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Conserved domains on  [gi|13423630|gb|AAK24110|]
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metallo-beta-lactamase superfamily protein [Caulobacter vibrioides CB15]

Protein Classification

CAU/MBL1b family subclass B3 metallo-beta-lactamase( domain architecture ID 10888866)

CAU/MBL1b family 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
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-280 5.29e-163

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: 452.68  E-value: 5.29e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  28 WTKPTKPYRVVGNIYYVGTEGISSWLITSSEGHVVLDGGPNaETGKLVERNITALGFQLADVKILINTHAHYDHAGGLAQ 107
Cdd:cd16310   1 WTAPTEPFRIVDNIYYVGTKGIGSYLITSNHGAILLDGGLE-ENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 108 LKADTGAKLWISRDDAPAMTAGHHIGDNIYGPTPMPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWTTAVVEKG 187
Cdd:cd16310  80 LKADTGAKLWASRGDRPALEAGKHIGDNITQPAPFPAVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTWSTTVKENG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 188 RPLTVTFPCSLSVAGNVLVGNKTHRTIVADYRASFAKLRAIPTDVMLPAHEEQGNLLAKRQKQLRGDPNAFVDPTELARF 267
Cdd:cd16310 160 RPLRVVFPCSLSVAGNVLVGNKTYPTIVEDYRASFARLRAMKADIVLTSHPEVADLLARKAKQDAGQANAFVDPGELARI 239

                       250
                ....*....|...
gi 13423630 268 VDASEAAFNKELA 280
Cdd:cd16310 240 VDQSEAAFNKELA 252
 
Name Accession Description Interval E-value
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-280 5.29e-163

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: 452.68  E-value: 5.29e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  28 WTKPTKPYRVVGNIYYVGTEGISSWLITSSEGHVVLDGGPNaETGKLVERNITALGFQLADVKILINTHAHYDHAGGLAQ 107
Cdd:cd16310   1 WTAPTEPFRIVDNIYYVGTKGIGSYLITSNHGAILLDGGLE-ENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 108 LKADTGAKLWISRDDAPAMTAGHHIGDNIYGPTPMPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWTTAVVEKG 187
Cdd:cd16310  80 LKADTGAKLWASRGDRPALEAGKHIGDNITQPAPFPAVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTWSTTVKENG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 188 RPLTVTFPCSLSVAGNVLVGNKTHRTIVADYRASFAKLRAIPTDVMLPAHEEQGNLLAKRQKQLRGDPNAFVDPTELARF 267
Cdd:cd16310 160 RPLRVVFPCSLSVAGNVLVGNKTYPTIVEDYRASFARLRAMKADIVLTSHPEVADLLARKAKQDAGQANAFVDPGELARI 239

                       250
                ....*....|...
gi 13423630 268 VDASEAAFNKELA 280
Cdd:cd16310 240 VDQSEAAFNKELA 252
B3_Acin_new1 NF033184
putative subclass B3 metallo-beta-lactamase; This is one of two families of putative ...
 24-279 1.93e-77

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


Pssm-ID: 439394  Cd Length: 283  Bit Score: 236.93  E-value: 1.93e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630   24 MPANWTKPTKPYRVVGNIYYVGTEGISSWLITSSEGHVVLDGGPnAETGKLVERNITALGFQLADVKILINTHAHYDHAG 103
Cdd:NF033184  24 LPDDWTQNTQPFQITENIYYVGTHGLAAYLLASGHQALLIDTGL-PENTEQIEQNIKQLGFKLSDVKIMVTSHAHWDHVG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  104 GLAQLKADTGAKLWISRDDAPAMTAGHHIGDNIYGPTPMPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWTTAV 183
Cdd:NF033184 103 ALARIKQDTGAKLIAMQQDVKALEIGKPIGENTFQTIPFTPVKVDKVIHDGEVVKLGKFKLKATLTPGHTPGCTTWSTEV 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  184 VEKGRPLTVTFPCSLSVAGNVLVGNKTHRTIVADYRASFAKLRAIPTDVMLPAHEEQGNLLAKRQKQLRGDPNAFVDPTE 263
Cdd:NF033184 183 KSNGKNLNVVFPCSLSVAGNVLQNNHQYPNIVADYRKSFERLKNMKADIVLTSHPEVADVLGNKARKDAGQTNAFIQPEK 262

                        250
                 ....*....|....*.
gi 13423630  264 LARFVDASEAAFNKEL 279
Cdd:NF033184 263 LSSIVKDAEMAFEKSL 278
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 35-239 9.06e-31

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 114.40  E-value: 9.06e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  35 YRVVGNIYYVGTeGISSWLITSSEGHVVLDGGPNAETGKLVERNITALGfqlADVKILINTHAHYDHAGGLAQLKADTGA 114
Cdd:COG0491   2 YVLPGGTPGAGL-GVNSYLIVGGDGAVLIDTGLGPADAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFGA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 115 KLWISRDDAPAMTAGHHIGDniygpTPMPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWttaVVEKGRPLtvtf 194
Cdd:COG0491  78 PVYAHAAEAEALEAPAAGAL-----FGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSF---YVPDEKVL---- 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 13423630 195 pcslsVAGNVLVGNKTHRTI-----VADYRASFAKLRAIPTDVMLPAHEE 239
Cdd:COG0491 146 -----FTGDALFSGGVGRPDlpdgdLAQWLASLERLLALPPDLVIPGHGP 190
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 50-237 4.13e-23

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: 93.39  E-value: 4.13e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630     50 SSWLITSSEGHVVLDGGPNAETGKLVErnITALGfqLADVKILINTHAHYDHAGGLAQLKADTGAKLWISRDDAPAMTAG 129
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAE--LKKLG--PKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630    130 HHIGDNIYGPTPMPavKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWttaVVEKGRpltVTFP-CSLSVAGNVLVGN 208
Cdd:smart00849  77 LALLGELGAEAEPA--PPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVL---YLPEGK---ILFTgDLLFAGGDGRTLV 148

                          170       180
                   ....*....|....*....|....*....
gi 13423630    209 KTHRTIVADYRASFAKLRAIPTDVMLPAH 237
Cdd:smart00849 149 DGGDAAASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
44-237 9.82e-23

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 92.82  E-value: 9.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630    44 VGTEGISSWLITSSEGHVVLDGGPNAETGKLVErnITALGFQLADVKILINTHAHYDHAGGLAQLKADTGAKLWISRDDA 123
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLLL--LAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630   124 PAMTAGHHIGDNIYGPTPMPAVKPDRSFGDQTKLKLGEIAMV---AHLTPGHTIGCTSwttaVVEKGRPL-----TVTFP 195
Cdd:pfam00753  79 RELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLgllVTHGPGHGPGHVV----VYYGGGKVlftgdLLFAG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 13423630   196 CSLSVAGNVLVGNKTHRTIVADYRASFAKLRAIPTDVMLPAH 237
Cdd:pfam00753 155 EIGRLDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 79-179 1.94e-05

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 45.22  E-value: 1.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630   79 ITALGFQLADVKILINTHAHYDHAGGLAQLKADTGAKLwisrddapamtaghhIGdniygptpmPAVKPDRSFGDQTKLK 158
Cdd:PLN02398 112 IDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKV---------------IG---------SAVDKDRIPGIDIVLK 167

