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Conserved domains on  [gi|114333358|gb|ABI70740|]
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Beta-lactamase [Shewanella frigidimarina NCIMB 400]

Protein Classification

DIM/GIM/SIM family subclass B1 metallo-beta-lactamase( domain architecture ID 10888857)

DIM/GIM/SIM 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
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 ...
 40-254 1.85e-125

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: 355.05  E-value: 1.85e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  40 KANQAQATQIQLFEYQSYFKTDDFGLVDANGLVVVEGKDAYLIDTPWSEKDTIALVEWIKQQNFILKASISTHSHADRTA 119
Cdd:cd16301    1 PKLKIEKLSDGVYLHTSYKEVEGWGLVDANGLVVVDGKEAYLIDTPWSESDTEKLVEWIKAQGLTLKASISTHFHEDRTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 120 GISYLNSIGVSTHVSAMTQKILTTQHKALASQPFDGDSFTLANGLLEARYLGAGHTIDNIVVWLPKAQLLFGGCLVKSAH 199
Cdd:cd16301   81 GIGYLNSHSIPTYASELTNQLLKKNGKELATHSFSGDEFWLLKGKIEVFYPGAGHTKDNLVVWLPKEKILFGGCLVKSLE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 114333358 200 SKSMGYIAEASLTDWPVTISKVKATFVDAEVVVPGHGAIGNAGLLNHTQELVNIY 254
Cdd:cd16301  161 SKGLGNTGDASISQWPASAQKVLSKYPNAKLVVPGHGKVGDVSLLEHTRKLAKKA 215
 
Name Accession Description Interval E-value
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 ...
 40-254 1.85e-125

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: 355.05  E-value: 1.85e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  40 KANQAQATQIQLFEYQSYFKTDDFGLVDANGLVVVEGKDAYLIDTPWSEKDTIALVEWIKQQNFILKASISTHSHADRTA 119
Cdd:cd16301    1 PKLKIEKLSDGVYLHTSYKEVEGWGLVDANGLVVVDGKEAYLIDTPWSESDTEKLVEWIKAQGLTLKASISTHFHEDRTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 120 GISYLNSIGVSTHVSAMTQKILTTQHKALASQPFDGDSFTLANGLLEARYLGAGHTIDNIVVWLPKAQLLFGGCLVKSAH 199
Cdd:cd16301   81 GIGYLNSHSIPTYASELTNQLLKKNGKELATHSFSGDEFWLLKGKIEVFYPGAGHTKDNLVVWLPKEKILFGGCLVKSLE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 114333358 200 SKSMGYIAEASLTDWPVTISKVKATFVDAEVVVPGHGAIGNAGLLNHTQELVNIY 254
Cdd:cd16301  161 SKGLGNTGDASISQWPASAQKVLSKYPNAKLVVPGHGKVGDVSLLEHTRKLAKKA 215
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 63-254 2.02e-24

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: 97.07  E-value: 2.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  63 FGLVDANGLVVVEGKDAYLIDTPWSEKDTIALVEWIKQQNFILKASISTHSHADRTAGISYL-NSIGVSTHVSAMTQKIL 141
Cdd:COG0491   10 GAGLGVNSYLIVGGDGAVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALaEAFGAPVYAHAAEAEAL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 142 TTQHKA--------LASQPF-DGDSFTLANGLLEARYLGaGHTIDNIVVWLPKAQLLFGGCLVksaHSKSMGYIA--EAS 210
Cdd:COG0491   90 EAPAAGalfgrepvPPDRTLeDGDTLELGGPGLEVIHTP-GHTPGHVSFYVPDEKVLFTGDAL---FSGGVGRPDlpDGD 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 114333358 211 LTDWPVTISKVKATfvDAEVVVPGHGAIGNAGLLNHTQELVNIY 254
Cdd:COG0491  166 LAQWLASLERLLAL--PPDLVIPGHGPPTTAEAIDYLEELLAAL 207
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 69-235 7.62e-18

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: 78.75  E-value: 7.62e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358    69 NGLVVVEGKDAYLIDTPWSEKDtiALVEWIKQQNFI-LKASISTHSHADRTAGISYLNSI-GVSTHVSAMTQKILTTQHK 146
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAE--DLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLEApGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358   147 ALASQPF------------DGDSFTLANGLLEARYLgAGHTIDNIVVWLPKAQLLFGGCLVKS-AHSKSMGYIAEASLTD 213
Cdd:smart00849  79 LLGELGAeaepappdrtlkDGDELDLGGGELEVIHT-PGHTPGSIVLYLPEGKILFTGDLLFAgGDGRTLVDGGDAAASD 157

