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Conserved domains on  [gi|1949903414|ref|WP_198669305|]
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subclass B3 metallo-beta-lactamase [Blastomonas sp. UPD001]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-299 1.13e-165

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: 460.41  E-value: 1.13e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  49 WNERMAPFTILGNVHYVGTAGIGVFLITTLEGHVLIDGALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGL 128
Cdd:cd16309     1 WNEPMEPFKLIGNIYYVGTAGLGVFLITTPEGHILIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 129 QRASGAKVIASAADKPYLEAGHVDHGPTKDALFPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTAKDSTGM 208
Cdd:cd16309    81 KKATGAQLVASAADKPLLESGYVGSGDTKNLQFPPVRVDRVIGDGDKVTLGGTTLTAHLTPGHSPGCTSWTTTVKDTAGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 209 PRKVFLHCSASLGG-QSLVPPAYPGMADNYRASFAKVRAMQADVFLANHDMFFGLHEKRARQLAGEKDAFVDPGELQRFN 287
Cdd:cd16309   161 PREVLFFCSATVAGnQLVGPPTYPGIVDDYRATFAKARAMKADVFLANHPEFFGLVAKRARQSAGEPDAFVDAGELQRFN 240

                         250
                  ....*....|..
gi 1949903414 288 ARMEAAFVKTLA 299
Cdd:cd16309   241 TKMEDDFEKALA 252
 
Name Accession Description Interval E-value
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-299 1.13e-165

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: 460.41  E-value: 1.13e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  49 WNERMAPFTILGNVHYVGTAGIGVFLITTLEGHVLIDGALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGL 128
Cdd:cd16309     1 WNEPMEPFKLIGNIYYVGTAGLGVFLITTPEGHILIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 129 QRASGAKVIASAADKPYLEAGHVDHGPTKDALFPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTAKDSTGM 208
Cdd:cd16309    81 KKATGAQLVASAADKPLLESGYVGSGDTKNLQFPPVRVDRVIGDGDKVTLGGTTLTAHLTPGHSPGCTSWTTTVKDTAGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 209 PRKVFLHCSASLGG-QSLVPPAYPGMADNYRASFAKVRAMQADVFLANHDMFFGLHEKRARQLAGEKDAFVDPGELQRFN 287
Cdd:cd16309   161 PREVLFFCSATVAGnQLVGPPTYPGIVDDYRATFAKARAMKADVFLANHPEFFGLVAKRARQSAGEPDAFVDAGELQRFN 240

                         250
                  ....*....|..
gi 1949903414 288 ARMEAAFVKTLA 299
Cdd:cd16309   241 TKMEDDFEKALA 252
B3_Acin_new1 NF033184
putative subclass B3 metallo-beta-lactamase; This is one of two families of putative ...
 49-303 1.66e-54

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: 179.15  E-value: 1.66e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  49 WNERMAPFTILGNVHYVGTAGIGVFLITTLEGHVLIDGALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGL 128
Cdd:NF033184   28 WTQNTQPFQITENIYYVGTHGLAAYLLASGHQALLIDTGLPENTEQIEQNIKQLGFKLSDVKIMVTSHAHWDHVGALARI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 129 QRASGAKVIASAADKPYLEAGH-VDHGPTKDALFPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTAKdSTG 207
Cdd:NF033184  108 KQDTGAKLIAMQQDVKALEIGKpIGENTFQTIPFTPVKVDKVIHDGEVVKLGKFKLKATLTPGHTPGCTTWSTEVK-SNG 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 208 MPRKVFLHCSASLGGQSLVPP-AYPGMADNYRASFAKVRAMQADVFLANHDMFFGLHEKRARQLAGEKDAFVDPGELQRF 286
Cdd:NF033184  187 KNLNVVFPCSLSVAGNVLQNNhQYPNIVADYRKSFERLKNMKADIVLTSHPEVADVLGNKARKDAGQTNAFIQPEKLSSI 266

                         250
                  ....*....|....*..
gi 1949903414 287 NARMEAAFVKTLADEQA 303
Cdd:NF033184  267 VKDAEMAFEKSLVSSHP 283
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 72-257 6.84e-33

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: 120.57  E-value: 6.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  72 VFLITTLEGHVLID-GALAQSVPQILDNIRTLGfepKDVKYILNTHGHFDHAAGLAGLQRASGAKVIASAADKPYLEAGH 150
Cdd:COG0491    17 SYLIVGGDGAVLIDtGLGPADAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEAPA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 151 vdhgPTKDALFPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLtakdstgmPRKVFLHCS-ASLGGQSLVPPA 229
Cdd:COG0491    94 ----AGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV--------PDEKVLFTGdALFSGGVGRPDL 161

                         170       180
                  ....*....|....*....|....*...
gi 1949903414 230 YPGMADNYRASFAKVRAMQADVFLANHD 257
Cdd:COG0491   162 PDGDLAQWLASLERLLALPPDLVIPGHG 189
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 72-256 3.41e-31

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 114.96  E-value: 3.41e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414   72 VFLITTLEGHVLIDgALAQSVPQILDNIRTLGfePKDVKYILNTHGHFDHAAGLAGLQRASGAKVIASAADKPYLEAGHV 151
Cdd:smart00849   2 SYLVRDDGGAILID-TGPGEAEDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  152 DHGPTKDaLFPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWsltakdstGMPRKVFLHC---SASLGGQSLVPP 228
Cdd:smart00849  79 LLGELGA-EAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVL--------YLPEGKILFTgdlLFAGGDGRTLVD 149

                          170       180
                   ....*....|....*....|....*...
gi 1949903414  229 AYPGMADNYRASFAKVRAMQADVFLANH 256
Cdd:smart00849 150 GGDAAASDALESLLKLLKLLPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
72-195 8.90e-20

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 85.50  E-value: 8.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  72 VFLITTLEGHVLIDGALAQSVPQILDnIRTLGFEPKDVKYILNTHGHFDHAAGLAGLQRASGAKVIASAADKPYLEAGHV 151
Cdd:pfam00753   8 SYLIEGGGGAVLIDTGGSAEAALLLL-LAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEEL 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1949903414 152 D----HGPTKDALFPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGC 195
Cdd:pfam00753  87 GlaasRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGH 134
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 99-198 6.62e-10

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 59.09  E-value: 6.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  99 IRTLGFEPKDVKYILNTHGHFDHAAGLAGLQRASGAKVIASAADKpyleaghvDHGPTkdalfppvrVDRTVGDGDTITL 178
Cdd:PLN02398  112 IDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVDK--------DRIPG---------IDIVLKDGDKWMF 174

                          90       100
                  ....*....|....*....|
gi 1949903414 179 AGTTLTAHLTPGHSPGCTSW 198
Cdd:PLN02398  175 AGHEVLVMETPGHTRGHISF 194
 
Name Accession Description Interval E-value
BJP-1-like_MBL-B3 cd16309
Bradyrhizobium diazoefficiens BJP-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-299 1.13e-165

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: 460.41  E-value: 1.13e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  49 WNERMAPFTILGNVHYVGTAGIGVFLITTLEGHVLIDGALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGL 128
Cdd:cd16309     1 WNEPMEPFKLIGNIYYVGTAGLGVFLITTPEGHILIDGAMPQSTPLIKDNIKKLGFDVKDVKYLLNTHAHFDHAGGLAEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 129 QRASGAKVIASAADKPYLEAGHVDHGPTKDALFPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTAKDSTGM 208
Cdd:cd16309    81 KKATGAQLVASAADKPLLESGYVGSGDTKNLQFPPVRVDRVIGDGDKVTLGGTTLTAHLTPGHSPGCTSWTTTVKDTAGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 209 PRKVFLHCSASLGG-QSLVPPAYPGMADNYRASFAKVRAMQADVFLANHDMFFGLHEKRARQLAGEKDAFVDPGELQRFN 287
Cdd:cd16309   161 PREVLFFCSATVAGnQLVGPPTYPGIVDDYRATFAKARAMKADVFLANHPEFFGLVAKRARQSAGEPDAFVDAGELQRFN 240

