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Conserved domains on  [gi|446665128|ref|WP_000742474|]
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BcII family subclass B1 metallo-beta-lactamase [Bacillus cereus]

Protein Classification

BCII family subclass B1 metallo-beta-lactamase( domain architecture ID 10888860)

BCII family subclass B1 metallo-beta-lactamase hydrolyzes the beta-lactam ring of beta-lactam antibiotics such as penicillin, cephalosporin and carbapenem, resulting in antibiotic resistance

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 46-247 7.92e-119

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: 338.10  E-value: 7.92e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  46 ISISQLNKNVWVHTELGSFNGEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGI 125
Cdd:cd16304    1 LEVTKLNKNVWVHTSYGLFNGTPVPSNGLIVETSKGVVLIDTPWDDEQTEELLDWIKKKLKKPVTLAIVTHAHDDRIGGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 126 KTLKERGIKAHSTALTAELAKKSGYEEPLGDLQTVTNLKFGNTKVETFYPGKGHTEDNIVVWLPQYKILAGGCLVKSAEA 205
Cdd:cd16304   81 KALQKRGIPVYSTKLTAQLAKKQGYPSPDGILKDDTTLKFGNTKIETFYPGEGHTADNIVVWLPQSKILFGGCLVKSLEA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446665128 206 KNLGNVADAYVNEWSTSIENMLKRYGNINSVVPGHGEVGDKG 247
Cdd:cd16304  161 KDLGNTADANLKEWPTSIRNVLKRYPNAEIVVPGHGEWGDKQ 202
 
Name Accession Description Interval E-value
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 46-247 7.92e-119

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: 338.10  E-value: 7.92e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  46 ISISQLNKNVWVHTELGSFNGEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGI 125
Cdd:cd16304    1 LEVTKLNKNVWVHTSYGLFNGTPVPSNGLIVETSKGVVLIDTPWDDEQTEELLDWIKKKLKKPVTLAIVTHAHDDRIGGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 126 KTLKERGIKAHSTALTAELAKKSGYEEPLGDLQTVTNLKFGNTKVETFYPGKGHTEDNIVVWLPQYKILAGGCLVKSAEA 205
Cdd:cd16304   81 KALQKRGIPVYSTKLTAQLAKKQGYPSPDGILKDDTTLKFGNTKIETFYPGEGHTADNIVVWLPQSKILFGGCLVKSLEA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446665128 206 KNLGNVADAYVNEWSTSIENMLKRYGNINSVVPGHGEVGDKG 247
Cdd:cd16304  161 KDLGNTADANLKEWPTSIRNVLKRYPNAEIVVPGHGEWGDKQ 202
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 55-246 5.47e-26

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: 100.92  E-value: 5.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  55 VWVHTELGSFNGEAVpsNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKfQKRVTDVIITHAHADRIGGIKTLKER-GI 133
Cdd:COG0491    1 VYVLPGGTPGAGLGV--NSYLIVGGDGAVLIDTGLGPADAEALLAALAAL-GLDIKAVLLTHLHPDHVGGLAALAEAfGA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 134 KAHSTALTAELAKKSGY-----EEPLGDLQTVTN---LKFGNTKVEtFYPGKGHTEDNIVVWLPQYKILAGGCLVKSAEA 205
Cdd:COG0491   78 PVYAHAAEAEALEAPAAgalfgREPVPPDRTLEDgdtLELGGPGLE-VIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGV 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446665128 206 KNLGNVaDAYVNEWSTSIENMLKRygNINSVVPGHGEVGDK 246
Cdd:COG0491  157 GRPDLP-DGDLAQWLASLERLLAL--PPDLVIPGHGPPTTA 194
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 72-240 3.98e-22

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 89.92  E-value: 3.98e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128    72 NGLVLNTSKGLVLVDSSWDDklTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKER-GIKAHSTALTAELAK---- 146
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGE--AEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEApGAPVYAPEGTAELLKdlla 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128   147 ----KSGYEEPLGDLQTVTN---LKFGNTKVETFYPGkGHTEDNIVVWLPQYKILAGGCLVKSAEAKNLGNVA-DAYVNE 218
Cdd:smart00849  79 llgeLGAEAEPAPPDRTLKDgdeLDLGGGELEVIHTP-GHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGgDAAASD 157

                          170       180
                   ....*....|....*....|..
gi 446665128   219 WSTSIENMLKRYGNInsVVPGH 240
Cdd:smart00849 158 ALESLLKLLKLLPKL--VVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
66-240 2.27e-16

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 75.10  E-value: 2.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128   66 GEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAH--------- 136
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVivvaeeare 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  137 -------STALTAELAKKSGYEEPLGDLQTVTNLKFGNTKVETFYPGKGHTEDNIVVWLPQYKILAGGCLVKSAE----A 205
Cdd:pfam00753  81 lldeelgLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEigrlD 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 446665128  206 KNLGNVADAYVNEWSTSIENMLK-RYGNINSVVPGH 240
Cdd:pfam00753 161 LPLGGLLVLHPSSAESSLESLLKlAKLKAAVIVPGH 196
 
Name Accession Description Interval E-value
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 46-247 7.92e-119

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: 338.10  E-value: 7.92e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  46 ISISQLNKNVWVHTELGSFNGEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGI 125
Cdd:cd16304    1 LEVTKLNKNVWVHTSYGLFNGTPVPSNGLIVETSKGVVLIDTPWDDEQTEELLDWIKKKLKKPVTLAIVTHAHDDRIGGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 126 KTLKERGIKAHSTALTAELAKKSGYEEPLGDLQTVTNLKFGNTKVETFYPGKGHTEDNIVVWLPQYKILAGGCLVKSAEA 205
Cdd:cd16304   81 KALQKRGIPVYSTKLTAQLAKKQGYPSPDGILKDDTTLKFGNTKIETFYPGEGHTADNIVVWLPQSKILFGGCLVKSLEA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446665128 206 KNLGNVADAYVNEWSTSIENMLKRYGNINSVVPGHGEVGDKG 247
Cdd:cd16304  161 KDLGNTADANLKEWPTSIRNVLKRYPNAEIVVPGHGEWGDKQ 202
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 46-247 1.20e-103

