIGDTEITCLLTPGHTPGSM 121
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 53-190 4.99e-07

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 49.03  E-value: 4.99e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  53 NTWyvgtaglsavLVTSPQGHVLLDgalPqsAPLIIANIAAL-----GFRIEDvkfILNSHAHWDHAGGIAALQAASGAT 127
Cdd:cd16278  19 NTY----------LLGAPDGVVVID---P--GPDDPAHLDALlaalgGGRVSA---ILVTHTHRDHSPGAARLAERTGAP 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13274146 128 VVASASGALGLQSGTNGKDDPqfqakpvvhvakvekvkvVGEGDAIKLGPLNLTAHMTPGHTP 190
Cdd:cd16278  81 VRAFGPHRAGGQDTDFAPDRP------------------LADGEVIEGGGLRLTVLHTPGHTS 125
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 55-191 5.55e-07

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 49.49  E-value: 5.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  55 WYVGTAGLsavlVTSPQGHVLLD-GALPQSAPLIIANIAALGFRieDVKFILNSHAHWDHAGGIAALQAAsGATVVASAS 133
Cdd:cd16282  12 GFISNIGF----IVGDDGVVVIDtGASPRLARALLAAIRKVTDK--PVRYVVNTHYHGDHTLGNAAFADA-GAPIIAHEN 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13274146 134 GALGLQSGTNGKDDPQFQAKPVVHVAKVEKV--KVVGEGDAIKLGPLNLTA-HMTPGHTPG 191
Cdd:cd16282  85 TREELAARGEAYLELMRRLGGDAMAGTELVLpdRTFDDGLTLDLGGRTVELiHLGPAHTPG 145
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 53-131 1.31e-06

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 47.96  E-value: 1.31e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13274146  53 NTWYVGTAGLSAVLVTSPQGHVLLDgALPQSAPLIIANIAALGFriEDVKFILNSHAHWDHAGGiAALQAASGATVVAS 131
Cdd:cd16276   1 GVYWVTDGGYQSMFLVTDKGVIVVD-APPSLGENLLAAIRKVTD--KPVTHVVYSHNHADHIGG-ASIFKDEGATIIAH 75
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 63-127 1.91e-06

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


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 47.26  E-value: 1.91e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13274146  63 SAVLVTSPQGHVLLD---GALPQsapliianIAALGFRIEDVKFILNSHAHWDHAGGIAALQAASGAT 127
Cdd:cd16272  18 SSYLLETGGTRILLDcgeGTVYR--------LLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFARRYG 77
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 58-120 3.35e-06

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 48.26  E-value: 3.35e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13274146  58 GTAGLSAVLVTSPQGHVLLDGALPQSAPLiiANIAALGFRIEDVKFILNSHAHWDHAGGIAAL 120
Cdd:COG1236  10 GEVTGSCYLLETGGTRILIDCGLFQGGKE--RNWPPFPFRPSDVDAVVLTHAHLDHSGALPLL 70
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 74-197 5.59e-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: 46.71  E-value: 5.59e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  74 VLLDGALPQSAPLIIANIAALgFRIEDVKFILNSHAHWDHAGGIAA-LQAASGATVVASASGALGLQSGTNGKDDPQFQA 152
Cdd:cd07709  43 ALIDTVKEPFFDEFLENLEEV-IDPRKIDYIVVNHQEPDHSGSLPElLELAPNAKIVCSKKAARFLKHFYPGIDERFVVV 121

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 13274146 153 KpvvhvakvekvkvvgEGDAIKLGPLNLTAHMTPG-HTPGaTTWTW 197
Cdd:cd07709 122 K---------------DGDTLDLGKHTLKFIPAPMlHWPD-TMVTY 151
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 65-118 6.54e-06

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: 46.04  E-value: 6.54e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 13274146  65 VLVTSPQGHVLLDGALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIA 118
Cdd:cd07711  25 TLIKDGGKNILVDTGTPWDRDLLLKALAEHGLSPEDIDYVVLTHGHPDHIGNLN 78
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 59-214 2.20e-05

