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Conserved domains on  [gi|802036284|emb|CFO96588|]
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cyclase [Bordetella pertussis]

Protein Classification

MBL fold metallo-hydrolase( domain architecture ID 10888684)

MBL fold metallo-hydrolase is most likely a hydrolytic enzyme that may have substrate towards phosphotriesters, esters, and/or lactones

CATH:  3.60.15.10
EC:  3.-.-.-
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  17597585|12177301|11471246|11513844
SCOP:  3001057

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 24-231 5.38e-75

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: 228.99  E-value: 5.38e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  24 NAYAYTAE----GDPNTGIIVGDDAVMVVDTQATPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVFGASAYGAQ--EIL 97
Cdd:cd16282    1 GVYALIGPdgggFISNIGFIVGDDGVVVIDTGASPRLARALLAAIRKVTDKPVRYVVNTHYHGDHTLGNAAFADAgaPII 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  98 ASRDTYDLIAERGEQDKAseigRFPRLFRNVESIPPgLVWPTMTFKGEMTVDLGNLEVKLLQVGRGHTKGDTIAWLPEQK 177
Cdd:cd16282   81 AHENTREELAARGEAYLE----LMRRLGGDAMAGTE-LVLPDRTFDDGLTLDLGGRTVELIHLGPAHTPGDLVVWLPEEG 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 802036284 178 ILFAGDLVEYQSTPYCGDCYFREWPATLDALAGFEAEKMVPGRGPALKSATEVR 231
Cdd:cd16282  156 VLFAGDLVFNGRIPFLPDGSLAGWIAALDRLLALDATVVVPGHGPVGDKADLRA 209
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 24-231 5.38e-75

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: 228.99  E-value: 5.38e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  24 NAYAYTAE----GDPNTGIIVGDDAVMVVDTQATPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVFGASAYGAQ--EIL 97
Cdd:cd16282    1 GVYALIGPdgggFISNIGFIVGDDGVVVIDTGASPRLARALLAAIRKVTDKPVRYVVNTHYHGDHTLGNAAFADAgaPII 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  98 ASRDTYDLIAERGEQDKAseigRFPRLFRNVESIPPgLVWPTMTFKGEMTVDLGNLEVKLLQVGRGHTKGDTIAWLPEQK 177
Cdd:cd16282   81 AHENTREELAARGEAYLE----LMRRLGGDAMAGTE-LVLPDRTFDDGLTLDLGGRTVELIHLGPAHTPGDLVVWLPEEG 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 802036284 178 ILFAGDLVEYQSTPYCGDCYFREWPATLDALAGFEAEKMVPGRGPALKSATEVR 231
Cdd:cd16282  156 VLFAGDLVFNGRIPFLPDGSLAGWIAALDRLLALDATVVVPGHGPVGDKADLRA 209
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 29-224 4.42e-32

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: 118.64  E-value: 4.42e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  29 TAEGDPNTGIIVGDDAVMVVDTQATPVMAQDVIRRVREVtDKPIKYILLSHYHAVRVFGASAYGAQ---EILASRDTYDL 105
Cdd:COG0491   10 GAGLGVNSYLIVGGDGAVLIDTGLGPADAEALLAALAAL-GLDIKAVLLTHLHPDHVGGLAALAEAfgaPVYAHAAEAEA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284 106 IAERGEQDKaseigrfprlfrnvesIPPGLVWPTMTFKGEMTVDLGNLEVKLLqVGRGHTKGDTIAWLPEQKILFAGDLV 185
Cdd:COG0491   89 LEAPAAGAL----------------FGREPVPPDRTLEDGDTLELGGPGLEVI-HTPGHTPGHVSFYVPDEKVLFTGDAL 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 802036284 186 EYQSTP----YCGDcyFREWPATLDALAGFEAEKMVPGRGPAL 224
Cdd:COG0491  152 FSGGVGrpdlPDGD--LAQWLASLERLLALPPDLVIPGHGPPT 192
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 35-219 2.81e-19

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: 83.37  E-value: 2.81e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284    35 NTGIIVGDDAVMVVDTqaTPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVFGA----SAYGAqEILASRDTYDLIAErg 110
Cdd:smart00849   1 NSYLVRDDGGAILIDT--GPGEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLpellEAPGA-PVYAPEGTAELLKD-- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284   111 eqdkaseigrfPRLFRNVESIPPGLVWPTMTFKGEMTVDLGNLEVKLLQVGrGHTKGDTIAWLPEQKILFAGDLVEYQST 190
Cdd:smart00849  76 -----------LLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTP-GHTPGSIVLYLPEGKILFTGDLLFAGGD 143

                          170       180       190
                   ....*....|....*....|....*....|...
gi 802036284   191 PYC----GDCYFREWPATLDALAGFEAEKMVPG 219
Cdd:smart00849 144 GRTlvdgGDAAASDALESLLKLLKLLPKLVVPG 176
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
31-219 6.23e-13

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 66.62  E-value: 6.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284   31 EGDPNTGIIVGDDAVMVVDTQATPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVFGAsaygaqEILASRDTYDLIAERG 110
Cdd:pfam00753   3 PGQVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGL------GELAEATDVPVIVVAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  111 EQDKASEIGRFPRLFRNVESIPPGLVWPTMTFKGEMTVDLGNLEVKLLQVGRGHTKGDTIAWLPEQKILFAGDLVEYQST 190
Cdd:pfam00753  77 EARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEI 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 802036284  191 PYCGDCYFREWP----------ATLDALAGFEAEKMVPG 219
Cdd:pfam00753 157 GRLDLPLGGLLVlhpssaesslESLLKLAKLKAAVIVPG 195
 