                         250
                  ....*....|..
gi 1949903414 288 ARMEAAFVKTLA 299
Cdd:cd16309   241 TKMEDDFEKALA 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 ...
 49-299 3.88e-109

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: 317.34  E-value: 3.88e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  49 WNERMAPFTILGNVHYVGTAGIGVFLITTLEGHVLIDGALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGL 128
Cdd:cd16288     1 WNAPFEPFRIAGNVYYVGTSGLASYLITTPQGLILIDTGLESSAPMIKANIRKLGFKPSDIKILLNSHAHLDHAGGLAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 129 QRASGAKVIASAADKPYLEAG-HVDHGPTKDAL-FPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTAKDSt 206
Cdd:cd16288    81 KKLTGAKLMASAEDAALLASGgKSDFHYGDDSLaFPPVKVDRVLKDGDRVTLGGTTLTAHLTPGHTRGCTTWTMTVKDD- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 207 GMPRKVFLHCSAS-LGGQSLV-PPAYPGMADNYRASFAKVRAMQADVFLANHDMFFGLHEKRARQLAGEKDAFVDPGELQ 284
Cdd:cd16288   160 GKVYQVVFADSLTvNPGYKLVgNPTYPGIAEDYRHSFATLRALQCDIFLASHAEYFDLKEKRARLAAGQPNAFIDPEGYR 239

                         250
                  ....*....|....*
gi 1949903414 285 RFNARMEAAFVKTLA 299
Cdd:cd16288   240 NFIEKAKADFEKQLA 254
Mbl1b-like_MBL-B3 cd16310
Caulobacter crescentus Mbl1b and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-299 9.31e-101

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: 295.90  E-value: 9.31e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  49 WNERMAPFTILGNVHYVGTAGIGVFLITTLEGHVLIDGALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGL 128
Cdd:cd16310     1 WTAPTEPFRIVDNIYYVGTKGIGSYLITSNHGAILLDGGLEENAALIEQNIKALGFKLSDIKIIINTHAHYDHAGGLAQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 129 QRASGAKVIASAADKPYLEAG-HVDHGPTKDALFPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTAKDStG 207
Cdd:cd16310    81 KADTGAKLWASRGDRPALEAGkHIGDNITQPAPFPAVKVDRILGDGEKIKLGDITLTATLTPGHTKGCTTWSTTVKEN-G 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 208 MPRKVFLHCSASLGGQSLVP-PAYPGMADNYRASFAKVRAMQADVFLANHDMFFGLHEKRARQLAGEKDAFVDPGELQRF 286
Cdd:cd16310   160 RPLRVVFPCSLSVAGNVLVGnKTYPTIVEDYRASFARLRAMKADIVLTSHPEVADLLARKAKQDAGQANAFVDPGELARI 239

                         250
                  ....*....|...
gi 1949903414 287 NARMEAAFVKTLA 299
Cdd:cd16310   240 VDQSEAAFNKELA 252
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 49-283 2.64e-86

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: 259.01  E-value: 2.64e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  49 WNERMAPFTILGNVHYVGTAGIGVFLITTLEGHVLIDGALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGL 128
Cdd:cd07708     1 WPNPFPPFQIAGNTYYVGTDDLAAYLIVTPQGNILIDGDMEQNAPMIKANIKKLGFKFSDTKLILISHAHFDHAGGSAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 129 QRASGAKVIASAADKPYLEAGHVDHGP---TKDALFPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTAKDS 205
Cdd:cd07708    81 KKQTGAKVMAGAEDVSLLLSGGSSDFHyanDSSTYFPQSTVDRAVHDGERVTLGGTVLTAHATPGHTPGCTTWTMTLKDH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 206 tGMPRKVFLHCSASL-GGQSLVP-PAYPGMADNYRASFAKVRAMQADVFLANHDMFFGLHEKRARQLAGEKDAFVDPGEL 283
Cdd:cd07708   161 -GKQYQVVFADSLTVnPGYRLVDnPTYPKIVEDYRHSFAVVEAMRCDILLGPHPGVFDMKNKYVLLSKGQNNPFVDPGGC 239
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 ...
 49-298 1.96e-81

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: 246.88  E-value: 1.96e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  49 WNERMAPFTILGNVHYVGTAGIGVFLITTLEGHVLIDGALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGL 128
Cdd:cd16290     1 WNQPQAPFRIHGNTYYVGTGGLSAVLITSPQGLILIDGALPQSAPQIEANIRALGFRLEDVKLILNSHAHFDHAGGIAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 129 QRASGAKVIASAADKPYLEAGHVDHG-PTKDAL--FPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTAKDS 205
Cdd:cd16290    81 QRDSGATVAASPAGAAALRSGGVDPDdPQAGAAdpFPPVAKVRVVADGEVVKLGPLAVTAHATPGHTPGGTSWTWRSCEG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 206 TGMPRKVFlhcSASL-----GGQSLVPPAYPGMADNYRASFAKVRAMQADVFLANHDMFFGLHEKRARQLAG-EKDAFVD 279
Cdd:cd16290   161 GRCLDIVY---ADSLtavsaDGFRFSDDAHPARVAAFRRSIATVAALPCDILISAHPDASGLWEKLARRAREpGPNPFID 237

                         250
                  ....*....|....*....
gi 1949903414 280 PGELQRFNARMEAAFVKTL 298
Cdd:cd16290   238 PNACRAYAAAAEARLEARL 256
FEZ-1-like_MBL-B3 cd16307
Fluoribacter gormanii FEZ-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-299 4.77e-71

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: 220.39  E-value: 4.77e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  49 WNERMAPFTILGNVHYVGTAGIGVFLITTLEGHVLIDGALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGL 128
Cdd:cd16307     1 WTTPFPPFRIAGNLYYVGSRDLASYLITTPRGNILINSNLESSVPQIKASIEKLGFKFSDTKILLISHAHFDHAAGSALI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 129 QRASGAKVIASAADKPYLEAG---HVDHGPTKDALFPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTAKDS 205
Cdd:cd16307    81 KRETHAKYMVMDGDVDVVESGgksDFFYGNDPSTYFPPAHVDKVLHDGEQVELGGTVLTAHLTAGHTKGCTTWTMKVKDH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 206 TGMPRKVFLHCSASLGGQSLV-PPAYPGMADNYRASFAKVRAMQADVFLANHDMFFGLHEKRARQLAGEKDAFVDPGELQ 284
Cdd:cd16307   161 GKTYDVVIVGSPNVNPGAKLVnNITYPGIAEDYAHTFAVLRSLPCDIFLGAHGGYFDLKNKYVRLQKGGANPFIDPEGYK 240

                         250
                  ....*....|....*
gi 1949903414 285 RFNARMEAAFVKTLA 299
Cdd:cd16307   241 AYVAEKEQAFRTELE 255
EVM-1-like_MBL-B3 cd16315
Erythrobacter vulgaris EVM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-298 2.82e-67

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: 210.67  E-value: 2.82e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  49 WNERMAPFTILGNVHYVGTAGIGVFLITTLEGHVLIDGALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGL 128
Cdd:cd16315     1 WDKPAPPARIFGNTYYVGTCGISAILITGDDGHVLIDSGTEEAAPLVLANIRKLGFDPKDVRWLLSSHEHFDHVGGLAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 129 QRASGAKVIASAADKPYLEAGHVDHGPTKDAL---FPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTAKDS 205
Cdd:cd16315    81 QRATGARVAASAAAAPVLESGKPAPDDPQAGLhepFPPVRVDRIVEDGDTVALGSLRLTAHATPGHTPGALSWTWRSCEG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 206 TGMPRKVFLHCSASLGGQSLVPPAYPGMADNYRASFAKVRAMQADVFLANH----DMFfglhekrarQLAGEKDAFVDPG 281
Cdd:cd16315   161 ADCRTIVYADSLSPVSADGYRFSDHPDYVAAYRAGLAKVAALPCDILLTPHpsasDMF---------ERLSGGAPLADPD 231

