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Conserved domains on  [gi|300503414|gb|EFK34554|]
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metallo-beta-lactamase domain protein [Chryseobacterium gleum ATCC 35910]

Protein Classification

IND family subclass B1 metallo-beta-lactamase( domain architecture ID 10888873)

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
IND_MBL-B1 cd16317
Chryseobacterium indologenes IND-1, IND-2, IND-7and related metallo-beta-lactamases, subclass ...
 27-241 3.31e-169

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: 464.88  E-value: 3.31e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  27 DFVIEPQIQPNFYIYKTFGVFGGKEYSTNAVYLVTKKGVVLFDVPWQKTQYQSLMDTIQKRHHLPVIAVFATHSHEDRAG 106
Cdd:cd16317    1 DFVIEPPIKPNLYIYKTFGVFGGKEYSANAVYLVTKKGVVLFDVPWQKVQYQSLMDTIQKRHHLPVIAVFATHSHDDRAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 107 DLSFYNKKGIKTYATAKTNEILKKEGKATSTEIIKTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKILDGGCLVKSK 186
Cdd:cd16317   81 DLSFYNNKGIKTYATAKTNEFLKKDGKATSTEIIKTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKVLDGGCLVKSN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 300503414 187 AAADLGYTGEANVAQWPKTMEKLKSKYAQATLIIPGHDEWKGGGHVEHTLDLLNK 241
Cdd:cd16317  161 SATDLGYTGEANVEQWPKTMNKLKAKYAQATLIIPGHDEWKGGGHVEHTLDLLNK 215
 
Name Accession Description Interval E-value
IND_MBL-B1 cd16317
Chryseobacterium indologenes IND-1, IND-2, IND-7and related metallo-beta-lactamases, subclass ...
 27-241 3.31e-169

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: 464.88  E-value: 3.31e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  27 DFVIEPQIQPNFYIYKTFGVFGGKEYSTNAVYLVTKKGVVLFDVPWQKTQYQSLMDTIQKRHHLPVIAVFATHSHEDRAG 106
Cdd:cd16317    1 DFVIEPPIKPNLYIYKTFGVFGGKEYSANAVYLVTKKGVVLFDVPWQKVQYQSLMDTIQKRHHLPVIAVFATHSHDDRAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 107 DLSFYNKKGIKTYATAKTNEILKKEGKATSTEIIKTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKILDGGCLVKSK 186
Cdd:cd16317   81 DLSFYNNKGIKTYATAKTNEFLKKDGKATSTEIIKTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKVLDGGCLVKSN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 300503414 187 AAADLGYTGEANVAQWPKTMEKLKSKYAQATLIIPGHDEWKGGGHVEHTLDLLNK 241
Cdd:cd16317  161 SATDLGYTGEANVEQWPKTMNKLKAKYAQATLIIPGHDEWKGGGHVEHTLDLLNK 215
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 40-239 7.46e-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: 95.14  E-value: 7.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  40 IYKTFGVFGGKEYSTNAVYLVTKKGVVLFDVPWQKTQYQSLMDTIqKRHHLPVIAVFATHSHEDRAGDLSFYNKK-GIKT 118
Cdd:COG0491    1 VYVLPGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEALLAAL-AALGLDIKAVLLTHLHPDHVGGLAALAEAfGAPV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 119 YATAKTNEILKKEGKATS--------TEIIKTGKPYRIGGEEFVVdFLGEGHTADNVVVWFPKYKILDGGCLVKskaAAD 190
Cdd:COG0491   80 YAHAAEAEALEAPAAGALfgrepvppDRTLEDGDTLELGGPGLEV-IHTPGHTPGHVSFYVPDEKVLFTGDALF---SGG 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 300503414 191 LGYTG--EANVAQWPKTMEKLKSKyaQATLIIPGHDEWKGGGHVEHTLDLL 239
Cdd:COG0491  156 VGRPDlpDGDLAQWLASLERLLAL--PPDLVIPGHGPPTTAEAIDYLEELL 204
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 55-223 1.72e-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: 90.31  E-value: 1.72e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414    55 NAVYLVTKKGVVLFDVPWqkTQYQSLMDTIQKRHHLPVIAVFATHSHEDRAGDL-SFYNKKGIKTYATAKTNEILKKEGK 133
Cdd:smart00849   1 NSYLVRDDGGAILIDTGP--GEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLpELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414   134 ATS-----------TEIIKTGKPYRIGGEEFVVDFLGeGHTADNVVVWFPKYKILDGGCLVKSKAAADLGYTG-EANVAQ 201
Cdd:smart00849  79 LLGelgaeaepappDRTLKDGDELDLGGGELEVIHTP-GHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGgDAAASD 157

