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Conserved domains on  [gi|501342302|ref|WP_012373937|]
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subclass B3 metallo-beta-lactamase [Opitutus terrae]

Protein Classification

subclass B3 metallo-beta-lactamase( domain architecture ID 10888713)

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
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 35-287 2.24e-140

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: 395.92  E-value: 2.24e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  35 WNQPVAPFRIVENVYYVGASDIAAYLITTPDGHILLETGFAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGLKAM 114
Cdd:cd16288    1 WNAPFEPFRIAGNVYYVGTSGLASYLITTPQGLILIDTGLESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 115 KALTGARLIASAPEAAALARGGRGDFHYGDQ-LAFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVRTGG 193
Cdd:cd16288   81 KKLTGAKLMASAEDAALLASGGKSDFHYGDDsLAFPPVKVDRVLKDGDRVTLGGTTLTAHLTPGHTRGCTTWTMTVKDDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 194 RELDVVFAASVSA-PGYQLVNNAAYPDIWRDLQASIAALRALPCDVFLAPHGQVFGLTNKARRLAEhPETHPFIDPDGYR 272
Cdd:cd16288  161 KVYQVVFADSLTVnPGYKLVGNPTYPGIAEDYRHSFATLRALQCDIFLASHAEYFDLKEKRARLAA-GQPNAFIDPEGYR 239

                        250
                 ....*....|....*
gi 501342302 273 AFCDDAEARLRKQHA 287
Cdd:cd16288  240 NFIEKAKADFEKQLA 254
 
Name Accession Description Interval E-value
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 35-287 2.24e-140

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: 395.92  E-value: 2.24e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  35 WNQPVAPFRIVENVYYVGASDIAAYLITTPDGHILLETGFAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGLKAM 114
Cdd:cd16288    1 WNAPFEPFRIAGNVYYVGTSGLASYLITTPQGLILIDTGLESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 115 KALTGARLIASAPEAAALARGGRGDFHYGDQ-LAFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVRTGG 193
Cdd:cd16288   81 KKLTGAKLMASAEDAALLASGGKSDFHYGDDsLAFPPVKVDRVLKDGDRVTLGGTTLTAHLTPGHTRGCTTWTMTVKDDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 194 RELDVVFAASVSA-PGYQLVNNAAYPDIWRDLQASIAALRALPCDVFLAPHGQVFGLTNKARRLAEhPETHPFIDPDGYR 272
Cdd:cd16288  161 KVYQVVFADSLTVnPGYKLVGNPTYPGIAEDYRHSFATLRALQCDIFLASHAEYFDLKEKRARLAA-GQPNAFIDPEGYR 239

                        250
                 ....*....|....*
gi 501342302 273 AFCDDAEARLRKQHA 287
Cdd:cd16288  240 NFIEKAKADFEKQLA 254
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 55-254 3.93e-29

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: 110.55  E-value: 3.93e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  55 DIAAYLITTPDGHILLETGF-AETVPLVRASLRQLGiepRDIRILLTSHAHIDHAGGLKAMKALTGARLIASAPEAAALA 133
Cdd:COG0491   14 GVNSYLIVGGDGAVLIDTGLgPADAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 134 RGGRGDFhygdqLAFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVR----TGgrelDVVFAASVSAPGY 209
Cdd:COG0491   91 APAAGAL-----FGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEkvlfTG----DALFSGGVGRPDL 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 501342302 210 QLVNnaaypdiWRDLQASIAALRALPCDVFLAPHGQVFGLTNKAR 254
Cdd:COG0491  162 PDGD-------LAQWLASLERLLALPPDLVIPGHGPPTTAEAIDY 199
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 58-243 8.13e-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: 89.92  E-value: 8.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302    58 AYLITTPDGHILLETGFAETVPLVrASLRQLGiePRDIRILLTSHAHIDHAGGLKAMKALTGARLIASAPEAAALARGGR 137
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDLL-AELKKLG--PKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302   138 GDFHYGDqlAFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCrvrtggRELDVVFAASVSAPGYQLVNNAAY 217
Cdd:smart00849  79 LLGELGA--EAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL------PEGKILFTGDLLFAGGDGRTLVDG 150

                          170       180
                   ....*....|....*....|....*..
gi 501342302   218 PDIWR-DLQASIAALRALPCDVFLAPH 243
Cdd:smart00849 151 GDAAAsDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
51-243 2.76e-18

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 80.88  E-value: 2.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302   51 VGASDIAAYLITTPDGHILLETGFAETVPLVRaSLRQLGIEPRDIRILLTSHAHIDHAGGLKAMKALTGARLIASAPEAA 130
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLL-LLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  131 ALARGGRGDF--HYGDQLAFEPVTVDEIVADGGTVTLGG-VTLTAHLTPGHTPGSttwtCRVRTGGREL----DVVFAAS 203
Cdd:pfam00753  80 ELLDEELGLAasRLGLPGPPVVPLPPDVVLEEGDGILGGgLGLLVTHGPGHGPGH----VVVYYGGGKVlftgDLLFAGE 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 501342302  204 -VSAPGYQLVNNAAYPDIWRDLQASIAALRALPCDVFLAPH 243
Cdd:pfam00753 156 iGRLDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
 
Name Accession Description Interval E-value
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 35-287 2.24e-140

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: 395.92  E-value: 2.24e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  35 WNQPVAPFRIVENVYYVGASDIAAYLITTPDGHILLETGFAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGLKAM 114
Cdd:cd16288    1 WNAPFEPFRIAGNVYYVGTSGLASYLITTPQGLILIDTGLESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 115 KALTGARLIASAPEAAALARGGRGDFHYGDQ-LAFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVRTGG 193
Cdd:cd16288   81 KKLTGAKLMASAEDAALLASGGKSDFHYGDDsLAFPPVKVDRVLKDGDRVTLGGTTLTAHLTPGHTRGCTTWTMTVKDDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 194 RELDVVFAASVSA-PGYQLVNNAAYPDIWRDLQASIAALRALPCDVFLAPHGQVFGLTNKARRLAEhPETHPFIDPDGYR 272
Cdd:cd16288  161 KVYQVVFADSLTVnPGYKLVGNPTYPGIAEDYRHSFATLRALQCDIFLASHAEYFDLKEKRARLAA-GQPNAFIDPEGYR 239

                        250
                 ....*....|....*
gi 501342302 273 AFCDDAEARLRKQHA 287
Cdd:cd16288  240 NFIEKAKADFEKQLA 254
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 35-279 6.41e-95

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: 280.59  E-value: 6.41e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  35 WNQPVAPFRIVENVYYVGASDIAAYLITTPDGHILLETGFAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGLKAM 114
Cdd:cd07708    1 WPNPFPPFQIAGNTYYVGTDDLAAYLIVTPQGNILIDGDMEQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 115 KALTGARLIASAPEAAALARGGRGDFHYGD--QLAFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVRTG 192
Cdd:cd07708   81 KKQTGAKVMAGAEDVSLLLSGGSSDFHYANdsSTYFPQSTVDRAVHDGERVTLGGTVLTAHATPGHTPGCTTWTMTLKDH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 193 GRELDVVFAASVSAP-GYQLVNNAAYPDIWRDLQASIAALRALPCDVFLAPHGQVFGLTNKARRLAEHpETHPFIDPDGY 271
Cdd:cd07708  161 GKQYQVVFADSLTVNpGYRLVDNPTYPKIVEDYRHSFAVVEAMRCDILLGPHPGVFDMKNKYVLLSKG-QNNPFVDPGGC 239