Name Accession Description Interval E-value
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 24-231 5.38e-75

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: 228.99  E-value: 5.38e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  24 NAYAYTAE----GDPNTGIIVGDDAVMVVDTQATPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVFGASAYGAQ--EIL 97
Cdd:cd16282    1 GVYALIGPdgggFISNIGFIVGDDGVVVIDTGASPRLARALLAAIRKVTDKPVRYVVNTHYHGDHTLGNAAFADAgaPII 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  98 ASRDTYDLIAERGEQDKAseigRFPRLFRNVESIPPgLVWPTMTFKGEMTVDLGNLEVKLLQVGRGHTKGDTIAWLPEQK 177
Cdd:cd16282   81 AHENTREELAARGEAYLE----LMRRLGGDAMAGTE-LVLPDRTFDDGLTLDLGGRTVELIHLGPAHTPGDLVVWLPEEG 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 802036284 178 ILFAGDLVEYQSTPYCGDCYFREWPATLDALAGFEAEKMVPGRGPALKSATEVR 231
Cdd:cd16282  156 VLFAGDLVFNGRIPFLPDGSLAGWIAALDRLLALDATVVVPGHGPVGDKADLRA 209
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 29-224 4.42e-32

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: 118.64  E-value: 4.42e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  29 TAEGDPNTGIIVGDDAVMVVDTQATPVMAQDVIRRVREVtDKPIKYILLSHYHAVRVFGASAYGAQ---EILASRDTYDL 105
Cdd:COG0491   10 GAGLGVNSYLIVGGDGAVLIDTGLGPADAEALLAALAAL-GLDIKAVLLTHLHPDHVGGLAALAEAfgaPVYAHAAEAEA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284 106 IAERGEQDKaseigrfprlfrnvesIPPGLVWPTMTFKGEMTVDLGNLEVKLLqVGRGHTKGDTIAWLPEQKILFAGDLV 185
Cdd:COG0491   89 LEAPAAGAL----------------FGREPVPPDRTLEDGDTLELGGPGLEVI-HTPGHTPGHVSFYVPDEKVLFTGDAL 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 802036284 186 EYQSTP----YCGDcyFREWPATLDALAGFEAEKMVPGRGPAL 224
Cdd:COG0491  152 FSGGVGrpdlPDGD--LAQWLASLERLLALPPDLVIPGHGPPT 192
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 24-230 1.02e-30

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: 114.22  E-value: 1.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  24 NAYAYTAEGDpNTGIIVGDDAVMVVDtqATPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVFGASAYGAQ--EILASRD 101
Cdd:cd16276    1 GVYWVTDGGY-QSMFLVTDKGVIVVD--APPSLGENLLAAIRKVTDKPVTHVVYSHNHADHIGGASIFKDEgaTIIAHEA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284 102 TYDLIAERGEqdkaseigrfprlfrnvesipPGLVWPTMTFKGEMTVDLGNLEVKLLQVGRGHTKGDTIAWLPEQKILFA 181
Cdd:cd16276   78 TAELLKRNPD---------------------PKRPVPTVTFDDEYTLEVGGQTLELSYFGPNHGPGNIVIYLPKQKVLMA 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 802036284 182 GDLVEYQSTP---YCGDCYFREWPATLDALAGFEAEKMVPGRGPALKSATEV 230
Cdd:cd16276  137 VDLINPGWVPffnFAGSEDIPGYIEALDELLEYDFDTFVGGHGNRLGTREDV 188
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 16-222 4.00e-22

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


Pssm-ID: 293793 [Multi-domain]  Cd Length: 219  Bit Score: 92.22  E-value: 4.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  16 VSFEKLSDNAYAYTAEGD-PNTGIIV-GDDAVMVVDTQATPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVFGASAY-- 91
Cdd:cd07707    1 LSLTQINGPVWVVTDLGSvPSNGLVYnGSKGLVLVDSTWTPKTTKELIKEIEKVSQKPVTEVINTHFHTDRAGGNAYLke 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  92 -GAqEILASRDTYDLiaerGEQDKASEIGRFPRLFRNVESIPPglVWPTMTFKGEMTvdLGNLEVKLLQVGRGHTKGDTI 170
Cdd:cd07707   81 rGA-KTVSTALTRDL----AKSEWAEIVAFTRKGLPEYPDLGY--ELPDGVLDGDFN--LQFGKVEAFYPGPAHTPDNIV 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 802036284 171 AWLPEQKILFAGDLVEYQSTPYCGDCYFREWPATLDALAGF--EAEKMVPGRGP 222
Cdd:cd07707  152 VYFPQENVLYGGCIIKETDLGNVADADVKEWPTSIERLKKRyrNIKAVIPGHGE 205
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 35-219 2.81e-19

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: 83.37  E-value: 2.81e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284    35 NTGIIVGDDAVMVVDTqaTPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVFGA----SAYGAqEILASRDTYDLIAErg 110
Cdd:smart00849   1 NSYLVRDDGGAILIDT--GPGEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLpellEAPGA-PVYAPEGTAELLKD-- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284   111 eqdkaseigrfPRLFRNVESIPPGLVWPTMTFKGEMTVDLGNLEVKLLQVGrGHTKGDTIAWLPEQKILFAGDLVEYQST 190
Cdd:smart00849  76 -----------LLALLGELGAEAEPAPPDRTLKDGDELDLGGGELEVIHTP-GHTPGSIVLYLPEGKILFTGDLLFAGGD 143