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: 299.58  E-value: 1.20e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  46 ISISQLNKNVWVHTELGSFNGEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGI 125
Cdd:cd16285    1 LRIRPLADNVWVHTSLAEFNGGAVPSNGLIVIDGKGLVLIDTPWTEAQTATLLDWIEKKLGKPVTAAISTHSHDDRTGGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 126 KTLKERGIKAHSTALTAELAKKSGYEEPLGDLQTVTNLKFGntKVETFYPGKGHTEDNIVVWLPQYKILAGGCLVKSAEA 205
Cdd:cd16285   81 KALNARGIPTYATALTNELAKKEGKPVPTHSLKGALTLGFG--PLEVFYPGPGHTPDNIVVWLPKSKILFGGCLVKSASA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446665128 206 KNLGNVADAYVNEWSTSIENMLKRYGNINSVVPGHGEVGDKG 247
Cdd:cd16285  159 TSLGNVGDADVEAWPKSIENLKAKYPEARMVVPGHGAPGGTE 200
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 46-247 5.63e-94

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: 275.58  E-value: 5.63e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  46 ISISQLNKNVWVHTELGSfngeaVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGI 125
Cdd:cd07707    1 LSLTQINGPVWVVTDLGS-----VPSNGLVYNGSKGLVLVDSTWTPKTTKELIKEIEKVSQKPVTEVINTHFHTDRAGGN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 126 KTLKERGIKAHSTALTAELAKK------------------SGYEEPLGDLQTVTNLKFGntKVETFYPGKGHTEDNIVVW 187
Cdd:cd07707   76 AYLKERGAKTVSTALTRDLAKSewaeivaftrkglpeypdLGYELPDGVLDGDFNLQFG--KVEAFYPGPAHTPDNIVVY 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 188 LPQYKILAGGCLVKSaeaKNLGNVADAYVNEWSTSIENMLKRYGNINSVVPGHGEVGDKG 247
Cdd:cd07707  154 FPQENVLYGGCIIKE---TDLGNVADADVKEWPTSIERLKKRYRNIKAVIPGHGEVGGPE 210
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 46-247 2.27e-64

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: 199.78  E-value: 2.27e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  46 ISISQLNKNVWVHT---ELGSFNgeAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRI 122
Cdd:cd16302    1 LEIIKLSDHVYVHVsylETETFG--KVPCNGMIVINGGEAVVFDTPTNDSQSEELIDWIENSLKAKVKAVVPTHFHDDCL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 123 GGIKTLKERGIKAHSTALTAELAKKSGYEEPLGDLQTVTNLKFGNTKVETFYPGKGHTEDNIVVWLPQYKILAGGCLVKS 202
Cdd:cd16302   79 GGLKAFHRRGIPSYANQKTIALAKEKGLPVPQHGFSDSLTLKLGGKKIVCRYFGEGHTKDNIVVYFPSEKVLFGGCMVKS 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446665128 203 AEAkNLGNVADAYVNEWSTSIENMLKRYGNINSVVPGHGEVGDKG 247
Cdd:cd16302  159 LGA-GKGNLEDANVEAWPKTVEKVKAKYPDVKIVIPGHGKIGGSE 202
IND_BlaB-like_MBL-B1 cd16299
IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 46-247 9.60e-62

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: 193.04  E-value: 9.60e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  46 ISISQLNKNVWVHTELGSFNGEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGI 125
Cdd:cd16299    1 LKIEKLNDNLYIYTTYNEFNGVKYSANAMYLVTKKGVILFDTPWDKDQYQPLLDSIRKKHNLPVIAVIATHSHEDRAGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 126 KTLKERGIKAHSTALTAELAKKSGYEEPLGDLQTVTNLKFGNTKVETFYPGKGHTEDNIVVWLPQYKILAGGCLVKSAEA 205
Cdd:cd16299   81 GYFNKIGIPTYATAMTNSILKKENKPQATYLIETDKTYKIGGEKFVVYFFGEGHTADNVVVWFPKEKVLDGGCLIKSAEA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446665128 206 KNLGNVADAYVNEWSTSIENMLKRYGNINSVVPGHGEVGDKG 247
Cdd:cd16299  161 TDLGYIGEANVKEWPKTIHKLKQKFKKAKVVIPGHDEWKDQG 202
VIM_type_MBL-B1 cd16303
VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona ...
 44-244 2.73e-61

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: 192.38  E-value: 2.73e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  44 GTISISQLNKNVWVHTELGSFNGEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIG 123
Cdd:cd16303    1 GEVRLYQIADGVWSHIATQSFDGAVYPSNGLIVRDGDELLLIDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 124 GIKTLKERGIKAHSTALTAELAKKSGYEEP---LGDLQTV-TNLKFGNtkVETFYPGKGHTEDNIVVWLPQYKILAGGCL 199
Cdd:cd16303   81 GVDVLRAAGVATYASPSTRRLAEAEGNEIPthsLEGLSSSgDAVRFGP--VELFYPGAAHSTDNLVVYVPSARVLYGGCA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446665128 200 VKSAEAKNLGNVADAYVNEWSTSIENMLKRYGNINSVVPGHGEVG 244
Cdd:cd16303  159 VRELSSTSAGNVADADLAEWPTSIERIQKHYPEAEFVIPGHGLPG 203
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 ...
 46-246 8.35e-61