                         250
                  ....*....|....*..
gi 1949903414 282 ELQRFNARMEAAFVKTL 298
Cdd:cd16315   232 ACAAYAAGAEKRLDERL 248
THIN-B-like_MBL-B3 cd16312
Janthinobacterium lividum THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-299 2.09e-64

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: 203.68  E-value: 2.09e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  49 WNERMAPFTILGNVHYVGTAGIGVFLITTLEGHVLIDGALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGL 128
Cdd:cd16312     1 WNQPVKPFNVFGNTWYVGTAGLSAVLVTSPQGHVLLDGALPQSAPLIIANIEALGFRIEDVKLILNSHAHWDHAGGIAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 129 QRASGAKVIASAADKPYLEAG-----HVDHGPTKDALFPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTAK 203
Cdd:cd16312    81 QKASGATVAASAHGAQVLQSGtngkdDPQYQAKPVVHVAKVAKVKEVGEGDTLKVGPLRLTAHMTPGHTPGGTTWTWTSC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 204 DSTGMPRKVF---LHCSASLGGQSLVPPAYPGMADNYRASFAKVRAMQADVFLANHDMFFGLHEKRARQlAGEKDAFVDP 280
Cdd:cd16312   161 EGQRCLDVVYadsLNPYSSGDFYYTGKGGYPDISASFRASIAKVAALPCDIIIAVHPGFTDVLDKAKRR-SGDTNPFIDA 239

                         250
                  ....*....|....*....
gi 1949903414 281 GELQRFNARMEAAFVKTLA 299
Cdd:cd16312   240 EACRAYAAGAAKSLEKRLA 258
GOB1-like_MBL-B3 cd16308
Elizabethkingia meningoseptica GOB-1 and related metallo-beta-lactamases, subclass B3; ...
 49-299 8.00e-62

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: 196.92  E-value: 8.00e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  49 WNERMAPFTILGNVHYVGTAGIGVFLITTLEGHVLIDGALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGL 128
Cdd:cd16308     1 WSQPYAPFRIAGNLYYVGTYDLACYLIVTPKGNILINTGLAESVPLIKKNIQALGFKFKDIKILLTTQAHYDHVGAMAAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 129 QRASGAKVIASAADKPYLEAGHVD------HGPTkdalFPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTA 202
Cdd:cd16308    81 KQQTGAKMMVDEKDAKVLADGGKSdyemggYGST----FAPVKADKLLHDGDTIKLGGTKLTLLHHPGHTKGSCSFLFDV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 203 KDStGMPRKVFLhcsASLGgqSLVP-------PAYPGMADNYRASFAKVRAMQADVFLANHDMFFGLHEKRARQLAGEKD 275
Cdd:cd16308   157 KDE-KRTYRVLI---ANMP--TILPdtklsgmPGYPGIAKDYAYTFEAMKALSFDIWLASHASQFDLHQKHKPGAPYNPA 230

                         250       260
                  ....*....|....*....|....
gi 1949903414 276 AFVDPGELQRFNARMEAAFVKTLA 299
Cdd:cd16308   231 AFADRAGYDKALAGLEKSYDKKIK 254
SMB-1-like_MBL-B3 cd16313
SMB-1, THIN-B and related metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase ...
 49-299 9.14e-61

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: 194.31  E-value: 9.14e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  49 WNERMAPFTILGNVHYVGTAGIGVFLITTLEGHVLIDGALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGL 128
Cdd:cd16313     1 WNAPQEPFQIYGNTYYVGTGGISAVLITSPQGHILIDGGFPKSPEQIAASIRQLGFKLEDVKYILSSHDHWDHAGGIAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 129 QRASGAKVIASAADKPYLEAGHVDHG-PTKDAL--FPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTAKDS 205
Cdd:cd16313    81 QKLTGAQVLASPATVAVLRSGSMGKDdPQFGGLtpMPPVASVRAVRDGEVVKLGPLAVTAHATPGHTTGGTSWTWQSCEQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 206 TGMPRKVFLHCSASLGGQSLVPPAYPGMADNYRASFAKVRAMQADVFLANHDMFFGLHEKRARQLAGEKDAFVDPGELQR 285
Cdd:cd16313   161 GRCANMVFADSLTAVSADGYRFSAHPAVLADVEQSIAAVEKLACDILVSAHPEFSDMWTRVKRGAAEGNAAFIDGGGCRA 240

                         250
                  ....*....|....
gi 1949903414 286 FNARMEAAFVKTLA 299
Cdd:cd16313   241 YAAKAREKLNKRLA 254
AIM-1-like_MBL-B3 cd16314
Pseudomonas Aeruginosa AIM-1 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-303 6.16e-57

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: 184.32  E-value: 6.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  49 WNERMAPFTILGNVHYVGTAGIGVFLITTLEGHVLIDGALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGL 128
Cdd:cd16314     1 WDDPAPPRRIYGNTWYVGTCGISALLVTSDAGHILIDGGTDKAAPLIEANIRALGFRPEDVRYIVSSHEHFDHAGGIARL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 129 QRASGAKVIASAADKPYLEAGHVDHGPTKDAL---FPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTAKDS 205
Cdd:cd16314    81 QRATGAPVVAREPAATTLERGRSDRSDPQFLVvekFPPVASVQRIGDGEVLRVGPLALTAHATPGHTPGGTSWTWRSCEG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 206 TGMPRKVFLHCSASLGGQSLVPPAYPGMADNYRASFAKVRAMQADVFLANHDMFFGLHEKRARQLAGekdAFVDPGELQR 285
Cdd:cd16314   161 AVCRDMVYADSVTAISDDIYRYSDHPGMVAAFRNTLDTVAALPCDILVTPHPSASGLWERLGPAAGI---PLADTGACRA 237

                         250
                  ....*....|....*...
gi 1949903414 286 FNARMEAAFVKTLADEQA 303
Cdd:cd16314   238 YAQTGRARLDARLADEAA 255
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 49-299 7.30e-57

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: 183.94  E-value: 7.30e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  49 WNERMAPFTILGNVHYVGTAGIGVFLITTLEGHVLIDgAL--AQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLA 126
Cdd:cd16280     1 KKGYVEPFQVFDNLYYVGNKWVSAWAIDTGDGLILID-ALnnNEAADLIVDGLEKLGLDPADIKYILITHGHGDHYGGAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 127 GLQRASGAKVIASAADKPYLEAGHVDHGPTKDalFPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTAKDSt 206
Cdd:cd16280    80 YLKDLYGAKVVMSEADWDMMEEPPEEGDNPRW--GPPPERDIVIKDGDTLTLGDTTITVYLTPGHTPGTLSLIFPVKDG- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 207 GMPRKVFLHcsaslGGQSLvpPAYPGMA--DNYRASFAKVRAM----QADVFLANHDMFFGLHEKRAR---QLAGEKDAF 277
Cdd:cd16280   157 GKTHRAGLW-----GGTGL--NTGPNLErrEQYIASLERFKKIaeeaGVDVFLSNHPFQDGSLEKREAlrnRKPGEPNPF 229

                         250       260
                  ....*....|....*....|..
gi 1949903414 278 VDPGELQRFNARMEAAFVKTLA 299
Cdd:cd16280   230 VDGQAWVDFYDEVLALCARVLA 251
L1_POM-1-like_MBL-B3 cd16289
Stenotrophomonas maltophilia L1, Pseudomonas otitidis POM-1 and related ...
 49-256 1.25e-56