                          170       180       190
                   ....*....|....*....|....*....|...
gi 802036284   191 PYC----GDCYFREWPATLDALAGFEAEKMVPG 219
Cdd:smart00849 144 GRTlvdgGDAAASDALESLLKLLKLLPKLVVPG 176
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 38-219 2.55e-18

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: 81.39  E-value: 2.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  38 IIVGDDAVMVVDTQATPVMAQDVIRRVREvTDKPIKYILLSHYHAVRVFGASAY-----GAQeILASRDTYDLIaergEQ 112
Cdd:cd07739   20 LIYGETEAVLVDAQFTRADAERLADWIKA-SGKTLTTIYITHGHPDHYFGLEVLleafpDAK-VVATPAVVAHI----KA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284 113 DKASEIGRFPRLFRNveSIPPGLVWPTMTFKGEMTVDlGNlEVKLLQVGRGHTKGDTIAWLPEQKILFAGDLVEYQSTPY 192
Cdd:cd07739   94 QLEPKLAFWGPLLGG--NAPARLVVPEPLDGDTLTLE-GH-PLEIVGVGGGDTDDTTYLWIPSLKTVVAGDVVYNGVHVW 169

                        170       180       190
                 ....*....|....*....|....*....|.
gi 802036284 193 CGDCYFRE----WPATLDALAGFEAEKMVPG 219
Cdd:cd07739  170 LADATTPElraaWLAALDKIEALNPETVVPG 200
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 16-222 3.40e-18

Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Bacillus cereus Beta-lactamase 2, also called BcII. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. BcII is a chromosome-encoded B1 MBL. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293862 [Multi-domain]  Cd Length: 212  Bit Score: 81.56  E-value: 3.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  16 VSFEKLSDNAYAYTAEGD------PNTGIIV-GDDAVMVVDTQATPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVFGA 88
Cdd:cd16304    1 LEVTKLNKNVWVHTSYGLfngtpvPSNGLIVeTSKGVVLIDTPWDDEQTEELLDWIKKKLKKPVTLAIVTHAHDDRIGGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  89 SAYGAQEI--LASRDTYDLIAERGeqdkaseigrFPRlfrnvesippglvwPTMTFKGEMTVDLGNLEVKLLQVGRGHTK 166
Cdd:cd16304   81 KALQKRGIpvYSTKLTAQLAKKQG----------YPS--------------PDGILKDDTTLKFGNTKIETFYPGEGHTA 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 802036284 167 GDTIAWLPEQKILFAGDLV---EYQSTPYCGDCYFREWPATLDAL-AGF-EAEKMVPGRGP 222
Cdd:cd16304  137 DNIVVWLPQSKILFGGCLVkslEAKDLGNTADANLKEWPTSIRNVlKRYpNAEIVVPGHGE 197
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 16-221 4.65e-18

metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. Subclass B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile. Includes chromosomally-encoded MBLs such as Bacillus cereus BcII, Bacteroides fragilis CcrA, and Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and acquired MBLs including IMP-1, VIM-1, VIM-2, GIM-1, NDM-1 and FIM-1.


Pssm-ID: 293843 [Multi-domain]  Cd Length: 210  Bit Score: 80.79  E-value: 4.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  16 VSFEKLSDNAYAYTAEGDPNTG-------IIVGDDAVMVVDTQATPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVFGA 88
Cdd:cd16285    1 LRIRPLADNVWVHTSLAEFNGGavpsnglIVIDGKGLVLIDTPWTEAQTATLLDWIEKKLGKPVTAAISTHSHDDRTGGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  89 SAYGAQEI--LASRDTYDLIAERGeqdkaseigrfprlfrnvesippgLVWPTMTFKGEMTVDLGNLEVKLLqvGRGHTK 166
Cdd:cd16285   81 KALNARGIptYATALTNELAKKEG------------------------KPVPTHSLKGALTLGFGPLEVFYP--GPGHTP 134

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284 167 GDTIAWLPEQKILFAGDLV---EYQSTPYCGDCYFREWPATLDAL-AGF-EAEKMVPGRG 221
Cdd:cd16285  135 DNIVVWLPKSKILFGGCLVksaSATSLGNVGDADVEAWPKSIENLkAKYpEARMVVPGHG 194
MUS_TUS_MBL-B1 cd16318
Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; ...
 16-219 1.50e-15

Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded MBLs Myroides odoratimimus MUS-1 and related MBLs. 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 MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293876  Cd Length: 214  Bit Score: 74.31  E-value: 1.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  16 VSFEKLSDNAYAYTA-------EGDPNTGIIVGDDAVMVVDTQATPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVFGA 88
Cdd:cd16318    1 LKIKQLNDNMYIYTTyqefqgvTYSSNSMYVLTDEGVILIDTPWDKDQYEPLLEYIRSNHNKEVKWVITTHFHEDRSGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  89 SAYgaQEILASRDTYDLIAERGEQdkaseigrfprlfRNVESippglvwPTMTFKGEMTVDLGNLEVKLLQVGRGHTKGD 168
Cdd:cd16318   81 GYF--NSIGAQTYTYALTNEILKE-------------RNEPQ-------AQFSFNKEKQFTFGNEKLAVYFLGEGHSLDN 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 802036284 169 TIAWLPEQKILFAGDLVEYQSTPYCG---DCYFREWPATLDALA-GFEAEK-MVPG 219
Cdd:cd16318  139 TVVWFPKEEVLYGGCLIKSAEATTIGniaDGNVIAWPKTIEAVKqKFKNAKvIIPG 194
CphA_ImiS-like_MBL-B2 cd16306
Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and related metallo-beta-lactamases, ...
 23-208 3.97e-15

Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and related metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis.