                         90       100
                 ....*....|....*....|....*..
gi 13423630  159 LGEIAMVA-HL-----TPGHTIGCTSW 179
Cdd:PLN02398 168 DGDKWMFAgHEvlvmeTPGHTRGHISF 194
 
Name Accession Description Interval E-value
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-280 5.29e-163

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: 452.68  E-value: 5.29e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  28 WTKPTKPYRVVGNIYYVGTEGISSWLITSSEGHVVLDGGPNaETGKLVERNITALGFQLADVKILINTHAHYDHAGGLAQ 107
Cdd:cd16310   1 WTAPTEPFRIVDNIYYVGTKGIGSYLITSNHGAILLDGGLE-ENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 108 LKADTGAKLWISRDDAPAMTAGHHIGDNIYGPTPMPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWTTAVVEKG 187
Cdd:cd16310  80 LKADTGAKLWASRGDRPALEAGKHIGDNITQPAPFPAVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTWSTTVKENG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 188 RPLTVTFPCSLSVAGNVLVGNKTHRTIVADYRASFAKLRAIPTDVMLPAHEEQGNLLAKRQKQLRGDPNAFVDPTELARF 267
Cdd:cd16310 160 RPLRVVFPCSLSVAGNVLVGNKTYPTIVEDYRASFARLRAMKADIVLTSHPEVADLLARKAKQDAGQANAFVDPGELARI 239

                       250
                ....*....|...
gi 13423630 268 VDASEAAFNKELA 280
Cdd:cd16310 240 VDQSEAAFNKELA 252
BJP-1_FEZ-1-like_MBL-B3 cd16288
BJP-1, FEZ-1, GOB-1, Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-280 6.85e-103

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: 300.78  E-value: 6.85e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  28 WTKPTKPYRVVGNIYYVGTEGISSWLITSSEGHVVLDGGPnAETGKLVERNITALGFQLADVKILINTHAHYDHAGGLAQ 107
Cdd:cd16288   1 WNAPFEPFRIAGNVYYVGTSGLASYLITTPQGLILIDTGL-ESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 108 LKADTGAKLWISRDDAPAMTAGHHiGDNIYGPTPM--PAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWTTAVVE 185
Cdd:cd16288  80 LKKLTGAKLMASAEDAALLASGGK-SDFHYGDDSLafPPVKVDRVLKDGDRVTLGGTTLTAHLTPGHTRGCTTWTMTVKD 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 186 KGRPLTVTFPCSLSVA-GNVLVGNKTHRTIVADYRASFAKLRAIPTDVMLPAHEEQGNLLAKRQKQLRGDPNAFVDPTEL 264
Cdd:cd16288 159 DGKVYQVVFADSLTVNpGYKLVGNPTYPGIAEDYRHSFATLRALQCDIFLASHAEYFDLKEKRARLAAGQPNAFIDPEGY 238

                       250
                ....*....|....*.
gi 13423630 265 ARFVDASEAAFNKELA 280
Cdd:cd16288 239 RNFIEKAKADFEKQLA 254
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-280 2.18e-99

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: 291.70  E-value: 2.18e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  28 WTKPTKPYRVVGNIYYVGTEGISSWLITSSEGHVVLDGGpNAETGKLVERNITALGFQLADVKILINTHAHYDHAGGLAQ 107
Cdd:cd16309   1 WNEPMEPFKLIGNIYYVGTAGLGVFLITTPEGHILIDGA-MPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 108 LKADTGAKLWISRDDAPAMTAGHhIGdniYGPTP---MPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWTTAVV 184
Cdd:cd16309  80 LKKATGAQLVASAADKPLLESGY-VG---SGDTKnlqFPPVRVDRVIGDGDKVTLGGTTLTAHLTPGHSPGCTSWTTTVK 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 185 EK-GRPLTVTFPCSLSVAGNVLVGNKTHRTIVADYRASFAKLRAIPTDVMLPAHEEQGNLLAKRQKQLRGDPNAFVDPTE 263
Cdd:cd16309 156 DTaGPPREVLFFCSATVAGNQLVGPPTYPGIVDDYRATFAKARAMKADVFLANHPEFFGLVAKRARQSAGEPDAFVDAGE 235

                       250
                ....*....|....*..
gi 13423630 264 LARFVDASEAAFNKELA 280
Cdd:cd16309 236 LQRFNTKMEDDFEKALA 252
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 28-272 1.40e-77

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: 235.90  E-value: 1.40e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  28 WTKPTKPYRVVGNIYYVGTEGISSWLITSSEGHVVLDGGPNAETGkLVERNITALGFQLADVKILINTHAHYDHAGGLAQ 107
Cdd:cd07708   1 WPNPFPPFQIAGNTYYVGTDDLAAYLIVTPQGNILIDGDMEQNAP-MIKANIKKLGFKFSDTKLILISHAHFDHAGGSAE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 108 LKADTGAKLWISRDDAPAMTAGH----HIGDNiyGPTPMPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWTTAV 183
Cdd:cd07708  80 IKKQTGAKVMAGAEDVSLLLSGGssdfHYAND--SSTYFPQSTVDRAVHDGERVTLGGTVLTAHATPGHTPGCTTWTMTL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 184 VEKGRPLTVTFPCSLSVA-GNVLVGNKTHRTIVADYRASFAKLRAIPTDVMLPAHEEQGNLLAKRQKQLRGDPNAFVDPT 262
Cdd:cd07708 158 KDHGKQYQVVFADSLTVNpGYRLVDNPTYPKIVEDYRHSFAVVEAMRCDILLGPHPGVFDMKNKYVLLSKGQNNPFVDPG 237

                       250
                ....*....|
gi 13423630 263 ELARFVDASE 272
Cdd:cd07708 238 GCKAYAEAKA 247
B3_Acin_new1 NF033184
putative subclass B3 metallo-beta-lactamase; This is one of two families of putative ...
 24-279 1.93e-77

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


Pssm-ID: 439394  Cd Length: 283  Bit Score: 236.93  E-value: 1.93e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630   24 MPANWTKPTKPYRVVGNIYYVGTEGISSWLITSSEGHVVLDGGPnAETGKLVERNITALGFQLADVKILINTHAHYDHAG 103
Cdd:NF033184  24 LPDDWTQNTQPFQITENIYYVGTHGLAAYLLASGHQALLIDTGL-PENTEQIEQNIKQLGFKLSDVKIMVTSHAHWDHVG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  104 GLAQLKADTGAKLWISRDDAPAMTAGHHIGDNIYGPTPMPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWTTAV 183
Cdd:NF033184 103 ALARIKQDTGAKLIAMQQDVKALEIGKPIGENTFQTIPFTPVKVDKVIHDGEVVKLGKFKLKATLTPGHTPGCTTWSTEV 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  184 VEKGRPLTVTFPCSLSVAGNVLVGNKTHRTIVADYRASFAKLRAIPTDVMLPAHEEQGNLLAKRQKQLRGDPNAFVDPTE 263
Cdd:NF033184 183 KSNGKNLNVVFPCSLSVAGNVLQNNHQYPNIVADYRKSFERLKNMKADIVLTSHPEVADVLGNKARKDAGQTNAFIQPEK 262

                        250
                 ....*....|....*.
gi 13423630  264 LARFVDASEAAFNKEL 279
Cdd:NF033184 263 LSSIVKDAEMAFEKSL 278
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 ...
 28-279 6.92e-74