                          170       180
                   ....*....|....*....|..
gi 114333358   214 WPVTISKVKATfvDAEVVVPGH 235
Cdd:smart00849 158 ALESLLKLLKL--LPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
64-235 5.62e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 57.38  E-value: 5.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358   64 GLVDANGLVVVEGKDAYLIDT-PWSEKDTIALVEWIKQQNFILKASISTHSHADRTAGISYL-NSIGVSTHVSAMTQKIL 141
Cdd:pfam00753   2 GPGQVNSYLIEGGGGAVLIDTgGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELaEATDVPVIVVAEEAREL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  142 TTQHKALASQ----------------PFDGDSFTLANGLLEARYLGAGHTIDNIVVWLPKAQLLFGGCLVKSAHSKSMGY 205
Cdd:pfam00753  82 LDEELGLAASrlglpgppvvplppdvVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDL 161

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 114333358  206 IAEASLTDWPVTISKVKATFV-----DAEVVVPGH 235
Cdd:pfam00753 162 PLGGLLVLHPSSAESSLESLLklaklKAAVIVPGH 196
 
Name Accession Description Interval E-value
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 ...
 40-254 1.85e-125

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: 355.05  E-value: 1.85e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  40 KANQAQATQIQLFEYQSYFKTDDFGLVDANGLVVVEGKDAYLIDTPWSEKDTIALVEWIKQQNFILKASISTHSHADRTA 119
Cdd:cd16301    1 PKLKIEKLSDGVYLHTSYKEVEGWGLVDANGLVVVDGKEAYLIDTPWSESDTEKLVEWIKAQGLTLKASISTHFHEDRTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 120 GISYLNSIGVSTHVSAMTQKILTTQHKALASQPFDGDSFTLANGLLEARYLGAGHTIDNIVVWLPKAQLLFGGCLVKSAH 199
Cdd:cd16301   81 GIGYLNSHSIPTYASELTNQLLKKNGKELATHSFSGDEFWLLKGKIEVFYPGAGHTKDNLVVWLPKEKILFGGCLVKSLE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 114333358 200 SKSMGYIAEASLTDWPVTISKVKATFVDAEVVVPGHGAIGNAGLLNHTQELVNIY 254
Cdd:cd16301  161 SKGLGNTGDASISQWPASAQKVLSKYPNAKLVVPGHGKVGDVSLLEHTRKLAKKA 215
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 58-252 5.31e-81

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: 242.19  E-value: 5.31e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  58 FKTDDFGLVDANGLVVVEGKDAYLIDTPWSEKDTIALVEWIKQQ-NFILKASISTHSHADRTAGISYLNSIGVSTHVSAM 136
Cdd:cd16285   16 LAEFNGGAVPSNGLIVIDGKGLVLIDTPWTEAQTATLLDWIEKKlGKPVTAAISTHSHDDRTGGIKALNARGIPTYATAL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 137 TQKILTTQHKALASQPFDgDSFTLANGLLEARYLGAGHTIDNIVVWLPKAQLLFGGCLVKSAHSKSMGYIAEASLTDWPV 216
Cdd:cd16285   96 TNELAKKEGKPVPTHSLK-GALTLGFGPLEVFYPGPGHTPDNIVVWLPKSKILFGGCLVKSASATSLGNVGDADVEAWPK 174

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 114333358 217 TISKVKATFVDAEVVVPGHGAIGNAGLLNHTQELVN 252
Cdd:cd16285  175 SIENLKAKYPEARMVVPGHGAPGGTELLDHTLDLAK 210
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 50-252 1.13e-66