Pssm-ID: 293864  Cd Length: 222  Bit Score: 73.06  E-value: 3.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  23 DNAYAytaegDPNTGIIVGDDAVMVVDTQATPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVfGASAY----GAQeILA 98
Cdd:cd16306   15 DNYYV-----QENSMVYFGAKGVTVVGATWTPDTARELHKLIKRVSRKPVLEVINTNYHTDRA-GGNAYwksiGAK-VVS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  99 SRDTYDLIaERGeqdkASEIGRFPRL-FRNVESIPpgLVWPTMTFKGEMTvdLGNLEVKLLQVGRGHTKGDTIAWLPEQK 177
Cdd:cd16306   88 TRQTRDLM-KSD----WAEIVAFTRKgLPEYPDLP--LVLPNVVHDGDFT--LQEGKVRAFYLGPAHTPDGIFVYFPDEQ 158

                        170       180       190
                 ....*....|....*....|....*....|....
gi 802036284 178 ILFAGDLVEyqstPYCGDCYF---REWPATLDAL 208
Cdd:cd16306  159 VLYGNCILK----EKLGNLSFadvKAYPQTLERL 188
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 20-219 6.45e-15

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


Pssm-ID: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 72.92  E-value: 6.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  20 KLSDNAYAYTAEGDPNTGIIVGDDAVMVVDTQATPVMAQDVIRRVREVT-DKPIKYILLSHYHAVRVFGASAYGAQE--- 95
Cdd:cd07710    4 EVTDGVYQVRGYDLSNMTFIEGDTGLIIIDTLESAEAAKAALELFRKHTgDKPVKAIIYTHSHPDHFGGAGGFVEEEdsg 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  96 ---ILASRDTYDLIA----------------------ERGEQDKASeIGRFPRLFRNVESIPPglvwPTMTFKGE-MTVD 149
Cdd:cd07710   84 kvpIIAPEGFMEEAVsenvlagnamsrraayqfgallPKGEKGQVG-AGLGPGLSTGTVGFIP----PTITITETgETLT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284 150 LGNLEVKLLqvgrgHTKGDT----IAWLPEQKILFAGDLVeYQS---------TPYcgdcyfR---EWPATLDALAGFEA 213
Cdd:cd07710  159 IDGVELEFQ-----HAPGEApdemMVWLPDYKVLFCADNV-YHTfpnlytlrgAKY------RdalAWAKSLDEAISLKA 226


                 ....*.
gi 802036284 214 EKMVPG 219
Cdd:cd07710  227 EVLFPS 232
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 19-221 3.67e-14

Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; 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 MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293860  Cd Length: 212  Bit Score: 70.35  E-value: 3.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  19 EKLSDNAYAYTA--EGDP------NTGIIVGDDAVMVVDTQATPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVFGASA 90
Cdd:cd16302    4 IKLSDHVYVHVSylETETfgkvpcNGMIVINGGEAVVFDTPTNDSQSEELIDWIENSLKAKVKAVVPTHFHDDCLGGLKA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  91 YGAQEI--LASRDTYDLIAERGeqdkaseigrfprlfrnvesippgLVWPTMTFKGEMTVDLGNLEVKLLQVGRGHTKGD 168
Cdd:cd16302   84 FHRRGIpsYANQKTIALAKEKG------------------------LPVPQHGFSDSLTLKLGGKKIVCRYFGEGHTKDN 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 802036284 169 TIAWLPEQKILFAGDLVEYQSTP--YCGDCYFREWPATLD-ALAGF-EAEKMVPGRG 221
Cdd:cd16302  140 IVVYFPSEKVLFGGCMVKSLGAGkgNLEDANVEAWPKTVEkVKAKYpDVKIVIPGHG 196
SPM-1-like_MBL-B1-B2-like cd16286
Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; ...
 40-221 1.13e-13

Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; MBL-fold metallo-hydrolase domain; SPM-1 was first identified in a Pseudomonas aeruginosa strain from a paediatric leukaemia patient and is a major clinical problem. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs are most closely related to each other. SPM-1 appears to be a hybrid B1/B2 MBL.


Pssm-ID: 293844 [Multi-domain]  Cd Length: 236  Bit Score: 69.10  E-value: 1.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  40 VGDDAVMVVDTQATPVMAQDVIRRVREvTDKPIKYILLS-HYHAVRVFGASAYGAQ--EILASRDTYDLIAERGEQD--K 114
Cdd:cd16286   34 MLDGTVVIVDSPYTNLATQTVLDWIAK-TMGPRKVVAINtHFHLDGTGGNEALKKRgiPTWGSDLTKQLLLERGKADriK 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284 115 ASEIGRFPRLFRNVESIPPglVWPTMTF--KGEMTVDLGNLEVKLLQVGRGHTKGDTIAWLPEQKILFAGDLVE-YQSTP 191
Cdd:cd16286  113 AAEFLKNEDLKRRIESSPP--VPPDNVFdlKEGKVFSFGNELVEVSFPGPAHAPDNVVVYFPERKILFGGCMIKpGKELG 190