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: 183.09  E-value: 1.25e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  49 WNERMAPFTILGNVHYVGTAGIGVFLITTLEGHVLIDGALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGL 128
Cdd:cd16289     1 WLQPMAPLQIADHTWYIGTESLTALLVKTPDGAVLLDGGMPQAADMLLDNMRALGVAPGDLKLILHSHAHADHAGPLAAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 129 QRASGAKVIASAADKPYLEAGHVDHGPTKDAL-FPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTAKDSTG 207
Cdd:cd16289    81 KRATGARVAANAESAVLLARGGSDDIHFGDGItFPPVQADRIVMDGEVVTLGGVTFTAHFTPGHTPGSTSWTWTDTRDGK 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1949903414 208 MPRKVFLHCSASLGGQSLVPPAYPGMADNYRASFAKVRAMQADVFLANH 256
Cdd:cd16289   161 PVRIAYADSLSAPGYQLLGNPRYPRIVEDYRRTFATVRALPCDVLLTPH 209
THIN-B2-like_MBL-B3 cd16311
Janthinobacterium lividum THIN-B2 and related metallo-beta-lactamases, subclass B3; MBL-fold ...
 49-299 3.12e-55

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: 180.18  E-value: 3.12e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  49 WNERMAPFTILGNVHYVGTAGIGVFLITTLEGHVLIDGALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGL 128
Cdd:cd16311     1 WNADQAPFRIFGNTYYVGVKGLSSVLVTSPQGHVLVDGGLPESAPKIIANIEALGFRIEDVKLILNSHGHIDHAGGLAEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 129 QRASGAKVIASAADKPYLEAGHV-DHGPTKDAL--FPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTAKDS 205
Cdd:cd16311    81 QRRSGALVAASPSAALDLASGEVgPDDPQYHALpkYPPVKDMRLARDGGQFNVGPVSLTAHATPGHTPGGLSWTWQSCDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 206 TGMPRKVF---LHCSASLGGQSLVPPAYPGMADNYRASFAKVRAMQADVFLANHDMFFGLHEKRARQLAGEKDAFVDPGE 282
Cdd:cd16311   161 PRCLNMVYadsQNAVSRPGFKFSASSEYPNAVADLRRSFETLEKLPCDVLISAHPEASQLWERLEASDRSARPALVDREA 240

                         250
                  ....*....|....*..
gi 1949903414 283 LQRFNARMEAAFVKTLA 299
Cdd:cd16311   241 CRRYASRAREALEKRIA 257
B3_Acin_new1 NF033184
putative subclass B3 metallo-beta-lactamase; This is one of two families of putative ...
 49-303 1.66e-54

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: 179.15  E-value: 1.66e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  49 WNERMAPFTILGNVHYVGTAGIGVFLITTLEGHVLIDGALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGL 128
Cdd:NF033184   28 WTQNTQPFQITENIYYVGTHGLAAYLLASGHQALLIDTGLPENTEQIEQNIKQLGFKLSDVKIMVTSHAHWDHVGALARI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 129 QRASGAKVIASAADKPYLEAGH-VDHGPTKDALFPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTAKdSTG 207
Cdd:NF033184  108 KQDTGAKLIAMQQDVKALEIGKpIGENTFQTIPFTPVKVDKVIHDGEVVKLGKFKLKATLTPGHTPGCTTWSTEVK-SNG 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 208 MPRKVFLHCSASLGGQSLVPP-AYPGMADNYRASFAKVRAMQADVFLANHDMFFGLHEKRARQLAGEKDAFVDPGELQRF 286
Cdd:NF033184  187 KNLNVVFPCSLSVAGNVLQNNhQYPNIVADYRKSFERLKNMKADIVLTSHPEVADVLGNKARKDAGQTNAFIQPEKLSSI 266

                         250
                  ....*....|....*..
gi 1949903414 287 NARMEAAFVKTLADEQA 303
Cdd:NF033184  267 VKDAEMAFEKSLVSSHP 283
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 72-257 6.84e-33

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: 120.57  E-value: 6.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  72 VFLITTLEGHVLID-GALAQSVPQILDNIRTLGfepKDVKYILNTHGHFDHAAGLAGLQRASGAKVIASAADKPYLEAGH 150
Cdd:COG0491    17 SYLIVGGDGAVLIDtGLGPADAEALLAALAALG---LDIKAVLLTHLHPDHVGGLAALAEAFGAPVYAHAAEAEALEAPA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 151 vdhgPTKDALFPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLtakdstgmPRKVFLHCS-ASLGGQSLVPPA 229
Cdd:COG0491    94 ----AGALFGREPVPPDRTLEDGDTLELGGPGLEVIHTPGHTPGHVSFYV--------PDEKVLFTGdALFSGGVGRPDL 161

                         170       180
                  ....*....|....*....|....*...
gi 1949903414 230 YPGMADNYRASFAKVRAMQADVFLANHD 257
Cdd:COG0491   162 PDGDLAQWLASLERLLALPPDLVIPGHG 189
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 61-197 1.76e-32

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 119.25  E-value: 1.76e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  61 NVHYV-GTAGIGVFLITTLEGHVLIDGALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGLQRASGAKVIAS 139
Cdd:cd07721     1 GVYQLpLLPPVNAYLIEDDDGLTLIDTGLPGSAKRILKALRELGLSPKDIRRILLTHGHIDHIGSLAALKEAPGAPVYAH 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949903414 140 AADKPYLEAGHVDHGPTKDALF---------PPVRVDRTVGDGDTITLAGtTLTAHLTPGHSPGCTS 197
Cdd:cd07721    81 EREAPYLEGEKPYPPPVRLGLLgllspllpvKPVPVDRTLEDGDTLDLAG-GLRVIHTPGHTPGHIS 146
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 72-197 1.37e-31

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: 116.62  E-value: 1.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  72 VFLITTLEGH-VLIDGAlAQSVPQILDNIRTLGfepKDVKYILNTHGHFDHAAGLAGLQRASGAKVIASAADKPYLEAGH 150
Cdd:cd06262    12 CYLVSDEEGEaILIDPG-AGALEKILEAIEELG---LKIKAILLTHGHFDHIGGLAELKEAPGAPVYIHEADAELLEDPE 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1949903414 151 VDHGPTKDALFPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTS 197
Cdd:cd06262    88 LNLAFFGGGPLPPPEPDILLEDGDTIELGGLELEVIHTPGHTPGSVC 134
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 72-256 3.41e-31

Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins contain this domain. These proteins include thiolesterases, members of the glyoxalase II family, that catalyse the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid and a competence protein that is essential for natural transformation in Neisseria gonorrhoeae and could be a transporter involved in DNA uptake. Except for the competence protein these proteins bind two zinc ions per molecule as cofactor.


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 114.96  E-value: 3.41e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414   72 VFLITTLEGHVLIDgALAQSVPQILDNIRTLGfePKDVKYILNTHGHFDHAAGLAGLQRASGAKVIASAADKPYLEAGHV 151
Cdd:smart00849   2 SYLVRDDGGAILID-TGPGEAEDLLAELKKLG--PKKIDAIILTHGHPDHIGGLPELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  152 DHGPTKDaLFPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWsltakdstGMPRKVFLHC---SASLGGQSLVPP 228
Cdd:smart00849  79 LLGELGA-EAEPAPPDRTLKDGDELDLGGGELEVIHTPGHTPGSIVL--------YLPEGKILFTgdlLFAGGDGRTLVD 149

                          170       180
                   ....*....|....*....|....*...
gi 1949903414  229 AYPGMADNYRASFAKVRAMQADVFLANH 256
Cdd:smart00849 150 GGDAAASDALESLLKLLKLLPKLVVPGH 177
ST1585-like_MBL-fold cd07726
uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo ...
 62-193 2.23e-20

uncharacterized subgroup which includes Sulfolobus tokodaii ST1585 protein; MBL-fold metallo hydrolase domain; This subgroup includes the uncharacterized Sulfolobus tokodaii ST1585 protein. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.