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: 205.94  E-value: 1.13e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  50 QLFEYQSYFKTDDFGLVDANGLVVVEGKDAYLIDTPWSEKDTIALVEWIKQQ-NFILKASISTHSHADRTAGISYLNSIG 128
Cdd:cd16302    9 HVYVHVSYLETETFGKVPCNGMIVINGGEAVVFDTPTNDSQSEELIDWIENSlKAKVKAVVPTHFHDDCLGGLKAFHRRG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 129 VSTHVSAMTQKILTtQHKALASQPFDGDSFTLANG--LLEARYLGAGHTIDNIVVWLPKAQLLFGGCLVKSAhSKSMGYI 206
Cdd:cd16302   89 IPSYANQKTIALAK-EKGLPVPQHGFSDSLTLKLGgkKIVCRYFGEGHTKDNIVVYFPSEKVLFGGCMVKSL-GAGKGNL 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 114333358 207 AEASLTDWPVTISKVKATFVDAEVVVPGHGAIGNAGLLNHTQELVN 252
Cdd:cd16302  167 EDANVEAWPKTVEKVKAKYPDVKIVIPGHGKIGGSELLDYTIDLFK 212
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 66-251 4.32e-58

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: 184.03  E-value: 4.32e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  66 VDANGLVVVEGKDAYLIDTPWSEKDTIALVEWIKQqNFI--LKASISTHSHADRTAGISYLNSIGVSTHVSAMTQKILTT 143
Cdd:cd16304   24 VPSNGLIVETSKGVVLIDTPWDDEQTEELLDWIKK-KLKkpVTLAIVTHAHDDRIGGIKALQKRGIPVYSTKLTAQLAKK 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 144 QHKALASQPFDGDS-FTLANGLLEARYLGAGHTIDNIVVWLPKAQLLFGGCLVKSAHSKSMGYIAEASLTDWPVTISKVK 222
Cdd:cd16304  103 QGYPSPDGILKDDTtLKFGNTKIETFYPGEGHTADNIVVWLPQSKILFGGCLVKSLEAKDLGNTADANLKEWPTSIRNVL 182

                        170       180
                 ....*....|....*....|....*....
gi 114333358 223 ATFVDAEVVVPGHGAIGNAGLLNHTQELV 251
Cdd:cd16304  183 KRYPNAEIVVPGHGEWGDKQLLRHTLDLL 211
IND_BlaB-like_MBL-B1 cd16299
IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 50-252 5.76e-57

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: 181.10  E-value: 5.76e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  50 QLFEYQSYfktDDFGLVD--ANGLVVVEGKDAYLIDTPWSEKDTIALVEWIKQQ-NFILKASISTHSHADRTAGISYLNS 126
Cdd:cd16299    9 NLYIYTTY---NEFNGVKysANAMYLVTKKGVILFDTPWDKDQYQPLLDSIRKKhNLPVIAVIATHSHEDRAGGLGYFNK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 127 IGVSTHVSAMTQKILTTQHKALASQPFD-GDSFTLANGLLEARYLGAGHTIDNIVVWLPKAQLLFGGCLVKSAHSKSMGY 205
Cdd:cd16299   86 IGIPTYATAMTNSILKKENKPQATYLIEtDKTYKIGGEKFVVYFFGEGHTADNVVVWFPKEKVLDGGCLIKSAEATDLGY 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 114333358 206 IAEASLTDWPVTISKVKATFVDAEVVVPGHGAIGNAGLLNHTQELVN 252
Cdd:cd16299  166 IGEANVKEWPKTIHKLKQKFKKAKVVIPGHDEWKDQGHIENTLKLLN 212
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 62-251 5.51e-54

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: 173.88  E-value: 5.51e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  62 DFGLVDANGLVVVEGKDAYLIDTPWSEKDTIALVEWIKQQnFILKAS--ISTHSHADRTAGISYLNSIGVSTHVSAMTQK 139
Cdd:cd07707   15 DLGSVPSNGLVYNGSKGLVLVDSTWTPKTTKELIKEIEKV-SQKPVTevINTHFHTDRAGGNAYLKERGAKTVSTALTRD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 140 ILTTQ------------------HKALASQPFDGDsFTLANGLLEARYLGAGHTIDNIVVWLPKAQLLFGGCLVKsahSK 201
Cdd:cd07707   94 LAKSEwaeivaftrkglpeypdlGYELPDGVLDGD-FNLQFGKVEAFYPGPAHTPDNIVVYFPQENVLYGGCIIK---ET 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 114333358 202 SMGYIAEASLTDWPVTISKVKATFVDAEVVVPGHGAIGNAGLLNHTQELV 251
Cdd:cd07707  170 DLGNVADADVKEWPTSIERLKKRYRNIKAVIPGHGEVGGPELLDHTLDLL 219
MUS_TUS_MBL-B1 cd16318
Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; ...
 28-254 3.06e-52