                        170       180       190
                 ....*....|....*....|....*....|
gi 802036284 192 YCGDCYFREWPATLDALAGFEAEKMVPGRG 221
Cdd:cd16286  191 NLGDANMKAWPDSVRRLKKFDAKIVIPGHG 220
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 35-185 2.54e-13

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: 67.31  E-value: 2.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  35 NTGIIVGDDA-VMVVDTQAtpvMAQDVIRRVREVTDKPIKYILLSHYH-----AVRVFgASAYGAqEILASRDTYDLIAE 108
Cdd:cd06262   11 NCYLVSDEEGeAILIDPGA---GALEKILEAIEELGLKIKAILLTHGHfdhigGLAEL-KEAPGA-PVYIHEADAELLED 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 802036284 109 RGEQDKASEIGRFPRlfrnvesippglVWPTMTFKGEMTVDLGNLEVKLLQVGrGHTKGDTIAWLPEQKILFAGDLV 185
Cdd:cd06262   86 PELNLAFFGGGPLPP------------PEPDILLEDGDTIELGGLELEVIHTP-GHTPGSVCFYIEEEGVLFTGDTL 149
IND_BlaB-like_MBL-B1 cd16299
IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 16-219 4.17e-13

IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded metallo-beta-lactamases Chryseobacterium indologenes IND-1, IND-2, and IND-7, Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB, Chryseobacterium gleum CGB-1, and Empedobacter brevis EBR-1. 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 MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293857  Cd Length: 212  Bit Score: 67.08  E-value: 4.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  16 VSFEKLSDNAYAYTA-------EGDPNTGIIVGDDAVMVVDTQATPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVFGA 88
Cdd:cd16299    1 LKIEKLNDNLYIYTTynefngvKYSANAMYLVTKKGVILFDTPWDKDQYQPLLDSIRKKHNLPVIAVIATHSHEDRAGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  89 SAYGAQEI--LASRDTYDLIAERGEqdkaseigrfPRlfrnvesippglvwPTMTFKGEMTVDLGNLEVKLLQVGRGHTK 166
Cdd:cd16299   81 GYFNKIGIptYATAMTNSILKKENK----------PQ--------------ATYLIETDKTYKIGGEKFVVYFFGEGHTA 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 802036284 167 GDTIAWLPEQKILFAGDLV---EYQSTPYCGDCYFREWPATLDAL-AGFEAEKMV-PG 219
Cdd:cd16299  137 DNVVVWFPKEKVLDGGCLIksaEATDLGYIGEANVKEWPKTIHKLkQKFKKAKVViPG 194
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
31-219 6.23e-13

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 66.62  E-value: 6.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284   31 EGDPNTGIIVGDDAVMVVDTQATPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVFGAsaygaqEILASRDTYDLIAERG 110
Cdd:pfam00753   3 PGQVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGL------GELAEATDVPVIVVAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  111 EQDKASEIGRFPRLFRNVESIPPGLVWPTMTFKGEMTVDLGNLEVKLLQVGRGHTKGDTIAWLPEQKILFAGDLVEYQST 190
Cdd:pfam00753  77 EARELLDEELGLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEI 156

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 802036284  191 PYCGDCYFREWP----------ATLDALAGFEAEKMVPG 219
Cdd:pfam00753 157 GRLDLPLGGLLVlhpssaesslESLLKLAKLKAAVIVPG 195
Sfh-1-like_MBL-B2 cd16305
Serratia fonticola Sfh-I and related metallo-beta-lactamases, subclass B2; MBL-fold ...
 27-211 6.34e-12

Serratia fonticola Sfh-I and related metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis.


Pssm-ID: 293863  Cd Length: 226  Bit Score: 64.25  E-value: 6.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  27 AYTAEgdpNTGIIVGDDAVMVVDTQATPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVfGASAY----GAQeILASRDT 102
Cdd:cd16305   17 EYVQE---NSMVYIGTDGITIIGATWTPETAETLEKEIRKVSPLPIKEVINTNYHTDRA-GGNAYwktlGAS-IVSTQMT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284 103 YDLiaergEQDKASEIGRFPRL----FRNVESIPPGLVWPtmtfkGEMtvDLGNLEVKLLQVGRGHTKGDTIAWLPEQKI 178
Cdd:cd16305   92 YDL-----EKSQWGSIVDFTRQgnnkYPNLEKSLPDTVYP-----GDF--NLQNGSVRALYLGEAHTEDGIFVYFPAERV 159

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 802036284 179 LFAGDLVEYQstpyCGDCYF---REWPATLDALAGF 211
Cdd:cd16305  160 LYGNCILKEK----LGNMSFanrTEYPKTLKKLKGL 191
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 38-185 2.11e-11

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: 62.24  E-value: 2.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  38 IIVGDDAVMVVDTqATPVMAQDVIRRVRE--VTDKPIKYILLSHYHAVRVFGASA----YGAqEILASRDTYDLIaERGE 111
Cdd:cd07721   15 LIEDDDGLTLIDT-GLPGSAKRILKALRElgLSPKDIRRILLTHGHIDHIGSLAAlkeaPGA-PVYAHEREAPYL-EGEK 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 802036284 112 QDKASEIGRFPRLFRnvESIPPGLVWPTMTFKGEMTVDL-GNLEVKLLQvgrGHTKGDTIAWLPEQKILFAGDLV 185
Cdd:cd07721   92 PYPPPVRLGLLGLLS--PLLPVKPVPVDRTLEDGDTLDLaGGLRVIHTP---GHTPGHISLYLEEDGVLIAGDAL 161
IMP_DIM-like_MBL-B1 cd16301
IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 17-221 3.72e-11