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: 190.96  E-value: 8.35e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  46 ISISQLNKNVWVHTELGSFNGEA-VPSNGLVLNTSKGLVLVDSSWDDKLTKELIE-MVEKKFQkrVTDVIITHAHADRIG 123
Cdd:cd16301    3 LKIEKLSDGVYLHTSYKEVEGWGlVDANGLVVVDGKEAYLIDTPWSESDTEKLVEwIKAQGLT--LKASISTHFHEDRTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 124 GIKTLKERGIKAHSTALTAELAKKSGYEEPLGDLqTVTNLKFGNTKVETFYPGKGHTEDNIVVWLPQYKILAGGCLVKSA 203
Cdd:cd16301   81 GIGYLNSHSIPTYASELTNQLLKKNGKELATHSF-SGDEFWLLKGKIEVFYPGAGHTKDNLVVWLPKEKILFGGCLVKSL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446665128 204 EAKNLGNVADAYVNEWSTSIENMLKRYGNINSVVPGHGEVGDK 246
Cdd:cd16301  160 ESKGLGNTGDASISQWPASAQKVLSKYPNAKLVVPGHGKVGDV 202
BlaB-like_MBL-B1 cd16316
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and related ...
 46-246 2.62e-57

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: 181.89  E-value: 2.62e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  46 ISISQLNKNVWVHTELGSFNGEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGI 125
Cdd:cd16316    1 LKISHLTGDLYVYTTYNTYKGTKTAANAVYVVTDKGVVVIDAPWDETQFQPFLDSIQKKHHKKVIMNIATHSHDDRAGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 126 KTLKERGIKAHSTALTAELAKKSGYEEPLGDLQTVTNLKFGNTKVETFYPGKGHTEDNIVVWLPQYKILAGGCLVKSAEA 205
Cdd:cd16316   81 EYFGKKGAKTYTTKLTDSILKKNNKPRAEYTFDNDTTFKVGKYEFQVYYPGKGHTADNIVVWFPKEKVLYGGCLIKSADA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446665128 206 KNLGNVADAYVNEWSTSIENMLKRYGNINSVVPGHGEVGDK 246
Cdd:cd16316  161 KDLGYLGEAYVNDWTQSIHNIQQKFPNPQYVIAGHDDWKDQ 201
NDM_FIM-like_MBL-B1 cd16300
NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase ...
 46-241 3.49e-52

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: 168.84  E-value: 3.49e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  46 ISISQLNKNVWVHTE-LGSFNGEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGG 124
Cdd:cd16300    1 VVFRQLAPGVWMHTSyLDMPGFGAVPSNGLIVRDGDRVLLVDTAWTDDQTAQILNWAKQELNLPVRLAVVTHAHQDKMGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 125 IKTLKERGIKAHSTALTAELAKKSGYEEPlgdlQTVTNLKFG-----NTKVETFYPGKGHTEDNIVVWLPQYKILAGGCL 199
Cdd:cd16300   81 MDALHAAGIATYANALSNQLAPQEGLVPA----QHSLTFAAEpstapNFPLKVFYPGPGHTRDNIVVGIDGTGIAFGGCL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446665128 200 VKSAEAKNLGNVADAYVNEWSTSIENMLKRYGNINSVVPGHG 241
Cdd:cd16300  157 IRPSKATSLGNLADADTEHWAASARAFGAAFPDASMIVPSHG 198
MUS_TUS_MBL-B1 cd16318
Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; ...
 46-242 2.85e-50

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: 164.06  E-value: 2.85e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  46 ISISQLNKNVWVHTELGSFNGEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGI 125
Cdd:cd16318    1 LKIKQLNDNMYIYTTYQEFQGVTYSSNSMYVLTDEGVILIDTPWDKDQYEPLLEYIRSNHNKEVKWVITTHFHEDRSGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 126 KTLKERGIKAHSTALTAELAKKSGYEEPLGDLQTVTNLKFGNTKVETFYPGKGHTEDNIVVWLPQYKILAGGCLVKSAEA 205
Cdd:cd16318   81 GYFNSIGAQTYTYALTNEILKERNEPQAQFSFNKEKQFTFGNEKLAVYFLGEGHSLDNTVVWFPKEEVLYGGCLIKSAEA 160

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446665128 206 KNLGNVADAYVNEWSTSIENMLKRYGNINSVVPGHGE 242
Cdd:cd16318  161 TTIGNIADGNVIAWPKTIEAVKQKFKNAKVIIPGHDE 197
IND_MBL-B1 cd16317
Chryseobacterium indologenes IND-1, IND-2, IND-7and related metallo-beta-lactamases, subclass ...
 50-242 7.65e-44

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: 147.47  E-value: 7.65e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  50 QLNKNVWVHTELGSFNGEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLK 129
Cdd:cd16317    7 PIKPNLYIYKTFGVFGGKEYSANAVYLVTKKGVVLFDVPWQKVQYQSLMDTIQKRHHLPVIAVFATHSHDDRAGDLSFYN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 130 ERGIKAHSTALTAELAKKSGYEEPLGDLQTVTNLKFGNTKVETFYPGKGHTEDNIVVWLPQYKILAGGCLVKSAEAKNLG 209
Cdd:cd16317   87 NKGIKTYATAKTNEFLKKDGKATSTEIIKTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKVLDGGCLVKSNSATDLG 166

                        170       180       190
                 ....*....|....*....|....*....|...
gi 446665128 210 NVADAYVNEWSTSIENMLKRYGNINSVVPGHGE 242
Cdd:cd16317  167 YTGEANVEQWPKTMNKLKAKYAQATLIIPGHDE 199
SPM-1-like_MBL-B1-B2-like cd16286
Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; ...
 71-247 2.54e-31

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: 115.71  E-value: 2.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  71 SNGLVLNTSKG-LVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAHSTALTAELAKKSG 149
Cdd:cd16286   27 SNVLVVKMLDGtVVIVDSPYTNLATQTVLDWIAKTMGPRKVVAINTHFHLDGTGGNEALKKRGIPTWGSDLTKQLLLERG 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 150 ----------YEE-----------PLG-----DLQTVTNLKFGNTKVETFYPGKGHTEDNIVVWLPQYKILAGGCLVKSa 203
Cdd:cd16286  107 kadrikaaefLKNedlkrriesspPVPpdnvfDLKEGKVFSFGNELVEVSFPGPAHAPDNVVVYFPERKILFGGCMIKP- 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446665128 204 eAKNLGNVADAYVNEWSTSIENmLKRYgNINSVVPGHGEVGDKG 247
Cdd:cd16286  186 -GKELGNLGDANMKAWPDSVRR-LKKF-DAKIVIPGHGERGDPG 226
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 54-246 3.31e-31