                          170       180
                   ....*....|....*....|..
gi 300503414   202 WPKTMEKLKSKyaQATLIIPGH 223
Cdd:smart00849 158 ALESLLKLLKL--LPKLVVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
49-223 1.04e-08

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 53.53  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414   49 GKEYSTNAVYLVTKKGVVLFD--VPWQKTQYQSLMDTIQKRhhLPVIAVFATHSHEDRAGDL-SFYNKKGIKTYATAKTN 125
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDtgGSAEAALLLLLAALGLGP--KDIDAVILTHGHFDHIGGLgELAEATDVPVIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  126 EILKKEGKATSTEIIKTGKPY---------------RIGGEEFVVDFLGEGHTADNVVVWFPKYKILDGGCLVKSKAAAD 190
Cdd:pfam00753  79 RELLDEELGLAASRLGLPGPPvvplppdvvleegdgILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGR 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 300503414  191 LGYTGEANVA----QWPKTMEKLKS-KYAQATLIIPGH 223
Cdd:pfam00753 159 LDLPLGGLLVlhpsSAESSLESLLKlAKLKAAVIVPGH 196
PRK11921 PRK11921
anaerobic nitric oxide reductase flavorubredoxin;
47-154 2.18e-03

anaerobic nitric oxide reductase flavorubredoxin;


Pssm-ID: 237023 [Multi-domain]  Cd Length: 394  Bit Score: 38.52  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  47 FGGKEYST------NAvYLVTKKGVVLFDVPWQKTQyQSLMDTIQKRHHLPVIA-VFATHSHEDRAGDLSFYNKK--GIK 117
Cdd:PRK11921  20 FHGEEYSThrgssyNS-YLIKDEKTVLIDTVWQPFA-KEFVENLKKEIDLDKIDyIVANHGEIDHSGALPELMKEipDTP 97

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 300503414 118 TYATAKTNEILKKE-GKATSTEIIKTGKPYRIGGEEFV 154
Cdd:PRK11921  98 IYCTKNGAKSLKGHyHQDWNFVVVKTGDRLEIGSNELI 135
 
Name Accession Description Interval E-value
IND_MBL-B1 cd16317
Chryseobacterium indologenes IND-1, IND-2, IND-7and related metallo-beta-lactamases, subclass ...
 27-241 3.31e-169

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: 464.88  E-value: 3.31e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  27 DFVIEPQIQPNFYIYKTFGVFGGKEYSTNAVYLVTKKGVVLFDVPWQKTQYQSLMDTIQKRHHLPVIAVFATHSHEDRAG 106
Cdd:cd16317    1 DFVIEPPIKPNLYIYKTFGVFGGKEYSANAVYLVTKKGVVLFDVPWQKVQYQSLMDTIQKRHHLPVIAVFATHSHDDRAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 107 DLSFYNKKGIKTYATAKTNEILKKEGKATSTEIIKTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKILDGGCLVKSK 186
Cdd:cd16317   81 DLSFYNNKGIKTYATAKTNEFLKKDGKATSTEIIKTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKVLDGGCLVKSN 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 300503414 187 AAADLGYTGEANVAQWPKTMEKLKSKYAQATLIIPGHDEWKGGGHVEHTLDLLNK 241
Cdd:cd16317  161 SATDLGYTGEANVEQWPKTMNKLKAKYAQATLIIPGHDEWKGGGHVEHTLDLLNK 215
IND_BlaB-like_MBL-B1 cd16299
IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 29-240 2.84e-131

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: 369.08  E-value: 2.84e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  29 VIEPQIQPNFYIYKTFGVFGGKEYSTNAVYLVTKKGVVLFDVPWQKTQYQSLMDTIQKRHHLPVIAVFATHSHEDRAGDL 108
Cdd:cd16299    1 LKIEKLNDNLYIYTTYNEFNGVKYSANAMYLVTKKGVILFDTPWDKDQYQPLLDSIRKKHNLPVIAVIATHSHEDRAGGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 109 SFYNKKGIKTYATAKTNEILKKEGKATSTEIIKTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKILDGGCLVKSKAA 188
Cdd:cd16299   81 GYFNKIGIPTYATAMTNSILKKENKPQATYLIETDKTYKIGGEKFVVYFFGEGHTADNVVVWFPKEKVLDGGCLIKSAEA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 300503414 189 ADLGYTGEANVAQWPKTMEKLKSKYAQATLIIPGHDEWKGGGHVEHTLDLLN 240
Cdd:cd16299  161 TDLGYIGEANVKEWPKTIHKLKQKFKKAKVVIPGHDEWKDQGHIENTLKLLN 212
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 29-240 6.16e-100