IMP-1, DIM-1, GIM-1, SIM-1, TMB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the acquired MBLs IMP-1(a beta-lactamase that is active on imipenem), DIM-1 (Dutch imipenemase), GIM-1 (German imipenemase), KHM-1 (Kyorin Health Science MBL 1), SIM-1 (Seoul imipenemase), and TMB-1 (Tripoli metallo-beta-lactamase). IMP-1, DIM-1, GIM-1, SIM-1, and TMB-1 are Class 1 integron-mediated MBLs, KMH-1 is plasmid-mediated. 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 acquired MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293859 [Multi-domain]  Cd Length: 215  Bit Score: 61.53  E-value: 3.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  17 SFEKLSDNAYAYTAEGDPNTGIIVGDDAVMVVD-TQA----TPVMAQDVIRRVREVTDKpiKYILL----SHYHAVRVFG 87
Cdd:cd16301    4 KIEKLSDGVYLHTSYKEVEGWGLVDANGLVVVDgKEAylidTPWSESDTEKLVEWIKAQ--GLTLKasisTHFHEDRTGG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  88 ASAYGAQEI--LASRDTYDLIAErgeQDKASeigrfprlfrnvesippglvwPTMTFKGeMTVDLGNLEVKLLQVGRGHT 165
Cdd:cd16301   82 IGYLNSHSIptYASELTNQLLKK---NGKEL---------------------ATHSFSG-DEFWLLKGKIEVFYPGAGHT 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 802036284 166 KGDTIAWLPEQKILFAGDLV---EYQSTPYCGDCYFREWPATL-DALAGF-EAEKMVPGRG 221
Cdd:cd16301  137 KDNLVVWLPKEKILFGGCLVkslESKGLGNTGDASISQWPASAqKVLSKYpNAKLVVPGHG 197
CphS_ImiS-like_MBL-B2 cd16287
metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas ...
 21-218 1.53e-09

metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and Serratia fonticola Sfh-I. MBLs (class B of the Ambler beta-lactamase classification) are a diverse group of metallo-enzymes that are capable of catalyzing the hydrolysis of a wide range of beta-lactam antibiotics. MBLs have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. B2 MBLs have a narrow substrate profile relative to subclass B1 MBLs that includes carbapenems, and they are active with one zinc ion bound in the Asp-Cys-His site, binding of a second zinc ion in the modified 3H site (Asn-His-His) inhibits catalysis.


Pssm-ID: 293845  Cd Length: 226  Bit Score: 57.05  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  21 LSDNAYAytaegDPNTGIIVGDDAVMVVDTQATPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVfGASAY----GAQeI 96
Cdd:cd16287   13 VEDKEYV-----QENSMVYIGTDGITIIGATWTPETAETLYKEIRKVSPLPINEVINTNYHTDRA-GGNAYwktlGAK-I 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  97 LASRDTYDLIaergeQDKASEIGRFPRlfRNVESIPP-GLVWPTMTFKGEMTVDLGnlEVKLLQVGRGHTKGDTIAWLPE 175
Cdd:cd16287   86 VATQMTYDLQ-----KSQWGSIVNFTR--QGNNKYPNlEKSLPDTVFPGDFNLQNG--SIRAMYLGEAHTKDGIFVYFPA 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 802036284 176 QKILFAGDLVEYQstpyCGDCYF---REWPATLDALAGFEAEKMVP 218
Cdd:cd16287  157 ERVLYGNCILKEN----LGNMSFanrTEYPKTLEKLKGLIEQGELK 198
VIM_type_MBL-B1 cd16303
VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona ...
 26-223 6.08e-09

VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona integron-encoded metallo-beta-lactamase)-type MBLs are integron-associated and are widely distributed acquired MBLs. MBLs (class B of the Ambler beta-lactamase classification) have been divided into three subclasses B1, B2 and B3, based on sequence/structural relationships and substrates, with the B1 and B2 MBLs being most closely related to each other. This subgroup of VIM-type MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293861 [Multi-domain]  Cd Length: 218  Bit Score: 55.25  E-value: 6.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  26 YAYTAEGDPNTGIIVGD-DAVMVVDTQATPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVFGAsaygaqeilasrdtyD 104
Cdd:cd16303   19 QSFDGAVYPSNGLIVRDgDELLLIDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGV---------------D 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284 105 LIAERGEQDKASEIGRfpRLfrnveSIPPGLVWPTMTFKGEMT----VDLGNLEvkLLQVGRGHTKGDTIAWLPEQKILF 180
Cdd:cd16303   84 VLRAAGVATYASPSTR--RL-----AEAEGNEIPTHSLEGLSSsgdaVRFGPVE--LFYPGAAHSTDNLVVYVPSARVLY 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 802036284 181 AGDLV-EYQSTPYCG--DCYFREWPATLDALAGF--EAEKMVPGRGPA 223
Cdd:cd16303  155 GGCAVrELSSTSAGNvaDADLAEWPTSIERIQKHypEAEFVIPGHGLP 202
NDM_FIM-like_MBL-B1 cd16300
NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase ...
 16-222 1.08e-08

NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the ISCR-mediated MBLs NDM-1 (NDM (New Delhi metallo-beta-lactamase) and FIM-1 (Florence imipenemase). 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 MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293858  Cd Length: 214  Bit Score: 54.44  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  16 VSFEKLSDNAYAYTAEGD-------PNTGIIVGD-DAVMVVDTQATPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVFG 87
Cdd:cd16300    1 VVFRQLAPGVWMHTSYLDmpgfgavPSNGLIVRDgDRVLLVDTAWTDDQTAQILNWAKQELNLPVRLAVVTHAHQDKMGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  88 ASAYGAQEI--LASRDTYDLIAERGEQDKASEIgrfprlfrNVESIPPGLVWptmtfkgemtvdlgnLEVKLLQVGRGHT 165
Cdd:cd16300   81 MDALHAAGIatYANALSNQLAPQEGLVPAQHSL--------TFAAEPSTAPN---------------FPLKVFYPGPGHT 137

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 802036284 166 KGDTIAWLPEQKILFAGDLVEYQSTPYCG---DCYFREWPATLDALA-GF-EAEKMVPGRGP 222
Cdd:cd16300  138 RDNIVVGIDGTGIAFGGCLIRPSKATSLGnlaDADTEHWAASARAFGaAFpDASMIVPSHGA 199
BlaB-like_MBL-B1 cd16316
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and related ...
 16-205 4.89e-08

Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded MBL Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and related MBLs. 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 MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293874  Cd Length: 214  Bit Score: 52.47  E-value: 4.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  16 VSFEKLSDNAYAYT-------AEGDPNTGIIVGDDAVMVVDTQATPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVFGA 88
Cdd:cd16316    1 LKISHLTGDLYVYTtyntykgTKTAANAVYVVTDKGVVVIDAPWDETQFQPFLDSIQKKHHKKVIMNIATHSHDDRAGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  89 SAYGAQEI--LASRDTYDLIAERGEqdkaseigrfPRlfrnvesippglvwPTMTFKGEMTVDLGNLEVKLLQVGRGHTK 166
Cdd:cd16316   81 EYFGKKGAktYTTKLTDSILKKNNK----------PR--------------AEYTFDNDTTFKVGKYEFQVYYPGKGHTA 136

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 802036284 167 GDTIAWLPEQKILFAGDLV---EYQSTPYCGDCYFREWPATL 205
Cdd:cd16316  137 DNIVVWFPKEKVLYGGCLIksaDAKDLGYLGEAYVNDWTQSI 178
TTHA1623-like_MBL-fold cd16322
uncharacterized Thermus thermophilus TTHA1623 and related proteins; MBL-fold metallo hydrolase ...
 21-185 4.19e-06

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: 46.57  E-value: 4.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  21 LSDNAYAYTAEGdpntgiivGDDAVmVVDTQATpvmAQDVIRRVREVTDKpIKYILLSHYHAVRVFGASAYGAQ---EIL 97
Cdd:cd16322    9 LQENTYLVADEG--------GGEAV-LVDPGDE---SEKLLARFGTTGLT-LLYILLTHAHFDHVGGVADLRRHpgaPVY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  98 ASRDTYDLIAERGEQDKASEIGRFPRlfrnvesiPPglvwPTMTFKGEMTVDLGNLEVKLLQVgRGHTKGDTIAWLPEQK 177
Cdd:cd16322   76 LHPDDLPLYEAADLGAKAFGLGIEPL--------PP----PDRLLEDGQTLTLGGLEFKVLHT-PGHSPGHVCFYVEEEG 142


                 ....*...
gi 802036284 178 ILFAGDLV 185
Cdd:cd16322  143 LLFSGDLL 150
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 31-219 5.07e-06

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


Pssm-ID: 293829 [Multi-domain]  Cd Length: 197  Bit Score: 46.37  E-value: 5.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  31 EGDPNTGIIV-GDDAVMVVDTQATpvmaQDVIRRVREVTDK---PIKYILLSHYHAVRvFGASAYGAQ----EILASRDT 102
Cdd:cd07743    5 PGPTNIGVYVfGDKEALLIDSGLD----EDAGRKIRKILEElgwKLKAIINTHSHADH-IGGNAYLQKktgcKVYAPKIE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284 103 yDLIAERgeqdkaSEI-------GRFPRLFRN-VESIPPGLVwpTMTFK-GEMTVDLGNLEVKLLQvgrGHTKGDtIAWL 173
Cdd:cd07743   80 -KAFIEN------PLLepsylggAYPPKELRNkFLMAKPSKV--DDIIEeGELELGGVGLEIIPLP---GHSFGQ-IGIL 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 802036284 174 PEQKILFAGDLV------EYQSTPYCGDcyFREWPATLDALAGFEAEKMVPG 219
Cdd:cd07743  147 TPDGVLFAGDALfgeevlEKYGIPFLYD--VEEQLETLEKLEELDADYYVPG 196
YmaE-like_MBL-fold cd07727
uncharacterized subgroup which includes Bacillus subtilis YmaE and related proteins; MBL-fold ...
 38-183 1.43e-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: 44.88  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  38 IIVGDDAVMVVDTqatPVMAQDVIRRVREVTDkpIKYILLSHYHAV--RVFGASAYGAQEILASRDtydliaeRGEQDKA 115
Cdd:cd07727   19 LILRPEGNILVDS---PRYSPPLAKRIEALGG--IRYIFLTHRDDVadHAKWAERFGAKRIIHEDD-------VNAVTRP 86