Pssm-ID: 293812 [Multi-domain]  Cd Length: 215  Bit Score: 87.16  E-value: 2.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  62 VHYVGTAG-IGVFLITTLEGHVLIDGALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHaAGLAG--LQRASGAKVIA 138
Cdd:cd07726     7 LGFLGFPGrIASYLLDGEGRPALIDTGPSSSVPRLLAALEALGIAPEDVDYIILTHIHLDH-AGGAGllAEALPNAKVYV 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949903414 139 SAADKPYLeaghVDhgPTK-------------DALF-PPVRVD----RTVGDGDTITLAGTTLTAHLTPGHSP 193
Cdd:cd07726    86 HPRGARHL----ID--PSKlwasaravygdeaDRLGgEILPVPeervIVLEDGETLDLGGRTLEVIDTPGHAP 152
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
72-195 8.90e-20

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 85.50  E-value: 8.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  72 VFLITTLEGHVLIDGALAQSVPQILDnIRTLGFEPKDVKYILNTHGHFDHAAGLAGLQRASGAKVIASAADKPYLEAGHV 151
Cdd:pfam00753   8 SYLIEGGGGAVLIDTGGSAEAALLLL-LAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVIVVAEEARELLDEEL 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1949903414 152 D----HGPTKDALFPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGC 195
Cdd:pfam00753  87 GlaasRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGH 134
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 73-194 5.40e-19

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


Pssm-ID: 293877 [Multi-domain]  Cd Length: 204  Bit Score: 83.17  E-value: 5.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  73 FLITTLEGH--VLIDGALAqsVPQILDNIRTLGFepkDVKYILNTHGHFDHAAGLAGLQRASGAKVIASAADKPYLEagh 150
Cdd:cd16322    14 YLVADEGGGeaVLVDPGDE--SEKLLARFGTTGL---TLLYILLTHAHFDHVGGVADLRRHPGAPVYLHPDDLPLYE--- 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1949903414 151 vdHGPTKDALF-----PPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPG 194
Cdd:cd16322    86 --AADLGAKAFglgiePLPPPDRLLEDGQTLTLGGLEFKVLHTPGHSPG 132
AHL_lactonase_MBL-fold cd07729
quorum-quenching N-acyl-homoserine lactonase, MBL-fold metallo-hydrolase domain; Acyl ...
 70-258 2.24e-17

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: 79.57  E-value: 2.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  70 IGVFLITTLEGHVLID-----------------GALAQSVPQILDN-IRTLGFEPKDVKYILNTHGHFDHAAGLAGLQra 131
Cdd:cd07729    32 VYAYLIEHPEGTILVDtgfhpdaaddpgglelaFPPGVTEEQTLEEqLARLGLDPEDIDYVILSHLHFDHAGGLDLFP-- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 132 sGAKVIASAADkpyLEAGHVDHGPTKDALFPPVRVDRTVGDGDTITLAGTT-----LTAHLTPGHSPGCTswSLTAKdst 206
Cdd:cd07729   110 -NATIIVQRAE---LEYATGPDPLAAGYYEDVLALDDDLPGGRVRLVDGDYdlfpgVTLIPTPGHTPGHQ--SVLVR--- 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949903414 207 gMPRKVFL------HCSASLGGQslVPPAYPGMADNYRASFAKVRAMQA---DVFLANHDM 258
Cdd:cd07729   181 -LPEGTVLlagdaaYTYENLEEG--RPPGINYDPEAALASLERLKALAEregARVIPGHDP 238
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 82-194 5.07e-16

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: 74.03  E-value: 5.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  82 VLIDGALAQSVpqiLDNIRTLGFEPKdvkYILNTHGHFDHAAGLAGLQRASG-AKVIASAADKpyleaghvdhgptkdal 160
Cdd:cd07723    23 AVVDPGEAEPV---LAALEKNGLTLT---AILTTHHHWDHTGGNAELKALFPdAPVYGPAEDR----------------- 79

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1949903414 161 FPPvrVDRTVGDGDTITLAGTTLTAHLTPGHSPG 194
Cdd:cd07723    80 IPG--LDHPVKDGDEIKLGGLEVKVLHTPGHTLG 111
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 62-194 3.29e-15

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: 72.56  E-value: 3.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  62 VHYV-GTAGIGVFLITTLEGhVLIDGALAQSVP-QILDNIRTLGFEPKdvkYILNTHGHFDHAAGLAGLQRASGAKVIAS 139
Cdd:cd07743     1 TYYIpGPTNIGVYVFGDKEA-LLIDSGLDEDAGrKIRKILEELGWKLK---AIINTHSHADHIGGNAYLQKKTGCKVYAP 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949903414 140 AADKPYLE-----------AGHVDHGPTKDALFPPVRVDRTVGDGDtITLAGTTLTAHLTPGHSPG 194
Cdd:cd07743    77 KIEKAFIEnpllepsylggAYPPKELRNKFLMAKPSKVDDIIEEGE-LELGGVGLEIIPLPGHSFG 141
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 74-194 1.08e-14

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


Pssm-ID: 293840 [Multi-domain]  Cd Length: 209  Bit Score: 71.44  E-value: 1.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  74 LITTLEGHVLID-GALAQSVPQILDNIRTLGfePKDVKYILNTHGHFDHAAGLAGLQRAsGAKVIASAADKPYLEAGHVD 152
Cdd:cd16282    19 FIVGDDGVVVIDtGASPRLARALLAAIRKVT--DKPVRYVVNTHYHGDHTLGNAAFADA-GAPIIAHENTREELAARGEA 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1949903414 153 HGPTKDALFP-------PVRVDRTVGDGDTITLAGTTLTA-HLTPGHSPG 194
Cdd:cd16282    96 YLELMRRLGGdamagteLVLPDRTFDDGLTLDLGGRTVELiHLGPAHTPG 145
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 82-204 5.00e-14

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: 68.97  E-value: 5.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  82 VLIDGALAQsVPQILDNIRTLGFEpkdVKYILNTHGHFDHAAGLAGLQRASGAKVIASAADkpyleaghvdhgptkdalf 161
Cdd:cd07724    26 AVIDPVRDS-VDRYLDLAAELGLK---ITYVLETHVHADHVSGARELAERTGAPIVIGEGA------------------- 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1949903414 162 PPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTAKD 204
Cdd:cd07724    83 PASFFDRLLKDGDVLELGNLTLEVLHTPGHTPESVSYLVGDPD 125
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 109-256 1.21e-13

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 67.90  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 109 VKYILNTHGHFDHAAGLAGLQRASGAKVIASAADkpylEAGHVDHGptkdalFPPvrvDRTVGDGDTITLAGTTLTAHLT 188
Cdd:cd16278    54 VSAILVTHTHRDHSPGAARLAERTGAPVRAFGPH----RAGGQDTD------FAP---DRPLADGEVIEGGGLRLTVLHT 120

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949903414 189 PGHSPGCTSWSLTAKDS--TG---MPRkvflhcsaslgGQSLVPPAYPGMADnYRASFAKVRAMQADVFLANH 256
Cdd:cd16278   121 PGHTSDHLCFALEDEGAlfTGdhvMGW-----------STTVIAPPDGDLGD-YLASLERLLALDDRLLLPGH 181
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 72-256 3.25e-13