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: 169.07  E-value: 3.06e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  28 LTITPLSSNALVkanqaqATQIQLFEYQSYfktddfglvDANGLVVVEGKDAYLIDTPWSEKDTIALVEWIKQQ-NFILK 106
Cdd:cd16318    1 LKIKQLNDNMYI------YTTYQEFQGVTY---------SSNSMYVLTDEGVILIDTPWDKDQYEPLLEYIRSNhNKEVK 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 107 ASISTHSHADRTAGISYLNSIGVSTHVSAMTQKILTTQHKALASQPFDGD-SFTLANGLLEARYLGAGHTIDNIVVWLPK 185
Cdd:cd16318   66 WVITTHFHEDRSGGLGYFNSIGAQTYTYALTNEILKERNEPQAQFSFNKEkQFTFGNEKLAVYFLGEGHSLDNTVVWFPK 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114333358 186 AQLLFGGCLVKSAHSKSMGYIAEASLTDWPVTISKVKATFVDAEVVVPGHGAIGNAGLLNHTQELVNIY 254
Cdd:cd16318  146 EEVLYGGCLIKSAEATTIGNIADGNVIAWPKTIEAVKQKFKNAKVIIPGHDEWDMSGHIENTERILSAY 214
BlaB-like_MBL-B1 cd16316
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and related ...
 54-254 2.76e-50

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: 164.17  E-value: 2.76e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  54 YQSYFKTddfgLVDANGLVVVEGKDAYLIDTPWSEKDTIALVEWI-KQQNFILKASISTHSHADRTAGISYLNSIGVSTH 132
Cdd:cd16316   16 YNTYKGT----KTAANAVYVVTDKGVVVIDAPWDETQFQPFLDSIqKKHHKKVIMNIATHSHDDRAGGLEYFGKKGAKTY 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 133 VSAMTQKILTTQHKALASQPFDGD-SFTLANGLLEARYLGAGHTIDNIVVWLPKAQLLFGGCLVKSAHSKSMGYIAEASL 211
Cdd:cd16316   92 TTKLTDSILKKNNKPRAEYTFDNDtTFKVGKYEFQVYYPGKGHTADNIVVWFPKEKVLYGGCLIKSADAKDLGYLGEAYV 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 114333358 212 TDWPVTISKVKATFVDAEVVVPGHGAIGNAGLLNHTQELVNIY 254
Cdd:cd16316  172 NDWTQSIHNIQQKFPNPQYVIAGHDDWKDQTSLQHTLKLISEY 214
VIM_type_MBL-B1 cd16303
VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona ...
 68-252 1.52e-47

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: 157.33  E-value: 1.52e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  68 ANGLVVVEGKDAYLIDTPWSEKDTIALVEWI-KQQNFILKASISTHSHADRTAGISYLNSIGVSTHVSAMTQKILTTQHK 146
Cdd:cd16303   28 SNGLIVRDGDELLLIDTAWGAKNTAALLAEIeKQIGLPVTRAVSTHFHDDRVGGVDVLRAAGVATYASPSTRRLAEAEGN 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 147 ALASQPFDGDSFTLAN---GLLEARYLGAGHTIDNIVVWLPKAQLLFGGCLVKSAHSKSMGYIAEASLTDWPVTISKVKA 223
Cdd:cd16303  108 EIPTHSLEGLSSSGDAvrfGPVELFYPGAAHSTDNLVVYVPSARVLYGGCAVRELSSTSAGNVADADLAEWPTSIERIQK 187

                        170       180
                 ....*....|....*....|....*....
gi 114333358 224 TFVDAEVVVPGHGAIGNAGLLNHTQELVN 252
Cdd:cd16303  188 HYPEAEFVIPGHGLPGGLDLLHHTKNVVK 216
IND_MBL-B1 cd16317
Chryseobacterium indologenes IND-1, IND-2, IND-7and related metallo-beta-lactamases, subclass ...
 68-252 2.23e-43