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


Pssm-ID: 293848 [Multi-domain]  Cd Length: 256  Bit Score: 226.85  E-value: 6.92e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  28 WTKPTKPYRVVGNIYYVGTEGISSWLITSSEGHVVLDGG-PNAetGKLVERNITALGFQLADVKILINTHAHYDHAGGLA 106
Cdd:cd16290   1 WNQPQAPFRIHGNTYYVGTGGLSAVLITSPQGLILIDGAlPQS--APQIEANIRALGFRLEDVKLILNSHAHFDHAGGIA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 107 QLKADTGAKLWISRDDAPAMTAGHHIGDNiygP-----TPMPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWTT 181
Cdd:cd16290  79 ALQRDSGATVAASPAGAAALRSGGVDPDD---PqagaaDPFPPVAKVRVVADGEVVKLGPLAVTAHATPGHTPGGTSWTW 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 182 AVVEKGRPLTVTFPCSLSV--AGNVLVGNKTHRTIVADYRASFAKLRAIPTDVMLPAHEEQGNLLAKRQKQLRG-DPNAF 258
Cdd:cd16290 156 RSCEGGRCLDIVYADSLTAvsADGFRFSDDAHPARVAAFRRSIATVAALPCDILISAHPDASGLWEKLARRAREpGPNPF 235

                       250       260
                ....*....|....*....|.
gi 13423630 259 VDPTELARFVDASEAAFNKEL 279
Cdd:cd16290 236 IDPNACRAYAAAAEARLEARL 256
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-280 2.82e-65

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: 204.99  E-value: 2.82e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  28 WTKPTKPYRVVGNIYYVGTEGISSWLITSSEGHVVLDGgpNAETG-KLVERNITALGFQLADVKILINTHAHYDHAGGLA 106
Cdd:cd16307   1 WTTPFPPFRIAGNLYYVGSRDLASYLITTPRGNILINS--NLESSvPQIKASIEKLGFKFSDTKILLISHAHFDHAAGSA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 107 QLKADTGAKLWISRDDAPAMTAGHHiGDNIYGPTP---MPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWTTAV 183
Cdd:cd16307  79 LIKRETHAKYMVMDGDVDVVESGGK-SDFFYGNDPstyFPPAHVDKVLHDGEQVELGGTVLTAHLTAGHTKGCTTWTMKV 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 184 VEKGRPLTVTFPCSLSV-AGNVLVGNKTHRTIVADYRASFAKLRAIPTDVMLPAHEEQGNLLAKRQKQLRGDPNAFVDPT 262
Cdd:cd16307 158 KDHGKTYDVVIVGSPNVnPGAKLVNNITYPGIAEDYAHTFAVLRSLPCDIFLGAHGGYFDLKNKYVRLQKGGANPFIDPE 237

                       250
                ....*....|....*...
gi 13423630 263 ELARFVDASEAAFNKELA 280
Cdd:cd16307 238 GYKAYVAEKEQAFRTELE 255
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 28-280 2.22e-57

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: 184.68  E-value: 2.22e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  28 WTKPTKPYRVVGNIYYVGTEGISSWLITSSEGHVVLDGGPNaETGKLVERNITALGFQLADVKILINTHAHYDHAGGLAQ 107
Cdd:cd16313   1 WNAPQEPFQIYGNTYYVGTGGISAVLITSPQGHILIDGGFP-KSPEQIAASIRQLGFKLEDVKYILSSHDHWDHAGGIAA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 108 LKADTGAKLWISRDDAPAMTAGHHIGDN--IYGPTPMPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWTTAVVE 185
Cdd:cd16313  80 LQKLTGAQVLASPATVAVLRSGSMGKDDpqFGGLTPMPPVASVRAVRDGEVVKLGPLAVTAHATPGHTTGGTSWTWQSCE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 186 KGRPLTVTFPCSLSVAGNVLVGNKTHRTIVADYRASFAKLRAIPTDVMLPAHEEQGNLLAKRQKQLRGDPNAFVDPTELA 265
Cdd:cd16313 160 QGRCANMVFADSLTAVSADGYRFSAHPAVLADVEQSIAAVEKLACDILVSAHPEFSDMWTRVKRGAAEGNAAFIDGGGCR 239

                       250
                ....*....|....*
gi 13423630 266 RFVDASEAAFNKELA 280
Cdd:cd16313 240 AYAAKAREKLNKRLA 254
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-279 4.98e-57

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: 183.70  E-value: 4.98e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  28 WTKPTKPYRVVGNIYYVGTEGISSWLITSSEGHVVLDGGPnAETGKLVERNITALGFQLADVKILINTHAHYDHAGGLAQ 107
Cdd:cd16315   1 WDKPAPPARIFGNTYYVGTCGISAILITGDDGHVLIDSGT-EEAAPLVLANIRKLGFDPKDVRWLLSSHEHFDHVGGLAA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 108 LKADTGAKLWISRDDAPAMTAGH-HIGDNIYGP-TPMPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWTTAVVE 185
Cdd:cd16315  80 LQRATGARVAASAAAAPVLESGKpAPDDPQAGLhEPFPPVRVDRIVEDGDTVALGSLRLTAHATPGHTPGALSWTWRSCE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 186 KGRPLTVTFPCSLSVagnvlVGNKTHR-----TIVADYRASFAKLRAIPTDVMLPAHEEQGNLLAKrqkqLRGDpNAFVD 260
Cdd:cd16315 160 GADCRTIVYADSLSP-----VSADGYRfsdhpDYVAAYRAGLAKVAALPCDILLTPHPSASDMFER----LSGG-APLAD 229

                       250
                ....*....|....*....
gi 13423630 261 PTELARFVDASEAAFNKEL 279
Cdd:cd16315 230 PDACAAYAAGAEKRLDERL 248
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-280 5.15e-57

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: 184.04  E-value: 5.15e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  28 WTKPTKPYRVVGNIYYVGTEGISSWLITSSEGHVVLDGGPnAETGKLVERNITALGFQLADVKILINTHAHYDHAGGLAQ 107
Cdd:cd16312   1 WNQPVKPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGAL-PQSAPLIIANIEALGFRIEDVKLILNSHAHWDHAGGIAA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 108 LKADTGAKLWISRDDAPAMTAGHHIGDNI-YGPTP---MPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWTTAV 183
Cdd:cd16312  80 LQKASGATVAASAHGAQVLQSGTNGKDDPqYQAKPvvhVAKVAKVKEVGEGDTLKVGPLRLTAHMTPGHTPGGTTWTWTS 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 184 VEKGRPLTVTFPCSL---SVAGNVLVGNKTHRTIVADYRASFAKLRAIPTDVMLPAHEEQGNLLAKRQKQlRGDPNAFVD 260
Cdd:cd16312 160 CEGQRCLDVVYADSLnpySSGDFYYTGKGGYPDISASFRASIAKVAALPCDIIIAVHPGFTDVLDKAKRR-SGDTNPFID 238

                       250       260
                ....*....|....*....|
gi 13423630 261 PTELARFVDASEAAFNKELA 280
Cdd:cd16312 239 AEACRAYAAGAAKSLEKRLA 258
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 28-280 2.65e-56