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: 66.94  E-value: 3.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  72 VFLITTLEGHVLIDGALA--QSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAaGLAG-LQRASGAKVIAsaadkpylea 148
Cdd:cd07725    17 VYLLRDGDETTLIDTGLAteEDAEALWEGLKELGLKPSDIDRVLLTHHHPDHI-GLAGkLQEKSGATVYI---------- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 149 ghvdhgptkdalfPPVRvdrTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTakdstgmPRKVFLHCSASLG----GQS 224
Cdd:cd07725    86 -------------LDVT---PVKDGDKIDLGGLRLKVIETPGHTPGHIVLYDE-------DRRELFVGDAVLPkitpNVS 142

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1949903414 225 LVPPAYPGMADNYRASFAKVRAMQADVFLANH 256
Cdd:cd07725   143 LWAVRVEDPLGAYLESLDKLEKLDVDLAYPGH 174
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 92-197 1.11e-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: 65.25  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  92 VPQILDNIRTLGFEPKDvkyILNTHGHFDHAAGLAGLQRASGAKVIASAADKPYLEaghvdhgptkdalFPPVRVdRTVG 171
Cdd:cd16275    34 IEKILAKLNELGLTLTG---ILLTHSHFDHVNLVEPLLAKYDAPVYMSKEEIDYYG-------------FRCPNL-IPLE 96

                          90       100
                  ....*....|....*....|....*.
gi 1949903414 172 DGDTITLAGTTLTAHLTPGHSPGCTS 197
Cdd:cd16275    97 DGDTIKIGDTEITCLLTPGHTPGSMC 122
YcbL-like_MBL-fold cd07737
Salmonella enterica serovar typhimurium YcbL and related proteins; MBL-fold metallo hydrolase ...
 92-194 8.98e-12

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: 62.96  E-value: 8.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  92 VPQILDNIRTLGFEpkdVKYILNTHGHFDHAAGLAGLQRASGAKVIAS-AADKPYLEAGHVD----HGPTKDALFPpvrv 166
Cdd:cd07737    33 ADKILQAIEDLGLT---LKKILLTHGHLDHVGGAAELAEHYGVPIIGPhKEDKFLLENLPEQsqmfGFPPAEAFTP---- 105

                          90       100
                  ....*....|....*....|....*...
gi 1949903414 167 DRTVGDGDTITLAGTTLTAHLTPGHSPG 194
Cdd:cd07737   106 DRWLEEGDTVTVGNLTLEVLHCPGHTPG 133
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 73-195 1.15e-11

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: 62.26  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  73 FLITTLEGHVLIDGALAQSvpQILDNIRTLGFEPKDVkyiLNTHGHFDHAAGLAglqraSGAKVIASAADKPYLEAGHVD 152
Cdd:cd07712    12 YLLRGRDRALLIDTGLGIG--DLKEYVRTLTDLPLLV---VATHGHFDHIGGLH-----EFEEVYVHPADAEILAAPDNF 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1949903414 153 HGPTKDAL---FPPVRVDRTVGDGDTITLAGTTLTAHLTPGHSPGC 195
Cdd:cd07712    82 ETLTWDAAtysVPPAGPTLPLRDGDVIDLGDRQLEVIHTPGHTPGS 127
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 67-204 1.63e-10

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: 60.25  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  67 TAGIGVFLITTLEGHVLID----GALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGL---AGLQRASGAKVIAS 139
Cdd:cd07720    46 ETSVNAFLVRTGGRLILVDtgagGLFGPTAGKLLANLAAAGIDPEDIDDVLLTHLHPDHIGGLvdaGGKPVFPNAEVHVS 125

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949903414 140 AADKPY-LEAGHVDHGPTKDALFPPVRVDR--------TVGDGDTItLAGttLTAHLTPGHSPGCTSWSLTAKD 204
Cdd:cd07720   126 EAEWDFwLDDANAAKAPEGAKRFFDAARDRlrpyaaagRFEDGDEV-LPG--ITAVPAPGHTPGHTGYRIESGG 196
PLN02398 PLN02398
hydroxyacylglutathione hydrolase
 99-198 6.62e-10

hydroxyacylglutathione hydrolase


Pssm-ID: 215223 [Multi-domain]  Cd Length: 329  Bit Score: 59.09  E-value: 6.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  99 IRTLGFEPKDVKYILNTHGHFDHAAGLAGLQRASGAKVIASAADKpyleaghvDHGPTkdalfppvrVDRTVGDGDTITL 178
Cdd:PLN02398  112 IDALSRKNRNLTYILNTHHHYDHTGGNLELKARYGAKVIGSAVDK--------DRIPG---------IDIVLKDGDKWMF 174

                          90       100
                  ....*....|....*....|
gi 1949903414 179 AGTTLTAHLTPGHSPGCTSW 198
Cdd:PLN02398  175 AGHEVLVMETPGHTRGHISF 194
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 73-195 1.79e-09

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


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 57.11  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  73 FLITTlEGHVLIDGALAQSVPQILDNIRTLgFEPKDVKYILNTHGHFDHAAGLAG-LQRASGAKVIASAADKPYLEaghv 151
Cdd:cd07709    35 YLIKD-EKTALIDTVKEPFFDEFLENLEEV-IDPRKIDYIVVNHQEPDHSGSLPElLELAPNAKIVCSKKAARFLK---- 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1949903414 152 DHGPTKDalfPPVRVdrtVGDGDTITLAGTTLTAHLTPG-HSPGC 195
Cdd:cd07709   109 HFYPGID---ERFVV---VKDGDTLDLGKHTLKFIPAPMlHWPDT 147
MBLAC1-like_MBL-fold cd07711
uncharacterized human metallo-beta-lactamase domain-containing protein 1 and related proteins; ...
 72-197 2.63e-09

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


Pssm-ID: 293797 [Multi-domain]  Cd Length: 190  Bit Score: 55.67  E-value: 2.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  72 VFLITTLEGHVLIDGALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHaAGLAGLqrASGAKVIASAADKPYLEAGHV 151
Cdd:cd07711    24 VTLIKDGGKNILVDTGTPWDRDLLLKALAEHGLSPEDIDYVVLTHGHPDH-IGNLNL--FPNATVIVGWDICGDSYDDHS 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1949903414 152 DHGPTKDALFPPVRVDRtvgdgdtitlagttltahlTPGHSPGCTS 197
Cdd:cd07711   101 LEEGDGYEIDENVEVIP-------------------TPGHTPEDVS 127
NorV COG0426
Flavorubredoxin [Energy production and conversion];
73-194 4.10e-09

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 57.15  E-value: 4.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  73 FLITTlEGHVLIDGALAQSVPQILDNIRTLgFEPKDVKYILNTHGHFDHAAGLAG-LQRASGAKVIASAADKPYLEAgHV 151
Cdd:COG0426    37 YLIVD-EKTALIDTVGESFFEEFLENLSKV-IDPKKIDYIIVNHQEPDHSGSLPElLELAPNAKIVCSKKAARFLPH-FY 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1949903414 152 DHgptkdalfPPVRVdRTVGDGDTITLAGTTLTAHLTPG-HSPG 194
Cdd:COG0426   114 GI--------PDFRF-IVVKEGDTLDLGGHTLQFIPAPMlHWPD 148
ElaC COG1234
Ribonuclease BN, tRNA processing enzyme [Translation, ribosomal structure and biogenesis];
73-206 1.61e-08

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


Pssm-ID: 440847 [Multi-domain]  Cd Length: 250  Bit Score: 54.43  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  73 FLITTLEGHVLID---GALAQsvpqildnIRTLGFEPKDVKYILNTHGHFDHAAGLAGLQRASGA-------KVIASAAD 142
Cdd:COG1234    22 YLLEAGGERLLIDcgeGTQRQ--------LLRAGLDPRDIDAIFITHLHGDHIAGLPGLLSTRSLagrekplTIYGPPGT 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949903414 143 KPYLEAgHVDHGPTKDALfpPVRVdRTVGDGDTITLAGTTLTAHLTPgHSPGCTSWSLTAKDST 206
Cdd:COG1234    94 KEFLEA-LLKASGTDLDF--PLEF-HEIEPGEVFEIGGFTVTAFPLD-HPVPAYGYRFEEPGRS 152
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 61-198 1.71e-08