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: 146.32  E-value: 2.23e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  68 ANGLVVVEGKDAYLIDTPWSEKDTIALVEWI-KQQNFILKASISTHSHADRTAGISYLNSIGVSTHVSAMTQKILTTQHK 146
Cdd:cd16317   28 ANAVYLVTKKGVVLFDVPWQKVQYQSLMDTIqKRHHLPVIAVFATHSHDDRAGDLSFYNNKGIKTYATAKTNEFLKKDGK 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 147 ALASQPFD-GDSFTLANGLLEARYLGAGHTIDNIVVWLPKAQLLFGGCLVKSAHSKSMGYIAEASLTDWPVTISKVKATF 225
Cdd:cd16317  108 ATSTEIIKtGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKVLDGGCLVKSNSATDLGYTGEANVEQWPKTMNKLKAKY 187

                        170       180
                 ....*....|....*....|....*..
gi 114333358 226 VDAEVVVPGHGAIGNAGLLNHTQELVN 252
Cdd:cd16317  188 AQATLIIPGHDEWKGGGHVEHTLDLLN 214
NDM_FIM-like_MBL-B1 cd16300
NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase ...
 56-250 7.59e-38

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: 132.25  E-value: 7.59e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  56 SYFKTDDFGLVDANGLVVVEGKDAYLIDTPWSEKDTIALVEWIKQQ-NFILKASISTHSHADRTAGISYLNSIGVSTHVS 134
Cdd:cd16300   15 SYLDMPGFGAVPSNGLIVRDGDRVLLVDTAWTDDQTAQILNWAKQElNLPVRLAVVTHAHQDKMGGMDALHAAGIATYAN 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 135 AMTQKiLTTQHKALASQP---FDGDSFTLANGLLEARYLGAGHTIDNIVVWLPKAQLLFGGCLVKSAHSKSMGYIAEASL 211
Cdd:cd16300   95 ALSNQ-LAPQEGLVPAQHsltFAAEPSTAPNFPLKVFYPGPGHTRDNIVVGIDGTGIAFGGCLIRPSKATSLGNLADADT 173

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 114333358 212 TDWPVTISKVKATFVDAEVVVPGHGAIGNAGLLNHTQEL 250
Cdd:cd16300  174 EHWAASARAFGAAFPDASMIVPSHGAPDGRAAITHTARL 212
SPM-1-like_MBL-B1-B2-like cd16286
Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; ...
 68-247 1.05e-30

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: 114.17  E-value: 1.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  68 ANGLVVVEG-KDAYLIDTPWSEKDTIALVEWI----KQQNFIlkaSISTHSHADRTAGISYLNSIGVSTHVSAMTQKILT 142
Cdd:cd16286   27 SNVLVVKMLdGTVVIVDSPYTNLATQTVLDWIaktmGPRKVV---AINTHFHLDGTGGNEALKKRGIPTWGSDLTKQLLL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 143 ------------------------TQHKALASQPFD---GDSFTLANGLLEARYLGAGHTIDNIVVWLPKAQLLFGGCLV 195
Cdd:cd16286  104 ergkadrikaaeflknedlkrrieSSPPVPPDNVFDlkeGKVFSFGNELVEVSFPGPAHAPDNVVVYFPERKILFGGCMI 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 114333358 196 KSAhsKSMGYIAEASLTDWPVTISKVKAtfVDAEVVVPGHGAIGNAGLLNHT 247
Cdd:cd16286  184 KPG--KELGNLGDANMKAWPDSVRRLKK--FDAKIVIPGHGERGDPGMVNKT 231
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 63-254 2.02e-24

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: 97.07  E-value: 2.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  63 FGLVDANGLVVVEGKDAYLIDTPWSEKDTIALVEWIKQQNFILKASISTHSHADRTAGISYL-NSIGVSTHVSAMTQKIL 141
Cdd:COG0491   10 GAGLGVNSYLIVGGDGAVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALaEAFGAPVYAHAAEAEAL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 142 TTQHKA--------LASQPF-DGDSFTLANGLLEARYLGaGHTIDNIVVWLPKAQLLFGGCLVksaHSKSMGYIA--EAS 210
Cdd:COG0491   90 EAPAAGalfgrepvPPDRTLeDGDTLELGGPGLEVIHTP-GHTPGHVSFYVPDEKVLFTGDAL---FSGGVGRPDlpDGD 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 114333358 211 LTDWPVTISKVKATfvDAEVVVPGHGAIGNAGLLNHTQELVNIY 254
Cdd:COG0491  166 LAQWLASLERLLAL--PPDLVIPGHGPPTTAEAIDYLEELLAAL 207
CphA_ImiS-like_MBL-B2 cd16306
Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and related metallo-beta-lactamases, ...
 57-251 3.16e-21