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: 114.59  E-value: 3.31e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  54 NVWVHTelGSFNGEAVPSNGLVLnTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGI 133
Cdd:cd16282    1 GVYALI--GPDGGGFISNIGFIV-GDDGVVVIDTGASPRLARALLAAIRKVTDKPVRYVVNTHYHGDHTLGNAAFADAGA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 134 KAHSTALTAELAKKSG--YEEPLGDL--------------QTVTN---LKFGNTKVETFYPGKGHTEDNIVVWLPQYKIL 194
Cdd:cd16282   78 PIIAHENTREELAARGeaYLELMRRLggdamagtelvlpdRTFDDgltLDLGGRTVELIHLGPAHTPGDLVVWLPEEGVL 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446665128 195 AGGCLVksaEAKNLGNVADAYVNEWSTSIENMLKRYGNInsVVPGHGEVGDK 246
Cdd:cd16282  158 FAGDLV---FNGRIPFLPDGSLAGWIAALDRLLALDATV--VVPGHGPVGDK 204
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 55-246 5.47e-26

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: 100.92  E-value: 5.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  55 VWVHTELGSFNGEAVpsNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKfQKRVTDVIITHAHADRIGGIKTLKER-GI 133
Cdd:COG0491    1 VYVLPGGTPGAGLGV--NSYLIVGGDGAVLIDTGLGPADAEALLAALAAL-GLDIKAVLLTHLHPDHVGGLAALAEAfGA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 134 KAHSTALTAELAKKSGY-----EEPLGDLQTVTN---LKFGNTKVEtFYPGKGHTEDNIVVWLPQYKILAGGCLVKSAEA 205
Cdd:COG0491   78 PVYAHAAEAEALEAPAAgalfgREPVPPDRTLEDgdtLELGGPGLE-VIHTPGHTPGHVSFYVPDEKVLFTGDALFSGGV 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446665128 206 KNLGNVaDAYVNEWSTSIENMLKRygNINSVVPGHGEVGDK 246
Cdd:COG0491  157 GRPDLP-DGDLAQWLASLERLLAL--PPDLVIPGHGPPTTA 194
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 72-240 3.98e-22

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


Pssm-ID: 214854 [Multi-domain]  Cd Length: 177  Bit Score: 89.92  E-value: 3.98e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128    72 NGLVLNTSKGLVLVDSSWDDklTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKER-GIKAHSTALTAELAK---- 146
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGE--AEDLLAELKKLGPKKIDAIILTHGHPDHIGGLPELLEApGAPVYAPEGTAELLKdlla 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128   147 ----KSGYEEPLGDLQTVTN---LKFGNTKVETFYPGkGHTEDNIVVWLPQYKILAGGCLVKSAEAKNLGNVA-DAYVNE 218
Cdd:smart00849  79 llgeLGAEAEPAPPDRTLKDgdeLDLGGGELEVIHTP-GHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGgDAAASD 157

                          170       180
                   ....*....|....*....|..
gi 446665128   219 WSTSIENMLKRYGNInsVVPGH 240
Cdd:smart00849 158 ALESLLKLLKLLPKL--VVPGH 177
CphA_ImiS-like_MBL-B2 cd16306
Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and related metallo-beta-lactamases, ...
 69-240 5.88e-22

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: 90.78  E-value: 5.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  69 VPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAHSTALTAELAkKS 148
Cdd:cd16306   19 VQENSMVYFGAKGVTVVGATWTPDTARELHKLIKRVSRKPVLEVINTNYHTDRAGGNAYWKSIGAKVVSTRQTRDLM-KS 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 149 GYEEPLG----------DLQTVT-------NLKFGNTKVETFYPGKGHTEDNIVVWLPQYKILAGGCLVKsaeaKNLGNV 211
Cdd:cd16306   98 DWAEIVAftrkglpeypDLPLVLpnvvhdgDFTLQEGKVRAFYLGPAHTPDGIFVYFPDEQVLYGNCILK----EKLGNL 173

                        170       180
                 ....*....|....*....|....*....
gi 446665128 212 ADAYVNEWSTSIENMLKRYGNINSVVPGH 240
Cdd:cd16306  174 SFADVKAYPQTLERLKAMKLPIKTVIGGH 202
CphS_ImiS-like_MBL-B2 cd16287
metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas ...
 69-240 5.53e-19

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: 82.86  E-value: 5.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  69 VPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAHSTALTAELAK-- 146
Cdd:cd16287   19 VQENSMVYIGTDGITIIGATWTPETAETLYKEIRKVSPLPINEVINTNYHTDRAGGNAYWKTLGAKIVATQMTYDLQKsq 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 147 --------KSGYEE----PLGDLQTVTNLKFG--NTKVETFYPGKGHTEDNIVVWLPQYKILAGGCLVKsaeaKNLGNVA 212
Cdd:cd16287   99 wgsivnftRQGNNKypnlEKSLPDTVFPGDFNlqNGSIRAMYLGEAHTKDGIFVYFPAERVLYGNCILK----ENLGNMS 174

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446665128 213 DAYVNEWSTSIENM----LKRYGNINSVVPGH 240
Cdd:cd16287  175 FANRTEYPKTLEKLkgliEQGELKVDSIIAGH 206
Sfh-1-like_MBL-B2 cd16305
Serratia fonticola Sfh-I and related metallo-beta-lactamases, subclass B2; MBL-fold ...
 67-240 1.77e-16