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: 53.36  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  61 NVHYVGTAGIGVFLITTLEGHVLIDgALAQSVPQILDNIRTLGFEPkdVKYILNTHGHFDHAAGlAGLQRASGAKVIASA 140
Cdd:cd16276     1 GVYWVTDGGYQSMFLVTDKGVIVVD-APPSLGENLLAAIRKVTDKP--VTHVVYSHNHADHIGG-ASIFKDEGATIIAHE 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949903414 141 ADKPYLEAghvdhgpTKDalfpPVRV--DRTVGDGDTITLAGTTLTAH-LTPGHSPGCTSW 198
Cdd:cd16276    77 ATAELLKR-------NPD----PKRPvpTVTFDDEYTLEVGGQTLELSyFGPNHGPGNIVI 126
DHPS-like_MBL-fold cd07713
Methanocaldococcus jannaschii dihydropteroate synthase, Thermoanaerobacter tengcongensis Tflp, ...
 73-139 4.20e-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: 53.39  E-value: 4.20e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949903414  73 FLITTLEGHVLID-GalaQSvPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAG-LQRASGAKVIAS 139
Cdd:cd07713    23 LLIETEGKKILFDtG---QS-GVLLHNAKKLGIDLSDIDAVVLSHGHYDHTGGLKAlLELNPKAPVYAH 87
metallo-hydrolase-like_MBL-fold cd07730
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 90-257 4.52e-08

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


Pssm-ID: 293816 [Multi-domain]  Cd Length: 250  Bit Score: 53.04  E-value: 4.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  90 QSVPQILdniRTLGFEPKDVKYILNTHGHFDHAAGLAGLqraSGAKVIASAADKPYLEAGHVDHGPTKDaLFPPVRVDRT 169
Cdd:cd07730    68 EDVAEQL---AAGGIDPEDIDAVILSHLHWDHIGGLSDF---PNARLIVGPGAKEALRPPGYPSGFLPE-LLPSDFEGRL 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 170 V---GDGDTITLAGTTLTAHL-----------TPGHSPGctSWSLTAKDSTGmpRKVFL-----HCSASLggqsLVPPAY 230
Cdd:cd07730   141 VrweEDDFLWVPLGPFPRALDlfgdgslylvdLPGHAPG--HLGLLARTTSG--TWVFLagdacHHRIGL----LRPSPL 212

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1949903414 231 PGMADN--------YRASFAKVRAMQAD----VFLAnHD 257
Cdd:cd07730   213 LPLPDLddgadreaARETLARLRELDAApdvrVVLA-HD 250
UlaG COG2220
L-ascorbate lactonase UlaG, metallo-beta-lactamase superfamily [Carbohydrate transport and ...
 62-194 6.35e-08

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


Pssm-ID: 441822 [Multi-domain]  Cd Length: 224  Bit Score: 52.23  E-value: 6.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  62 VHYVGTAGigvFLITTLEGHVLID----GALAQSVPQILDnirtlGFEPKDVKYILNTHGHFDHA--AGLAGLQRAsGAK 135
Cdd:COG2220     6 ITWLGHAT---FLIETGGKRILIDpvfsGRASPVNPLPLD-----PEDLPKIDAVLVTHDHYDHLddATLRALKRT-GAT 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 136 VIASAADKPYLEAghvdHGptkdalFPPVRVdrtVGDGDTITLAGTTLTAhlTPG-HSPG 194
Cdd:COG2220    77 VVAPLGVAAWLRA----WG------FPRVTE---LDWGESVELGGLTVTA--VPArHSSG 121
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 55-192 7.05e-08

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


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 51.77  E-value: 7.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  55 PFTILG-NVHYVGTaGIGVFLITTLEGHVLIDGALAQSVPQildnirtlgFEPKDVKYILNTHGHFDHAAGLAGLQRA-S 132
Cdd:cd07722    12 PFTLQGtNTYLVGT-GKRRILIDTGEGRPSYIPLLKSVLDS---------EGNATISDILLTHWHHDHVGGLPDVLDLlR 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 133 GAKVIASaadKpyleagHVDHGPTKDALFPPVRVDRtVGDGDTITLAGTTLTAHLTPGHS 192
Cdd:cd07722    82 GPSPRVY---K------FPRPEEDEDPDEDGGDIHD-LQDGQVFKVEGATLRVIHTPGHT 131
RNaseZ_MBL-fold cd16272
Ribonuclease Z; MBL-fold metallo-hydrolase domain; The tRNA maturase RNase Z (also known as ...
 57-195 9.13e-08

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


Pssm-ID: 293830 [Multi-domain]  Cd Length: 180  Bit Score: 51.11  E-value: 9.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  57 TILGNVHYVGTAGIGV--FLITTLEGHVLID---GALAQsvpqildnIRTLGFEPKDVKYILNTHGHFDHAAGLAGLQRA 131
Cdd:cd16272     2 TFLGTGGAVPSLTRNTssYLLETGGTRILLDcgeGTVYR--------LLKAGVDPDKLDAIFLSHFHLDHIGGLPTLLFA 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949903414 132 SGA-------KVIASAADKPYLEAgHVDHGPTKDALFPPVRVDRTVGDGDTITLAGTTLTAHLTPgHSPGC 195
Cdd:cd16272    74 RRYggrkkplTIYGPKGIKEFLEK-LLNFPVEILPLGFPLEIEELEEGGEVLELGDLKVEAFPVK-HSVES 142
metallo-hydrolase-like_MBL-fold cd16277
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 69-208 1.35e-07

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


Pssm-ID: 293835 [Multi-domain]  Cd Length: 222  Bit Score: 51.37  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  69 GIGVFLITTlEGH-VLID------------GALAQSVPQILDNIRTLGFEPKDVKYILNTHGHFDHaaglAG--LQRASG 133
Cdd:cd16277    12 LIHSWLVRT-PGRtILVDtgigndkprpgpPAFHNLNTPYLERLAAAGVRPEDVDYVLCTHLHVDH----VGwnTRLVDG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 134 --------AKVIASAADKPYLEAGHVDHGPTKDALFPPVR--VD----RTVGDGDTITlagTTLTAHLTPGHSPGCTSWS 199
Cdd:cd16277    87 rwvptfpnARYLFSRAEYDHWSSPDAGGPPNRGVFEDSVLpvIEaglaDLVDDDHEIL---DGIRLEPTPGHTPGHVSVE 163


                  ....*....
gi 1949903414 200 LTAKDSTGM 208
Cdd:cd16277   164 LESGGERAL 172
COG1237 COG1237
Metal-dependent hydrolase, beta-lactamase superfamily II [General function prediction only];
73-138 6.73e-07

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


Pssm-ID: 440850  Cd Length: 273  Bit Score: 49.88  E-value: 6.73e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  73 FLITTLEGHVLID---GALaqsvpqILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAG-LQRASGAKVIA 138
Cdd:COG1237    25 ALIETEGKRILFDtgqSDV------LLKNAEKLGIDLSDIDAVVLSHGHYDHTGGLPAlLELNPKAPVYA 88
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 56-194 5.06e-06