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: 88.85  E-value: 3.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  57 YFKTDDFgLVDANGLVVVEGKDAYLIDTPWSEKDTIALVEWIKQ--QNFILKAsISTHSHADRTAGISYLNSIG---VST 131
Cdd:cd16306   11 YVVEDNY-YVQENSMVYFGAKGVTVVGATWTPDTARELHKLIKRvsRKPVLEV-INTNYHTDRAGGNAYWKSIGakvVST 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 132 HVSAMTQK-----ILTTQHKALASQP----------FDGDsFTLANGLLEARYLGAGHTIDNIVVWLPKAQLLFGGCLVK 196
Cdd:cd16306   89 RQTRDLMKsdwaeIVAFTRKGLPEYPdlplvlpnvvHDGD-FTLQEGKVRAFYLGPAHTPDGIFVYFPDEQVLYGNCILK 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 114333358 197 sahsKSMGYIAEASLTDWPVTISKVKATFVDAEVVVPGH-GAIGNAGLLNHTQELV 251
Cdd:cd16306  168 ----EKLGNLSFADVKAYPQTLERLKAMKLPIKTVIGGHdSPLHGPELIDHYEALI 219
Sfh-1-like_MBL-B2 cd16305
Serratia fonticola Sfh-I and related metallo-beta-lactamases, subclass B2; MBL-fold ...
 61-246 1.69e-20

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: 86.97  E-value: 1.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  61 DDFGLVDANGLVVVEGKDAYLIDTPWSEKDTIALVEWIKQQNFI-LKASISTHSHADRTAGISYLNSIGVSTHVSAMTQK 139
Cdd:cd16305   14 EDKEYVQENSMVYIGTDGITIIGATWTPETAETLEKEIRKVSPLpIKEVINTNYHTDRAGGNAYWKTLGASIVSTQMTYD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 140 ILTTQ------------------HKALASQPFDGDsFTLANGLLEARYLGAGHTIDNIVVWLPKAQLLFGGCLVKsahsK 201
Cdd:cd16305   94 LEKSQwgsivdftrqgnnkypnlEKSLPDTVYPGD-FNLQNGSVRALYLGEAHTEDGIFVYFPAERVLYGNCILK----E 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 114333358 202 SMGYIAEASLTDWPVTISKVKATFVDAEV----VVPGHGA-IGNAGLLNH 246
Cdd:cd16305  169 KLGNMSFANRTEYPKTLKKLKGLIEQGELkvesIIAGHDTpIHDVELIDH 218
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 69-235 7.62e-18

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: 78.75  E-value: 7.62e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358    69 NGLVVVEGKDAYLIDTPWSEKDtiALVEWIKQQNFI-LKASISTHSHADRTAGISYLNSI-GVSTHVSAMTQKILTTQHK 146
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAE--DLLAELKKLGPKkIDAIILTHGHPDHIGGLPELLEApGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358   147 ALASQPF------------DGDSFTLANGLLEARYLgAGHTIDNIVVWLPKAQLLFGGCLVKS-AHSKSMGYIAEASLTD 213
Cdd:smart00849  79 LLGELGAeaepappdrtlkDGDELDLGGGELEVIHT-PGHTPGSIVLYLPEGKILFTGDLLFAgGDGRTLVDGGDAAASD 157

                          170       180
                   ....*....|....*....|..
gi 114333358   214 WPVTISKVKATfvDAEVVVPGH 235
Cdd:smart00849 158 ALESLLKLLKL--LPKLVVPGH 177
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 57-244 4.21e-17

