NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1028105373|ref|WP_063860522|]
View 

subclass B1 metallo-beta-lactamase GIM-2 [Enterobacter cloacae]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 22-236 2.30e-133

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: 374.70  E-value: 2.30e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  22 KPLEVIKIEDGVYLHTSFKNIEGYGLVDSNGLVVLDNNQAYIIDTPWSEEDTKLLLSWATDRGYQVMASISTHSHGDRTA 101
Cdd:cd16301     1 PKLKIEKLSDGVYLHTSYKEVEGWGLVDANGLVVVDGKEAYLIDTPWSESDTEKLVEWIKAQGLTLKASISTHFHEDRTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 102 GIKLLNSKSIPTYTSELTKKLLAREGKPVPTHYFKDDEFTLGNGLIELYYPGAGHTEDNIVAWLPKSKILFGGCLVRSHE 181
Cdd:cd16301    81 GIGYLNSHSIPTYASELTNQLLKKNGKELATHSFSGDEFWLLKGKIEVFYPGAGHTKDNLVVWLPKEKILFGGCLVKSLE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1028105373 182 WEGLGYVGDASISSWADSIKNIVSKKYPIQMVVPGHGKVGSSDILDHTIDLAESA 236
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 ...
 22-236 2.30e-133

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: 374.70  E-value: 2.30e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  22 KPLEVIKIEDGVYLHTSFKNIEGYGLVDSNGLVVLDNNQAYIIDTPWSEEDTKLLLSWATDRGYQVMASISTHSHGDRTA 101
Cdd:cd16301     1 PKLKIEKLSDGVYLHTSYKEVEGWGLVDANGLVVVDGKEAYLIDTPWSESDTEKLVEWIKAQGLTLKASISTHFHEDRTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 102 GIKLLNSKSIPTYTSELTKKLLAREGKPVPTHYFKDDEFTLGNGLIELYYPGAGHTEDNIVAWLPKSKILFGGCLVRSHE 181
Cdd:cd16301    81 GIGYLNSHSIPTYASELTNQLLKKNGKELATHSFSGDEFWLLKGKIEVFYPGAGHTKDNLVVWLPKEKILFGGCLVKSLE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1028105373 182 WEGLGYVGDASISSWADSIKNIVSKKYPIQMVVPGHGKVGSSDILDHTIDLAESA 236
Cdd:cd16301   161 SKGLGNTGDASISQWPASAQKVLSKYPNAKLVVPGHGKVGDVSLLEHTRKLAKKA 215
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 47-234 2.59e-25

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: 98.99  E-value: 2.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  47 LVDSNGLVVLDNNQAYIIDTPWSEEDTKLLLSWATDRGYQVMASISTHSHGDRTAGIKLLNSKS-IPTYTSELTKKLLAR 125
Cdd:COG0491    12 GLGVNSYLIVGGDGAVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFgAPVYAHAAEAEALEA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 126 EGK--------PVPTHYFKD-DEFTLGNGLIELYYpGAGHTEDNIVAWLPKSKILFGGCLVRSHEWeGLGYVGDASISSW 196
Cdd:COG0491    92 PAAgalfgrepVPPDRTLEDgDTLELGGPGLEVIH-TPGHTPGHVSFYVPDEKVLFTGDALFSGGV-GRPDLPDGDLAQW 169

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1028105373 197 ADSIKNIvsKKYPIQMVVPGHGKVGSSDILDHTIDLAE 234
Cdd:COG0491   170 LASLERL--LALPPDLVIPGHGPPTTAEAIDYLEELLA 205
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 51-217 3.66e-21

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: 87.22  E-value: 3.66e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373   51 NGLVVLDNNQAYIIDTPWSEEDtKLLLSWATDRGYQVMASISTHSHGDRTAGI-KLLNSKSIPTYTSELTKKLLARE--- 126
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAE-DLLAELKKLGPKKIDAIILTHGHPDHIGGLpELLEAPGAPVYAPEGTAELLKDLlal 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  127 --------GKPVPTHYFKD-DEFTLGNGLIELYYPgAGHTEDNIVAWLPKSKILFGGCLVRSHEWEGLGYVG-DASISSW 196
Cdd:smart00849  80 lgelgaeaEPAPPDRTLKDgDELDLGGGELEVIHT-PGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGgDAAASDA 158

                          170       180
                   ....*....|....*....|.
gi 1028105373  197 ADSIKNIVSKKYPIqmVVPGH 217
Cdd:smart00849 159 LESLLKLLKLLPKL--VVPGH 177
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
45-217 6.16e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 56.99  E-value: 6.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  45 YGLVDSNGLVVLDNNQAYIIDT-PWSEEDTKLLLSWATDRGYQVMASISTHSHGDRTAGI-KLLNSKSIPTYTSELTKKL 122
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTgGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLgELAEATDVPVIVVAEEARE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 123 LAREGKPVPTHYFK----------------DDEFTLGNGLIELYYPGAGHTEDNIVAWLPKSKILFGGCLVRSHEWE--- 183
Cdd:pfam00753  81 LLDEELGLAASRLGlpgppvvplppdvvleEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGrld 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1028105373 184 ---GLGYVGDASI-SSWADSIKNIVSKKYPIqmVVPGH 217
Cdd:pfam00753 161 lplGGLLVLHPSSaESSLESLLKLAKLKAAV--IVPGH 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 ...
 22-236 2.30e-133