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: 75.80  E-value: 1.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  67 EAVPSNGLVLNTSKGLVLVDSSWddklTKELIEMVEKKFQK----RVTDVIITHAHADRIGGIKTLKERGIKAHSTALTA 142
Cdd:cd16305   17 EYVQENSMVYIGTDGITIIGATW----TPETAETLEKEIRKvsplPIKEVINTNYHTDRAGGNAYWKTLGASIVSTQMTY 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 143 ELAK----------KSGY------EEPLGDLQTVTNLKFGNTKVETFYPGKGHTEDNIVVWLPQYKILAGGCLVKsaeaK 206
Cdd:cd16305   93 DLEKsqwgsivdftRQGNnkypnlEKSLPDTVYPGDFNLQNGSVRALYLGEAHTEDGIFVYFPAERVLYGNCILK----E 168

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446665128 207 NLGNVADAYVNEWSTSIENM--LKRYGN--INSVVPGH 240
Cdd:cd16305  169 KLGNMSFANRTEYPKTLKKLkgLIEQGElkVESIIAGH 206
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
66-240 2.27e-16

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 75.10  E-value: 2.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128   66 GEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAH--------- 136
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTGGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELAEATDVPVivvaeeare 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  137 -------STALTAELAKKSGYEEPLGDLQTVTNLKFGNTKVETFYPGKGHTEDNIVVWLPQYKILAGGCLVKSAE----A 205
Cdd:pfam00753  81 lldeelgLAASRLGLPGPPVVPLPPDVVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEigrlD 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 446665128  206 KNLGNVADAYVNEWSTSIENMLK-RYGNINSVVPGH 240
Cdd:pfam00753 161 LPLGGLLVLHPSSAESSLESLLKlAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 78-246 3.61e-16

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: 74.16  E-value: 3.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  78 TSKGLVLVDSSwdDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIK--AHstALTAELAKKsgyeEPLG 155
Cdd:cd16276   17 TDKGVIVVDAP--PSLGENLLAAIRKVTDKPVTHVVYSHNHADHIGGASIFKDEGATiiAH--EATAELLKR----NPDP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 156 DL----QTVTN---LKFGNTKVETFYPGKGHTEDNIVVWLPQYKILAGGCLV--KSAEAKNLGnvADAYVNEWstsIENM 226
Cdd:cd16276   89 KRpvptVTFDDeytLEVGGQTLELSYFGPNHGPGNIVIYLPKQKVLMAVDLInpGWVPFFNFA--GSEDIPGY---IEAL 163

                        170       180
                 ....*....|....*....|...
gi 446665128 227 --LKRYgNINSVVPGHG-EVGDK 246
Cdd:cd16276  164 deLLEY-DFDTFVGGHGnRLGTR 185
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 63-240 9.70e-14

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: 67.70  E-value: 9.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  63 SFNGEAVPSNG-LVLNTSKGLVLVDSSWDDKltKELIEMVEKKfQKRVTDVIITHAHADRIGGIKTLKER-GIKAHSTAL 140
Cdd:cd06262    2 RLPVGPLQTNCyLVSDEEGEAILIDPGAGAL--EKILEAIEEL-GLKIKAILLTHGHFDHIGGLAELKEApGAPVYIHEA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 141 TAELAKKSG------------YEEPLGDLQTVTNLKFGNTKVETFY-PgkGHTEDNIVVWLPQYKIL-AGGCLVKSAeak 206
Cdd:cd06262   79 DAELLEDPElnlaffgggplpPPEPDILLEDGDTIELGGLELEVIHtP--GHTPGSVCFYIEEEGVLfTGDTLFAGS--- 153

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446665128 207 nLGNVADAYVN--EWSTSIENMLKRYGNINSVVPGH 240
Cdd:cd06262  154 -IGRTDLPGGDpeQLIESIKKLLLLLPDDTVVYPGH 188
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 70-241 4.30e-10

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: 57.62  E-value: 4.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  70 PSNGLVLNTSKGLVLVDSSWDDKLtKELIEMVEKKF--QKRVTDVIITHAHADRIGGIKTLKER-GIK--AHS------- 137
Cdd:cd07721   10 PVNAYLIEDDDGLTLIDTGLPGSA-KRILKALRELGlsPKDIRRILLTHGHIDHIGSLAALKEApGAPvyAHEreapyle 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 138 ------TALTAELAKKSGYEEPLGDLQTVTNLKfGNTKVETFYPGK-----GHTEDNIVVWLPQYKILAGGCLVKSAEaK 206
Cdd:cd07721   89 gekpypPPVRLGLLGLLSPLLPVKPVPVDRTLE-DGDTLDLAGGLRvihtpGHTPGHISLYLEEDGVLIAGDALVTVG-G 166

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446665128 207 NLGNVADAYVNEWST---SIENMLKRygNINSVVPGHG 241
Cdd:cd07721  167 ELVPPPPPFTWDMEEaleSLRKLAEL--DPEVLAPGHG 202
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 74-198 1.61e-09

hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione hydrolase (EC 3.1.2.6, also known as, glyoxalase II; S-2-hydroxylacylglutathione hydrolase; hydroxyacylglutathione hydrolase; acetoacetylglutathione hydrolase). In the second step of the glycoxlase system this enzyme hydrolyzes S-d-lactoylglutathione to d-lactate and regenerates glutathione in the process. It has broad substrate specificity for glutathione thiol esters, hydrolyzing a number of these species to their corresponding carboxylic acids and reduced glutathione. It appears to hydrolyze 2-hydroxy thiol esters with greatest efficiency. It belongs to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 55.54  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  74 LVLNTSKGLVLVDSSWDDKLTKELiemveKKFQKRVTDVIITHAHADRIGGIKTLKER--GIK--AHStaltaeLAKKSG 149
Cdd:cd07723   14 IVDEATGEAAVVDPGEAEPVLAAL-----EKNGLTLTAILTTHHHWDHTGGNAELKALfpDAPvyGPA------EDRIPG 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446665128 150 YEEPLGDLQTVtnlKFGNTKVETFY-PgkGHTEDNIVVWLPQYKIL-------AGGC 198
Cdd:cd07723   83 LDHPVKDGDEI---KLGGLEVKVLHtP--GHTLGHICYYVPDEPALftgdtlfSGGC 134
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 70-142 2.53e-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) 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: 52.53  E-value: 2.53e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446665128  70 PSN-GLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKrVTDVIITHAHADRIGGIKTLKER-GIKAHSTALTA 142
Cdd:cd07743    7 PTNiGVYVFGDKEALLIDSGLDEDAGRKIRKILEELGWK-LKAIINTHSHADHIGGNAYLQKKtGCKVYAPKIEK 80
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 80-241 4.85e-08