                 ....*...
gi 501342302 272 RAFCDDAE 279
Cdd:cd07708  240 KAYAEAKA 247
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 35-285 1.07e-93

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: 277.79  E-value: 1.07e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  35 WNQPVAPFRIVENVYYVGASDIAAYLITTPDGHILLETGFAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGLKAM 114
Cdd:cd16307    1 WTTPFPPFRIAGNLYYVGSRDLASYLITTPRGNILINSNLESSVPQIKASIEKLGFKFSDTKILLISHAHFDHAAGSALI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 115 KALTGARLIASAPEAAALARGGRGDFHYGDQLA--FEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVRTG 192
Cdd:cd16307   81 KRETHAKYMVMDGDVDVVESGGKSDFFYGNDPStyFPPAHVDKVLHDGEQVELGGTVLTAHLTAGHTKGCTTWTMKVKDH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 193 GRELDVVFAASVSA-PGYQLVNNAAYPDIWRDLQASIAALRALPCDVFLAPHGQVFGLTNKARRL-AEHPetHPFIDPDG 270
Cdd:cd16307  161 GKTYDVVIVGSPNVnPGAKLVNNITYPGIAEDYAHTFAVLRSLPCDIFLGAHGGYFDLKNKYVRLqKGGA--NPFIDPEG 238

                        250
                 ....*....|....*
gi 501342302 271 YRAFCDDAEARLRKQ 285
Cdd:cd16307  239 YKAYVAEKEQAFRTE 253
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 35-287 6.29e-84

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: 252.79  E-value: 6.29e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  35 WNQPVAPFRIVENVYYVGASDIAAYLITTPDGHILLETGFAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGLKAM 114
Cdd:cd16309    1 WNEPMEPFKLIGNIYYVGTAGLGVFLITTPEGHILIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 115 KALTGARLIASAPEAAALARG--GRGDFHYgdqLAFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVRTG 192
Cdd:cd16309   81 KKATGAQLVASAADKPLLESGyvGSGDTKN---LQFPPVRVDRVIGDGDKVTLGGTTLTAHLTPGHSPGCTSWTTTVKDT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 193 GREL-DVVFAASVSAPGYQLVNNAAYPDIWRDLQASIAALRALPCDVFLAPHGQVFGLTNKARRLAEHpETHPFIDPDGY 271
Cdd:cd16309  158 AGPPrEVLFFCSATVAGNQLVGPPTYPGIVDDYRATFAKARAMKADVFLANHPEFFGLVAKRARQSAG-EPDAFVDAGEL 236

                        250
                 ....*....|....*.
gi 501342302 272 RAFCDDAEARLRKQHA 287
Cdd:cd16309  237 QRFNTKMEDDFEKALA 252
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 ...
 35-284 1.16e-82

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: 249.57  E-value: 1.16e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  35 WNQPVAPFRIVENVYYVGASDIAAYLITTPDGHILLETGFAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGLKAM 114
Cdd:cd16290    1 WNQPQAPFRIHGNTYYVGTGGLSAVLITSPQGLILIDGALPQSAPQIEANIRALGFRLEDVKLILNSHAHFDHAGGIAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 115 KALTGARLIASAPEAAALARG--GRGDFHYGDQLAFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVRTG 192
Cdd:cd16290   81 QRDSGATVAASPAGAAALRSGgvDPDDPQAGAADPFPPVAKVRVVADGEVVKLGPLAVTAHATPGHTPGGTSWTWRSCEG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 193 GRELDVVFAAS---VSAPGYQLvNNAAYPDIWRDLQASIAALRALPCDVFLAPHGQVFGLTNKARRLAEHPETHPFIDPD 269
Cdd:cd16290  161 GRCLDIVYADSltaVSADGFRF-SDDAHPARVAAFRRSIATVAALPCDILISAHPDASGLWEKLARRAREPGPNPFIDPN 239

                        250
                 ....*....|....*
gi 501342302 270 GYRAFCDDAEARLRK 284
Cdd:cd16290  240 ACRAYAAAAEARLEA 254
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 35-280 7.93e-80

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: 242.03  E-value: 7.93e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  35 WNQPVAPFRIVENVYYVGASDIAAYLITTPDGHILLETGFAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGLKAM 114
Cdd:cd16289    1 WLQPMAPLQIADHTWYIGTESLTALLVKTPDGAVLLDGGMPQAADMLLDNMRALGVAPGDLKLILHSHAHADHAGPLAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 115 KALTGARLIASAPEAAALARGGRGDFHYGDQLAFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVRTGGR 194
Cdd:cd16289   81 KRATGARVAANAESAVLLARGGSDDIHFGDGITFPPVQADRIVMDGEVVTLGGVTFTAHFTPGHTPGSTSWTWTDTRDGK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 195 ELDVVFAASVSAPGYQLVNNAAYPDIWRDLQASIAALRALPCDVFLAPHGQVFGLTNKArrlAEHPETHPFidpdGYRAF 274
Cdd:cd16289  161 PVRIAYADSLSAPGYQLLGNPRYPRIVEDYRRTFATVRALPCDVLLTPHPGASGWDYAA---GAAPHAKPM----TCKAY 233


                 ....*.
gi 501342302 275 CDDAEA 280
Cdd:cd16289  234 ADAAEQ 239
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 35-287 1.05e-79

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: 241.97  E-value: 1.05e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  35 WNQPVAPFRIVENVYYVGASDIAAYLITTPDGHILLETGFAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGLKAM 114
Cdd:cd16310    1 WTAPTEPFRIVDNIYYVGTKGIGSYLITSNHGAILLDGGLEENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 115 KALTGARLIASAPEAAALARGGRGDFHYGDQLAFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVRTGGR 194
Cdd:cd16310   81 KADTGAKLWASRGDRPALEAGKHIGDNITQPAPFPAVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTWSTTVKENGR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 195 ELDVVFAASVSAPGYQLVNNAAYPDIWRDLQASIAALRALPCDVFLAPHGQVFGL-TNKARRLAEHPEthPFIDPDGYRA 273
Cdd:cd16310  161 PLRVVFPCSLSVAGNVLVGNKTYPTIVEDYRASFARLRAMKADIVLTSHPEVADLlARKAKQDAGQAN--AFVDPGELAR 238

                        250
                 ....*....|....
gi 501342302 274 FCDDAEARLRKQHA 287
Cdd:cd16310  239 IVDQSEAAFNKELA 252
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 35-285 1.31e-75