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: 374.70  E-value: 2.30e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  22 KPLEVIKIEDGVYLHTSFKNIEGYGLVDSNGLVVLDNNQAYIIDTPWSEEDTKLLLSWATDRGYQVMASISTHSHGDRTA 101
Cdd:cd16301     1 PKLKIEKLSDGVYLHTSYKEVEGWGLVDANGLVVVDGKEAYLIDTPWSESDTEKLVEWIKAQGLTLKASISTHFHEDRTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 102 GIKLLNSKSIPTYTSELTKKLLAREGKPVPTHYFKDDEFTLGNGLIELYYPGAGHTEDNIVAWLPKSKILFGGCLVRSHE 181
Cdd:cd16301    81 GIGYLNSHSIPTYASELTNQLLKKNGKELATHSFSGDEFWLLKGKIEVFYPGAGHTKDNLVVWLPKEKILFGGCLVKSLE 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1028105373 182 WEGLGYVGDASISSWADSIKNIVSKKYPIQMVVPGHGKVGSSDILDHTIDLAESA 236
Cdd:cd16301   161 SKGLGNTGDASISQWPASAQKVLSKYPNAKLVVPGHGKVGDVSLLEHTRKLAKKA 215
MBL-B1 cd16285
metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; MBLs (class B of the ...
 24-234 2.04e-111

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: 318.84  E-value: 2.04e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  24 LEVIKIEDGVYLHTSFKNIEGyGLVDSNGLVVLDNNQAYIIDTPWSEEDTKLLLSWATDR-GYQVMASISTHSHGDRTAG 102
Cdd:cd16285     1 LRIRPLADNVWVHTSLAEFNG-GAVPSNGLIVIDGKGLVLIDTPWTEAQTATLLDWIEKKlGKPVTAAISTHSHDDRTGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 103 IKLLNSKSIPTYTSELTKKLLAREGKPVPTHYFKDdEFTLGNGLIELYYPGAGHTEDNIVAWLPKSKILFGGCLVRSHEW 182
Cdd:cd16285    80 IKALNARGIPTYATALTNELAKKEGKPVPTHSLKG-ALTLGFGPLEVFYPGPGHTPDNIVVWLPKSKILFGGCLVKSASA 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1028105373 183 EGLGYVGDASISSWADSIKNIVSKKYPIQMVVPGHGKVGSSDILDHTIDLAE 234
Cdd:cd16285   159 TSLGNVGDADVEAWPKSIENLKAKYPEARMVVPGHGAPGGTELLDHTLDLAK 210
BcII-like_MBL-B1 cd16304
Bacillus cereus Beta-lactamase 2 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 24-232 8.64e-79

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: 236.41  E-value: 8.64e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  24 LEVIKIEDGVYLHTSFKNIEGyGLVDSNGLVVLDNNQAYIIDTPWSEEDTKLLLSWATDRGYQ-VMASISTHSHGDRTAG 102
Cdd:cd16304     1 LEVTKLNKNVWVHTSYGLFNG-TPVPSNGLIVETSKGVVLIDTPWDDEQTEELLDWIKKKLKKpVTLAIVTHAHDDRIGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 103 IKLLNSKSIPTYTSELTKKLLAREGKPVPTHYFKDDE-FTLGNGLIELYYPGAGHTEDNIVAWLPKSKILFGGCLVRSHE 181
Cdd:cd16304    80 IKALQKRGIPVYSTKLTAQLAKKQGYPSPDGILKDDTtLKFGNTKIETFYPGEGHTADNIVVWLPQSKILFGGCLVKSLE 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1028105373 182 WEGLGYVGDASISSWADSIKNiVSKKYP-IQMVVPGHGKVGSSDILDHTIDL 232
Cdd:cd16304   160 AKDLGNTADANLKEWPTSIRN-VLKRYPnAEIVVPGHGEWGDKQLLRHTLDL 210
CcrA-like_MBL-B1 cd16302
Bacteroides fragilis CcrA and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 24-234 4.17e-75

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: 226.74  E-value: 4.17e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  24 LEVIKIEDGVYLHTSFKNIEGYGLVDSNGLVVLDNNQAYIIDTPWSEEDTKLLLSWATDR-GYQVMASISTHSHGDRTAG 102
Cdd:cd16302     1 LEIIKLSDHVYVHVSYLETETFGKVPCNGMIVINGGEAVVFDTPTNDSQSEELIDWIENSlKAKVKAVVPTHFHDDCLGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 103 IKLLNSKSIPTYTSELTKKLLAREGKPVPTHYFKDD-EFTLGNGLIELYYPGAGHTEDNIVAWLPKSKILFGGCLVRSHE 181
Cdd:cd16302    81 LKAFHRRGIPSYANQKTIALAKEKGLPVPQHGFSDSlTLKLGGKKIVCRYFGEGHTKDNIVVYFPSEKVLFGGCMVKSLG 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1028105373 182 wEGLGYVGDASISSWADSIKNiVSKKYP-IQMVVPGHGKVGSSDILDHTIDLAE 234
Cdd:cd16302   161 -AGKGNLEDANVEAWPKTVEK-VKAKYPdVKIVIPGHGKIGGSELLDYTIDLFK 212
BlaB-like_MBL-B1 cd16316
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum) BlaB and related ...
 24-233 6.25e-56