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 802036284 116 SEIgrfprlfrnvesippglvwptMTFKGEMTVDLGNlEVKLLQVGrGHTKGDTIAWLPEQKILFAGD 183
Cdd:cd07727   87 DEV---------------------IVLWGGDPWELDP-DLTLIPVP-GHTRGSVVLLYKEKGVLFTGD 131
IND_MBL-B1 cd16317
Chryseobacterium indologenes IND-1, IND-2, IND-7and related metallo-beta-lactamases, subclass ...
 31-219 1.88e-05

Chryseobacterium indologenes IND-1, IND-2, IND-7and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; Includes the chromosome-encoded MBLs Chryseobacterium indologenes IND-1, IND-2, and IND-7 and related MBLs. 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 MBLs belongs to the B1 subclass. B1 enzymes are most active with two zinc ions bound in the active site, and have a broad-spectrum substrate profile.


Pssm-ID: 293875  Cd Length: 215  Bit Score: 45.01  E-value: 1.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  31 EGDPNTGIIVGDDAVMVVDTQATPVMAQDVIRRVREVTDKPIKYILLSHYHAVRVFGASAYGAQEI--LASRDTYDLIAE 108
Cdd:cd16317   25 EYSANAVYLVTKKGVVLFDVPWQKVQYQSLMDTIQKRHHLPVIAVFATHSHDDRAGDLSFYNNKGIktYATAKTNEFLKK 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284 109 RGeqdKASeigrfprlfrNVESIPPGLvwPTMTFKGEMTVDLgnlevkllqVGRGHTKGDTIAWLPEQKILFAGDLVEYQ 188
Cdd:cd16317  105 DG---KAT----------STEIIKTGK--PYRIGGEEFVVDF---------LGEGHTADNVVVWFPKYKVLDGGCLVKSN 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 802036284 189 STP---YCGDCYFREWPATLDALAG--FEAEKMVPG 219
Cdd:cd16317  161 SATdlgYTGEANVEQWPKTMNKLKAkyAQATLIIPG 196
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 30-222 5.59e-05

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: 43.06  E-value: 5.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  30 AEGDPNTGIIVGDDAVMVVDTQ-ATPVMAQDVIRRVREVTDKP--IKYILLSHYHAVRVFGAsaygaqeilasrdtyDLI 106
Cdd:cd07725   11 PLGHVNVYLLRDGDETTLIDTGlATEEDAEALWEGLKELGLKPsdIDRVLLTHHHPDHIGLA---------------GKL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284 107 AERGEQDKASEigrfprlfrNVESIPPGlvwptmtfkgeMTVDLGNLEVKLLQVGrGHTKGDTIAWLPEQKILFAGDLVE 186
Cdd:cd07725   76 QEKSGATVYIL---------DVTPVKDG-----------DKIDLGGLRLKVIETP-GHTPGHIVLYDEDRRELFVGDAVL 134

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 802036284 187 YQSTPYCG-DCYFREWP-----ATLDALAGFEAEKMVPG-RGP 222
Cdd:cd07725  135 PKITPNVSlWAVRVEDPlgaylESLDKLEKLDVDLAYPGhGGP 177
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 38-185 2.00e-04

uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; MBL-fold metallo hydrolase domain; Includes the MBL-fold metallo hydrolase domain of uncharacterized human MBLAC2 and related proteins. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 41.46  E-value: 2.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  38 IIVGDDAVMVVDTqATPVmaQDVIRRVREVTDKPIKyILLSHYHAVRVFGASAYgaQEILASRDTYDLIAErgeQDKASE 117
Cdd:cd07712   13 LLRGRDRALLIDT-GLGI--GDLKEYVRTLTDLPLL-VVATHGHFDHIGGLHEF--EEVYVHPADAEILAA---PDNFET 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284 118 IGRFPRLFRNVESIPPGLVWptmtfKGEMtVDLGN--LEVKLLQvgrGHTKGDTIAWLPEQKILFAGDLV 185
Cdd:cd07712   84 LTWDAATYSVPPAGPTLPLR-----DGDV-IDLGDrqLEVIHTP---GHTPGSIALLDRANRLLFSGDVV 144
BDS1 COG2015
Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary ...
 35-185 5.01e-03

Alkyl sulfatase BDS1 and related hydrolases, metallo-beta-lactamase superfamily [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 441618 [Multi-domain]  Cd Length: 629  Bit Score: 38.67  E-value: 5.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284  35 NTGIIVGDDAVMVVDTQATPVMAQDVIRRVRE-VTDKPIKYILLSHYHAVRVFGASAYGAQEILASRDTyDLIAERGEQD 113
Cdd:COG2015  104 NMTFIEGDTGWIVIDPLTSVETAAAALALYRKhLGDRPVKAVIYTHSHVDHFGGVRGVVDEEDVKSGKV-PIIAPEGFME 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802036284 114 KA-SE-------IGR---------FPR---------LFRNVESIPPGLVWPTMTFKG---EMTVDlGnLEVKLLqvgrgH 164
Cdd:COG2015  183 HAvSEnvyagnaMGRraqymygtlLPRgpkgqvdagLGKTTSTGTVGLIPPTDTITKtgeELTID-G-VRMEFQ-----L 255

                        170       180
                 ....*....|....*....|....*..
gi 802036284 165 TKGdTIA------WLPEQKILFAGDLV 185
Cdd:COG2015  256 TPG-TEApaemnfYFPDFKALCMAENA 281
 
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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