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: 52.12  E-value: 4.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  80 KGLVLVDSSWDDKLTKELIEMVEKKFQKR-VTDVIITHAHADRIGGIKTLKERG------IKAHSTaLTAELAKKSGYEE 152
Cdd:cd07710   27 TGLIIIDTLESAEAAKAALELFRKHTGDKpVKAIIYTHSHPDHFGGAGGFVEEEdsgkvpIIAPEG-FMEEAVSENVLAG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 153 PL---------------GDLQTVT-----------------NLKFGNTKVE--------TFYPGKGHTEDNIVVWLPQYK 192
Cdd:cd07710  106 NAmsrraayqfgallpkGEKGQVGaglgpglstgtvgfippTITITETGETltidgvelEFQHAPGEAPDEMMVWLPDYK 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446665128 193 ILAGGCLVksaeAKNLGNVadaY---------VNEWSTSIENMLKRygNINSVVPGHG 241
Cdd:cd07710  186 VLFCADNV----YHTFPNL---YtlrgakyrdALAWAKSLDEAISL--KAEVLFPSHT 234
BaeB-like_MBL-fold cd16275
Bacillus amyloliquefaciens BaeB and related proteins; MBL-fold metallo hydrolase domain; ...
 83-180 5.34e-08

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


Pssm-ID: 293833 [Multi-domain]  Cd Length: 174  Bit Score: 51.38  E-value: 5.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  83 VLVDSSWD-DKLTKELiemveKKFQKRVTDVIITHAHADRIGGIKTLKER-GIKAHSTALTAELakksgYEEPLGDLQTV 160
Cdd:cd16275   26 AVVDPAWDiEKILAKL-----NELGLTLTGILLTHSHFDHVNLVEPLLAKyDAPVYMSKEEIDY-----YGFRCPNLIPL 95

                         90       100
                 ....*....|....*....|...
gi 446665128 161 ---TNLKFGNTKVeTFYPGKGHT 180
Cdd:cd16275   96 edgDTIKIGDTEI-TCLLTPGHT 117
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 83-241 6.89e-08

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: 51.72  E-value: 6.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  83 VLVDSsWDDKLTKELIEMVEKKFQ-KRVTDVIITHAHADRIGGIKTLKER--GIKAHSTALTAELAK------------- 146
Cdd:cd07709   43 ALIDT-VKEPFFDEFLENLEEVIDpRKIDYIVVNHQEPDHSGSLPELLELapNAKIVCSKKAARFLKhfypgiderfvvv 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 147 KSGYEEPLGDlqtvTNLKFgntkVETFYPgkgHTEDNIVVWLPQYKIL----AGGCLVKSAE--AKNLGNVADA------ 214
Cdd:cd07709  122 KDGDTLDLGK----HTLKF----IPAPML---HWPDTMVTYDPEDKILfsgdAFGAHGASGElfDDEVEDYLEEarryya 190

                        170       180       190
                 ....*....|....*....|....*....|
gi 446665128 215 -YVNEWSTSIENMLKRYG--NINSVVPGHG 241
Cdd:cd07709  191 nIMGPFSKQVRKALEKLEalDIKMIAPSHG 220
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 83-240 8.75e-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) 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: 50.96  E-value: 8.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  83 VLVDSSWDDKLTKELIEMVeKKFQKRVTDVIITHAHADRIGGIKTLKER--GIKAHSTALTAE-----LAKKSGYEEPLG 155
Cdd:cd07739   28 VLVDAQFTRADAERLADWI-KASGKTLTTIYITHGHPDHYFGLEVLLEAfpDAKVVATPAVVAhikaqLEPKLAFWGPLL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 156 DLQTVTNL-----KFGNT------KVETFYPGKGHTEDNIVVWLPQYKILAGGCLVKS------AEAKNlgnvaDAYVNE 218
Cdd:cd07739  107 GGNAPARLvvpepLDGDTltleghPLEIVGVGGGDTDDTTYLWIPSLKTVVAGDVVYNgvhvwlADATT-----PELRAA 181

                        170       180
                 ....*....|....*....|..
gi 446665128 219 WSTSIENMLKRygNINSVVPGH 240
Cdd:cd07739  182 WLAALDKIEAL--NPETVVPGH 201
metallo-hydrolase-like_MBL-fold cd16280
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 75-181 2.98e-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: 293838 [Multi-domain]  Cd Length: 251  Bit Score: 49.89  E-value: 2.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  75 VLNTSKGLVLVDSSWDDKLTKELIEMVEK-KFQ-KRVTDVIITHAHADRIGGIKTLKER-GIK-------AHSTALTAEL 144
Cdd:cd16280   26 AIDTGDGLILIDALNNNEAADLIVDGLEKlGLDpADIKYILITHGHGDHYGGAAYLKDLyGAKvvmseadWDMMEEPPEE 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446665128 145 AKKSGYEEP------LGDLQTVTnlkFGNTKVeTFYPGKGHTE 181
Cdd:cd16280  106 GDNPRWGPPperdivIKDGDTLT---LGDTTI-TVYLTPGHTP 144
NorV COG0426
Flavorubredoxin [Energy production and conversion];
83-241 3.93e-07