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: 181.90  E-value: 2.65e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  28 WTKPTKPYRVVGNIYYVGTEGISSWLITSSEGHVVLDGGpNAETGKLVERNITALGFQLADVKILINTHAHYDHAGGLAQ 107
Cdd:cd16308   1 WSQPYAPFRIAGNLYYVGTYDLACYLIVTPKGNILINTG-LAESVPLIKKNIQALGFKFKDIKILLTTQAHYDHVGAMAA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 108 LKADTGAKLWISRDDAPAMTAG----HHIGDniYGPTPMPaVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWTTAV 183
Cdd:cd16308  80 IKQQTGAKMMVDEKDAKVLADGgksdYEMGG--YGSTFAP-VKADKLLHDGDTIKLGGTKLTLLHHPGHTKGSCSFLFDV 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 184 VEKGRPLTVTFPCSLSVAGNV-LVGNKTHRTIVADYRASFAKLRAIPTDVMLPAHEEQGNLLAKRQKQLRGDPNAFVDPT 262
Cdd:cd16308 157 KDEKRTYRVLIANMPTILPDTkLSGMPGYPGIAKDYAYTFEAMKALSFDIWLASHASQFDLHQKHKPGAPYNPAAFADRA 236

                       250
                ....*....|....*...
gi 13423630 263 ELARFVDASEAAFNKELA 280
Cdd:cd16308 237 GYDKALAGLEKSYDKKIK 254
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-280 4.83e-56

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: 181.34  E-value: 4.83e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  28 WTKPTKPYRVVGNIYYVGTEGISSWLITSSEGHVVLDGGPNAETGKLVErNITALGFQLADVKILINTHAHYDHAGGLAQ 107
Cdd:cd16311   1 WNADQAPFRIFGNTYYVGVKGLSSVLVTSPQGHVLVDGGLPESAPKIIA-NIEALGFRIEDVKLILNSHGHIDHAGGLAE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 108 LKADTGAKLWISRDDAPAMTAGHHIGDN-IYGPTP-MPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWTTAVVE 185
Cdd:cd16311  80 LQRRSGALVAASPSAALDLASGEVGPDDpQYHALPkYPPVKDMRLARDGGQFNVGPVSLTAHATPGHTPGGLSWTWQSCD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 186 KGRPLTVTFPCSL---SVAGNVLVGNKTHRTIVADYRASFAKLRAIPTDVMLPAHEEQGNLLAKRQKQLRGDPNAFVDPT 262
Cdd:cd16311 160 GPRCLNMVYADSQnavSRPGFKFSASSEYPNAVADLRRSFETLEKLPCDVLISAHPEASQLWERLEASDRSARPALVDRE 239

                       250
                ....*....|....*...
gi 13423630 263 ELARFVDASEAAFNKELA 280
Cdd:cd16311 240 ACRRYASRAREALEKRIA 257
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 28-280 4.05e-54

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: 176.24  E-value: 4.05e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  28 WTKPTKPYRVVGNIYYVGTEGISSWLITSSEGHVVLDGGPNAETGKLVERNITALGFQLADVKILINTHAHYDHAGGLAQ 107
Cdd:cd16280   1 KKGYVEPFQVFDNLYYVGNKWVSAWAIDTGDGLILIDALNNNEAADLIVDGLEKLGLDPADIKYILITHGHGDHYGGAAY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 108 LKADTGAKLWISRDDAPAMTAGHHIGDNiYGPTPMPavKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWTTAVVEKG 187
Cdd:cd16280  81 LKDLYGAKVVMSEADWDMMEEPPEEGDN-PRWGPPP--ERDIVIKDGDTLTLGDTTITVYLTPGHTPGTLSLIFPVKDGG 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 188 RPLTVtfpcslSVAGNVLVGNKTHRTIVADYRASFAKLRAIPT----DVMLPAHEEQGNLLAKRQK---QLRGDPNAFVD 260
Cdd:cd16280 158 KTHRA------GLWGGTGLNTGPNLERREQYIASLERFKKIAEeagvDVFLSNHPFQDGSLEKREAlrnRKPGEPNPFVD 231

                       250       260
                ....*....|....*....|
gi 13423630 261 PTELARFVDASEAAFNKELA 280
Cdd:cd16280 232 GQAWVDFYDEVLALCARVLA 251
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 28-284 4.84e-49

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: 163.14  E-value: 4.84e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  28 WTKPTKPYRVVGNIYYVGTEGISSWLITSSEGHVVLDGGpNAETGKLVERNITALGFQLADVKILINTHAHYDHAGGLAQ 107
Cdd:cd16314   1 WDDPAPPRRIYGNTWYVGTCGISALLVTSDAGHILIDGG-TDKAAPLIEANIRALGFRPEDVRYIVSSHEHFDHAGGIAR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 108 LKADTGAKLWISRDDAPAMTAGHHIGDN--IYGPTPMPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWTTAVVE 185
Cdd:cd16314  80 LQRATGAPVVAREPAATTLERGRSDRSDpqFLVVEKFPPVASVQRIGDGEVLRVGPLALTAHATPGHTPGGTSWTWRSCE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 186 KGRPLTVTFPCSLSVAGNVLVGNKTHRTIVADYRASFAKLRAIPTDVMLPAHEEQGNLLAkrqkqlRGDPNA---FVDPT 262
Cdd:cd16314 160 GAVCRDMVYADSVTAISDDIYRYSDHPGMVAAFRNTLDTVAALPCDILVTPHPSASGLWE------RLGPAAgipLADTG 233

                       250       260
                ....*....|....*....|..
gi 13423630 263 ELARFVDASEAAFNKELARQQA 284
Cdd:cd16314 234 ACRAYAQTGRARLDARLADEAA 255
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 28-242 3.89e-48

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: 160.37  E-value: 3.89e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  28 WTKPTKPYRVVGNIYYVGTEGISSWLITSSEGHVVLDGG-PNAETGKLveRNITALGFQLADVKILINTHAHYDHAGGLA 106
Cdd:cd16289   1 WLQPMAPLQIADHTWYIGTESLTALLVKTPDGAVLLDGGmPQAADMLL--DNMRALGVAPGDLKLILHSHAHADHAGPLA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 107 QLKADTGAKLWISRDDAPAMTAGH----HIGDNIYgptpMPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWTTA 182
Cdd:cd16289  79 ALKRATGARVAANAESAVLLARGGsddiHFGDGIT----FPPVQADRIVMDGEVVTLGGVTFTAHFTPGHTPGSTSWTWT 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 183 VVEKGRPLTVTFPCSLSVAGNVLVGNKTHRTIVADYRASFAKLRAIPTDVMLPAHEEQGN 242
Cdd:cd16289 155 DTRDGKPVRIAYADSLSAPGYQLLGNPRYPRIVEDYRRTFATVRALPCDVLLTPHPGASG 214
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 35-239 9.06e-31

Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];


Pssm-ID: 440257 [Multi-domain]  Cd Length: 215  Bit Score: 114.40  E-value: 9.06e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  35 YRVVGNIYYVGTeGISSWLITSSEGHVVLDGGPNAETGKLVERNITALGfqlADVKILINTHAHYDHAGGLAQLKADTGA 114
Cdd:COG0491   2 YVLPGGTPGAGL-GVNSYLIVGGDGAVLIDTGLGPADAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFGA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 115 KLWISRDDAPAMTAGHHIGDniygpTPMPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWttaVVEKGRPLtvtf 194
Cdd:COG0491  78 PVYAHAAEAEALEAPAAGAL-----FGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSF---YVPDEKVL---- 145