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: 178.04  E-value: 6.25e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  24 LEVIKIEDGVYLHTSFKNIEGyGLVDSNGLVVLDNNQAYIIDTPWSEEDTKLLL-SWATDRGYQVMASISTHSHGDRTAG 102
Cdd:cd16316     1 LKISHLTGDLYVYTTYNTYKG-TKTAANAVYVVTDKGVVVIDAPWDETQFQPFLdSIQKKHHKKVIMNIATHSHDDRAGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 103 IKLLNSKSIPTYTSELTKKLLAREGKPVPTHYFKDDE-FTLGNGLIELYYPGAGHTEDNIVAWLPKSKILFGGCLVRSHE 181
Cdd:cd16316    80 LEYFGKKGAKTYTTKLTDSILKKNNKPRAEYTFDNDTtFKVGKYEFQVYYPGKGHTADNIVVWFPKEKVLYGGCLIKSAD 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1028105373 182 WEGLGYVGDASISSWADSIKNIVSKKYPIQMVVPGHGKVGSSDILDHTIDLA 233
Cdd:cd16316   160 AKDLGYLGEAYVNDWTQSIHNIQQKFPNPQYVIAGHDDWKDQTSLQHTLKLI 211
VIM_type_MBL-B1 cd16303
VIM-type metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase domain; VIM (Verona ...
 24-234 4.81e-54

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: 173.51  E-value: 4.81e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  24 LEVIKIEDGVYLHTSFKNIEGyGLVDSNGLVVLDNNQAYIIDTPWSEEDTKLLLSW-ATDRGYQVMASISTHSHGDRTAG 102
Cdd:cd16303     3 VRLYQIADGVWSHIATQSFDG-AVYPSNGLIVRDGDELLLIDTAWGAKNTAALLAEiEKQIGLPVTRAVSTHFHDDRVGG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 103 IKLLNSKSIPTYTSELTKKLLAREGKPVPTHYFKDDEfTLGN----GLIELYYPGAGHTEDNIVAWLPKSKILFGGCLVR 178
Cdd:cd16303    82 VDVLRAAGVATYASPSTRRLAEAEGNEIPTHSLEGLS-SSGDavrfGPVELFYPGAAHSTDNLVVYVPSARVLYGGCAVR 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1028105373 179 SHEWEGLGYVGDASISSWADSIKNIvSKKYP-IQMVVPGHGKVGSSDILDHTIDLAE 234
Cdd:cd16303   161 ELSSTSAGNVADADLAEWPTSIERI-QKHYPeAEFVIPGHGLPGGLDLLHHTKNVVK 216
MBL-B1-B2-like cd07707
metallo-beta-lactamases; subclasses B1 and B2 and related proteins; MBL-fold metallo-hydrolase ...
 24-233 1.50e-52

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: 169.65  E-value: 1.50e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  24 LEVIKIEDGVYLHTSfkniegYGLVDSNGLVVLDNNQAYIIDTPWSEEDTKLLLSW-ATDRGYQVMASISTHSHGDRTAG 102
Cdd:cd07707     1 LSLTQINGPVWVVTD------LGSVPSNGLVYNGSKGLVLVDSTWTPKTTKELIKEiEKVSQKPVTEVINTHFHTDRAGG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 103 IKLLNSKSIPTYTSELTKKL----------LAREGKP--------VPTHYFkDDEFTLGNGLIELYYPGAGHTEDNIVAW 164
Cdd:cd07707    75 NAYLKERGAKTVSTALTRDLaksewaeivaFTRKGLPeypdlgyeLPDGVL-DGDFNLQFGKVEAFYPGPAHTPDNIVVY 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1028105373 165 LPKSKILFGGCLVRSHEwegLGYVGDASISSWADSIKNIVSKKYPIQMVVPGHGKVGSSDILDHTIDLA 233
Cdd:cd07707   154 FPQENVLYGGCIIKETD---LGNVADADVKEWPTSIERLKKRYRNIKAVIPGHGEVGGPELLDHTLDLL 219
IND_BlaB-like_MBL-B1 cd16299
IND1, IND2, BlaB-1 and related metallo-beta-lactamases, subclass B1; MBL-fold ...
 24-232 2.09e-52

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: 169.16  E-value: 2.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  24 LEVIKIEDGVYLHTSFKNIEGYGlVDSNGLVVLDNNQAYIIDTPWSEEDTKLLLSWATDR-GYQVMASISTHSHGDRTAG 102
Cdd:cd16299     1 LKIEKLNDNLYIYTTYNEFNGVK-YSANAMYLVTKKGVILFDTPWDKDQYQPLLDSIRKKhNLPVIAVIATHSHEDRAGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 103 IKLLNSKSIPTYTSELTKKLLAREGKPVPTHYFKDDE-FTLGNGLIELYYPGAGHTEDNIVAWLPKSKILFGGCLVRSHE 181
Cdd:cd16299    80 LGYFNKIGIPTYATAMTNSILKKENKPQATYLIETDKtYKIGGEKFVVYFFGEGHTADNVVVWFPKEKVLDGGCLIKSAE 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1028105373 182 WEGLGYVGDASISSWADSIKNIVSKKYPIQMVVPGHGKVGSSDILDHTIDL 232
Cdd:cd16299   160 ATDLGYIGEANVKEWPKTIHKLKQKFKKAKVVIPGHDEWKDQGHIENTLKL 210
NDM_FIM-like_MBL-B1 cd16300
NDM-1, FIM-1 and related metallo-beta-lactamases, subclass B1; MBL-fold metallo-hydrolase ...
 24-234 7.90e-51