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 47.49  E-value: 5.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  56 FTILGNVHYVGTAGigvFLITTLEGHVLIDGALAQSVPqiLDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGLQRASG-A 134
Cdd:COG1236     3 LTFLGAAGEVTGSC---YLLETGGTRILIDCGLFQGGK--ERNWPPFPFRPSDVDAVVLTHAHLDHSGALPLLVKEGFrG 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949903414 135 KVIASAADKP-----YLEAGHVDHgptKDALFPP----------VRVDRTVGDGDTITLAGTTLTahLTP-GHSPG 194
Cdd:COG1236    78 PIYATPATADlarilLGDSAKIQE---EEAEAEPlyteedaeraLELFQTVDYGEPFEIGGVRVT--FHPaGHILG 148
YtnP-like_MBL-fold cd07728
Bacillus subtilis YtnP and related proteins; MBL-fold metallo hydrolase domain; Bacillus ...
 74-129 7.03e-06

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: 46.48  E-value: 7.03e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949903414  74 LITTLEGHVLID----------------GALAQSvpQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGLQ 129
Cdd:cd07728    47 LIQYQGKNYLIDagigngkltekqkrnfGVTEES--SIEESLAELGLTPEDIDYVLMTHLHFDHASGLTKVK 116
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 61-196 2.26e-05

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


Pssm-ID: 293813 [Multi-domain]  Cd Length: 181  Bit Score: 44.11  E-value: 2.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  61 NVHYVGTA---GIGV--FLITTLEGHVLIDGAlaQSVPQILDNIRTLGfepkDVKYILNTHGhfDHAAGLAGLQRASGAK 135
Cdd:cd07727     1 GVYYCGFHsekSFGAasYLILRPEGNILVDSP--RYSPPLAKRIEALG----GIRYIFLTHR--DDVADHAKWAERFGAK 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949903414 136 VIAsaadkpyleagHVDhgptkDALFPPVRVDRTVGDG-DTITLAGTtLTAHLTPGHSPGCT 196
Cdd:cd07727    73 RII-----------HED-----DVNAVTRPDEVIVLWGgDPWELDPD-LTLIPVPGHTRGSV 117
metallo-hydrolase-like_MBL-fold cd07742
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 99-126 2.41e-05

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


Pssm-ID: 293828 [Multi-domain]  Cd Length: 249  Bit Score: 44.92  E-value: 2.41e-05
                          10        20
                  ....*....|....*....|....*...
gi 1949903414  99 IRTLGFEPKDVKYILNTHGHFDHAAGLA 126
Cdd:cd07742    71 IEALGFDPSDVRHIVLTHLDLDHAGGLA 98
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 73-196 2.97e-05

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 44.50  E-value: 2.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  73 FLITTLEGHVLIDGAlaqsvPQILDNIRTLGFEPKDVKYILNTHGHFDHAAGLAGLQRASGAK---VIASAADKPYLEag 149
Cdd:COG1235    38 ILVEADGTRLLIDAG-----PDLREQLLRLGLDPSKIDAILLTHEHADHIAGLDDLRPRYGPNpipVYATPGTLEALE-- 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1949903414 150 hvDHGPTKDALFPPVRVDRTVGDGDTITLAGTTLTAHLTPgHSPGCT 196
Cdd:COG1235   111 --RRFPYLFAPYPGKLEFHEIEPGEPFEIGGLTVTPFPVP-HDAGDP 154
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 74-192 8.00e-05

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


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 42.87  E-value: 8.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  74 LITTLEGHVLIDgalAQ-SVPQ---ILDNIRTLGfepKDVKYILNTHGHFDHAAGLAGLQRA-SGAKVIASAADKPYLEA 148
Cdd:cd07739    20 LIYGETEAVLVD---AQfTRADaerLADWIKASG---KTLTTIYITHGHPDHYFGLEVLLEAfPDAKVVATPAVVAHIKA 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1949903414 149 GHVDHGPTKDALFPPVRVDRTV----GDGDTITLAGTTLTAhLTPGHS 192
Cdd:cd07739    94 QLEPKLAFWGPLLGGNAPARLVvpepLDGDTLTLEGHPLEI-VGVGGG 140
PLN02962 PLN02962
hydroxyacylglutathione hydrolase
 82-213 1.02e-04

hydroxyacylglutathione hydrolase


Pssm-ID: 178547 [Multi-domain]  Cd Length: 251  Bit Score: 42.86  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  82 VLIDgALAQSVPQILDNIRTLGFEpkdVKYILNTHGHFDHAAGLAGLQ-RASGAKVIASAADKPyleaghvdhgptkdal 160
Cdd:PLN02962   39 LLID-PVDKTVDRDLSLVKELGLK---LIYAMNTHVHADHVTGTGLLKtKLPGVKSIISKASGS---------------- 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1949903414 161 fppvRVDRTVGDGDTITLAGTTLTAHLTPGHSPGCTSWSLTAKDSTGMPRKVF 213
Cdd:PLN02962   99 ----KADLFVEPGDKIYFGDLYLEVRATPGHTAGCVTYVTGEGPDQPQPRMAF 147
PRK00685 PRK00685
metal-dependent hydrolase; Provisional
 72-140 1.40e-04

metal-dependent hydrolase; Provisional


Pssm-ID: 234811 [Multi-domain]  Cd Length: 228  Bit Score: 42.49  E-value: 1.40e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  72 VFLITTLEGHVLIDgalaqsvPQILDNIRT-LGFEPKDVKYILNTHGHFDHAAGLAGLQRASGAKVIASA 140
Cdd:PRK00685   10 AFLIETGGKKILID-------PFITGNPLAdLKPEDVKVDYILLTHGHGDHLGDTVEIAKRTGATVIANA 72
Lactamase_B_2 pfam12706
Beta-lactamase superfamily domain; This family is part of the beta-lactamase superfamily and ...
 108-192 8.10e-04

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


Pssm-ID: 432732 [Multi-domain]  Cd Length: 196  Bit Score: 39.99  E-value: 8.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414 108 DVKYILNTHGHFDHAAGLAGLQRASGAKVIASAADKPYLEAGhvdhGPTKDALFPPVRVDRTVGDGDTITLAGTTLTAHL 187
Cdd:pfam12706  28 PIDAVLLTHDHYDHLAGLLDLREGRPRPLYAPLGVLAHLRRN----FPYLFLLEHYGVRVHEIDWGESFTVGDGGLTVTA 103


                  ....*
gi 1949903414 188 TPGHS 192
Cdd:pfam12706 104 TPARH 108
ComEC COG2333
DNA uptake channel protein ComEC C-terminal domain, metallo-beta-lactamase superfamily ...
 73-184 1.25e-03

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: 39.84  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949903414  73 FLITTLEGH-VLIDG------ALAQSVpqILDNIRTLGFepKDVKYILNTHGHFDHAAGLAGLQRASGAKVIasaadkpy 145
Cdd:COG2333    14 ILIRTPDGKtILIDTgprpsfDAGERV--VLPYLRALGI--RRLDLLVLTHPDADHIGGLAAVLEAFPVGRV-------- 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1949903414 146 LEAGHVDHGPTKDALFPPVRVD----RTVGDGDTITLAGTTLT 184
Cdd:COG2333    82 LVSGPPDTSETYERLLEALKEKgipvRPCRAGDTWQLGGVRFE 124
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 73-121 1.32e-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: 1.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1949903414  73 FLITTLEGHVLIDGALAQSVPQILD-NIRTLGFEPKDVKYILNTHGHFDH 121
Cdd:cd16295    15 YLLETGGKRILLDCGLFQGGKELEElNNEPFPFDPKEIDAVILTHAHLDH 64
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 74-143 2.55e-03

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: 38.27  E-value: 2.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949903414  74 LITTLEGHVLID--GALAQSVPQILDNIRTLGFepKDVKYILNTHGHFDHAAGLAGLQRA-SGAKVIASAADK 143
Cdd:cd07731    14 LIQTPGKTILIDtgPRDSFGEDVVVPYLKARGI--KKLDYLILTHPDADHIGGLDAVLKNfPVKEVYMPGVTH 84
 
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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