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: 77.22  E-value: 4.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  57 YFKTDDFGLVDAN-GLVVveGKD-AYLIDTPWSEKDTIALVEWIKQqnfILKASIS----THSHADRTAGISYLNSIGVS 130
Cdd:cd16282    4 ALIGPDGGGFISNiGFIV--GDDgVVVIDTGASPRLARALLAAIRK---VTDKPVRyvvnTHYHGDHTLGNAAFADAGAP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 131 THVSAMTQKILTTQHKA-------------------LASQPFDGD-SFTLANGLLEARYLGAGHTIDNIVVWLPKAQLLF 190
Cdd:cd16282   79 IIAHENTREELAARGEAylelmrrlggdamagtelvLPDRTFDDGlTLDLGGRTVELIHLGPAHTPGDLVVWLPEEGVLF 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 114333358 191 GGCLV-KSAHsksmGYIAEASLTDWPVTISKVKATfvDAEVVVPGHGAIGNAGLL 244
Cdd:cd16282  159 AGDLVfNGRI----PFLPDGSLAGWIAALDRLLAL--DATVVVPGHGPVGDKADL 207
CphS_ImiS-like_MBL-B2 cd16287
metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas ...
 58-251 6.34e-16

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: 74.39  E-value: 6.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  58 FKTDDFGLVDANGLVVVEGKDAYLIDTPWSEKDTIALVEWIKQ--QNFILKAsISTHSHADRTAGISYLNSIGVSTHVSA 135
Cdd:cd16287   11 YIVEDKEYVQENSMVYIGTDGITIIGATWTPETAETLYKEIRKvsPLPINEV-INTNYHTDRAGGNAYWKTLGAKIVATQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 136 MTQKILTTQ--------HKALASQP----------FDGDsFTLANGLLEARYLGAGHTIDNIVVWLPKAQLLFGGCLVKs 197
Cdd:cd16287   90 MTYDLQKSQwgsivnftRQGNNKYPnlekslpdtvFPGD-FNLQNGSIRAMYLGEAHTKDGIFVYFPAERVLYGNCILK- 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 114333358 198 ahsKSMGYIAEASLTDWPVTISKVKATFVDA----EVVVPGHGA-IGNAGLLNHTQELV 251
Cdd:cd16287  168 ---ENLGNMSFANRTEYPKTLEKLKGLIEQGelkvDSIIAGHDTpIHDVGLIDHYLTLL 223
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 63-235 1.41e-15

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: 72.70  E-value: 1.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  63 FGLVDANGLVVV-EGKDAYLIDTPWSEKDtiALVEWIKQQNFILKASISTHSHADRTAGISYL-NSIGVSTHVSAMTQKI 140
Cdd:cd06262    5 VGPLQTNCYLVSdEEGEAILIDPGAGALE--KILEAIEELGLKIKAILLTHGHFDHIGGLAELkEAPGAPVYIHEADAEL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 141 LTTQHKALASQPF-------------DGDSFTLANGLLEARYLGaGHTIDNIVVWLPKAQLLFGGCLVksaHSKSMGyia 207
Cdd:cd06262   83 LEDPELNLAFFGGgplpppepdilleDGDTIELGGLELEVIHTP-GHTPGSVCFYIEEEGVLFTGDTL---FAGSIG--- 155

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 114333358 208 easLTDWPV--------TISKVKATFVDAEVVVPGH 235
Cdd:cd06262  156 ---RTDLPGgdpeqlieSIKKLLLLLPDDTVVYPGH 188
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 72-235 6.37e-14

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 68.30  E-value: 6.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  72 VVVEG-KDAYLIDTPWSEKDTIALVEWIKQQNFILKASISTHSHADRTAGISYLNSI----------GVSTHVSA----- 135
Cdd:cd07739   19 TLIYGeTEAVLVDAQFTRADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLLEAfpdakvvatpAVVAHIKAqlepk 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 136 --MTQKILTTQ--HKALASQPFDGDSFTLANGLLEARYLGAGHTIDNIVVWLPKAQLLFGGCLVksaHSKSMGYIAE--- 208
Cdd:cd07739   99 laFWGPLLGGNapARLVVPEPLDGDTLTLEGHPLEIVGVGGGDTDDTTYLWIPSLKTVVAGDVV---YNGVHVWLADatt 175

                        170       180
                 ....*....|....*....|....*...
gi 114333358 209 -ASLTDWPVTISKVKAtfVDAEVVVPGH 235
Cdd:cd07739  176 pELRAAWLAALDKIEA--LNPETVVPGH 201
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
64-235 5.62e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 57.38  E-value: 5.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358   64 GLVDANGLVVVEGKDAYLIDT-PWSEKDTIALVEWIKQQNFILKASISTHSHADRTAGISYL-NSIGVSTHVSAMTQKIL 141
Cdd:pfam00753   2 GPGQVNSYLIEGGGGAVLIDTgGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLGELaEATDVPVIVVAEEAREL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  142 TTQHKALASQ----------------PFDGDSFTLANGLLEARYLGAGHTIDNIVVWLPKAQLLFGGCLVKSAHSKSMGY 205
Cdd:pfam00753  82 LDEELGLAASrlglpgppvvplppdvVLEEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGRLDL 161