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: 44.85  E-value: 2.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  59 TAGLSAVLVTSPQGHVLLD----GALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGiaaLQAASG------ATV 128
Cdd:cd07720  46 ETSVNAFLVRTGGRLILVDtgagGLFGPTAGKLLANLAAAGIDPEDIDDVLLTHLHPDHIGG---LVDAGGkpvfpnAEV 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 129 VASASGALGLQSGTNGKDDPQFQAKPVVHVAKV----EKVKVVGEGDAIKLGplnLTAHMTPGHTPGATTWTWTScEGQR 204
Cdd:cd07720 123 HVSEAEWDFWLDDANAAKAPEGAKRFFDAARDRlrpyAAAGRFEDGDEVLPG---ITAVPAPGHTPGHTGYRIES-GGER 198

                       170
                ....*....|...
gi 13274146 205 CL---DVVYADSL 214
Cdd:cd07720 199 LLiwgDIVHHPAL 211
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 101-191 4.91e-05

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 43.29  E-value: 4.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 101 VKFILNSHAHWDHAGGIAALQAASGATVVASA----------------SGALGLQSGTNgkddPQFQAKPVVHVAKVekv 164
Cdd:cd07743  46 LKAIINTHSHADHIGGNAYLQKKTGCKVYAPKiekafienpllepsylGGAYPPKELRN----KFLMAKPSKVDDII--- 118

                        90       100
                ....*....|....*....|....*..
gi 13274146 165 kvvgEGDAIKLGPLNLTAHMTPGHTPG 191
Cdd:cd07743 119 ----EEGELELGGVGLEIIPLPGHSFG 141
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 64-123 5.17e-05

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 43.28  E-value: 5.17e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13274146  64 AVLVTSPQGHVLLD--GALPQSAPLIIANIAALGfrIEDVKFILNSHAHWDHAGGIAALQAA 123
Cdd:cd07731  12 AILIQTPGKTILIDtgPRDSFGEDVVVPYLKARG--IKKLDYLILTHPDADHIGGLDAVLKN 71
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 92-134 9.38e-05

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


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 43.03  E-value: 9.38e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 13274146  92 AALGFRIEDVKFILNSHAHWDHAGGIAALqaaSGATVVASASG 134
Cdd:cd07730  75 AAGGIDPEDIDAVILSHLHWDHIGGLSDF---PNARLIVGPGA 114
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 91-132 1.19e-04

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 43.29  E-value: 1.19e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 13274146   91 IAALGFRIEDVKFILNSHAHWDHAGGIAALQAASGATVVASA 132
Cdd:PLN02398 112 IDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSA 153
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 88-118 1.68e-04

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


Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 42.23  E-value: 1.68e-04
                        10        20        30
                ....*....|....*....|....*....|.
gi 13274146  88 IANIAALGFRIEDVKFILNSHAHWDHAGGIA 118
Cdd:cd07742  68 VRQIEALGFDPSDVRHIVLTHLDLDHAGGLA 98
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 63-117 2.01e-04

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 42.19  E-value: 2.01e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13274146  63 SAVLVTSPQGHVLLD---GALPQsapliianIAALGFRIEDVKFILNSHAHWDHAGGI 117
Cdd:COG1235  36 SSILVEADGTRLLIDagpDLREQ--------LLRLGLDPSKIDAILLTHEHADHIAGL 85
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
58-123 2.32e-04

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 41.72  E-value: 2.32e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13274146  58 GTAG--------LSAVLVTSPQGHVLLD---GALPQsapliianIAALGFRIEDVKFILNSHAHWDHAGGIAALQAA 123
Cdd:COG1234   7 GTGGavptpgraTSSYLLEAGGERLLIDcgeGTQRQ--------LLRAGLDPRDIDAIFITHLHGDHIAGLPGLLST 75
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 105-257 2.36e-04

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: 41.07  E-value: 2.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 105 LNSHAHWDHAGGI-----AALQAASgATVVASASGALGLqsgTNGKDDPQFQAKPVVHVAKvekvkvvgEGDAIKLGPLN 179
Cdd:cd07712  47 VATHGHFDHIGGLhefeeVYVHPAD-AEILAAPDNFETL---TWDAATYSVPPAGPTLPLR--------DGDVIDLGDRQ 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146 180 LTAHMTPGHTPG-------ATTWTWTScegqrclDVVYADSLnpyssgdFTYtgkGDGPDISAsFAASIAKVAALPcDII 252
Cdd:cd07712 115 LEVIHTPGHTPGsialldrANRLLFSG-------DVVYDGPL-------IMD---LPHSDLDD-YLASLEKLSKLP-DEF 175