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 13423630 195 pcslsVAGNVLVGNKTHRTI-----VADYRASFAKLRAIPTDVMLPAHEE 239
Cdd:COG0491 146 -----FTGDALFSGGVGRPDlpdgdLAQWLASLERLLALPPDLVIPGHGP 190
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 50-237 4.13e-23

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: 93.39  E-value: 4.13e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630     50 SSWLITSSEGHVVLDGGPNAETGKLVErnITALGfqLADVKILINTHAHYDHAGGLAQLKADTGAKLWISRDDAPAMTAG 129
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAEDLLAE--LKKLG--PKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630    130 HHIGDNIYGPTPMPavKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWttaVVEKGRpltVTFP-CSLSVAGNVLVGN 208
Cdd:smart00849  77 LALLGELGAEAEPA--PPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVL---YLPEGK---ILFTgDLLFAGGDGRTLV 148

                          170       180
                   ....*....|....*....|....*....
gi 13423630    209 KTHRTIVADYRASFAKLRAIPTDVMLPAH 237
Cdd:smart00849 149 DGGDAAASDALESLLKLLKLLPKLVVPGH 177
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 40-237 6.14e-23

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: 93.44  E-value: 6.14e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  40 NIYYV-GTEGISSWLITSSEGHVVLDGGPnAETGKLVERNITALGFQLADVK-ILInTHAHYDHAGGLAQLKADTGAKLW 117
Cdd:cd07721   1 GVYQLpLLPPVNAYLIEDDDGLTLIDTGL-PGSAKRILKALRELGLSPKDIRrILL-THGHIDHIGSLAALKEAPGAPVY 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 118 ISRDDAPAMTAGH--------HIGDNIYGPTPMPAVKPDRSFGDQTKLKLGEIAMVAHlTPGHTIGCTSwttAVVEKGRP 189
Cdd:cd07721  79 AHEREAPYLEGEKpypppvrlGLLGLLSPLLPVKPVPVDRTLEDGDTLDLAGGLRVIH-TPGHTPGHIS---LYLEEDGV 154

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13423630 190 LtvtfpcslsVAGNVLVGNKTHRTIVADY--------RASFAKLRAIPTDVMLPAH 237
Cdd:cd07721 155 L---------IAGDALVTVGGELVPPPPPftwdmeeaLESLRKLAELDPEVLAPGH 201
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
44-237 9.82e-23

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 92.82  E-value: 9.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630    44 VGTEGISSWLITSSEGHVVLDGGPNAETGKLVErnITALGFQLADVKILINTHAHYDHAGGLAQLKADTGAKLWISRDDA 123
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLLL--LAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630   124 PAMTAGHHIGDNIYGPTPMPAVKPDRSFGDQTKLKLGEIAMV---AHLTPGHTIGCTSwttaVVEKGRPL-----TVTFP 195
Cdd:pfam00753  79 RELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLgllVTHGPGHGPGHVV----VYYGGGKVlftgdLLFAG 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 13423630   196 CSLSVAGNVLVGNKTHRTIVADYRASFAKLRAIPTDVMLPAH 237
Cdd:pfam00753 155 EIGRLDLPLGGLLVLHPSSAESSLESLLKLAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 51-178 2.61e-22

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: 91.58  E-value: 2.61e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  51 SWLITSSEGHVVL-DGGPNAetgklVERNITALGFQLADVKILINTHAHYDHAGGLAQLKADTGAKLWISRDDAPAMTAG 129
Cdd:cd06262  12 CYLVSDEEGEAILiDPGAGA-----LEKILEAIEELGLKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAELLEDP 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 13423630 130 hHIGDNIYGPTPMPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTS 178
Cdd:cd06262  87 -ELNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVC 134
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 49-238 1.78e-16

quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl Homoserine Lactones (also known as AHLs) are signal molecules which coordinate gene expression in quorum sensing, in many Gram-negative bacteria. Quorum-quenching N-acyl-homoserine lactonase (also known as AHL lactonase, N-acyl-L-homoserine lactone hydrolase, EC 3.1.1.81) catalyzes the hydrolysis and opening of the homoserine lactone rings of AHLs, a reaction that can block quorum sensing. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293815 [Multi-domain]  Cd Length: 238  Bit Score: 76.87  E-value: 1.78e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  49 ISSWLITSSEGHVVLDGGPNAET-----------------GKLVERNITALGFQLADVKILINTHAHYDHAGGLAQLKad 111
Cdd:cd07729  32 VYAYLIEHPEGTILVDTGFHPDAaddpgglelafppgvteEQTLEEQLARLGLDPEDIDYVILSHLHFDHAGGLDLFP-- 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 112 tGAKLWISRDD-----APAMTAGHHIGDNIYGPTPMPAVKPDRSFGDQtklklgEIA--MVAHLTPGHTIGCTS------ 178
Cdd:cd07729 110 -NATIIVQRAEleyatGPDPLAAGYYEDVLALDDDLPGGRVRLVDGDY------DLFpgVTLIPTPGHTPGHQSvlvrlp 182

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13423630 179 -----------WTTAVVEKGRPLTVTfpcslsvagnvlvgnkthrTIVADYRASFAKLRAI---PTDVMLPAHE 238
Cdd:cd07729 183 egtvllagdaaYTYENLEEGRPPGIN-------------------YDPEAALASLERLKALaerEGARVIPGHD 237
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 52-175 3.68e-14

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: 69.69  E-value: 3.68e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  52 WLITSSEGH--VVLDggPNAETGKLVERnitaLGFQLADVKILINTHAHYDHAGGLAQLKADTGAKLWISRDDAPAMTAG 129
Cdd:cd16322  14 YLVADEGGGeaVLVD--PGDESEKLLAR----FGTTGLTLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDLPLYEAA 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 13423630 130 HHiGDNIYGPTPMPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIG 175
Cdd:cd16322  88 DL-GAKAFGLGIEPLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPG 132
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 77-178 1.57e-12

Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; Bacillus amyloliquefaciens BaeB may play a role in the synthesis of the antibiotic polyketide bacillaene. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293833 [Multi-domain]  Cd Length: 174  Bit Score: 64.48  E-value: 1.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  77 RNITALGFQLadVKILInTHAHYDHAGGLAQLKADTGAKLWISRDDAPamtaghhigdnIYGPTPmpavkPD-RSFGDQT 155
Cdd:cd16275  39 AKLNELGLTL--TGILL-THSHFDHVNLVEPLLAKYDAPVYMSKEEID-----------YYGFRC-----PNlIPLEDGD 99

                        90       100
                ....*....|....*....|...
gi 13423630 156 KLKLGEIAMVAHLTPGHTIGCTS 178
Cdd:cd16275 100 TIKIGDTEITCLLTPGHTPGSMC 122
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 47-237 3.16e-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: 63.66  E-value: 3.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  47 EGISSWLITSSEGHVVLDGGPNAET------GKLVERNITAlgfqladvkILInTHAHYDHAGGLAQLKADTGaklwisr 120
Cdd:cd16278  16 DGTNTYLLGAPDGVVVIDPGPDDPAhldallAALGGGRVSA---------ILV-THTHRDHSPGAARLAERTG------- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 121 ddAPAMTAGHHIGDNIygptpMPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWttAVVEKGRPLTvtfpcslsv 200
Cdd:cd16278  79 --APVRAFGPHRAGGQ-----DTDFAPDRPLADGEVIEGGGLRLTVLHTPGHTSDHLCF--ALEDEGALFT--------- 140