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: 231.59  E-value: 1.31e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  35 WNQPVAPFRIVENVYYVGASDIAAYLITTPDGHILLETGFAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGLKAM 114
Cdd:cd16308    1 WSQPYAPFRIAGNLYYVGTYDLACYLIVTPKGNILINTGLAESVPLIKKNIQALGFKFKDIKILLTTQAHYDHVGAMAAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 115 KALTGARLIASAPEAAALARGGRGDFHYGDQ-LAFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVRTGG 193
Cdd:cd16308   81 KQQTGAKMMVDEKDAKVLADGGKSDYEMGGYgSTFAPVKADKLLHDGDTIKLGGTKLTLLHHPGHTKGSCSFLFDVKDEK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 194 RELDVVFAASVSA-PGYQLVNNAAYPDIWRDLQASIAALRALPCDVFLAPHGQVFGLTNKarrlaeHPETHP-----FID 267
Cdd:cd16308  161 RTYRVLIANMPTIlPDTKLSGMPGYPGIAKDYAYTFEAMKALSFDIWLASHASQFDLHQK------HKPGAPynpaaFAD 234

                        250
                 ....*....|....*...
gi 501342302 268 PDGYRAFCDDAEARLRKQ 285
Cdd:cd16308  235 RAGYDKALAGLEKSYDKK 252
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 35-284 6.99e-72

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: 221.84  E-value: 6.99e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  35 WNQPVAPFRIVENVYYVGASDIAAYLITTPDGHILLETGFAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGLKAM 114
Cdd:cd16315    1 WDKPAPPARIFGNTYYVGTCGISAILITGDDGHVLIDSGTEEAAPLVLANIRKLGFDPKDVRWLLSSHEHFDHVGGLAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 115 KALTGARLIASAPEAAALARG--GRGDFHYGDQLAFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVRTG 192
Cdd:cd16315   81 QRATGARVAASAAAAPVLESGkpAPDDPQAGLHEPFPPVRVDRIVEDGDTVALGSLRLTAHATPGHTPGALSWTWRSCEG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 193 GRELDVVFAAS---VSAPGYQLvnnAAYPDIWRDLQASIAALRALPCDVFLAPHGqvfGLTNKARRLAehpETHPFIDPD 269
Cdd:cd16315  161 ADCRTIVYADSlspVSADGYRF---SDHPDYVAAYRAGLAKVAALPCDILLTPHP---SASDMFERLS---GGAPLADPD 231

                        250
                 ....*....|....*
gi 501342302 270 GYRAFCDDAEARLRK 284
Cdd:cd16315  232 ACAAYAAGAEKRLDE 246
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 35-287 1.65e-67

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: 210.87  E-value: 1.65e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  35 WNQPVAPFRIVENVYYVGASDIAAYLITTPDGHILLETGFAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGLKAM 114
Cdd:cd16313    1 WNAPQEPFQIYGNTYYVGTGGISAVLITSPQGHILIDGGFPKSPEQIAASIRQLGFKLEDVKYILSSHDHWDHAGGIAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 115 KALTGARLIASAPEAAALARG--GRGDFHYGDQLAFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVRTG 192
Cdd:cd16313   81 QKLTGAQVLASPATVAVLRSGsmGKDDPQFGGLTPMPPVASVRAVRDGEVVKLGPLAVTAHATPGHTTGGTSWTWQSCEQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 193 GRELDVVFAAS---VSAPGYQLvnnAAYPDIWRDLQASIAALRALPCDVFLAPHGQVFGLTNKARRLAehPETHP-FIDP 268
Cdd:cd16313  161 GRCANMVFADSltaVSADGYRF---SAHPAVLADVEQSIAAVEKLACDILVSAHPEFSDMWTRVKRGA--AEGNAaFIDG 235

                        250
                 ....*....|....*....
gi 501342302 269 DGYRAFCDDAEARLRKQHA 287
Cdd:cd16313  236 GGCRAYAAKAREKLNKRLA 254
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 35-287 1.34e-65

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: 206.38  E-value: 1.34e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  35 WNQPVAPFRIVENVYYVGASDIAAYLITTPDGHILLETGFAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGLKAM 114
Cdd:cd16312    1 WNQPVKPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIEALGFRIEDVKLILNSHAHWDHAGGIAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 115 KALTGARLIASAPEAAALARG--GRGDFHY-GDQLAFEP-VTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVR 190
Cdd:cd16312   81 QKASGATVAASAHGAQVLQSGtnGKDDPQYqAKPVVHVAkVAKVKEVGEGDTLKVGPLRLTAHMTPGHTPGGTTWTWTSC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 191 TGGRELDVVFAAS---VSAPGYQLVNNAAYPDIWRDLQASIAALRALPCDVFLAPHGQVFGLTNKARRlaEHPETHPFID 267
Cdd:cd16312  161 EGQRCLDVVYADSlnpYSSGDFYYTGKGGYPDISASFRASIAKVAALPCDIIIAVHPGFTDVLDKAKR--RSGDTNPFID 238

                        250       260
                 ....*....|....*....|
gi 501342302 268 PDGYRAFCDDAEARLRKQHA 287
Cdd:cd16312  239 AEACRAYAAGAAKSLEKRLA 258
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 35-285 2.37e-59

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: 190.20  E-value: 2.37e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  35 WNQPVAPFRIVENVYYVGASDIAAYLITTPDGHILLETGFAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGLKAM 114
Cdd:cd16311    1 WNADQAPFRIFGNTYYVGVKGLSSVLVTSPQGHVLVDGGLPESAPKIIANIEALGFRIEDVKLILNSHGHIDHAGGLAEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 115 KALTGARLIASAPEAAALARG--GRGDFHYGDQLAFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVRTG 192
Cdd:cd16311   81 QRRSGALVAASPSAALDLASGevGPDDPQYHALPKYPPVKDMRLARDGGQFNVGPVSLTAHATPGHTPGGLSWTWQSCDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 193 GRELDVVFAAS---VSAPGYQLVNNAAYPDIWRDLQASIAALRALPCDVFLAPHGQVFGLTnkaRRLA--EHPETHPFID 267
Cdd:cd16311  161 PRCLNMVYADSqnaVSRPGFKFSASSEYPNAVADLRRSFETLEKLPCDVLISAHPEASQLW---ERLEasDRSARPALVD 237

                        250
                 ....*....|....*...
gi 501342302 268 PDGYRAFCDDAEARLRKQ 285
Cdd:cd16311  238 REACRRYASRAREALEKR 255
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 35-291 2.95e-58

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: 187.41  E-value: 2.95e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  35 WNQPVAPFRIVENVYYVGASDIAAYLITTPDGHILLETGFAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGLKAM 114
Cdd:cd16314    1 WDDPAPPRRIYGNTWYVGTCGISALLVTSDAGHILIDGGTDKAAPLIEANIRALGFRPEDVRYIVSSHEHFDHAGGIARL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 115 KALTGARLIASAPEAAALARG--GRGDFHYGDQLAFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVRTG 192
Cdd:cd16314   81 QRATGAPVVAREPAATTLERGrsDRSDPQFLVVEKFPPVASVQRIGDGEVLRVGPLALTAHATPGHTPGGTSWTWRSCEG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 193 GRELDVVFAASVSAPGYQLVNNAAYPDIWRDLQASIAALRALPCDVFLAPHGQVFGLTNkarRLAEHPEThPFIDPDGYR 272
Cdd:cd16314  161 AVCRDMVYADSVTAISDDIYRYSDHPGMVAAFRNTLDTVAALPCDILVTPHPSASGLWE---RLGPAAGI-PLADTGACR 236