                ....*
gi 13274146 253 LSVHP 257
Cdd:cd07712 176 DKVLP 180
NorV COG0426
Flavorubredoxin [Energy production and conversion];
74-191 3.88e-04

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 41.74  E-value: 3.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  74 VLLDGALPQSAPLIIANIAALgFRIEDVKFILNSHAHWDHAGGIAA-LQAASGATVVASASGALGLQsGTNGKDDPQFQA 152
Cdd:COG0426  45 ALIDTVGESFFEEFLENLSKV-IDPKKIDYIIVNHQEPDHSGSLPElLELAPNAKIVCSKKAARFLP-HFYGIPDFRFIV 122

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 13274146 153 KPvvhvakvekvkvvgEGDAIKLGPLNLTAHMTPG-HTPG 191
Cdd:COG0426 123 VK--------------EGDTLDLGGHTLQFIPAPMlHWPD 148
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 63-120 4.52e-04

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


Pssm-ID: 293853 [Multi-domain]  Cd Length: 197  Bit Score: 40.52  E-value: 4.52e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13274146  63 SAVLVTSPQGHVLLD-GALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGIAAL 120
Cdd:cd16295  13 SCYLLETGGKRILLDcGLFQGGKELEELNNEPFPFDPKEIDAVILTHAHLDHSGRLPLL 71
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 54-132 6.11e-04

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 40.57  E-value: 6.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146   54 TWYvgtaGLSAVLVTSPQGHVLLDgalpqsaPLIIANIAAlGFRIEDVK--FILNSHAHWDHAGGIAALQAASGATVVAS 131
Cdd:PRK00685   4 TWL----GHSAFLIETGGKKILID-------PFITGNPLA-DLKPEDVKvdYILLTHGHGDHLGDTVEIAKRTGATVIAN 71


                 .
gi 13274146  132 A 132
Cdd:PRK00685  72 A 72
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 64-123 6.20e-04

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 40.61  E-value: 6.20e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13274146  64 AVLVTSPQGHVLL-D-GALPQSAP---LIIANIAALGfrIEDVKFILNSHAHWDHAGGIAALQAA 123
Cdd:COG2333  13 AILIRTPDGKTILiDtGPRPSFDAgerVVLPYLRALG--IRRLDLLVLTHPDADHIGGLAAVLEA 75
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 81-117 1.37e-03

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


Pssm-ID: 293839  Cd Length: 252  Bit Score: 39.40  E-value: 1.37e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 13274146  81 PQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGGI 117
Cdd:cd16281  75 QHSEHSLLKSLARLGLSPEDITDVILTHLHFDHCGGA 111
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 87-121 1.64e-03

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


Pssm-ID: 293814  Cd Length: 249  Bit Score: 39.16  E-value: 1.64e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 13274146  87 IIANIAALGFRIEDVKFILNSHAHWDHAGGIAALQ 121
Cdd:cd07728  82 IEESLAELGLTPEDIDYVLMTHLHFDHASGLTKVK 116
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 53-193 2.85e-03

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: 37.95  E-value: 2.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13274146  53 NTWYVGTA-----GLSAVLVTSPQGHVLLDGalPQSAPLIIANIAALGfrieDVKFILNSHAhwDHAGGIAALQAASGAT 127
Cdd:cd07727   1 GVYYCGFHseksfGAASYLILRPEGNILVDS--PRYSPPLAKRIEALG----GIRYIFLTHR--DDVADHAKWAERFGAK 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13274146 128 VVASAsgalglqsgtngkDDPQFQAKPVVHVAKvekvkvvGEGDAIKLGPlNLTAHMTPGHTPGAT 193
Cdd:cd07727  73 RIIHE-------------DDVNAVTRPDEVIVL-------WGGDPWELDP-DLTLIPVPGHTRGSV 117
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 61-116 3.39e-03

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: 38.08  E-value: 3.39e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13274146  61 GLSAVLVTSPQGHVLLDGALPQSAPLIIANIAALGFRIEDVKFILNSHAHWDHAGG 116
Cdd:cd07734  10 GRSCFLVEFKGRTVLLDCGMNPGKEDPEACLPQFELLPPEIDAILISHFHLDHCGA 65
 
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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