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 13423630 201 aGNVLVGNKThrTIVA-------DYRASFAKLRAIPTDVMLPAH 237
Cdd:cd16278 141 -GDHVMGWST--TVIAppdgdlgDYLASLERLLALDDRLLLPGH 181
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 53-237 4.19e-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) 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: 63.70  E-value: 4.19e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  53 LITSSEGHVVL-DGGPNAETGKLVERNITALGFQLadvKILINTHAHYDHAGGLAQLKADTGAKLWISRDDAPAMtaghh 131
Cdd:cd07743  12 VYVFGDKEALLiDSGLDEDAGRKIRKILEELGWKL---KAIINTHSHADHIGGNAYLQKKTGCKVYAPKIEKAFI----- 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 132 igDN-------IYGPTPMPAVKPDRSFG---------DQTKLKLGEIAMVAHLTPGHT---IGctswttAVVEKGrpltV 192
Cdd:cd07743  84 --ENpllepsyLGGAYPPKELRNKFLMAkpskvddiiEEGELELGGVGLEIIPLPGHSfgqIG------ILTPDG----V 151

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 13423630 193 TFpcslsvAGNVLVG----NKTHrtI-----VADYRASFAKLRAIPTDVMLPAH 237
Cdd:cd07743 152 LF------AGDALFGeevlEKYG--IpflydVEEQLETLEKLEELDADYYVPGH 197
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 79-179 3.99e-11

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


Pssm-ID: 293810 [Multi-domain]  Cd Length: 177  Bit Score: 60.49  E-value: 3.99e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  79 ITALGFQLADVkilINTHAHYDHAGGLAQLKADTGAKLWISRDDapamtaghhigdniygptpmPAVKPDRSFGDQTKLK 158
Cdd:cd07724  42 AAELGLKITYV---LETHVHADHVSGARELAERTGAPIVIGEGA--------------------PASFFDRLLKDGDVLE 98

                        90       100
                ....*....|....*....|.
gi 13423630 159 LGEIAMVAHLTPGHTIGCTSW 179
Cdd:cd07724  99 LGNLTLEVLHTPGHTPESVSY 119
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 53-237 5.34e-11

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 60.66  E-value: 5.34e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  53 LITSSEGHVVLDGGPNAETGKLVERNITALGFQLadVKILINTHAHYDHAGGLAQLkADTGAKLW--------ISRDDAP 124
Cdd:cd16282  19 FIVGDDGVVVIDTGASPRLARALLAAIRKVTDKP--VRYVVNTHYHGDHTLGNAAF-ADAGAPIIahentreeLAARGEA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 125 AMTAGHHIGDNIYGPTpmPAVKPDRSFGDQTKLKLGEIAMVA-HLTPGHTIGCtswTTAVVEKGRpltVTFpcslsvAGN 203
Cdd:cd16282  96 YLELMRRLGGDAMAGT--ELVLPDRTFDDGLTLDLGGRTVELiHLGPAHTPGD---LVVWLPEEG---VLF------AGD 161

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 13423630 204 vLVGNKTHRTI----VADYRASFAKLRAIPTDVMLPAH 237
Cdd:cd16282 162 -LVFNGRIPFLpdgsLAGWIAALDRLLALDATVVVPGH 198
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 42-172 3.48e-10

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: 58.66  E-value: 3.48e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  42 YYVGTEG-ISSWLITSSEGHVVLDGGPNAETGKLVERnITALGFQLADVKILINTHAHYDHAGGLAQL-KADTGAKLWIS 119
Cdd:cd07726   8 GFLGFPGrIASYLLDGEGRPALIDTGPSSSVPRLLAA-LEALGIAPEDVDYIILTHIHLDHAGGAGLLaEALPNAKVYVH 86

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13423630 120 RDDAPAMT--------AGHHIGDNI--YGPTPMPaVKPDR--SFGDQTKLKLGEIAMVAHLTPGH 172
Cdd:cd07726  87 PRGARHLIdpsklwasARAVYGDEAdrLGGEILP-VPEERviVLEDGETLDLGGRTLEVIDTPGH 150
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 38-237 4.47e-10

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: 57.69  E-value: 4.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  38 VGNIYYVGTegISSWLITSSEGHVVLDGG-PNAETGKLVERNITALGFQLADVKILINTHAHYDHAGGLAQLKADTGAKL 116
Cdd:cd07725   6 LPLPGPLGH--VNVYLLRDGDETTLIDTGlATEEDAEALWEGLKELGLKPSDIDRVLLTHHHPDHIGLAGKLQEKSGATV 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 117 WISrddapamtaghhigdniygptpmpavkPDRSFGDQTKLKLGEIAMVAHLTPGHTIGCTSWttaVVEKGRPLtvtfpc 196
Cdd:cd07725  84 YIL---------------------------DVTPVKDGDKIDLGGLRLKVIETPGHTPGHIVL---YDEDRREL------ 127

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 13423630 197 slsVAGNVLVGNKT-----HRTIV----ADYRASFAKLRAIPTDVMLPAH 237
Cdd:cd07725 128 ---FVGDAVLPKITpnvslWAVRVedplGAYLESLDKLEKLDVDLAYPGH 174
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 61-175 9.52e-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: 56.79  E-value: 9.52e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  61 VVLDggPNAETGKLVERnITALGFQLadVKILInTHAHYDHAGGLAQLKADTGAKLWisrddapamtaGHHIGDN----- 135
Cdd:cd07737  25 AVID--PGGDADKILQA-IEDLGLTL--KKILL-THGHLDHVGGAAELAEHYGVPII-----------GPHKEDKfllen 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 13423630 136 ------IYGPTPMPAVKPDRSFGDQTKLKLGEIAM-VAHlTPGHTIG 175
Cdd:cd07737  88 lpeqsqMFGFPPAEAFTPDRWLEEGDTVTVGNLTLeVLH-CPGHTPG 133
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 73-175 1.10e-09

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: 56.31  E-value: 1.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  73 KLVERNITALGFQLADVkilINTHAHYDHAGGLAQLKADTGaklwisrdDAPamtaghhigdnIYGPTPMPAVKPDRSFG 152
Cdd:cd07723  31 EPVLAALEKNGLTLTAI---LTTHHHWDHTGGNAELKALFP--------DAP-----------VYGPAEDRIPGLDHPVK 88

                        90       100
                ....*....|....*....|...
gi 13423630 153 DQTKLKLGEIAMVAHLTPGHTIG 175
Cdd:cd07723  89 DGDEIKLGGLEVKVLHTPGHTLG 111
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 42-237 4.20e-09