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 50.22  E-value: 3.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  83 VLVDSsWDDKLTKELIEMVEKKFQ-KRVTDVIITHAHADRIGGIKTLKER--GIKAHSTALTAELAKKSgYEEPLGDLQT 159
Cdd:COG0426   45 ALIDT-VGESFFEEFLENLSKVIDpKKIDYIIVNHQEPDHSGSLPELLELapNAKIVCSKKAARFLPHF-YGIPDFRFIV 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 160 VTN---LKFGNTK---VETFYPgkgHTEDNIVVWLPQYKIL----AGGCLVKSAE--AKNLGNVADA-----YVNEW--- 219
Cdd:COG0426  123 VKEgdtLDLGGHTlqfIPAPML---HWPDTMFTYDPEDKILfsgdAFGSHGASDElfDDEVDEHLEEearryYANIMmpf 199

                        170       180
                 ....*....|....*....|....
gi 446665128 220 STSIENMLKRYGN--INSVVPGHG 241
Cdd:COG0426  200 SKQVLKALKKVRGldIDMIAPSHG 223
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 71-243 6.27e-07

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: 48.30  E-value: 6.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  71 SNGLVLNTSKGLVLVDS-----SWDDKLTKELIEMVekkfQKRVTDVIITHAHADRIGGIKTLKER----GIKAHSTALT 141
Cdd:cd07722   18 TNTYLVGTGKRRILIDTgegrpSYIPLLKSVLDSEG----NATISDILLTHWHHDHVGGLPDVLDLlrgpSPRVYKFPRP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 142 AELAKKSGYEEPLGDLQTVTNLKFGNTKVETFY-PgkGHTEDNIVVWLPQYKIL-AGGCLvksaeaknLGnvadayvnEW 219
Cdd:cd07722   94 EEDEDPDEDGGDIHDLQDGQVFKVEGATLRVIHtP--GHTTDHVCFLLEEENALfTGDCV--------LG--------HG 155

                        170       180       190
                 ....*....|....*....|....*....|..
gi 446665128 220 STSIEN----M--LKRYGNINSVV--PGHGEV 243
Cdd:cd07722  156 TAVFEDlaayMasLKKLLSLGPGRiyPGHGPV 187
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 96-240 9.92e-06

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


Pssm-ID: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 44.93  E-value: 9.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  96 ELIEMVEKKFQKRVTdVIITHAHADRIGGIKTLKERGIKAHSTALtaeLAKKSGYEEPLGDLQTVTNLKFGNTKV----E 171
Cdd:cd07712   31 DLKEYVRTLTDLPLL-VVATHGHFDHIGGLHEFEEVYVHPADAEI---LAAPDNFETLTWDAATYSVPPAGPTLPlrdgD 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446665128 172 TFYPGK---------GHTEDNIVVWLPQYKILAGGCLVKSAEAKNLGNVADayVNEWSTSIENMLKRYGNINSVVPGH 240
Cdd:cd07712  107 VIDLGDrqlevihtpGHTPGSIALLDRANRLLFSGDVVYDGPLIMDLPHSD--LDDYLASLEKLSKLPDEFDKVLPGH 182
RnjA COG0595
mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];
106-173 1.80e-05

mRNA degradation ribonuclease J1/J2 [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440360 [Multi-domain]  Cd Length: 553  Bit Score: 45.44  E-value: 1.80e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446665128 106 QKRVTDVIITHAHADRIGGIK-TLKERGIKAHSTALTAELAKKSGYEEPLG---DLQTVTN---LKFGNTKVETF 173
Cdd:COG0595   61 KDKIKGIVLTHGHEDHIGALPyLLKELNVPVYGTPLTLALLEAKLKEHGLLkkvKLHVVKPgdrIKFGPFKVEFF 135
RNaseJ_MBL-fold cd07714
RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a ...
 103-173 3.18e-05

RNAaseJ, MBL-fold metallo-hydrolase domain; RNase J, also called Ribonuclease J, is a prokaryotic ribonuclease which plays a key part in RNA processing and in RNA degradation. It can act as an endonuclease which is specific for single-stranded regions of RNA irrespective of their sequence or location, and as a processive 5' exonuclease which only acts on substrates having a single phosphate or a hydroxyl at the 5' end. Many bacterial species have only one RNase J, but some, such as Bacillus subtilis, have two. 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: 293800 [Multi-domain]  Cd Length: 248  Bit Score: 43.93  E-value: 3.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446665128 103 KKFQKRVTDVIITHAHADRIGGI-KTLKERGIKAHSTALTAELAKKSGYEEPLG---DLQTV---TNLKFGNTKVETF 173
Cdd:cd07714   50 EENKDKIKGIFITHGHEDHIGALpYLLPELNVPIYATPLTLALIKKKLEEFKLIkkvKLNEIkpgERIKLGDFEVEFF 127
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 72-243 4.33e-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: 4.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  72 NGLVLNTSKGLVLVDS----SWDDKLTKELIEMVEKKFQkRVTDVIITHAHADRIGGIKTLKERGIkahstaltAELAKK 147
Cdd:cd07725   16 NVYLLRDGDETTLIDTglatEEDAEALWEGLKELGLKPS-DIDRVLLTHHHPDHIGLAGKLQEKSG--------ATVYIL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 148 SgyEEPLGDLQTVTNLKFGNTKVETfyPgkGHTEDNIVVWLPQYKILAGGCLV-------KSAEAKNLGNVADAYVNEWS 220
Cdd:cd07725   87 D--VTPVKDGDKIDLGGLRLKVIET--P--GHTPGHIVLYDEDRRELFVGDAVlpkitpnVSLWAVRVEDPLGAYLESLD 160

                        170       180
                 ....*....|....*....|...
gi 446665128 221 tSIENMlkrygNINSVVPGHGEV 243
Cdd:cd07725  161 -KLEKL-----DVDLAYPGHGGP 177
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 83-199 4.63e-05