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: 164.99  E-value: 7.90e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  24 LEVIKIEDGVYLHTSFKNIEGYGLVDSNGLVVLDNNQAYIIDTPWSEEDTKLLLSWATDR-GYQVMASISTHSHGDRTAG 102
Cdd:cd16300     1 VVFRQLAPGVWMHTSYLDMPGFGAVPSNGLIVRDGDRVLLVDTAWTDDQTAQILNWAKQElNLPVRLAVVTHAHQDKMGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 103 IKLLNSKSIPTYTSELTKKLLAREG-KPVPTHYFKDDE-FTLGNGLIELYYPGAGHTEDNIVAWLPKSKILFGGCLVRSH 180
Cdd:cd16300    81 MDALHAAGIATYANALSNQLAPQEGlVPAQHSLTFAAEpSTAPNFPLKVFYPGPGHTRDNIVVGIDGTGIAFGGCLIRPS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1028105373 181 EWEGLGYVGDASISSWADSIKNIVSKKYPIQMVVPGHGKVGSSDILDHTIDLAE 234
Cdd:cd16300   161 KATSLGNLADADTEHWAASARAFGAAFPDASMIVPSHGAPDGRAAITHTARLAD 214
MUS_TUS_MBL-B1 cd16318
Myroides odoratimimus MUS-1, MUS-2, TUS-1 and related metallo-beta-lactamases, subclass B1; ...
 24-229 1.56e-43

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: 146.34  E-value: 1.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  24 LEVIKIEDGVYLHTSFKNIEGYGLvDSNGLVVLDNNQAYIIDTPWSEEDTKLLLSWA-TDRGYQVMASISTHSHGDRTAG 102
Cdd:cd16318     1 LKIKQLNDNMYIYTTYQEFQGVTY-SSNSMYVLTDEGVILIDTPWDKDQYEPLLEYIrSNHNKEVKWVITTHFHEDRSGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 103 IKLLNSKSIPTYTSELTKKLLAREGKPVPTHYF-KDDEFTLGNGLIELYYPGAGHTEDNIVAWLPKSKILFGGCLVRSHE 181
Cdd:cd16318    80 LGYFNSIGAQTYTYALTNEILKERNEPQAQFSFnKEKQFTFGNEKLAVYFLGEGHSLDNTVVWFPKEEVLYGGCLIKSAE 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1028105373 182 WEGLGYVGDASISSWADSIKNIVSKKYPIQMVVPGHGKVGSSDILDHT 229
Cdd:cd16318   160 ATTIGNIADGNVIAWPKTIEAVKQKFKNAKVIIPGHDEWDMSGHIENT 207
SPM-1-like_MBL-B1-B2-like cd16286
Pseudomonas areoginosa SPM-1 and related metallo-beta-lactamases, subclasses B1 and B2 like; ...
 24-234 3.50e-43

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: 146.14  E-value: 3.50e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  24 LEVIKIEDGVYLHTsfkNIEGYGlvdSNGLVVL-DNNQAYIIDTPWSEEDTKLLLSW-ATDRGYQVMASISTHSHGDRTA 101
Cdd:cd16286     7 LTAREIDPDVFVIT---HRDPWS---SNVLVVKmLDGTVVIVDSPYTNLATQTVLDWiAKTMGPRKVVAINTHFHLDGTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 102 GIKLLNSKSIPTYTSELTKKLLAREGK-----------------------PV-PTHYFKDDE---FTLGNGLIELYYPGA 154
Cdd:cd16286    81 GNEALKKRGIPTWGSDLTKQLLLERGKadrikaaeflknedlkrriesspPVpPDNVFDLKEgkvFSFGNELVEVSFPGP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 155 GHTEDNIVAWLPKSKILFGGCLVRSHewEGLGYVGDASISSWADSIKNIvsKKYPIQMVVPGHGKVGSSDILDHTIDLAE 234
Cdd:cd16286   161 AHAPDNVVVYFPERKILFGGCMIKPG--KELGNLGDANMKAWPDSVRRL--KKFDAKIVIPGHGERGDPGMVNKTIKVLE 236
IND_MBL-B1 cd16317
Chryseobacterium indologenes IND-1, IND-2, IND-7and related metallo-beta-lactamases, subclass ...
 29-232 8.38e-37

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: 128.98  E-value: 8.38e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  29 IEDGVYLHTSFkNIEGYGLVDSNGLVVLDNNQAYIIDTPWSEEDTKLLLSWATDRGY-QVMASISTHSHGDRTAGIKLLN 107
Cdd:cd16317     8 IKPNLYIYKTF-GVFGGKEYSANAVYLVTKKGVVLFDVPWQKVQYQSLMDTIQKRHHlPVIAVFATHSHDDRAGDLSFYN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 108 SKSIPTYTSELTKKLLAREGKPVPTHYFKDDE-FTLGNGLIELYYPGAGHTEDNIVAWLPKSKILFGGCLVRSHEWEGLG 186
Cdd:cd16317    87 NKGIKTYATAKTNEFLKKDGKATSTEIIKTGKpYRIGGEEFVVDFLGEGHTADNVVVWFPKYKVLDGGCLVKSNSATDLG 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1028105373 187 YVGDASISSWADSIKNIVSKKYPIQMVVPGHGKVGSSDILDHTIDL 232
Cdd:cd16317   167 YTGEANVEQWPKTMNKLKAKYAQATLIIPGHDEWKGGGHVEHTLDL 212
metallo-hydrolase-like_MBL-fold cd16282
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 32-227 1.10e-25