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: 289.57  E-value: 6.16e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  29 VIEPQIQPNFYIYKTFGVFGGKEYSTNAVYLVTKKGVVLFDVPWQKTQYQSLMDTIQKRHHLPVIAVFATHSHEDRAGDL 108
Cdd:cd16285    1 LRIRPLADNVWVHTSLAEFNGGAVPSNGLIVIDGKGLVLIDTPWTEAQTATLLDWIEKKLGKPVTAAISTHSHDDRTGGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 109 SFYNKKGIKTYATAKTNEILKKEGKATSTEIIKTGKPYRIGgeEFVVDFLGEGHTADNVVVWFPKYKILDGGCLVKSKAA 188
Cdd:cd16285   81 KALNARGIPTYATALTNELAKKEGKPVPTHSLKGALTLGFG--PLEVFYPGPGHTPDNIVVWLPKSKILFGGCLVKSASA 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 300503414 189 ADLGYTGEANVAQWPKTMEKLKSKYAQATLIIPGHDEWKGGGHVEHTLDLLN 240
Cdd:cd16285  159 TSLGNVGDADVEAWPKSIENLKAKYPEARMVVPGHGAPGGTELLDHTLDLAK 210
BlaB-like_MBL-B1 cd16316
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and related ...
 37-242 3.80e-86

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: 254.70  E-value: 3.80e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  37 NFYIYKTFGVFGGKEYSTNAVYLVTKKGVVLFDVPWQKTQYQSLMDTIQKRHHLPVIAVFATHSHEDRAGDLSFYNKKGI 116
Cdd:cd16316    9 DLYVYTTYNTYKGTKTAANAVYVVTDKGVVVIDAPWDETQFQPFLDSIQKKHHKKVIMNIATHSHDDRAGGLEYFGKKGA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 117 KTYATAKTNEILKKEGKATSTEIIKTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKILDGGCLVKSKAAADLGYTGE 196
Cdd:cd16316   89 KTYTTKLTDSILKKNNKPRAEYTFDNDTTFKVGKYEFQVYYPGKGHTADNIVVWFPKEKVLYGGCLIKSADAKDLGYLGE 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 300503414 197 ANVAQWPKTMEKLKSKYAQATLIIPGHDEWKGGGHVEHTLDLLNKK 242
Cdd:cd16316  169 AYVNDWTQSIHNIQQKFPNPQYVIAGHDDWKDQTSLQHTLKLISEY 214
MUS_TUS_MBL-B1 cd16318
Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; ...
 33-240 4.20e-76

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: 229.16  E-value: 4.20e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  33 QIQPNFYIYKTFGVFGGKEYSTNAVYLVTKKGVVLFDVPWQKTQYQSLMDTIQKRHHLPVIAVFATHSHEDRAGDLSFYN 112
Cdd:cd16318    5 QLNDNMYIYTTYQEFQGVTYSSNSMYVLTDEGVILIDTPWDKDQYEPLLEYIRSNHNKEVKWVITTHFHEDRSGGLGYFN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 113 KKGIKTYATAKTNEILKKEGKATSTEIIKTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKILDGGCLVKSKAAADLG 192
Cdd:cd16318   85 SIGAQTYTYALTNEILKERNEPQAQFSFNKEKQFTFGNEKLAVYFLGEGHSLDNTVVWFPKEEVLYGGCLIKSAEATTIG 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 300503414 193 YTGEANVAQWPKTMEKLKSKYAQATLIIPGHDEWKGGGHVEHTLDLLN 240
Cdd:cd16318  165 NIADGNVIAWPKTIEAVKQKFKNAKVIIPGHDEWDMSGHIENTERILS 212
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 33-239 5.63e-71