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: 42.77  E-value: 4.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  83 VLVDSSWDDklTKELIEMVEKKfQKRVTDVIITHAHADRIGGIKTLKER-GIK-AHStaltaELAKKSGYEEPLGDLQTv 160
Cdd:cd07724   26 AVIDPVRDS--VDRYLDLAAEL-GLKITYVLETHVHADHVSGARELAERtGAPiVIG-----EGAPASFFDRLLKDGDV- 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446665128 161 tnLKFGNTKVETFY-PgkGHTEDNI-VVWLPQYKILAGGCL 199
Cdd:cd07724   97 --LELGNLTLEVLHtP--GHTPESVsYLVGDPDAVFTGDTL 133
OPHC2-like_MBL-fold cd07720
Pseudomonas pseudoalcaligenes organophosphorus hydrolase C2, and related proteins; MBL-fold ...
 64-125 3.71e-04

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: 40.99  E-value: 3.71e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446665128  64 FNGEAVPS--NGLVLNTSKGLVLVDS-------SWDDKLTKELIEM-VEkkfQKRVTDVIITHAHADRIGGI 125
Cdd:cd07720   40 LPPDPVETsvNAFLVRTGGRLILVDTgagglfgPTAGKLLANLAAAgID---PEDIDDVLLTHLHPDHIGGL 108
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 72-173 6.65e-04

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


Pssm-ID: 293819 [Multi-domain]  Cd Length: 151  Bit Score: 39.17  E-value: 6.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  72 NGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQkRVTDVIITHAHADRIGGIKTLKER-GIKAHSTALTAELAKKSGY 150
Cdd:cd07733   10 NCTYLETEDGKLLIDAGLSGRKITGRLAEIGRDPE-DIDAILVTHEHADHIKGLGVLARKyNVPIYATAGTLRAMERKVG 88

                         90       100
                 ....*....|....*....|....*.
gi 446665128 151 EEPLGDLQTV---TNLKFGNTKVETF 173
Cdd:cd07733   89 LIDVDQKQIFepgETFSIGDFDVESF 114
YSH1 COG1236
RNA processing exonuclease, beta-lactamase fold, Cft2 family [Translation, ribosomal structure ...
 107-146 7.30e-04

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


Pssm-ID: 440849 [Multi-domain]  Cd Length: 404  Bit Score: 40.17  E-value: 7.30e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446665128 107 KRVTDVIITHAHADRIGGIKTLKERGIKA--HSTALTAELAK 146
Cdd:COG1236   49 SDVDAVVLTHAHLDHSGALPLLVKEGFRGpiYATPATADLAR 90
ComA-like_MBL-fold cd07731
Competence protein ComA, ComEC and related proteins; MBL-fold metallo hydrolase domain; This ...
 112-240 2.08e-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: 37.88  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 112 VIITHAHADRIGGIKTLKER--------GIKAHSTA-----LTAELAKKSGYEEPL-GDlqtvtNLKFGNTKVETFYPGK 177
Cdd:cd07731   52 LILTHPDADHIGGLDAVLKNfpvkevymPGVTHTTKtyedlLDAIKEKGIPVTPCKaGD-----RWQLGGVSFEVLSPPK 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446665128 178 GHTEDN----IVVWL--PQYKILAGGCLVKSAEaknlgnvadayvnewstsiENMLKRYGNINS---VVPGH 240
Cdd:cd07731  127 DDYDDLnnnsCVLRLtyGGTSFLLTGDAEKEAE-------------------EELLASGPDLLAdvlKVGHH 179
MBL-B3-like cd07708
metallo-beta-lactamases, subclass B3; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 74-131 2.33e-03

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: 38.30  E-value: 2.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446665128  74 LVLNTSKGLVLVDSSwddklTKELIEMVEKKFQKR---VTDV---IITHAHADRIGGIKTLKER 131
Cdd:cd07708   25 YLIVTPQGNILIDGD-----MEQNAPMIKANIKKLgfkFSDTkliLISHAHFDHAGGSAEIKKQ 83
metallo-hydrolase-like_MBL-fold cd16278
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 108-194 2.49e-03

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


Pssm-ID: 293836 [Multi-domain]  Cd Length: 185  Bit Score: 37.86  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128 108 RVTDVIITHAHADRIGGIKTLKERG---IKAHSTALTAELAKKSGYEEPLGDLQTVTnlkFGNTKVETFY-PgkGHTEDN 183
Cdd:cd16278   53 RVSAILVTHTHRDHSPGAARLAERTgapVRAFGPHRAGGQDTDFAPDRPLADGEVIE---GGGLRLTVLHtP--GHTSDH 127

                         90
                 ....*....|.
gi 446665128 184 IVVWLPQYKIL 194
Cdd:cd16278  128 LCFALEDEGAL 138
TTHA0252-CPSF-like_MBL-fold cd16295
Thermus thermophilus TTHA0252 and related cleavage and polyadenylation specificity factors; ...
 107-146 3.68e-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: 37.44  E-value: 3.68e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446665128 107 KRVTDVIITHAHADRIGGIKTLKERGIKA--HSTALTAELAK 146
Cdd:cd16295   50 KEIDAVILTHAHLDHSGRLPLLVKEGFRGpiYATPATKDLAE 91
PhnP COG1235
Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase [Inorganic ion transport and metabolism]; ...
 72-173 7.03e-03

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


Pssm-ID: 440848 [Multi-domain]  Cd Length: 259  Bit Score: 36.80  E-value: 7.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446665128  72 NGLVLNTSKGLVLVDSSWDdklTKELIEMVEKKFqKRVTDVIITHAHADRIGGIKTLKER----GIKAHSTALTAE-LAK 146
Cdd:COG1235   36 SSILVEADGTRLLIDAGPD---LREQLLRLGLDP-SKIDAILLTHEHADHIAGLDDLRPRygpnPIPVYATPGTLEaLER 111

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446665128 147 KSGYEEPLG----DLQTVTN---LKFGNTKVETF 173
Cdd:COG1235  112 RFPYLFAPYpgklEFHEIEPgepFEIGGLTVTPF 145
 
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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