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: 99.95  E-value: 1.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  32 GVYLHTSfkniEGYGLVDSN-GLVVLDNnQAYIIDTPWSEEDTKLLLSWA---TDRGyqVMASISTHSHGDRTAGIKLLN 107
Cdd:cd16282     1 GVYALIG----PDGGGFISNiGFIVGDD-GVVVIDTGASPRLARALLAAIrkvTDKP--VRYVVNTHYHGDHTLGNAAFA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 108 SKSIPTYTSELTKKLLAREGKP-------------------VPTHYFKDD-EFTLGNGLIELYYPGAGHTEDNIVAWLPK 167
Cdd:cd16282    74 DAGAPIIAHENTREELAARGEAylelmrrlggdamagtelvLPDRTFDDGlTLDLGGRTVELIHLGPAHTPGDLVVWLPE 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 168 SKILFGGCLVrshEWEGLGYVGDASISSWADSIKNIvsKKYPIQMVVPGHGKVGSSDILD 227
Cdd:cd16282   154 EGVLFAGDLV---FNGRIPFLPDGSLAGWIAALDRL--LALDATVVVPGHGPVGDKADLR 208
GloB COG0491
Glyoxylase or a related metal-dependent hydrolase, beta-lactamase superfamily II [General ...
 47-234 2.59e-25

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: 98.99  E-value: 2.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  47 LVDSNGLVVLDNNQAYIIDTPWSEEDTKLLLSWATDRGYQVMASISTHSHGDRTAGIKLLNSKS-IPTYTSELTKKLLAR 125
Cdd:COG0491    12 GLGVNSYLIVGGDGAVLIDTGLGPADAEALLAALAALGLDIKAVLLTHLHPDHVGGLAALAEAFgAPVYAHAAEAEALEA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 126 EGK--------PVPTHYFKD-DEFTLGNGLIELYYpGAGHTEDNIVAWLPKSKILFGGCLVRSHEWeGLGYVGDASISSW 196
Cdd:COG0491    92 PAAgalfgrepVPPDRTLEDgDTLELGGPGLEVIH-TPGHTPGHVSFYVPDEKVLFTGDALFSGGV-GRPDLPDGDLAQW 169

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1028105373 197 ADSIKNIvsKKYPIQMVVPGHGKVGSSDILDHTIDLAE 234
Cdd:COG0491   170 LASLERL--LALPPDLVIPGHGPPTTAEAIDYLEELLA 205
Lactamase_B smart00849
Metallo-beta-lactamase superfamily; Apart from the beta-lactamases a number of other proteins ...
 51-217 3.66e-21

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: 87.22  E-value: 3.66e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373   51 NGLVVLDNNQAYIIDTPWSEEDtKLLLSWATDRGYQVMASISTHSHGDRTAGI-KLLNSKSIPTYTSELTKKLLARE--- 126
Cdd:smart00849   1 NSYLVRDDGGAILIDTGPGEAE-DLLAELKKLGPKKIDAIILTHGHPDHIGGLpELLEAPGAPVYAPEGTAELLKDLlal 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  127 --------GKPVPTHYFKD-DEFTLGNGLIELYYPgAGHTEDNIVAWLPKSKILFGGCLVRSHEWEGLGYVG-DASISSW 196
Cdd:smart00849  80 lgelgaeaEPAPPDRTLKDgDELDLGGGELEVIHT-PGHTPGSIVLYLPEGKILFTGDLLFAGGDGRTLVDGgDAAASDA 158

                          170       180
                   ....*....|....*....|.
gi 1028105373  197 ADSIKNIVSKKYPIqmVVPGH 217
Cdd:smart00849 159 LESLLKLLKLLPKL--VVPGH 177
metallo-hydrolase-like_MBL-fold cd06262
mainly hydrolytic enzymes and related proteins which carry out various biological functions; ...
 46-217 1.86e-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: 72.32  E-value: 1.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  46 GLVDSNGLVVLD-NNQAYIIDTPWSEEDtkLLLSWATDRGYQVMASISTHSHGDRTAGI-KLLNSKSIPTYTSELTKKLL 123
Cdd:cd06262     6 GPLQTNCYLVSDeEGEAILIDPGAGALE--KILEAIEELGLKIKAILLTHGHFDHIGGLaELKEAPGAPVYIHEADAELL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 124 AREGK------------PVPTHYFKD-DEFTLGNGLIE-LYYPGagHTEDNIVAWLPKSKILFGGCLV--RSHEWEGLGY 187
Cdd:cd06262    84 EDPELnlaffgggplppPEPDILLEDgDTIELGGLELEvIHTPG--HTPGSVCFYIEEEGVLFTGDTLfaGSIGRTDLPG 161

                         170       180       190
                  ....*....|....*....|....*....|
gi 1028105373 188 VGDASISswaDSIKNIVSKKYPIQMVVPGH 217
Cdd:cd06262   162 GDPEQLI---ESIKKLLLLLPDDTVVYPGH 188
metallo-hydrolase-like_MBL-fold cd16276
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 91-222 3.10e-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: 71.46  E-value: 3.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  91 ISTHSHGDRTAGIKLLNSKSIPTYTSELTKKLLAREGK---PVPTHYFKDD-EFTLGNGLIELYYPGAGHTEDNIVAWLP 166
Cdd:cd16276    50 VYSHNHADHIGGASIFKDEGATIIAHEATAELLKRNPDpkrPVPTVTFDDEyTLEVGGQTLELSYFGPNHGPGNIVIYLP 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1028105373 167 KSKILFGGCLVRSHEWEGLGYVGDASISSWADSIKNIVSkkYPIQMVVPGHG-KVGS 222
Cdd:cd16276   130 KQKVLMAVDLINPGWVPFFNFAGSEDIPGYIEALDELLE--YDFDTFVGGHGnRLGT 184
Sfh-1-like_MBL-B2 cd16305
Serratia fonticola Sfh-I and related metallo-beta-lactamases, subclass B2; MBL-fold ...
 37-236 6.69e-13