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: 54.94  E-value: 4.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  42 YYVGTEGISSWLITSSEGHVVLDGG-PNAETGKLVeRNITALGFqladvkILINTHAHYDHAGGLAQLkadtgAKLWISR 120
Cdd:cd07712   2 FIEEDDRVNIYLLRGRDRALLIDTGlGIGDLKEYV-RTLTDLPL------LVVATHGHFDHIGGLHEF-----EEVYVHP 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 121 DDAPAMTAG--HHIGDNIYGPTPMPAVKPDRSFGDQTKLKLGEIAM-VAHlTPGHTIGCtswtTAVVEKGRPLTVTfpcs 197
Cdd:cd07712  70 ADAEILAAPdnFETLTWDAATYSVPPAGPTLPLRDGDVIDLGDRQLeVIH-TPGHTPGS----IALLDRANRLLFS---- 140

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 13423630 198 lsvaGNV-----LVGNKTHRTiVADYRASFAKLRAIPT--DVMLPAH 237
Cdd:cd07712 141 ----GDVvydgpLIMDLPHSD-LDDYLASLEKLSKLPDefDKVLPGH 182
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 51-121 2.84e-08

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: 53.78  E-value: 2.84e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13423630  51 SWLITSSEGHVVLDGGPNAetgkLVERNITALGFQLADVKILINTHAHYDHAGGLAQ-LKADTGAKLWISRD 121
Cdd:cd07713  22 SLLIETEGKKILFDTGQSG----VLLHNAKKLGIDLSDIDAVVLSHGHYDHTGGLKAlLELNPKAPVYAHPD 89
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
51-121 3.90e-08

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 53.35  E-value: 3.90e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13423630  51 SWLITSSEGHVVLDGGpnaeTGKLVERNITALGFQLADVKILINTHAHYDHAGGLAQ-LKADTGAKLWISRD 121
Cdd:COG1237  24 SALIETEGKRILFDTG----QSDVLLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLPAlLELNPKAPVYAHPD 91
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 77-175 1.97e-06

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


Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 48.00  E-value: 1.97e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  77 RNITALGFQLADVKILINTHAHYDHAGGLA------------QLKADTGAKLWISRDDAPAMTAGHHI--------GDNI 136
Cdd:cd07742  69 RQIEALGFDPSDVRHIVLTHLDLDHAGGLAdfphatvhvhaaELDAATSPRTRYERRRYRPQQLAHGPwwvtyaagGERW 148

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 13423630 137 YGptpMPAVKPDRSFGDqtklklgEIAMVaHLtPGHTIG 175
Cdd:cd07742 149 FG---FEAVRPLDGLPP-------EILLV-PL-PGHTRG 175
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 71-175 3.50e-06

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: 47.16  E-value: 3.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  71 TGKLVErNITALGFQLADVKILINTHAHYDHAGGLaqLKADTG-----AKLWISR-------DDAPAMTAGHHIGDNIYG 138
Cdd:cd07720  75 AGKLLA-NLAAAGIDPEDIDDVLLTHLHPDHIGGL--VDAGGKpvfpnAEVHVSEaewdfwlDDANAAKAPEGAKRFFDA 151

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 13423630 139 ptPMPAVKPdrsFGDQTKLKLG-EIA--MVAHLTPGHTIG 175
Cdd:cd07720 152 --ARDRLRP---YAAAGRFEDGdEVLpgITAVPAPGHTPG 186
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 79-179 1.94e-05

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 45.22  E-value: 1.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630   79 ITALGFQLADVKILINTHAHYDHAGGLAQLKADTGAKLwisrddapamtaghhIGdniygptpmPAVKPDRSFGDQTKLK 158
Cdd:PLN02398 112 IDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKV---------------IG---------SAVDKDRIPGIDIVLK 167

                         90       100
                 ....*....|....*....|....*..
gi 13423630  159 LGEIAMVA-HL-----TPGHTIGCTSW 179
Cdd:PLN02398 168 DGDKWMFAgHEvlvmeTPGHTRGHISF 194
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 73-181 2.64e-05

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 44.79  E-value: 2.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630   73 KLVERN---ITALGFQLadvKILINTHAHYDHAGGLAQLKADT-GAKLWISRddAPAMTAGHHI--GDNIYgptpmpavk 146
Cdd:PLN02962  46 KTVDRDlslVKELGLKL---IYAMNTHVHADHVTGTGLLKTKLpGVKSIISK--ASGSKADLFVepGDKIY--------- 111

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 13423630  147 pdrsFGDqtklklgeIAMVAHLTPGHTIGCTSWTT 181
Cdd:PLN02962 112 ----FGD--------LYLEVRATPGHTAGCVTYVT 134
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 53-127 4.03e-05

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


Pssm-ID: 293817 [Multi-domain]  Cd Length: 179  Bit Score: 43.28  E-value: 4.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  53 LITSsEGHVVL-DGGPNAETGKLV------ERNITALgfqlaDVkiLINTHAHYDHAGGLAQ-LKADTGAKLWISRDDAP 124
Cdd:cd07731  14 LIQT-PGKTILiDTGPRDSFGEDVvvpylkARGIKKL-----DY--LILTHPDADHIGGLDAvLKNFPVKEVYMPGVTHT 85


                ...
gi 13423630 125 AMT 127
Cdd:cd07731  86 TKT 88
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 53-124 5.89e-05

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


Pssm-ID: 441904 [Multi-domain]  Cd Length: 253  Bit Score: 43.69  E-value: 5.89e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13423630  53 LITSSEGHVVL-DGGPNAET---GKLVERNITALGfqLADVKILINTHAHYDHAGGLAQ-LKADTGAKLWISRDDAP 124
Cdd:COG2333  15 LIRTPDGKTILiDTGPRPSFdagERVVLPYLRALG--IRRLDLLVLTHPDADHIGGLAAvLEAFPVGRVLVSGPPDT 89
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 38-178 1.53e-04

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 42.12  E-value: 1.53e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  38 VGN--IYYVgTEGISSWLITSsEGHVVL-DGG-------------PNAETGKLveRNITALGFQLADVKILINTHAHYDH 101
Cdd:cd16277   1 VGDvtITRI-VELIHSWLVRT-PGRTILvDTGigndkprpgppafHNLNTPYL--ERLAAAGVRPEDVDYVLCTHLHVDH 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 102 AGGLAQLKADT------GAKLWISRDDAPAMTAGHHIGDNiygptpmpavkPDRSFGDQT-------KLKL----GEIA- 163
Cdd:cd16277  77 VGWNTRLVDGRwvptfpNARYLFSRAEYDHWSSPDAGGPP-----------NRGVFEDSVlpvieagLADLvdddHEILd 145

                       170
                ....*....|....*.
gi 13423630 164 -MVAHLTPGHTIGCTS 178
Cdd:cd16277 146 gIRLEPTPGHTPGHVS 161
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 75-120 3.80e-04

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: 41.09  E-value: 3.80e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 13423630  75 VERNITALGFQLADVKILINTHAHYDHAGGLAQLKADT------GAKLWISR 120
Cdd:cd07728  82 IEESLAELGLTPEDIDYVLMTHLHFDHASGLTKVKGEQlvsvfpNATIYVSE 133
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 53-178 4.45e-04

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: 40.26  E-value: 4.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  53 LITSSEGHVVLD-GGPNAETG---KLVERNITAlgfqlADVKILINTHAHYDHAGGLAQLKadtgaklwisrdDAPamta 128
Cdd:cd07711  26 LIKDGGKNILVDtGTPWDRDLllkALAEHGLSP-----EDIDYVVLTHGHPDHIGNLNLFP------------NAT---- 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 13423630 129 gHHIGDNIYGPTpmpaVKPDRSFGDQTKLKLGEIAMVAhlTPGHTIGCTS 178
Cdd:cd07711  85 -VIVGWDICGDS----YDDHSLEEGDGYEIDENVEVIP--TPGHTPEDVS 127
CphA_ImiS-like_MBL-B2 cd16306
Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and related metallo-beta-lactamases, ...
 92-251 7.07e-04

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


Pssm-ID: 293864  Cd Length: 222  Bit Score: 39.93  E-value: 7.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  92 LINTHAHYDHAGGLAQLKAdTGAKLWISRDDAPAMTAGHhigDNIYGPT--------PMPAVKPDRSFGDQTKLKLGEIA 163
Cdd:cd16306  62 VINTNYHTDRAGGNAYWKS-IGAKVVSTRQTRDLMKSDW---AEIVAFTrkglpeypDLPLVLPNVVHDGDFTLQEGKVR 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 164 MVaHLTPGHTigctswttavvEKGrpLTVTFPCSLSVAGNVLVGNK---THRTIVADYRASFAKLRA--IPTDVMLPAHE 238
Cdd:cd16306 138 AF-YLGPAHT-----------PDG--IFVYFPDEQVLYGNCILKEKlgnLSFADVKAYPQTLERLKAmkLPIKTVIGGHD 203

                       170
                ....*....|....*
gi 13423630 239 --EQGNLLAKRQKQL 251
Cdd:cd16306 204 spLHGPELIDHYEAL 218
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 40-177 9.28e-04

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: 39.49  E-value: 9.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  40 NIYYVGTE-----GISSWLITSSEGHVVLDGgPNAEtgKLVERNITALGfqlaDVKILINTHAHY--DHAgglaQLKADT 112
Cdd:cd07727   1 GVYYCGFHseksfGAASYLILRPEGNILVDS-PRYS--PPLAKRIEALG----GIRYIFLTHRDDvaDHA----KWAERF 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13423630 113 GAKLWISRDDAPAMTAGHHIGdnIYGPTPMPAVKPDrsfgdqtklklgeiaMVAHLTPGHTIGCT 177
Cdd:cd07727  70 GAKRIIHEDDVNAVTRPDEVI--VLWGGDPWELDPD---------------LTLIPVPGHTRGSV 117
metallo-hydrolase-like_MBL-fold cd16281
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 76-120 1.08e-03

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


Pssm-ID: 293839  Cd Length: 252  Bit Score: 39.79  E-value: 1.08e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 13423630  76 ERNITALGFQLADVKILINTHAHYDHAGGLAQLKADTG-------AKLWISR 120
Cdd:cd16281  82 LKSLARLGLSPEDITDVILTHLHFDHCGGATRADDDGLvellfpnATYWVQK 133
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 40-173 1.38e-03

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: 39.05  E-value: 1.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  40 NIYYVGTeGISSWLITSSEGHV--------VLDGGPNAEtgklvernITalgfqladvKILInTHAHYDHAGGLAQLKA- 110
Cdd:cd07722  19 NTYLVGT-GKRRILIDTGEGRPsyipllksVLDSEGNAT--------IS---------DILL-THWHHDHVGGLPDVLDl 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13423630 111 --DTGAKLW---ISRDDAPAMTAGHHIgdniygptpmpavkpdRSFGDQTKLKLGEIAMVAHLTPGHT 173
Cdd:cd07722  80 lrGPSPRVYkfpRPEEDEDPDEDGGDI----------------HDLQDGQVFKVEGATLRVIHTPGHT 131
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 50-105 1.46e-03

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: 38.98  E-value: 1.46e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13423630  50 SSWLITSSEGHVVLDGGPNAETGKLVERNITALGFQLADVKILINTHAHYDHAGGL 105
Cdd:cd16295  13 SCYLLETGGKRILLDCGLFQGGKELEELNNEPFPFDPKEIDAVILTHAHLDHSGRL 68
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 40-160 1.74e-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: 38.72  E-value: 1.74e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  40 NIYYVGTEGISSWLITSSEGHVVLDGGPNAETGKLVE-RNITALgfqlaDVKILINTHAHYDHAGGlAQLKADTGAKLWI 118
Cdd:cd16276   1 GVYWVTDGGYQSMFLVTDKGVIVVDAPPSLGENLLAAiRKVTDK-----PVTHVVYSHNHADHIGG-ASIFKDEGATIIA 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 13423630 119 SRDDAPAMTAGHHIGdniygpTPMpavkPDRSFGDQTKLKLG 160
Cdd:cd16276  75 HEATAELLKRNPDPK------RPV----PTVTFDDEYTLEVG 106
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 45-105 2.35e-03

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 39.01  E-value: 2.35e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13423630  45 GTEGISSWLITSSEGHVVLDGGPNAetgKLVERNITALGFQLADVKILINTHAHYDHAGGL 105
Cdd:COG1236  10 GEVTGSCYLLETGGTRILIDCGLFQ---GGKERNWPPFPFRPSDVDAVVLTHAHLDHSGAL 67
PRK10241 PRK10241
hydroxyacylglutathione hydrolase; Provisional
 52-175 4.60e-03

hydroxyacylglutathione hydrolase; Provisional


Pssm-ID: 182327 [Multi-domain]  Cd Length: 251  Bit Score: 37.88  E-value: 4.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630   52 WLITSSEGH-VVLDGGPNAETGKLVERNitalgfQLADVKILInTHAHYDHAGGLAQLKADTgaklwisrddaPAMTagh 130
Cdd:PRK10241  15 WVLNDEAGRcLIVDPGEAEPVLNAIAEN------NWQPEAIFL-THHHHDHVGGVKELVEKF-----------PQIV--- 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 13423630  131 higdnIYGPTPMPAVKPDRSFGDQTKLKLGEIAMVAHLTPGHTIG 175
Cdd:PRK10241  74 -----VYGPQETQDKGTTQVVKDGETAFVLGHEFSVFATPGHTLG 113
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 89-243 6.85e-03

metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. B1 MBls include chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1. B2 MBLs have a narrow substrate profile that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis. B2 MBLs include Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I.


Pssm-ID: 293793 [Multi-domain]  Cd Length: 219  Bit Score: 37.14  E-value: 6.85e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630  89 VKILINTHAHYDHAGGLAQLKAdTGAKLWISR-------DDAPAMTAGHHIGDNIYgpTPMPAVKPDRSFGDQTKLKLGE 161
Cdd:cd07707  59 VTEVINTHFHTDRAGGNAYLKE-RGAKTVSTAltrdlakSEWAEIVAFTRKGLPEY--PDLGYELPDGVLDGDFNLQFGK 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13423630 162 IAmVAHLTPGHTigctswTTAVVekgrpltVTFPcslsvAGNVLVGNKTHRTIVADYrASFAKLRAIPT----------- 230
Cdd:cd07707 136 VE-AFYPGPAHT------PDNIV-------VYFP-----QENVLYGGCIIKETDLGN-VADADVKEWPTsierlkkryrn 195

                       170
                ....*....|....
gi 13423630 231 -DVMLPAHEEQGNL 243
Cdd:cd07707 196 iKAVIPGHGEVGGP 209
 
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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