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 114333358  206 IAEASLTDWPVTISKVKATFV-----DAEVVVPGH 235
Cdd:pfam00753 162 PLGGLLVLHPSSAESSLESLLklaklKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 70-124 2.27e-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: 52.92  E-value: 2.27e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 114333358  70 GLVVVEGKDAYLIDTPWSEKDTIALVEWIKQQNFILKASISTHSHADRTAGISYL 124
Cdd:cd07743   11 GVYVFGDKEALLIDSGLDEDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYL 65
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 77-193 2.58e-06

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: 46.30  E-value: 2.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  77 KDAYLIDTPWSEKdtiaLVEWIKQQNFILKASISTHSHADRTAGISYLnsigvsthvSAMTQKILTTQHKALASQP---- 152
Cdd:cd07723   20 GEAAVVDPGEAEP----VLAALEKNGLTLTAILTTHHHWDHTGGNAEL---------KALFPDAPVYGPAEDRIPGldhp 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 114333358 153 -FDGDSFTLANGLLEARYLgAGHTIDNIVVWLPKAQLLF-------GGC 193
Cdd:cd07723   87 vKDGDEIKLGGLEVKVLHT-PGHTLGHICYYVPDEPALFtgdtlfsGGC 134
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 74-235 1.01e-05

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: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  74 VEGKD-AYLIDTPWSEKDTIALVEWIKQQNFILkasISTHSHADRTAGISYLNSIGV--------STHVSAMTQKILTTQ 144
Cdd:cd07712   14 LRGRDrALLIDTGLGIGDLKEYVRTLTDLPLLV---VATHGHFDHIGGLHEFEEVYVhpadaeilAAPDNFETLTWDAAT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 145 HKALASQPF----DGDSFTLANGLLEArYLGAGHTIDNIVVWLPKAQLLFGGCLVKSAHSKSMGYIAEasLTDWPVTISK 220
Cdd:cd07712   91 YSVPPAGPTlplrDGDVIDLGDRQLEV-IHTPGHTPGSIALLDRANRLLFSGDVVYDGPLIMDLPHSD--LDDYLASLEK 167

                        170
                 ....*....|....*
gi 114333358 221 VKATFVDAEVVVPGH 235
Cdd:cd07712  168 LSKLPDEFDKVLPGH 182
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 109-240 1.02e-04

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


Pssm-ID: 293834 [Multi-domain]  Cd Length: 188  Bit Score: 42.19  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358 109 ISTHSHADRTAGISYLNSIGVSTHVSAMTQKILTTQHKA---LASQPFDGD-SFTLANGLLEARYLGAGHTIDNIVVWLP 184
Cdd:cd16276   50 VYSHNHADHIGGASIFKDEGATIIAHEATAELLKRNPDPkrpVPTVTFDDEyTLEVGGQTLELSYFGPNHGPGNIVIYLP 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 114333358 185 KAQLLFGGCLVKSAHSKSMGYIAEASLTDWPVTISKVKAtfVDAEVVVPGHGA-IGN 240
Cdd:cd16276  130 KQKVLMAVDLINPGWVPFFNFAGSEDIPGYIEALDELLE--YDFDTFVGGHGNrLGT 184
POD-like_MBL-fold cd07724
ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; ...
 75-194 3.96e-04

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: 40.08  E-value: 3.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114333358  75 EGKDAYLIDtpwSEKDTI-ALVEWIKQQNFILKASISTHSHADRTAGISYL-NSIGVSTHVSAmtqkilttqhKALASQP 152
Cdd:cd07724   21 ETGEAAVID---PVRDSVdRYLDLAAELGLKITYVLETHVHADHVSGARELaERTGAPIVIGE----------GAPASFF 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 114333358 153 F----DGDSFTLANGLLEARYLgAGHTIDNIVVWLPKAQLLF-GGCL 194
Cdd:cd07724   88 DrllkDGDVLELGNLTLEVLHT-PGHTPESVSYLVGDPDAVFtGDTL 133
 
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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