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: 65.79  E-value: 6.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  37 TSFKN----IEGYGLVDSNGLVVLDNNQAYIIDTPWSEEDTKLLLSWATD-RGYQVMASISTHSHGDRTAG---IKLLNS 108
Cdd:cd16305     4 THFKGplyiVEDKEYVQENSMVYIGTDGITIIGATWTPETAETLEKEIRKvSPLPIKEVINTNYHTDRAGGnayWKTLGA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 109 KSIPT-YTSELTKKL------LAREG--------KPVPTHYFKDDeFTLGNGLIELYYPGAGHTEDNIVAWLPKSKILFG 173
Cdd:cd16305    84 SIVSTqMTYDLEKSQwgsivdFTRQGnnkypnleKSLPDTVYPGD-FNLQNGSVRALYLGEAHTEDGIFVYFPAERVLYG 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1028105373 174 GCLVRshewEGLGYVGDASISSWADSIKN----IVSKKYPIQMVVPGHGK-VGSSDILDHTIDLAESA 236
Cdd:cd16305   163 NCILK----EKLGNMSFANRTEYPKTLKKlkglIEQGELKVESIIAGHDTpIHDVELIDHYLTLLEKA 226
CphA_ImiS-like_MBL-B2 cd16306
Aeromonas hydrophyla CphA, Aeromonas veronii ImiS, and related metallo-beta-lactamases, ...
 24-236 1.51e-12

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: 64.97  E-value: 1.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  24 LEVIKIEDGVYLhtsfknIEGYGLVDSNGLVVLDNNQAYIIDTPWSEEDTKLL---LSWATDRgyQVMASISTHSHGDRT 100
Cdd:cd16306     1 MSLTQVSGPVYV------VEDNYYVQENSMVYFGAKGVTVVGATWTPDTARELhklIKRVSRK--PVLEVINTNYHTDRA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 101 AGIKLLNSKSIPTYTSELTKKLL----------AREGKP--------VPTHYFKDDeFTLGNGLIELYYPGAGHTEDNIV 162
Cdd:cd16306    73 GGNAYWKSIGAKVVSTRQTRDLMksdwaeivafTRKGLPeypdlplvLPNVVHDGD-FTLQEGKVRAFYLGPAHTPDGIF 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028105373 163 AWLPKSKILFGGCLVRshewEGLGYVGDASISSWADSIKNIVSKKYPIQMVVPGH-GKVGSSDILDHTIDLAESA 236
Cdd:cd16306   152 VYFPDEQVLYGNCILK----EKLGNLSFADVKAYPQTLERLKAMKLPIKTVIGGHdSPLHGPELIDHYEALIKAA 222
CphS_ImiS-like_MBL-B2 cd16287
metallo-beta-lactamases, subclass B2; MBL-fold metallo-hydrolase domain; Includes Aeromonas ...
 48-236 2.20e-12

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: 64.37  E-value: 2.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  48 VDSNGLVVLDNNQAYIIDTPWSEEDTKLLLSWATDRGYQ-VMASISTHSHGDRTAGIKLLNSKSIPTYTSELTKKLL--- 123
Cdd:cd16287    19 VQENSMVYIGTDGITIIGATWTPETAETLYKEIRKVSPLpINEVINTNYHTDRAGGNAYWKTLGAKIVATQMTYDLQksq 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 124 -------AREGKP-------VPTHYFKDDEFTLGNGLIELYYPGAGHTEDNIVAWLPKSKILFGGCLVRshewEGLGYVG 189
Cdd:cd16287    99 wgsivnfTRQGNNkypnlekSLPDTVFPGDFNLQNGSIRAMYLGEAHTKDGIFVYFPAERVLYGNCILK----ENLGNMS 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1028105373 190 DASISSWADSIKNIVSKK----YPIQMVVPGH-GKVGSSDILDHTIDLAESA 236
Cdd:cd16287   175 FANRTEYPKTLEKLKGLIeqgeLKVDSIIAGHdTPIHDVGLIDHYLTLLEKA 226
Lactamase_B pfam00753
Metallo-beta-lactamase superfamily;
45-217 6.16e-10

Metallo-beta-lactamase superfamily;


Pssm-ID: 425851 [Multi-domain]  Cd Length: 196  Bit Score: 56.99  E-value: 6.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  45 YGLVDSNGLVVLDNNQAYIIDT-PWSEEDTKLLLSWATDRGYQVMASISTHSHGDRTAGI-KLLNSKSIPTYTSELTKKL 122
Cdd:pfam00753   1 LGPGQVNSYLIEGGGGAVLIDTgGSAEAALLLLLAALGLGPKDIDAVILTHGHFDHIGGLgELAEATDVPVIVVAEEARE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 123 LAREGKPVPTHYFK----------------DDEFTLGNGLIELYYPGAGHTEDNIVAWLPKSKILFGGCLVRSHEWE--- 183
Cdd:pfam00753  81 LLDEELGLAASRLGlpgppvvplppdvvleEGDGILGGGLGLLVTHGPGHGPGHVVVYYGGGKVLFTGDLLFAGEIGrld 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1028105373 184 ---GLGYVGDASI-SSWADSIKNIVSKKYPIqmVVPGH 217
Cdd:pfam00753 161 lplGGLLVLHPSSaESSLESLLKLAKLKAAV--IVPGH 196
hydroxyacylglutathione_hydrolase_MBL-fold cd07723
hydroxyacylglutathione hydrolase, MBL-fold metallo-hydrolase domain; hydroxyacylglutathione ...
 57-175 9.40e-09