                        250
                 ....*....|....*....
gi 501342302 273 AFCDDAEARLRKQHAEQAA 291
Cdd:cd16314  237 AYAQTGRARLDARLADEAA 255
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 35-285 2.56e-48

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: 161.60  E-value: 2.56e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  35 WNQPVAPFRIVENVYYVGASDIAAYLITTPDGHILLETGF-AETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGLKA 113
Cdd:cd16280    1 KKGYVEPFQVFDNLYYVGNKWVSAWAIDTGDGLILIDALNnNEAADLIVDGLEKLGLDPADIKYILITHGHGDHYGGAAY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 114 MKALTGARLIASAPEAAALARGGRGDFHYGDqlaFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVRTGG 193
Cdd:cd16280   81 LKDLYGAKVVMSEADWDMMEEPPEEGDNPRW---GPPPERDIVIKDGDTLTLGDTTITVYLTPGHTPGTLSLIFPVKDGG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 194 RELDVVFAasvsapGYQLVNNAAYPDIWRDLQASIAALRAL----PCDVFLAPHGQVFGLTNKARRLAE--HPETHPFID 267
Cdd:cd16280  158 KTHRAGLW------GGTGLNTGPNLERREQYIASLERFKKIaeeaGVDVFLSNHPFQDGSLEKREALRNrkPGEPNPFVD 231

                        250
                 ....*....|....*...
gi 501342302 268 PDGYRAFCDDAEARLRKQ 285
Cdd:cd16280  232 GQAWVDFYDEVLALCARV 249
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 55-254 3.93e-29

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: 110.55  E-value: 3.93e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  55 DIAAYLITTPDGHILLETGF-AETVPLVRASLRQLGiepRDIRILLTSHAHIDHAGGLKAMKALTGARLIASAPEAAALA 133
Cdd:COG0491   14 GVNSYLIVGGDGAVLIDTGLgPADAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 134 RGGRGDFhygdqLAFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVR----TGgrelDVVFAASVSAPGY 209
Cdd:COG0491   91 APAAGAL-----FGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYVPDEkvlfTG----DALFSGGVGRPDL 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 501342302 210 QLVNnaaypdiWRDLQASIAALRALPCDVFLAPHGQVFGLTNKAR 254
Cdd:COG0491  162 PDGD-------LAQWLASLERLLALPPDLVIPGHGPPTTAEAIDY 199
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 58-244 2.45e-25

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: 99.99  E-value: 2.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  58 AYLITTPDGHILLETGFAETVPLVRASLRQLGIEPRDI-RILLTsHAHIDHAGGLKAMKALTGA---------RLIASAP 127
Cdd:cd07721   13 AYLIEDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIrRILLT-HGHIDHIGSLAALKEAPGApvyahereaPYLEGEK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 128 EAAALARGGRGDFHYGDqLAFEPVTVDEIVADGGTVTLGGvTLTAHLTPGHTPGSttwTCRVRtggRELDVVFA--ASVS 205
Cdd:cd07721   92 PYPPPVRLGLLGLLSPL-LPVKPVPVDRTLEDGDTLDLAG-GLRVIHTPGHTPGH---ISLYL---EEDGVLIAgdALVT 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 501342302 206 APGY-QLVNNAAYPDiWRDLQASIAALRALPCDVFLAPHG 244
Cdd:cd07721  164 VGGElVPPPPPFTWD-MEEALESLRKLAELDPEVLAPGHG 202
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 56-243 2.92e-23

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: 94.87  E-value: 2.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  56 IAAYLITTPDGHILLETGFAETVPLVRASLRQLGIEPRDIR-ILLTsHAHIDHAGGLKA-MKALTGARLIasapeaaALA 133
Cdd:cd07726   16 IASYLLDGEGRPALIDTGPSSSVPRLLAALEALGIAPEDVDyIILT-HIHLDHAGGAGLlAEALPNAKVY-------VHP 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 134 RGGRgdfH--------------YGDQ---LAFEPVTVDE----IVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVR-- 190
Cdd:cd07726   88 RGAR---HlidpsklwasaravYGDEadrLGGEILPVPEerviVLEDGETLDLGGRTLEVIDTPGHAPHHLSFLDEESdg 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501342302 191 -----TGG---RELDVVFAASVSAPGYQlvnnaayPDIWRdlqASIAALRALPCDVFLAPH 243
Cdd:cd07726  165 lftgdAAGvryPELDVVGPPSTPPPDFD-------PEAWL---ESLDRLLSLKPERIYLTH 215
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 58-243 8.13e-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: 89.92  E-value: 8.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302    58 AYLITTPDGHILLETGFAETVPLVrASLRQLGiePRDIRILLTSHAHIDHAGGLKAMKALTGARLIASAPEAAALARGGR 137
Cdd:smart00849   2 SYLVRDDGGAILIDTGPGEAEDLL-AELKKLG--PKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302   138 GDFHYGDqlAFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCrvrtggRELDVVFAASVSAPGYQLVNNAAY 217
Cdd:smart00849  79 LLGELGA--EAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVLYL------PEGKILFTGDLLFAGGDGRTLVDG 150

                          170       180
                   ....*....|....*....|....*..
gi 501342302   218 PDIWR-DLQASIAALRALPCDVFLAPH 243
Cdd:smart00849 151 GDAAAsDALESLLKLLKLLPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 58-204 1.06e-19

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: 84.64  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  58 AYLITTPDGH-ILLETGfAETVPLVRASLRQLGIEPRdiRILLTsHAHIDHAGGLKAMKALTGARLIASAPEAAALARGG 136
Cdd:cd06262   12 CYLVSDEEGEaILIDPG-AGALEKILEAIEELGLKIK--AILLT-HGHFDHIGGLAELKEAPGAPVYIHEADAELLEDPE 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501342302 137 RGDFHYGDQLaFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVR----TGgrelDVVFAASV 204
Cdd:cd06262   88 LNLAFFGGGP-LPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVCFYIEEEgvlfTG----DTLFAGSI 154
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 55-182 1.44e-18

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: 82.65  E-value: 1.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  55 DIAAYLITTPDGHILLETGFAETVP------------------LVRASLRQLGIEPRDIRILLTSHAHIDHAGGLkamKA 116
Cdd:cd07729   31 PVYAYLIEHPEGTILVDTGFHPDAAddpgglelafppgvteeqTLEEQLARLGLDPEDIDYVILSHLHFDHAGGL---DL 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501342302 117 LTGARLI----------ASAPEAAALARGGRGDFHYGDQLAFEPVtvdeivaDGGTVTLGGVTLtaHLTPGHTPGS 182
Cdd:cd07729  108 FPNATIIvqraeleyatGPDPLAAGYYEDVLALDDDLPGGRVRLV-------DGDYDLFPGVTL--IPTPGHTPGH 174
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
51-243 2.76e-18