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: 216.00  E-value: 5.63e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  33 QIQPNFYIYKTFGVFGGKEYSTNAVYLVTKKGVVLFDVPWQKTQYQSLMDTIQKRHHLPVIAVFATHSHEDRAGDLSFYN 112
Cdd:cd16304    5 KLNKNVWVHTSYGLFNGTPVPSNGLIVETSKGVVLIDTPWDDEQTEELLDWIKKKLKKPVTLAIVTHAHDDRIGGIKALQ 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 113 KKGIKTYATAKTNEILKKEGKATSTEIIKTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKILDGGCLVKSKAAADLG 192
Cdd:cd16304   85 KRGIPVYSTKLTAQLAKKQGYPSPDGILKDDTTLKFGNTKIETFYPGEGHTADNIVVWLPQSKILFGGCLVKSLEAKDLG 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 300503414 193 YTGEANVAQWPKTMEKLKSKYAQATLIIPGHDEWKGGGHVEHTLDLL 239
Cdd:cd16304  165 NTADANLKEWPTSIRNVLKRYPNAEIVVPGHGEWGDKQLLRHTLDLL 211
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 ...
 33-241 3.66e-60

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: 188.64  E-value: 3.66e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  33 QIQPNFYIYKTFGVFGG-KEYSTNAVYLVTKKGVVLFDVPWQKTQYQSLMDTIQKRHhLPVIAVFATHSHEDRAGDLSFY 111
Cdd:cd16301    7 KLSDGVYLHTSYKEVEGwGLVDANGLVVVDGKEAYLIDTPWSESDTEKLVEWIKAQG-LTLKASISTHFHEDRTGGIGYL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 112 NKKGIKTYATAKTNEILKKEGKATSTEIIkTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKILDGGCLVKSKAAADL 191
Cdd:cd16301   86 NSHSIPTYASELTNQLLKKNGKELATHSF-SGDEFWLLKGKIEVFYPGAGHTKDNLVVWLPKEKILFGGCLVKSLESKGL 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 300503414 192 GYTGEANVAQWPKTMEKLKSKYAQATLIIPGHDEWKGGGHVEHTLDLLNK 241
Cdd:cd16301  165 GNTGDASISQWPASAQKVLSKYPNAKLVVPGHGKVGDVSLLEHTRKLAKK 214
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 33-240 2.03e-55

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: 176.28  E-value: 2.03e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  33 QIQPNFYIYKTF---GVFGgkEYSTNAVYLVTKKGVVLFDVPWQKTQYQSLMDTIQKRHHLPVIAVFATHSHEDRAGDLS 109
Cdd:cd16302    5 KLSDHVYVHVSYletETFG--KVPCNGMIVINGGEAVVFDTPTNDSQSEELIDWIENSLKAKVKAVVPTHFHDDCLGGLK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 110 FYNKKGIKTYATAKTNEILKKEGKATSTEIIKTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKILDGGCLVKSkAAA 189
Cdd:cd16302   83 AFHRRGIPSYANQKTIALAKEKGLPVPQHGFSDSLTLKLGGKKIVCRYFGEGHTKDNIVVYFPSEKVLFGGCMVKS-LGA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 300503414 190 DLGYTGEANVAQWPKTMEKLKSKYAQATLIIPGHDEWKGGGHVEHTLDLLN 240
Cdd:cd16302  162 GKGNLEDANVEAWPKTVEKVKAKYPDVKIVIPGHGKIGGSELLDYTIDLFK 212
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 52-239 3.99e-50

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: 163.10  E-value: 3.99e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  52 YSTNAVYLVTKKGVVLFDVPWQKTQYQSLMDTIQKRHHLPVIAVFATHSHEDRAGDLSFYNKKGIKTYATAKTNEILKKE 131
Cdd:cd07707   19 VPSNGLVYNGSKGLVLVDSTWTPKTTKELIKEIEKVSQKPVTEVINTHFHTDRAGGNAYLKERGAKTVSTALTRDLAKSE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 132 GKATSTEIIKTGKPY----------------RIGGEEFVVDFLGEGHTADNVVVWFPKYKILDGGCLVKSKaaaDLGYTG 195
Cdd:cd07707   99 WAEIVAFTRKGLPEYpdlgyelpdgvldgdfNLQFGKVEAFYPGPAHTPDNIVVYFPQENVLYGGCIIKET---DLGNVA 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 300503414 196 EANVAQWPKTMEKLKSKYAQATLIIPGHDEWKGGGHVEHTLDLL 239
Cdd:cd07707  176 DADVKEWPTSIERLKKRYRNIKAVIPGHGEVGGPELLDHTLDLL 219
VIM_type_MBL-B1 cd16303
VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona ...
 33-242 7.38e-41