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


Pssm-ID: 293809 [Multi-domain]  Cd Length: 165  Bit Score: 53.23  E-value: 9.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  57 DNNQAYIIDTPWSEEdtklLLSWATDRGYQVMASISTHSHGDRTAGIKLL--NSKSIPTYTSELTKkllaregKPVPTHY 134
Cdd:cd07723    18 ATGEAAVVDPGEAEP----VLAALEKNGLTLTAILTTHHHWDHTGGNAELkaLFPDAPVYGPAEDR-------IPGLDHP 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1028105373 135 FKD-DEFTLGNGLIE-LYYPgaGHTEDNIVAWLPKSKILF-------GGC 175
Cdd:cd07723    87 VKDgDEIKLGGLEVKvLHTP--GHTLGHICYYVPDEPALFtgdtlfsGGC 134
arylsulfatase_Sdsa1-like_MBL-fold cd07710
Pseudomonas aeruginosa arylsulfatase SdsA1, Pseudomonas sp. DSM6611 arylsulfatase Pisa1, and ...
 25-218 4.38e-08

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


Pssm-ID: 293796 [Multi-domain]  Cd Length: 239  Bit Score: 52.12  E-value: 4.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  25 EVIKIEDGVYlhtsfkNIEGYGLvdSNGLVVLDNNQAYIIDTPWSEEDTK----LLLSWATDRgyQVMASISTHSHGDRT 100
Cdd:cd07710     1 GLFEVTDGVY------QVRGYDL--SNMTFIEGDTGLIIIDTLESAEAAKaaleLFRKHTGDK--PVKAIIYTHSHPDHF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 101 AGIKLL----NSKSIPTYTSELTKKLLARE--------------------------------GKPV---------PTHYF 135
Cdd:cd07710    71 GGAGGFveeeDSGKVPIIAPEGFMEEAVSEnvlagnamsrraayqfgallpkgekgqvgaglGPGLstgtvgfipPTITI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 136 KDD--EFTLGnGL-IELYY-PGAghTEDNIVAWLPKSKILFG---------------GCLVRsheweglgyvgdaSISSW 196
Cdd:cd07710   151 TETgeTLTID-GVeLEFQHaPGE--APDEMMVWLPDYKVLFCadnvyhtfpnlytlrGAKYR-------------DALAW 214

                         250       260
                  ....*....|....*....|..
gi 1028105373 197 ADSIKNIVSkkYPIQMVVPGHG 218
Cdd:cd07710   215 AKSLDEAIS--LKAEVLFPSHT 234
metallo-hydrolase-like_MBL-fold cd07739
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 61-217 6.31e-08

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


Pssm-ID: 293825 [Multi-domain]  Cd Length: 201  Bit Score: 51.35  E-value: 6.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  61 AYIIDTPWSEEDTKLLLSWATDRGYQVMASISTHSHGDRTAGIKLL-----------NSKSIPTYTSELTKKLL---ARE 126
Cdd:cd07739    27 AVLVDAQFTRADAERLADWIKASGKTLTTIYITHGHPDHYFGLEVLleafpdakvvaTPAVVAHIKAQLEPKLAfwgPLL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 127 GKPVPTH-----YFKDDEFTLGNGLIELYYPGAGHTEDNIVAWLPKSKILFGGCLV--RSHEWeglgyVGD----ASISS 195
Cdd:cd07739   107 GGNAPARlvvpePLDGDTLTLEGHPLEIVGVGGGDTDDTTYLWIPSLKTVVAGDVVynGVHVW-----LADattpELRAA 181

                         170       180
                  ....*....|....*....|..
gi 1028105373 196 WADSIKNIVSKKyPiQMVVPGH 217
Cdd:cd07739   182 WLAALDKIEALN-P-ETVVPGH 201
yflN-like_MBL-fold cd07721
uncharacterized subgroup which includes Bacillus subtilis yflN; MBL-fold metallo hydrolase ...
 54-218 2.92e-07

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


Pssm-ID: 293807 [Multi-domain]  Cd Length: 202  Bit Score: 49.53  E-value: 2.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  54 VVLDNNQAYIIDT--PWSEedtKLLLSWATDRGYQVmASIS----THSHGDRTAGIKLLNSKS-IPTYTSELTKKLLARE 126
Cdd:cd07721    15 LIEDDDGLTLIDTglPGSA---KRILKALRELGLSP-KDIRrillTHGHIDHIGSLAALKEAPgAPVYAHEREAPYLEGE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 127 GKPVPTHYF--------------KDDEFTLGNGLIELYYPGA------GHTEDNIVAWLPKSKILFGGCLVRSHEweglg 186
Cdd:cd07721    91 KPYPPPVRLgllgllspllpvkpVPVDRTLEDGDTLDLAGGLrvihtpGHTPGHISLYLEEDGVLIAGDALVTVG----- 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1028105373 187 yvGDASISSWA---------DSIKNIvsKKYPIQMVVPGHG 218
Cdd:cd07721   166 --GELVPPPPPftwdmeealESLRKL--AELDPEVLAPGHG 202
LACTB2-like_MBL-fold cd07722
uncharacterized subgroup which includes human lactamase beta 2 and related proteins; MBL-fold ...
 89-174 2.26e-06