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 80.88  E-value: 2.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302   51 VGASDIAAYLITTPDGHILLETGFAETVPLVRaSLRQLGIEPRDIRILLTSHAHIDHAGGLKAMKALTGARLIASAPEAA 130
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLL-LLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  131 ALARGGRGDF--HYGDQLAFEPVTVDEIVADGGTVTLGG-VTLTAHLTPGHTPGSttwtCRVRTGGREL----DVVFAAS 203
Cdd:pfam00753  80 ELLDEELGLAasRLGLPGPPVVPLPPDVVLEEGDGILGGgLGLLVTHGPGHGPGH----VVVYYGGGKVlftgDLLFAGE 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 501342302  204 -VSAPGYQLVNNAAYPDIWRDLQASIAALRALPCDVFLAPH 243
Cdd:pfam00753 156 iGRLDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 56-207 9.67e-15

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: 72.20  E-value: 9.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  56 IAAYLITTPDGHILLETG----FAETVPLVRASLRQLGIEPRDI-RILLTsHAHIDHAGGL---KAMKALTGARLIASAP 127
Cdd:cd07720   49 VNAFLVRTGGRLILVDTGagglFGPTAGKLLANLAAAGIDPEDIdDVLLT-HLHPDHIGGLvdaGGKPVFPNAEVHVSEA 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 128 --------EAAALARGGRGDFHYGDQLAFEPVTVDEIVADGGTVtLGGVtlTAHLTPGHTPGSTTWtcRVRTGGREL--- 196
Cdd:cd07720  128 ewdfwlddANAAKAPEGAKRFFDAARDRLRPYAAAGRFEDGDEV-LPGI--TAVPAPGHTPGHTGY--RIESGGERLliw 202

                        170
                 ....*....|..
gi 501342302 197 -DVVFAASVSAP 207
Cdd:cd07720  203 gDIVHHPALQFA 214
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 58-247 1.90e-14

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: 70.02  E-value: 1.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  58 AYLITTPDGHILLETGFA--ETVPLVRASLRQLGIEPRDI-RILLTsHAHIDHAGGLKAMKALTGARLIASApeaaalar 134
Cdd:cd07725   17 VYLLRDGDETTLIDTGLAteEDAEALWEGLKELGLKPSDIdRVLLT-HHHPDHIGLAGKLQEKSGATVYILD-------- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 135 ggrgdfhygdqlafepvtvDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVRTggreldVVFAASVSAPGYQL--- 211
Cdd:cd07725   88 -------------------VTPVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDEDRR------ELFVGDAVLPKITPnvs 142

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 501342302 212 VNNAAYPDIWRDLQASIAALRALPCDVFLAPHGQVF 247
Cdd:cd07725  143 LWAVRVEDPLGAYLESLDKLEKLDVDLAYPGHGGPI 178
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 59-182 2.86e-12

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: 64.05  E-value: 2.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  59 YLITTPDGHILLETGfaetvPLVRASLRQL--GIEPRDIR-ILLTsHAHIDHAGGLKAMKALTGARLiasapeaaalaRG 135
Cdd:cd16278   21 YLLGAPDGVVVIDPG-----PDDPAHLDALlaALGGGRVSaILVT-HTHRDHSPGAARLAERTGAPV-----------RA 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 501342302 136 GRGDFHYGDQLAFEPvtvDEIVADGGTVTLGGVTLTAHLTPGHTPGS 182
Cdd:cd16278   84 FGPHRAGGQDTDFAP---DRPLADGEVIEGGGLRLTVLHTPGHTSDH 127
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 58-244 3.23e-12

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: 64.29  E-value: 3.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  58 AYLITTPDGH--ILLETGFAETvplvrASLRQLGIEPRDIRILLTSHAHIDHAGGLKAMKALTGARLiasapeaaALARG 135
Cdd:cd16322   13 TYLVADEGGGeaVLVDPGDESE-----KLLARFGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPV--------YLHPD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 136 GRGDFHYGDQLA-------FEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCRVRTGGRELDVVFAASVSA-- 206
Cdd:cd16322   80 DLPLYEAADLGAkafglgiEPLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPGHVCFYVEEEGLLFSGDLLFQGSIGRtd 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 501342302 207 -PGyqlvnnaAYPdiwRDLQASIAALRALPCDVFLAP-HG 244
Cdd:cd16322  160 lPG-------GDP---KAMAASLRRLLTLPDETRVFPgHG 189
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 81-182 1.94e-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: 61.32  E-value: 1.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  81 VRASLRQLGIEPRDIrilLTSHAHIDHAGGLKAMKALTG-ARLIasapeaaalarGGRGDfhygdqlafEPVTVDEIVAD 159
Cdd:cd07723   33 VLAALEKNGLTLTAI---LTTHHHWDHTGGNAELKALFPdAPVY-----------GPAED---------RIPGLDHPVKD 89

                         90       100
                 ....*....|....*....|...
gi 501342302 160 GGTVTLGGVTLTAHLTPGHTPGS 182
Cdd:cd07723   90 GDEIKLGGLEVKVLHTPGHTLGH 112
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 47-246 1.31e-10

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 59.89  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  47 NVYYVGASDIA-----AYLITTPDGHILLETGFAETV-PLVRASLRQLGiePRDIRILLTSHAHIDHAGGLKAMKALtGA 120
Cdd:cd16282    1 GVYALIGPDGGgfisnIGFIVGDDGVVVIDTGASPRLaRALLAAIRKVT--DKPVRYVVNTHYHGDHTLGNAAFADA-GA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 121 RLIASAPEAAALARGGRGDFHYGDQLA------FEPVTVDEIVADGGTVTLGGVTLTA-HLTPGHTPGSTT-WTcrvrtg 192
Cdd:cd16282   78 PIIAHENTREELAARGEAYLELMRRLGgdamagTELVLPDRTFDDGLTLDLGGRTVELiHLGPAHTPGDLVvWL------ 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 501342302 193 gRELDVVFAASVSAPGYQLVNNAAYPDIWRdlqASIAALRALPCDVFLAPHGQV 246
Cdd:cd16282  152 -PEEGVLFAGDLVFNGRIPFLPDGSLAGWI---AALDRLLALDATVVVPGHGPV 201
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 78-204 3.66e-10

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


Pssm-ID: 293823 [Multi-domain]  Cd Length: 190  Bit Score: 58.33  E-value: 3.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  78 VPLVRASLRQLGIEPrdIRILLTsHAHIDHAGGLKAMKALTGARLIasapeaaalarG-GRGDFHYGDQL---------- 146
Cdd:cd07737   33 ADKILQAIEDLGLTL--KKILLT-HGHLDHVGGAAELAEHYGVPII-----------GpHKEDKFLLENLpeqsqmfgfp 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501342302 147 AFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTTWTCR----VRTGgrelDVVFAASV 204
Cdd:cd07737   99 PAEAFTPDRWLEEGDTVTVGNLTLEVLHCPGHTPGHVVFFNResklAIVG----DVLFKGSI 156
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 76-185 1.28e-09

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: 56.25  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  76 ETVPLVRASLRQLGIEPRdiRILLTsHAHIDHAGGLKAMKALTGARLIAsapeaaalarGGRGDFHYGDQLafepvtvde 155
Cdd:cd07724   33 DSVDRYLDLAAELGLKIT--YVLET-HVHADHVSGARELAERTGAPIVI----------GEGAPASFFDRL--------- 90

                         90       100       110
                 ....*....|....*....|....*....|
gi 501342302 156 iVADGGTVTLGGVTLTAHLTPGHTPGSTTW 185
Cdd:cd07724   91 -LKDGDVLELGNLTLEVLHTPGHTPESVSY 119
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 44-182 1.39e-09

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: 57.11  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  44 IVENVYYVGASDIA-----------------AYLITTpDGHILLETGFAETVPLVRASLRQLgIEPRDIRILLTSHAHID 106
Cdd:cd07709    3 IADDIYWVGVNDWDlrlfegeyptprgtsynSYLIKD-EKTALIDTVKEPFFDEFLENLEEV-IDPRKIDYIVVNHQEPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 107 HAGGLKAMKALT----------GARLIAsapeaaalarggrgdfHYGDQLAFEPVTVDeivaDGGTVTLGGVTLTAHLTP 176
Cdd:cd07709   81 HSGSLPELLELApnakivcskkAARFLK----------------HFYPGIDERFVVVK----DGDTLDLGKHTLKFIPAP 140


                 ....*..
gi 501342302 177 G-HTPGS 182
Cdd:cd07709  141 MlHWPDT 147
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 60-184 2.40e-09

uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC1 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 55.67  E-value: 2.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  60 LITTPDGHILLETGFAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGLkamkAL-TGARLIasapeAAALARGGRG 138
Cdd:cd07711   26 LIKDGGKNILVDTGTPWDRDLLLKALAEHGLSPEDIDYVVLTHGHPDHIGNL----NLfPNATVI-----VGWDICGDSY 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 501342302 139 DFHYGDQLafEPVTVDEivadggtvtlgGVTLTAhlTPGHTPGSTT 184
Cdd:cd07711   97 DDHSLEEG--DGYEIDE-----------NVEVIP--TPGHTPEDVS 127
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 59-179 6.90e-09

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


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 54.46  E-value: 6.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  59 YLITTPDGHILLETG--FAETVPLVRASLRQLGIEPRDiRILLTsHAHIDHAGGLKA-MKALTGARLI---ASAPEAAAL 132
Cdd:cd07722   21 YLVGTGKRRILIDTGegRPSYIPLLKSVLDSEGNATIS-DILLT-HWHHDHVGGLPDvLDLLRGPSPRvykFPRPEEDED 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 501342302 133 ARGGRGDFHYgdqlafepvtvdeiVADGGTVTLGGVTLTAHLTPGHT 179
Cdd:cd07722   99 PDEDGGDIHD--------------LQDGQVFKVEGATLRVIHTPGHT 131
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
44-123 8.01e-08

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 52.58  E-value: 8.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  44 IVENvyYVGASDIAA-----YLITTPDGHILLETGFAETVpLVRAslRQLGIEPRDIRILLTSHAHIDHAGGLKA-MKAL 117
Cdd:COG1237    7 LVDN--TAGDEGLLAehglsALIETEGKRILFDTGQSDVL-LKNA--EKLGIDLSDIDAVVLSHGHYDHTGGLPAlLELN 81


                 ....*.
gi 501342302 118 TGARLI 123
Cdd:COG1237   82 PKAPVY 87
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 48-202 1.21e-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) 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: 50.99  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  48 VYYV-GASDIAAYLITTPDGhILLETGFAETVPL-VRASLRQLGIEPRDIrilLTSHAHIDHAGGLKAMKALTGAR---- 121
Cdd:cd07743    1 TYYIpGPTNIGVYVFGDKEA-LLIDSGLDEDAGRkIRKILEELGWKLKAI---INTHSHADHIGGNAYLQKKTGCKvyap 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 122 -----------LIASAPEAAALARGGRGDFhygdqLAFEPVTVDEIVADgGTVTLGGVTLTAHLTPGHTPGSTTwtcrVR 190
Cdd:cd07743   77 kiekafienplLEPSYLGGAYPPKELRNKF-----LMAKPSKVDDIIEE-GELELGGVGLEIIPLPGHSFGQIG----IL 146

                        170
                 ....*....|..
gi 501342302 191 TggrELDVVFAA 202
Cdd:cd07743  147 T---PDGVLFAG 155
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 81-183 1.59e-07

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: 50.23  E-value: 1.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  81 VRASLRQLGIEPRDIR-ILLTsHAHIDHAGGLKAMKALTGARLIASAPEAAALarggrgDFHYGDQLAFEpvtvdeivaD 159
Cdd:cd16275   34 IEKILAKLNELGLTLTgILLT-HSHFDHVNLVEPLLAKYDAPVYMSKEEIDYY------GFRCPNLIPLE---------D 97

                         90       100
                 ....*....|....*....|....
gi 501342302 160 GGTVTLGGVTLTAHLTPGHTPGST 183
Cdd:cd16275   98 GDTIKIGDTEITCLLTPGHTPGSM 121
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 58-123 3.05e-07

Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, and related proteins; MBL-fold metallo hydrolase domain; This subgroup includes Methanocaldococcus jannaschii 7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase (EC 2.5.1.15), a folate biosynthetic enzyme also known as dihydropteroate synthase and 7,8 dihydropteroate synthase. Thermoanaerobacter tengcongensis Tflp is a ferredoxin-like member. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293799  Cd Length: 269  Bit Score: 50.70  E-value: 3.05e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501342302  58 AYLITTPDGHILLETGFAetvPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGLKA-MKALTGARLI 123
Cdd:cd07713   22 SLLIETEGKKILFDTGQS---GVLLHNAKKLGIDLSDIDAVVLSHGHYDHTGGLKAlLELNPKAPVY 85
NorV COG0426
Flavorubredoxin [Energy production and conversion];
41-182 3.59e-07

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 50.99  E-value: 3.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  41 PFRIVENVYYVGASD-------IA----------AYLITtpDGHI-LLETGFAETVPLVRASLRQLgIEPRDIRILLTSH 102
Cdd:COG0426    2 AVEIAHGVYWVGVLDwdrrlfeGEyptprgttynSYLIV--DEKTaLIDTVGESFFEEFLENLSKV-IDPKKIDYIIVNH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 103 AHIDHAGGLKA-MKALTGARLIasapeaaALARGGRGDFHYGDQLAFEPVTVDeivaDGGTVTLGGVTLTAHLTPG-HTP 180
Cdd:COG0426   79 QEPDHSGSLPElLELAPNAKIV-------CSKKAARFLPHFYGIPDFRFIVVK----EGDTLDLGGHTLQFIPAPMlHWP 147


                 ..
gi 501342302 181 GS 182
Cdd:COG0426  148 DT 149
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 47-247 4.81e-07

uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold metallo hydrolase domain; Includes the uncharacterized Bacillus subtilis YmaE and Nostoc all1228 proteins.Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 49.12  E-value: 4.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  47 NVYYVG---ASDI--AAYLITTPDGHILLET-GFAEtvPLVRAsLRQLGieprDIR-ILLTshaHIDHAGGLKAMKALTG 119
Cdd:cd07727    1 GVYYCGfhsEKSFgaASYLILRPEGNILVDSpRYSP--PLAKR-IEALG----GIRyIFLT---HRDDVADHAKWAERFG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 120 ARLIasapeaaalarggrgdFHYGDqLAFEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGSTT--WtcrvrtggRELD 197
Cdd:cd07727   71 AKRI----------------IHEDD-VNAVTRPDEVIVLWGGDPWELDPDLTLIPVPGHTRGSVVllY--------KEKG 125

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 501342302 198 VVFAA---SVSAPGYQLV-NNAAYPDIWRDLQASIAALRALPCDVFLAPHGQVF 247
Cdd:cd07727  126 VLFTGdhlAWSRRRGWLSaFRYVCWYSWPEQAESVERLADLDFEWVLPGHGRRV 179
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 51-111 4.98e-07

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: 49.38  E-value: 4.98e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501342302  51 VGASdiaAYLITTPDGHILLETG-FAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGL 111
Cdd:cd16295   10 VTGS---CYLLETGGKRILLDCGlFQGGKELEELNNEPFPFDPKEIDAVILTHAHLDHSGRL 68
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 57-182 5.17e-07

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: 48.80  E-value: 5.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  57 AAYLITTPDGHILLETGFAetvplVRASLRQLGIEPRDIRILLTSHAHIDHAGGL----------KAMKALT--GARLIA 124
Cdd:cd16272   18 SSYLLETGGTRILLDCGEG-----TVYRLLKAGVDPDKLDAIFLSHFHLDHIGGLptllfarrygGRKKPLTiyGPKGIK 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 501342302 125 SAPEAAALARGGRGDFHYgdqlafePVTVDEIVADGGTVTLGGVTLTAHLTPgHTPGS 182
Cdd:cd16272   93 EFLEKLLNFPVEILPLGF-------PLEIEELEEGGEVLELGDLKVEAFPVK-HSVES 142
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 51-194 1.89e-06

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 48.64  E-value: 1.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  51 VGASdiaAYLITTPDGHILLETGFAETvpLVRASLRQLGIEPRDI-RILLTsHAHIDHAGGL---------------KAM 114
Cdd:COG1236   12 VTGS---CYLLETGGTRILIDCGLFQG--GKERNWPPFPFRPSDVdAVVLT-HAHLDHSGALpllvkegfrgpiyatPAT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 115 KALTGARLiasapeaaalarGGRGDFHYGDQLAFEPVTVDEI---------VADGGTVTLGGVTLTahLTP-GHTPGSTT 184
Cdd:COG1236   86 ADLARILL------------GDSAKIQEEEAEAEPLYTEEDAeralelfqtVDYGEPFEIGGVRVT--FHPaGHILGSAQ 151

                        170
                 ....*....|
gi 501342302 185 WtcRVRTGGR 194
Cdd:COG1236  152 V--ELEVGGK 159
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 51-243 1.99e-06

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: 47.93  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  51 VGASDiaAYLITTPDGHILL-----ETGFAETVPLVRASLRQLGIepRDIRILLTSHAHIDHAGGLKA-MKALTGARLIa 124
Cdd:COG2333    8 VGQGD--AILIRTPDGKTILidtgpRPSFDAGERVVLPYLRALGI--RRLDLLVLTHPDADHIGGLAAvLEAFPVGRVL- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 125 sapeAAALARGGRGDFHYGDQLAFEPVTVDEIVAdGGTVTLGGVTLTAhLTPGHTPGSTTW------TCRVRTGGRelDV 198
Cdd:COG2333   83 ----VSGPPDTSETYERLLEALKEKGIPVRPCRA-GDTWQLGGVRFEV-LWPPEDLLEGSDennnslVLRLTYGGF--SF 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 501342302 199 VFAASVSAPGyqlvnnaaypdiWRDLqasIAALRALPCDVFLAPH 243
Cdd:COG2333  155 LLTGDAEAEA------------EAAL---LARGPDLKADVLKVPH 184
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 59-182 3.33e-06

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: 46.47  E-value: 3.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  59 YLITTPDGHILLETGF--AETVPLVRaSLRQLGIeprdirILLTSHAHIDHAGGLK-----AMKALTGARLiasapeaaa 131
Cdd:cd07712   12 YLLRGRDRALLIDTGLgiGDLKEYVR-TLTDLPL------LVVATHGHFDHIGGLHefeevYVHPADAEIL--------- 75

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 501342302 132 laRGGRGDFHYGDQLA---FEPVTVDEIVADGGTVTLGGVTLTAHLTPGHTPGS 182
Cdd:cd07712   76 --AAPDNFETLTWDAAtysVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGS 127
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 60-111 3.60e-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: 293839  Cd Length: 252  Bit Score: 47.10  E-value: 3.60e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501342302  60 LITTPDGHILLETG-------------FAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGL 111
Cdd:cd16281   47 LIETGGRNILIDTGigdkqdpkfrsiyVQHSEHSLLKSLARLGLSPEDITDVILTHLHFDHCGGA 111
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 81-123 2.04e-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: 44.95  E-value: 2.04e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 501342302  81 VRASLRQLGIEPRDIRILLTSHAHIDHAGGLkamKALTGARLI 123
Cdd:cd07730   70 VAEQLAAGGIDPEDIDAVILSHLHWDHIGGL---SDFPNARLI 109
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 60-111 5.16e-05

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


Pssm-ID: 293814  Cd Length: 249  Bit Score: 43.79  E-value: 5.16e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501342302  60 LITTPDGHILLETG-------------FAETVP-LVRASLRQLGIEPRDIRILLTSHAHIDHAGGL 111
Cdd:cd07728   47 LIQYQGKNYLIDAGigngkltekqkrnFGVTEEsSIEESLAELGLTPEDIDYVLMTHLHFDHASGL 112
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 51-123 5.18e-05

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 42.89  E-value: 5.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501342302  51 VGASDiaAYLITTPDGHILLETG----FAETVplVRASLRQLGIepRDIRILLTSHAHIDHAGGLKA-MKALTGARLI 123
Cdd:cd07731    7 VGQGD--AILIQTPGKTILIDTGprdsFGEDV--VVPYLKARGI--KKLDYLILTHPDADHIGGLDAvLKNFPVKEVY 78
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 57-201 6.58e-05

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 43.35  E-value: 6.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  57 AAYLITTPDGHILLETGFAetvplVRASLRQLGIEPRDIR-ILLTsHAHIDHAGGLKAMKALTGARLI----ASAPEAAA 131
Cdd:COG1235   36 SSILVEADGTRLLIDAGPD-----LREQLLRLGLDPSKIDaILLT-HEHADHIAGLDDLRPRYGPNPIpvyaTPGTLEAL 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 132 LARGGRGDFHYGDQLAFEPVTVDEivadggTVTLGGVTLTAHLTPGhtPGSTTWTCRVRTGGRelDVVFA 201
Cdd:COG1235  110 ERRFPYLFAPYPGKLEFHEIEPGE------PFEIGGLTVTPFPVPH--DAGDPVGYRIEDGGK--KLAYA 169
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 60-111 1.19e-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: 42.61  E-value: 1.19e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501342302  60 LITTPDGHILLETGF-------------AETVPLVRASLR----------QLGIEPRDIR-ILLTsHAHIDHAGGL 111
Cdd:cd07742   23 LVETDDGLVLVDTGFgladvadpkrrlgGPFRRLLRPRLDedetavrqieALGFDPSDVRhIVLT-HLDLDHAGGL 97
COG1782 COG1782
Predicted metal-dependent RNase, contains metallo-beta-lactamase and KH domains [General ...
 51-111 1.22e-04

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


Pssm-ID: 441388 [Multi-domain]  Cd Length: 460  Bit Score: 43.19  E-value: 1.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501342302  51 VGASdiaAYLITTPDGHILLETG-FAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGL 111
Cdd:COG1782   12 VTGS---CHLLETGESRILLDCGlFQGGREERERNNDAFPFDPEELDAVVLTHAHLDHSGLL 70
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 58-114 2.64e-04

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


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 40.71  E-value: 2.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 501342302  58 AYLITTPDGHILLETGFAETVPLVRasLRQLGIEPRDIRILLTSHAHIDHAGGLKAM 114
Cdd:cd07733   11 CTYLETEDGKLLIDAGLSGRKITGR--LAEIGRDPEDIDAILVTHEHADHIKGLGVL 65
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 42-180 2.68e-04

Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and related proteins; MBL-fold metallo-hydrolase domain; Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudomonas aeruginosa SdsA1 is a secreted SDS hydrolase that allows the bacterium to use primary sulfates such as the detergent SDS common in commercial personal hygiene products as a sole carbon or sulfur source. Pseudomonas inverting secondary alkylsulfatase 1 (Pisa1) is specific for secondary alkyl sulfates. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 41.33  E-value: 2.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  42 FRIVENVYYVGASDIA-AYLITTPDGHILLETGF-AETVPLVRASLRQLgIEPRDIRILLTSHAHIDHAGGLKA------ 113
Cdd:cd07710    3 FEVTDGVYQVRGYDLSnMTFIEGDTGLIIIDTLEsAEAAKAALELFRKH-TGDKPVKAIIYTHSHPDHFGGAGGfveeed 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 114 ------------MKALTGARLIASAPeaaalaRGGRGDFHYGDQL---------------------AFEPVTvDEIVADG 160
Cdd:cd07710   82 sgkvpiiapegfMEEAVSENVLAGNA------MSRRAAYQFGALLpkgekgqvgaglgpglstgtvGFIPPT-ITITETG 154

                        170       180
                 ....*....|....*....|
gi 501342302 161 GTVTLGGVTLTAHLTPGHTP 180
Cdd:cd07710  155 ETLTIDGVELEFQHAPGEAP 174
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
57-111 6.66e-04

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 40.56  E-value: 6.66e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 501342302  57 AAYLITTPDGHILLETGfaetvPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGL 111
Cdd:COG1234   20 SSYLLEAGGERLLIDCG-----EGTQRQLLRAGLDPRDIDAIFITHLHGDHIAGL 69
metallo-hydrolase-like_MBL-fold cd07740
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 60-111 7.09e-04

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


Pssm-ID: 293826 [Multi-domain]  Cd Length: 194  Bit Score: 39.93  E-value: 7.09e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501342302  60 LITTPDGHILLETGfAETVPlvraSLRQLGIEPRDIRILLTSHAHIDHAGGL 111
Cdd:cd07740   20 HVASEAGRFLIDCG-ASSLI----ALKRAGIDPNAIDAIFITHLHGDHFGGL 66
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 57-185 9.04e-04

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 39.90  E-value: 9.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  57 AAYLITTPDGHILLETGFAETVPLVRASLRQLGiEPRDIRILLTSHAHIDHAG--GLKAMKAlTGARLIasapeaaalar 134
Cdd:COG2220   12 ATFLIETGGKRILIDPVFSGRASPVNPLPLDPE-DLPKIDAVLVTHDHYDHLDdaTLRALKR-TGATVV----------- 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 501342302 135 GGRGDFHYGDQLAFEPVTVdeiVADGGTVTLGGVTLTA----HLTPGHTPGSTTW 185
Cdd:COG2220   79 APLGVAAWLRAWGFPRVTE---LDWGESVELGGLTVTAvparHSSGRPDRNGGLW 130
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 47-185 1.00e-03

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 39.49  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  47 NVYYVGASDIAAYLITTPDGHILLETgfaetVPLVRASLRQlGIE---PRDIRILLTSHAHIDHAGGLKAMKALtGARLI 123
Cdd:cd16276    1 GVYWVTDGGYQSMFLVTDKGVIVVDA-----PPSLGENLLA-AIRkvtDKPVTHVVYSHNHADHIGGASIFKDE-GATII 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501342302 124 ASAPEAaalarggrgdfhygDQLAFEP----VTVDEIVADGGTVTLGGVTLTAH-LTPGHTPGSTTW 185
Cdd:cd16276   74 AHEATA--------------ELLKRNPdpkrPVPTVTFDDEYTLEVGGQTLELSyFGPNHGPGNIVI 126
metallo-hydrolase-like_MBL-fold cd07741
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 80-114 2.18e-03

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


Pssm-ID: 293827 [Multi-domain]  Cd Length: 212  Bit Score: 38.71  E-value: 2.18e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 501342302  80 LVRASlrQLGIEPRDIRILLTSHAHIDHAGGLKAM 114
Cdd:cd07741   41 LVRMC--RPKLDPTKLDAIILSHRHLDHSNDANVL 73
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 56-204 5.67e-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: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 37.50  E-value: 5.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302  56 IAAYLITTPDGHILLETG------------FAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGLkamkalT----- 118
Cdd:cd16277   13 IHSWLVRTPGRTILVDTGigndkprpgppaFHNLNTPYLERLAAAGVRPEDVDYVLCTHLHVDHVGWN------Trlvdg 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501342302 119 -------GAR-LIASAPEAAALARGGRGDFH---YGDQLAfePVtVDEIVA---DGGTVTLGGVTLTAhlTPGHTPGSTt 184
Cdd:cd16277   87 rwvptfpNARyLFSRAEYDHWSSPDAGGPPNrgvFEDSVL--PV-IEAGLAdlvDDDHEILDGIRLEP--TPGHTPGHV- 160

                        170       180
                 ....*....|....*....|
gi 501342302 185 wTCRVRTGGREldVVFAASV 204
Cdd:cd16277  161 -SVELESGGER--ALFTGDV 177
Int9-11_CPSF2-3-like_MBL-fold cd07734
Int9, Int11, CPSF2, CPSF3 and related cleavage and polyadenylation specificity factors; ...
 51-111 7.06e-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: 36.93  E-value: 7.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501342302  51 VGASdiaAYLITTPDGHILLETGFAETVPLVRASLRQLGIEPRDIRILLTSHAHIDHAGGL 111
Cdd:cd07734    9 VGRS---CFLVEFKGRTVLLDCGMNPGKEDPEACLPQFELLPPEIDAILISHFHLDHCGAL 66
 
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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