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: 139.23  E-value: 7.38e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  33 QIQPNFYIYKTFGVFGGKEYSTNAVYLVTKKGVVLFDVPWQKTQYQSLMDTIQKRHHLPVIAVFATHSHEDRAGDLSFYN 112
Cdd:cd16303    7 QIADGVWSHIATQSFDGAVYPSNGLIVRDGDELLLIDTAWGAKNTAALLAEIEKQIGLPVTRAVSTHFHDDRVGGVDVLR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 113 KKGIKTYATAKTNEILKKEGKATSTEII----KTGKPYRIGGEEfvVDFLGEGHTADNVVVWFPKYKILDGGCLVKSKAA 188
Cdd:cd16303   87 AAGVATYASPSTRRLAEAEGNEIPTHSLeglsSSGDAVRFGPVE--LFYPGAAHSTDNLVVYVPSARVLYGGCAVRELSS 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 300503414 189 ADLGYTGEANVAQWPKTMEKLKSKYAQATLIIPGHDEWKGGGHVEHTLDLLNKK 242
Cdd:cd16303  165 TSAGNVADADLAEWPTSIERIQKHYPEAEFVIPGHGLPGGLDLLHHTKNVVKAH 218
SPM-1-like_MBL-B1-B2-like cd16286
Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; ...
 52-239 2.58e-36

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: 128.03  E-value: 2.58e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  52 YSTNA-VYLVTKKGVVLFDVPWQKTQYQSLMDTIQKRHHLPVIAVFATHSHEDRAGDLSFYNKKGIKTYATAKTNEILKK 130
Cdd:cd16286   25 WSSNVlVVKMLDGTVVIVDSPYTNLATQTVLDWIAKTMGPRKVVAINTHFHLDGTGGNEALKKRGIPTWGSDLTKQLLLE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 131 EGKATSTEI--------------------------IKTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKILDGGCLVk 184
Cdd:cd16286  105 RGKADRIKAaeflknedlkrriessppvppdnvfdLKEGKVFSFGNELVEVSFPGPAHAPDNVVVYFPERKILFGGCMI- 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 300503414 185 sKAAADLGYTGEANVAQWPKTMEKLKSkyAQATLIIPGHDEWKGGGHVEHTLDLL 239
Cdd:cd16286  184 -KPGKELGNLGDANMKAWPDSVRRLKK--FDAKIVIPGHGERGDPGMVNKTIKVL 235
NDM_FIM-like_MBL-B1 cd16300
NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase ...
 33-238 4.36e-30

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: 111.45  E-value: 4.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  33 QIQPNFYIYKTF-GVFGGKEYSTNAVYLVTKKGVVLFDVPWQKTQYQSLMDTIQKRHHLPVIAVFATHSHEDRAGDLSFY 111
Cdd:cd16300    5 QLAPGVWMHTSYlDMPGFGAVPSNGLIVRDGDRVLLVDTAWTDDQTAQILNWAKQELNLPVRLAVVTHAHQDKMGGMDAL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 112 NKKGIKTYATAKTNEILKKEG-KATSTEIIKTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKILDGGCLVKSKAAAD 190
Cdd:cd16300   85 HAAGIATYANALSNQLAPQEGlVPAQHSLTFAAEPSTAPNFPLKVFYPGPGHTRDNIVVGIDGTGIAFGGCLIRPSKATS 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 300503414 191 LGYTGEANVAQWPKTMEKLKSKYAQATLIIPGHDEWKGGGHVEHTLDL 238
Cdd:cd16300  165 LGNLADADTEHWAASARAFGAAFPDASMIVPSHGAPDGRAAITHTARL 212
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 40-239 7.46e-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: 95.14  E-value: 7.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  40 IYKTFGVFGGKEYSTNAVYLVTKKGVVLFDVPWQKTQYQSLMDTIqKRHHLPVIAVFATHSHEDRAGDLSFYNKK-GIKT 118
Cdd:COG0491    1 VYVLPGGTPGAGLGVNSYLIVGGDGAVLIDTGLGPADAEALLAAL-AALGLDIKAVLLTHLHPDHVGGLAALAEAfGAPV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 119 YATAKTNEILKKEGKATS--------TEIIKTGKPYRIGGEEFVVdFLGEGHTADNVVVWFPKYKILDGGCLVKskaAAD 190
Cdd:COG0491   80 YAHAAEAEALEAPAAGALfgrepvppDRTLEDGDTLELGGPGLEV-IHTPGHTPGHVSFYVPDEKVLFTGDALF---SGG 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 300503414 191 LGYTG--EANVAQWPKTMEKLKSKyaQATLIIPGHDEWKGGGHVEHTLDLL 239
Cdd:COG0491  156 VGRPDlpDGDLAQWLASLERLLAL--PPDLVIPGHGPPTTAEAIDYLEELL 204
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 55-223 1.72e-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: 90.31  E-value: 1.72e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414    55 NAVYLVTKKGVVLFDVPWqkTQYQSLMDTIQKRHHLPVIAVFATHSHEDRAGDL-SFYNKKGIKTYATAKTNEILKKEGK 133
Cdd:smart00849   1 NSYLVRDDGGAILIDTGP--GEAEDLLAELKKLGPKKIDAIILTHGHPDHIGGLpELLEAPGAPVYAPEGTAELLKDLLA 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414   134 ATS-----------TEIIKTGKPYRIGGEEFVVDFLGeGHTADNVVVWFPKYKILDGGCLVKSKAAADLGYTG-EANVAQ 201
Cdd:smart00849  79 LLGelgaeaepappDRTLKDGDELDLGGGELEVIHTP-GHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGgDAAASD 157

                          170       180
                   ....*....|....*....|..
gi 300503414   202 WPKTMEKLKSKyaQATLIIPGH 223
Cdd:smart00849 158 ALESLLKLLKL--LPKLVVPGH 177
Sfh-1-like_MBL-B2 cd16305
Serratia fonticola Sfh-I and related metallo-beta-lactamases, subclass B2; MBL-fold ...
 50-241 2.59e-21

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: 88.52  E-value: 2.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  50 KEY-STNAVYLVTKKGVVLFDVPWQKTQYQSLMDTIQKRHHLPVIAVFATHSHEDRAGDLSFYNKKGIKTYATAKTNEIL 128
Cdd:cd16305   16 KEYvQENSMVYIGTDGITIIGATWTPETAETLEKEIRKVSPLPIKEVINTNYHTDRAGGNAYWKTLGASIVSTQMTYDLE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 129 KKEGKA---------TSTEIIKTGKPYRIGGEEFVVD-------FLGEGHTADNVVVWFPKYKILDGGCLVKSKaaadLG 192
Cdd:cd16305   96 KSQWGSivdftrqgnNKYPNLEKSLPDTVYPGDFNLQngsvralYLGEAHTEDGIFVYFPAERVLYGNCILKEK----LG 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 300503414 193 YTGEANVAQWPKTMEKLKSKYAQATL----IIPGHDE-WKGGGHVEHTLDLLNK 241
Cdd:cd16305  172 NMSFANRTEYPKTLKKLKGLIEQGELkvesIIAGHDTpIHDVELIDHYLTLLEK 225
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 55-223 3.33e-20

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: 85.31  E-value: 3.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  55 NAVYLVTKKGVVLFDvpwqkTQY-----QSLMDTIQKRHHLPVIAVFATHSHEDRAGDLSFYNKKGIKTYATAKTNEILK 129
Cdd:cd16282   16 NIGFIVGDDGVVVID-----TGAsprlaRALLAAIRKVTDKPVRYVVNTHYHGDHTLGNAAFADAGAPIIAHENTREELA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 130 KEGKATS-------------------TEIIKTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKILDGGCLVkskAAAD 190
Cdd:cd16282   91 ARGEAYLelmrrlggdamagtelvlpDRTFDDGLTLDLGGRTVELIHLGPAHTPGDLVVWLPEEGVLFAGDLV---FNGR 167

                        170       180       190
                 ....*....|....*....|....*....|...
gi 300503414 191 LGYTGEANVAQWPKTMEKLKSkyAQATLIIPGH 223
Cdd:cd16282  168 IPFLPDGSLAGWIAALDRLLA--LDATVVVPGH 198
CphA_ImiS-like_MBL-B2 cd16306
Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and related metallo-beta-lactamases, ...
 55-239 8.96e-19

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: 81.92  E-value: 8.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  55 NAVYLVTKKGVVLFDVPWQKTQYQSLMDTIQKRHHLPVIAVFATHSHEDRAGDLSFYNKKGIKTYATAKTNEILKKeGKA 134
Cdd:cd16306   22 NSMVYFGAKGVTVVGATWTPDTARELHKLIKRVSRKPVLEVINTNYHTDRAGGNAYWKSIGAKVVSTRQTRDLMKS-DWA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 135 TSTEIIKTGKP-----------------YRIGGEEFVVDFLGEGHTADNVVVWFPKYKILDGGCLVKSKaaadLGYTGEA 197
Cdd:cd16306  101 EIVAFTRKGLPeypdlplvlpnvvhdgdFTLQEGKVRAFYLGPAHTPDGIFVYFPDEQVLYGNCILKEK----LGNLSFA 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 300503414 198 NVAQWPKTMEKLKSKYAQATLIIPGHDEWKGGGH-VEHTLDLL 239
Cdd:cd16306  177 DVKAYPQTLERLKAMKLPIKTVIGGHDSPLHGPElIDHYEALI 219
CphS_ImiS-like_MBL-B2 cd16287
metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas ...
 55-224 2.25e-15

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: 72.46  E-value: 2.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  55 NAVYLVTKKGVVLFDVPWQKTQYQSLMDTIQKRHHLPVIAVFATHSHEDRAGDLSFYNKKGIKTYATAKTNEILKKEGkA 134
Cdd:cd16287   22 NSMVYIGTDGITIIGATWTPETAETLYKEIRKVSPLPINEVINTNYHTDRAGGNAYWKTLGAKIVATQMTYDLQKSQW-G 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 135 TSTEIIKTGKPYR----------IGGEEFVVD-------FLGEGHTADNVVVWFPKYKILDGGCLVKSKaaadLGYTGEA 197
Cdd:cd16287  101 SIVNFTRQGNNKYpnlekslpdtVFPGDFNLQngsiramYLGEAHTKDGIFVYFPAERVLYGNCILKEN----LGNMSFA 176

                        170       180       190
                 ....*....|....*....|....*....|.
gi 300503414 198 NVAQWPKTMEKLKS----KYAQATLIIPGHD 224
Cdd:cd16287  177 NRTEYPKTLEKLKGlieqGELKVDSIIAGHD 207
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 55-177 3.48e-15

uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain; Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) 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: 71.08  E-value: 3.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  55 NAVYLVTKKGVVLFDVPWQKTQYqsLMDTIQKRHHLPVIAVFATHSHEDRAGDLSFYNKKGIKTYATAKTNEILKKEGKA 134
Cdd:cd16276   11 QSMFLVTDKGVIVVDAPPSLGEN--LLAAIRKVTDKPVTHVVYSHNHADHIGGASIFKDEGATIIAHEATAELLKRNPDP 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 300503414 135 ---TSTEIIKTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKIL 177
Cdd:cd16276   89 krpVPTVTFDDEYTLEVGGQTLELSYFGPNHGPGNIVIYLPKQKVL 134
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 46-177 3.35e-10

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: 57.68  E-value: 3.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  46 VFGGKEYSTNAvYLVT--KKGVVLFDVPWQKTQYqsLMDTIqKRHHLPVIAVFATHSHEDRAGDLSFY-NKKGIKTYATA 122
Cdd:cd06262    2 RLPVGPLQTNC-YLVSdeEGEAILIDPGAGALEK--ILEAI-EELGLKIKAILLTHGHFDHIGGLAELkEAPGAPVYIHE 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300503414 123 KTNEILKKEGKATS------------TEIIKTGKPYRIGGEEFVVDFLGeGHTADNVVVWFPKYKIL 177
Cdd:cd06262   78 ADAELLEDPELNLAffgggplpppepDILLEDGDTIELGGLELEVIHTP-GHTPGSVCFYIEEEGVL 143
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
49-223 1.04e-08

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 53.53  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414   49 GKEYSTNAVYLVTKKGVVLFD--VPWQKTQYQSLMDTIQKRhhLPVIAVFATHSHEDRAGDL-SFYNKKGIKTYATAKTN 125
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDtgGSAEAALLLLLAALGLGP--KDIDAVILTHGHFDHIGGLgELAEATDVPVIVVAEEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  126 EILKKEGKATSTEIIKTGKPY---------------RIGGEEFVVDFLGEGHTADNVVVWFPKYKILDGGCLVKSKAAAD 190
Cdd:pfam00753  79 RELLDEELGLAASRLGLPGPPvvplppdvvleegdgILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGR 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 300503414  191 LGYTGEANVA----QWPKTMEKLKS-KYAQATLIIPGH 223
Cdd:pfam00753 159 LDLPLGGLLVlhpsSAESSLESLLKlAKLKAAVIVPGH 196
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 54-223 1.29e-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) 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: 38.64  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  54 TNAVYLVTKKGVVLFDVPWQKTQYQSLMDTIqKRHHLPVIAVFATHSHEDR---AGDLsfynKK---GIKTYATAKTNEI 127
Cdd:cd07739   16 VTSTLIYGETEAVLVDAQFTRADAERLADWI-KASGKTLTTIYITHGHPDHyfgLEVL----LEafpDAKVVATPAVVAH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 128 LKKE-------------GKATSTEII---KTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYKILDGGclvkskaaaDL 191
Cdd:cd07739   91 IKAQlepklafwgpllgGNAPARLVVpepLDGDTLTLEGHPLEIVGVGGGDTDDTTYLWIPSLKTVVAG---------DV 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 300503414 192 GY------TGEAN----VAQWPKTMEKLKSkyAQATLIIPGH 223
Cdd:cd07739  162 VYngvhvwLADATtpelRAAWLAALDKIEA--LNPETVVPGH 201
PRK11921 PRK11921
anaerobic nitric oxide reductase flavorubredoxin;
47-154 2.18e-03

anaerobic nitric oxide reductase flavorubredoxin;


Pssm-ID: 237023 [Multi-domain]  Cd Length: 394  Bit Score: 38.52  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  47 FGGKEYST------NAvYLVTKKGVVLFDVPWQKTQyQSLMDTIQKRHHLPVIA-VFATHSHEDRAGDLSFYNKK--GIK 117
Cdd:PRK11921  20 FHGEEYSThrgssyNS-YLIKDEKTVLIDTVWQPFA-KEFVENLKKEIDLDKIDyIVANHGEIDHSGALPELMKEipDTP 97

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 300503414 118 TYATAKTNEILKKE-GKATSTEIIKTGKPYRIGGEEFV 154
Cdd:PRK11921  98 IYCTKNGAKSLKGHyHQDWNFVVVKTGDRLEIGSNELI 135
TTHA1429-like_MBL-fold cd07725
uncharacterized Thermus thermophilus TTHA1429 and related proteins; MBL-fold metallo hydrolase ...
 95-223 3.10e-03

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: 37.28  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  95 VFATHSHEDRAGDLS-FYNKKGIKTYataktneilkkegkATSTEIIKTGKPYRIGGEEFVVDFLGeGHTADNVVVWFPK 173
Cdd:cd07725   59 VLLTHHHPDHIGLAGkLQEKSGATVY--------------ILDVTPVKDGDKIDLGGLRLKVIETP-GHTPGHIVLYDED 123

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 300503414 174 YKILDGGCLVKSKaaadlgYTgeANVAQWPKTMEKLKSKYAQ---------ATLIIPGH 223
Cdd:cd07725  124 RRELFVGDAVLPK------IT--PNVSLWAVRVEDPLGAYLEsldklekldVDLAYPGH 174
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 53-223 4.26e-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) 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: 37.12  E-value: 4.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  53 STNA-VYLVTKKGVVLFDvPWQKTQYQSLMDTIQKRHHLPVIAVFATHSHEDRAGDLSF-YNKKGIKTYATAKTNEILK- 129
Cdd:cd07743    7 PTNIgVYVFGDKEALLID-SGLDEDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYlQKKTGCKVYAPKIEKAFIEn 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414 130 ---------------------KEGKATSTEIIKTGKPYRIGGEEFVVDFLGeGH--------TADNvvVWF--------- 171
Cdd:cd07743   86 pllepsylggayppkelrnkfLMAKPSKVDDIIEEGELELGGVGLEIIPLP-GHsfgqigilTPDG--VLFagdalfgee 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 300503414 172 --PKYKILdggclvkskaaadlgYTgeANVAQWPKTMEKLKSKyaQATLIIPGH 223
Cdd:cd07743  163 vlEKYGIP---------------FL--YDVEEQLETLEKLEEL--DADYYVPGH 197
YycJ-like_MBL-fold cd07733
uncharacterized subgroup which includes Bacillus subtilis YycJ and related proteins; MBL-fold ...
 55-150 4.28e-03

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: 36.47  E-value: 4.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300503414  55 NAVYLVTKKGVVLFD--VPWQKTQyqSLMDTIQkRHHLPVIAVFATHSHEDRAGDL-SFYNKKGIKTYATAKTNEIL--- 128
Cdd:cd07733   10 NCTYLETEDGKLLIDagLSGRKIT--GRLAEIG-RDPEDIDAILVTHEHADHIKGLgVLARKYNVPIYATAGTLRAMerk 86

                         90       100
                 ....*....|....*....|..
gi 300503414 129 KKEGKATSTEIIKTGKPYRIGG 150
Cdd:cd07733   87 VGLIDVDQKQIFEPGETFSIGD 108
 
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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