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


Pssm-ID: 293808 [Multi-domain]  Cd Length: 188  Bit Score: 46.76  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  89 ASIS----THSHGDRTAGI----KLLNSKSIPTYTSELTKKLLAREGKPVPTHYFKD-DEFTLGNGLIELYY-PgaGHTE 158
Cdd:cd07722    55 ATISdillTHWHHDHVGGLpdvlDLLRGPSPRVYKFPRPEEDEDPDEDGGDIHDLQDgQVFKVEGATLRVIHtP--GHTT 132

                          90
                  ....*....|....*.
gi 1028105373 159 DNIVAWLPKSKILFGG 174
Cdd:cd07722   133 DHVCFLLEEENALFTG 148
flavodiiron_proteins_MBL-fold cd07709
catalytic domain of flavodiiron proteins (FDPs) and related proteins; MBL-fold ...
 91-233 1.82e-05

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


Pssm-ID: 293795 [Multi-domain]  Cd Length: 238  Bit Score: 44.40  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  91 ISTHSHGDRTAGIKLLNSK--SIPTYTSELTKKLL-------AREGKPVPThyfkDDEFTLGNGLIELY---YPgagHTE 158
Cdd:cd07709    73 VVNHQEPDHSGSLPELLELapNAKIVCSKKAARFLkhfypgiDERFVVVKD----GDTLDLGKHTLKFIpapML---HWP 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 159 DNIVAWLPKSKILF----GGCLVRSHEWEglgyvgDASISSWADSIK----NIVS-------------KKYPIQMVVPGH 217
Cdd:cd07709   146 DTMVTYDPEDKILFsgdaFGAHGASGELF------DDEVEDYLEEARryyaNIMGpfskqvrkaleklEALDIKMIAPSH 219

                         170
                  ....*....|....*....
gi 1028105373 218 G---KVGSSDILDHTIDLA 233
Cdd:cd07709   220 GpiwRKDPGEIIDLYRDWS 238
MBLAC2-like_MBL-fold cd07712
uncharacterized human metallo-beta-lactamase domain-containing protein 2 and related proteins; ...
 59-217 1.59e-04

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


Pssm-ID: 293798 [Multi-domain]  Cd Length: 182  Bit Score: 41.46  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  59 NQAYIIDTPWSEEDTKLLLSWATDRGYQVmasISTHSHGDRTAGIK-----LLNSKS---IPTYTSELTKKLLAREG--- 127
Cdd:cd07712    18 DRALLIDTGLGIGDLKEYVRTLTDLPLLV---VATHGHFDHIGGLHefeevYVHPADaeiLAAPDNFETLTWDAATYsvp 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 128 KPVPTHYFKD-DEFTLGNGLIELYY-PGagHTEDNIVAWLPKSKILFGGCLVRSHEWEGLGYVGDasISSWADSIKNIVS 205
Cdd:cd07712    95 PAGPTLPLRDgDVIDLGDRQLEVIHtPG--HTPGSIALLDRANRLLFSGDVVYDGPLIMDLPHSD--LDDYLASLEKLSK 170

                         170
                  ....*....|..
gi 1028105373 206 KKYPIQMVVPGH 217
Cdd:cd07712   171 LPDEFDKVLPGH 182
metallo-hydrolase-like_MBL-fold cd07743
uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo ...
 52-217 2.41e-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) 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: 40.98  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  52 GLVVLDNNQAYIIDTPWSEEDTKLLLSWATDRGYQVMASISTHSHGDRTAGIKLLNSKS-------------------IP 112
Cdd:cd07743    11 GVYVFGDKEALLIDSGLDEDAGRKIRKILEELGWKLKAIINTHSHADHIGGNAYLQKKTgckvyapkiekafienpllEP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373 113 TYTS------ELTKKLLarEGKPVP-THYFKDDEFTLGNGLIELyYPGAGHTEDNIvAWLPKSKILF-GGCLVRSHEWE- 183
Cdd:cd07743    91 SYLGgayppkELRNKFL--MAKPSKvDDIIEEGELELGGVGLEI-IPLPGHSFGQI-GILTPDGVLFaGDALFGEEVLEk 166

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1028105373 184 -GLGYVGDasISSWADSIKNIVSKKYpiQMVVPGH 217
Cdd:cd07743   167 yGIPFLYD--VEEQLETLEKLEELDA--DYYVPGH 197
NorV COG0426
Flavorubredoxin [Energy production and conversion];
98-218 4.09e-03

Flavorubredoxin [Energy production and conversion];


Pssm-ID: 440195 [Multi-domain]  Cd Length: 390  Bit Score: 37.89  E-value: 4.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1028105373  98 DRTAGIKLLNSKS--IPTYTSELTKKLL-------AREGKPVPThyfkDDEFTLGNGLIELY---YPgagHTEDNIVAWL 165
Cdd:COG0426    82 DHSGSLPELLELApnAKIVCSKKAARFLphfygipDFRFIVVKE----GDTLDLGGHTLQFIpapML---HWPDTMFTYD 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1028105373 166 PKSKILF----GGCLVRSH-----EWEGLgYVGDA-------------SISSWADSIKNIvskkyPIQMVVPGHG 218
Cdd:COG0426   155 PEDKILFsgdaFGSHGASDelfddEVDEH-LEEEArryyanimmpfskQVLKALKKVRGL-----DIDMIAPSHG 223
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH